CXC-R4
CXCR-4
Stromal cell-derived factor 1 receptor
SDF-1 receptor
Fusin
Leukocyte-derived seven transmembrane domain receptor
LESTR
LCR1
FB22
NPYRL
HM89
CD184 antigen

Gene name

Name:

CXCR4

From

Homo sapiens (Human)

[TaxID: 9606]

Taxonomy

Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; Homo.

Protein existence

1: Evidence at protein level;

References

[1]	NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND PRELIMINARY FUNCTION. TISSUE=Lung; DOI=10.1089/dna.1993.12.465; PubMed=8329116 [NCBI, ExPASy, EBI, Israel, Japan] Herzog H., Hort Y.J., Shine J., Selbie L.A.; "Molecular cloning, characterization, and localization of the human homolog to the reported bovine NPY Y3 receptor: lack of NPY binding and activation."; DNA Cell Biol. 12:465-471(1993).
[2]	NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND PRELIMINARY FUNCTION. TISSUE=Fetal brain; DOI=10.1016/0167-0115(93)90392-L; PubMed=8234909 [NCBI, ExPASy, EBI, Israel, Japan] Jazin E.E., Yoo H., Blomqvist A.G., Yee F., Weng G., Walker M.W., Salon J., Larhammar D., Wahlestedt C.R.; "A proposed bovine neuropeptide Y (NPY) receptor cDNA clone, or its human homologue, confers neither NPY binding sites nor NPY responsiveness on transfected cells."; Regul. Pept. 47:247-258(1993).
[3]	NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). TISSUE=Fetal spleen; DOI=10.1006/geno.1993.1251; PubMed=8325644 [NCBI, ExPASy, EBI, Israel, Japan] Federsppiel B., Melhado I.G., Duncan A.M.V., Delaney A.D., Schappert K., Clark-Lewis I., Jirik F.R.; "Molecular cloning of the cDNA and chromosomal localization of the gene for a putative seven-transmembrane segment (7-TMS) receptor isolated from human spleen."; Genomics 16:707-712(1993).
[4]	NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). TISSUE=Monocyte; PubMed=8276799 [NCBI, ExPASy, EBI, Israel, Japan] Loetscher M., Geiser T., O'Reilly T., Zwahlen R., Baggiolini M., Moser B.; "Cloning of a human seven-transmembrane domain receptor, LESTR, that is highly expressed in leukocytes."; J. Biol. Chem. 269:232-237(1994).
[5]	NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). DOI=10.1093/intimm/5.10.1239; PubMed=7505609 [NCBI, ExPASy, EBI, Israel, Japan] Nomura H., Nielsen B.W., Matsushima K.; "Molecular cloning of cDNAs encoding a LD78 receptor and putative leukocyte chemotactic peptide receptors."; Int. Immunol. 5:1239-1249(1993).
[6]	NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND CHARACTERIZATION OF ITS HIV-1 CORECEPTOR FUNCTION. DOI=10.1126/science.272.5263.872; PubMed=8629022 [NCBI, ExPASy, EBI, Israel, Japan] Feng Y., Broder C.C., Kennedy P.E., Berger E.A.; "HIV-1 entry cofactor: functional cDNA cloning of a seven-transmembrane, G protein-coupled receptor."; Science 272:872-877(1996).
[7]	NUCLEOTIDE SEQUENCE [GENOMIC DNA]. TISSUE=Peripheral blood leukocyte; DOI=10.1074/jbc.273.8.4754; PubMed=9468539 [NCBI, ExPASy, EBI, Israel, Japan] Wegner S.A., Ehrenberg P.K., Chang G., Dayhoff D.E., Sleeker A.L., Michael N.L.; "Genomic organization and functional characterization of the chemokine receptor CXCR4, a major entry co-receptor for human immunodeficiency virus type 1."; J. Biol. Chem. 273:4754-4760(1998).
[8]	NUCLEOTIDE SEQUENCE [GENOMIC DNA]. DOI=10.1016/S0014-5793(98)00359-7; PubMed=9599023 [NCBI, ExPASy, EBI, Israel, Japan] Caruz A., Samsom M., Alonso J.M., Alcami J., Baleux F., Virelizier J.-L., Parmentier M., Arenzana-Seisdedos F.; "Genomic organization and promoter characterization of human CXCR4 gene."; FEBS Lett. 426:271-278(1998).
[9]	NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). DOI=10.1089/088922299310296; PubMed=10480633 [NCBI, ExPASy, EBI, Israel, Japan] Xiao L., Weiss S.H., Qari S.H., Rudolph D., Zhao C., Denny T.N., Hodge T., Lal R.B.; "Partial resistance to infection by R5X4 primary HIV type 1 isolates in an exposed-uninfected individual homozygous for CCR5 32-base pair deletion."; AIDS Res. Hum. Retroviruses 15:1201-1208(1999).
[10]	NUCLEOTIDE SEQUENCE [GENOMIC DNA]. TISSUE=Peripheral blood lymphocyte; PubMed=9879064 [NCBI, ExPASy, EBI, Israel, Japan] Frodl R., Gierschik P., Moepps B.; "Genomic organization and expression of the CXCR4 gene in mouse and man: absence of a splice variant corresponding to mouse CXCR4-B in human tissues."; J. Recept. Signal Transduct. 18:321-344(1998).
[11]	NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2). TISSUE=Neutrophil; PubMed=10452968 [NCBI, ExPASy, EBI, Israel, Japan] Gupta S.K., Pillarisetti K.; "CXCR4-Lo: molecular cloning and functional expression of a novel human CXCR4 splice variant."; J. Immunol. 163:2368-2372(1999).
[12]	NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). TISSUE=Lung; Warren C.N., Aronstam R.S., Sharma S.V.; "cDNA clones of human proteins involved in signal transduction sequenced by the Guthrie cDNA resource center (www.cdna.org)."; Submitted (FEB-2003) to the EMBL/GenBank/DDBJ databases.
[13]	NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., Phelan M., Farmer A.; "Cloning of human full-length CDSs in BD Creator(TM) system donor vector."; Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
[14]	NUCLEOTIDE SEQUENCE [GENOMIC DNA]. SeattleSNPs variation discovery resource; Submitted (AUG-2004) to the EMBL/GenBank/DDBJ databases.
[15]	NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). TISSUE=Colon; DOI=10.1101/gr.2596504; PubMed=15489334 [NCBI, ExPASy, EBI, Israel, Japan] The MGC Project Team; "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."; Genome Res. 14:2121-2127(2004).
[16]	FUNCTION. DOI=10.1038/382829a0; PubMed=8752280 [NCBI, ExPASy, EBI, Israel, Japan] Bleul C.C., Farzan M., Choe H., Parolin C., Clark-Lewis I., Sodroski J., Springer T.A.; "The lymphocyte chemoattractant SDF-1 is a ligand for LESTR/fusin and blocks HIV-1 entry."; Nature 382:829-833(1996).
[17]	FUNCTION. DOI=10.1038/382833a0; PubMed=8752281 [NCBI, ExPASy, EBI, Israel, Japan] Oberlin E., Amara A., Bachelerie F., Bessia C., Virelizier J.-L., Arenzana-Seisdedos F., Schwartz O., Heard J.-M., Clark-Lewis I., Legler D.F., Loetscher M., Baggiolini M., Moser B.; "The CXC chemokine SDF-1 is the ligand for LESTR/fusin and prevents infection by T-cell-line-adapted HIV-1."; Nature 382:833-835(1996).
[18]	ERRATUM. Oberlin E., Amara A., Bachelerie F., Bessia C., Virelizier J.-L., Arenzana-Seisdedos F., Schwartz O., Heard J.-M., Clark-Lewis I., Legler D.F., Loetscher M., Baggiolini M., Moser B.; Nature 384:288-288(1996).
[19]	CHARACTERIZATION AS HIV-1 CORECEPTOR. DOI=10.1126/science.274.5287.602; PubMed=8849450 [NCBI, ExPASy, EBI, Israel, Japan] Lapham C.K., Ouyang J., Chandrasekhar B., Nguyen N.Y., Dimitrov D.S., Golding H.; "Evidence for cell-surface association between fusin and the CD4-gp120 complex in human cell lines."; Science 274:602-605(1996).
[20]	CHARACTERIZATION AS HIV-2 PRIMARY RECEPTOR IN SOME ISOLATES. DOI=10.1016/S0092-8674(00)81393-8; PubMed=8929542 [NCBI, ExPASy, EBI, Israel, Japan] Endres M.J., Clapham P.R., Marsh M., Ahuja M., Turner J.D., McKnight A., Thomas J.F., Stoebenau-Haggarty B., Choe S., Vance P.J., Wells T.N.C., Power C.A., Sutterwala S.S., Doms R.W., Landau N.R., Hoxie J.A.; "CD4-independent infection by HIV-2 is mediated by fusin/CXCR4."; Cell 87:745-756(1996).
[21]	SULFATION. DOI=10.1016/S0092-8674(00)80577-2; PubMed=10089882 [NCBI, ExPASy, EBI, Israel, Japan] Farzan M., Mirzabekov T., Kolchinsky P., Wyatt R., Cayabyab M., Gerard N.P., Gerard C., Sodroski J., Choe H.; "Tyrosine sulfation of the amino terminus of CCR5 facilitates HIV-1 entry."; Cell 96:667-676(1999).
[22]	DOMAINS, AND INTERACTION WITH HIV-1 SURFACE PROTEIN GP120. PubMed=10074122 [NCBI, ExPASy, EBI, Israel, Japan] Doranz B.J., Orsini M.J., Turner J.D., Hoffman T.L., Berson J.F., Hoxie J.A., Peiper S.C., Brass L.F., Doms R.W.; "Identification of CXCR4 domains that support coreceptor and chemokine receptor functions."; J. Virol. 73:2752-2761(1999).
[23]	GLYCOSYLATION AT ASN-11, INTERACTION WITH HIV-1 ENV, SUBUNIT, AND MUTAGENESIS OF ASN-11; THR-13 AND ASN-176. DOI=10.1128/JVI.74.9.4404-4413.2000; PubMed=10756055 [NCBI, ExPASy, EBI, Israel, Japan] Chabot D.J., Chen H., Dimitrov D.S., Broder C.C.; "N-linked glycosylation of CXCR4 masks coreceptor function for CCR5-dependent human immunodeficiency virus type 1 isolates."; J. Virol. 74:4404-4413(2000).
[24]	INTERACTION WITH HIV-1 TAT. DOI=10.1073/pnas.97.21.11466; PubMed=11027346 [NCBI, ExPASy, EBI, Israel, Japan] Xiao H., Neuveut C., Tiffany H.L., Benkirane M., Rich E.A., Murphy P.M., Jeang K.-T.; "Selective CXCR4 antagonism by Tat: implications for in vivo expansion of coreceptor use by HIV-1."; Proc. Natl. Acad. Sci. U.S.A. 97:11466-11471(2000).
[25]	GLYCOSYLATION AT SER-18, IDENTIFICATION OF PROTEOGLYCAN, INTERACTION WITH CXCL12, SULFATION AT TYR-21, AND MUTAGENESIS OF TYR-7; THR-8; SER-9; TYR-12; SER-18 AND TYR-21. DOI=10.1074/jbc.M203361200; PubMed=12034737 [NCBI, ExPASy, EBI, Israel, Japan] Farzan M., Babcock G.J., Vasilieva N., Wright P.L., Kiprilov E., Mirzabekov T., Choe H.; "The role of post-translational modifications of the CXCR4 amino terminus in stromal-derived factor 1 alpha association and HIV-1 entry."; J. Biol. Chem. 277:29484-29489(2002).
[26]	DISEASE. DOI=10.1038/ng1149; PubMed=12692554 [NCBI, ExPASy, EBI, Israel, Japan] Hernandez P.A., Gorlin R.J., Lukens J.N., Taniuchi S., Bohinjec J., Francois F., Klotman M.E., Diaz G.A.; "Mutations in the chemokine receptor gene CXCR4 are associated with WHIM syndrome, a combined immunodeficiency disease."; Nat. Genet. 34:70-74(2003).
[27]	PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-319, AND MASS SPECTROMETRY. DOI=10.1021/pr0705441; PubMed=18220336 [NCBI, ExPASy, EBI, Israel, Japan] Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III; "Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient phosphoproteomic analysis."; J. Proteome Res. 7:1346-1351(2008).
[28]	PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-319; SER-348 AND SER-351, AND MASS SPECTROMETRY. DOI=10.1073/pnas.0805139105; PubMed=18669648 [NCBI, ExPASy, EBI, Israel, Japan] Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.; "A quantitative atlas of mitotic phosphorylation."; Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
[29]	STRUCTURE BY NMR OF 1-38, SULFATION AT TYR-21, MASS SPECTROMETRY, AND INTERACTION WITH CXCL12. DOI=10.1016/j.jmb.2006.04.052; PubMed=16725153 [NCBI, ExPASy, EBI, Israel, Japan] Veldkamp C.T., Seibert C., Peterson F.C., Sakmar T.P., Volkman B.F.; "Recognition of a CXCR4 sulfotyrosine by the chemokine stromal cell-derived factor-1alpha (SDF-1alpha/CXCL12)."; J. Mol. Biol. 359:1400-1409(2006).

Comments

FUNCTION: Receptor for the C-X-C chemokine CXCL12/SDF-1. Transduces a signal by increasing the intracellular calcium ions level. Involved in haematopoiesis and in cardiac ventricular septum formation. Plays also an essential role in vascularization of the gastrointestinal tract, probably by regulating vascular branching and/or remodeling processes in endothelial cells. Could be involved in cerebellar development. In the CNS, could mediate hippocampal-neuron survival. Acts as a coreceptor (CD4 being the primary receptor) for HIV-1 X4 isolates and as a primary receptor for some HIV-2 isolates. Promotes Env-mediated fusion of the virus.
SUBUNIT: Monomer. Can form dimers. Interacts with HIV-1 surface protein gp120 and Tat.
INTERACTION:
P35579:MYH9; NbExp=4; IntAct=EBI-489411, EBI-350338;
SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein.

ALTERNATIVE PRODUCTS: 2 named isoforms [FASTA] produced by alternative splicing. Additional isoforms seem to exist.

Name	1
Isoform ID	P61073-1, P30991-1
This is the isoform sequence displayed in this entry.

Name	2
Synonyms	CXCR4-LO
Isoform ID	P61073-2, P30991-2
Features which should be applied to build the isoform sequence: VSP_001890.

TISSUE SPECIFICITY: Expressed in numerous tissues, such as peripheral blood leukocytes, spleen, thymus, spinal cord, heart, placenta, lung, liver, skeletal muscle, kidney, pancreas, cerebellum, cerebral cortex and medulla (in microglia as well as in astrocytes), brain microvascular, coronary artery and umbilical cord endothelial cells. Isoform 1 is predominant in all tissues tested.
DOMAIN: The amino-terminus is critical for ligand binding. Residues in all four extracellular regions contribute to HIV-1 coreceptor activity.
PTM: Sulfation on Tyr-21 is required for efficient binding of CXCL12/SDF-1alpha and promotes its dimerization.
PTM: O- and N-glycosylated. Asn-11 is the principal site of N-glycosylation. There appears to be very little or no glycosylation on Asn-176. N-glycosylation masks coreceptor function in both X4 and R5 laboratory-adapted and primary HIV-1 strains through inhibiting interaction with their Env glycoproteins. The O-glycosylation chondroitin sulfate attachment does not affect interaction with CXCL12/SDF-1alpha nor its coreceptor activity.
DISEASE: Defects in CXCR4 are a cause of WHIM syndrome [MIM:193670]; also called warts, hypogammaglobulinemia, infections, and myelokathexis. WHIM syndrome is an immunodeficiency disease characterized by neutropenia, hypogammaglobulinemia and extensive human papillomavirus (HPV) infection. Despite the peripheral neutropenia, bone marrow aspirates from affected individuals contain abundant mature myeloid cells, a condition termed myelokathexis.
SIMILARITY: Belongs to the G-protein coupled receptor 1 family [view classification].
CAUTION: Was originally (PubMed:8329116 and PubMed:8234909) thought to be a receptor for neuropeptide Y type 3 (NPY3R) (NPY3-R).
WEB RESOURCE: Name=CXCR4base; Note=CXCR4 mutation db; URL="http://bioinf.uta.fi/CXCR4base/";.
WEB RESOURCE: Name=Wikipedia; Note=CXC chemokine receptors entry; URL="http://en.wikipedia.org/wiki/CXC_chemokine_receptors";.
WEB RESOURCE: Name=Wikipedia; Note=CXCR4 entry; URL="http://en.wikipedia.org/wiki/CXCR4";.
WEB RESOURCE: Name=SeattleSNPs; URL="http://pga.gs.washington.edu/data/cxcr4/";.

Copyright

Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.

Cross-references

Sequence databases

EMBL

L01639; AAA16594.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
M99293; AAA16617.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
X71635; CAA50641.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
L06797; AAA03209.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
D10924; BAA01722.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AF005058; AAB93982.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AF052572; AAC34581.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AF025375; AAB81970.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
Y14739; CAA75034.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AJ224869; CAA12166.1; ALT_SEQ; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AF147204; AAF00130.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AY242129; AAO92296.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
BT006660; AAP35306.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AY728138; AAU05775.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
BC020968; AAH20968.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

IPI

IPI00028159; -.
IPI00216445; -.

PIR

A45747; A45747.

RefSeq

NP_001008540.1; -.
NP_003458.1; -.

UniGene

Hs.593413

3D structure databases

PDB

2K03; NMR; -; B/D=1-38.	[ExPASy / RCSB / EBI]
2K04; NMR; -; B/D=1-38.	[ExPASy / RCSB / EBI]
2K05; NMR; -; B/D=1-38.	[ExPASy / RCSB / EBI]

Detailed list of linked structures.

PDBsum

2K03; -.
2K04; -.
2K05; -.

ModBase

P61073.

Protein-protein interaction databases

IntAct

P61073; 2.

Protein family/group databases

GPCRDB

P61073; CXCR4_HUMAN.

PTM databases

PhosphoSite

P61073; -.

Enzyme and pathway databases

Pathway_Interaction_DB

ephrinbrevpathway; Ephrin B reverse signaling.
hif1_tfpathway; HIF-1-alpha transcription factor network.
s1p_s1p3_pathway; S1P3 pathway.
syndecan_4_pathway; Syndecan-4-mediated signaling events.

Reactome

REACT_14797; Signaling by GPCR.
REACT_6185; HIV Infection.

Organism-specific databases

GC02M136588; -.

HIX0002482; -.

HGNC:2561; CXCR4.

CAB011447; -.

162643; gene. [NCBI / EBI]
193670; phenotype. [NCBI / EBI]

Orphanet

51636; WHIM syndrome.

PharmGKB

PA27058; -.

Gene expression databases

P61073; -.

P61073; -.

HS_CXCR4; -.

ENSG00000121966; Homo sapiens.

Ontologies

GO:0031252;	Cellular component: cell leading edge (inferred from direct assay from UniProtKB).
GO:0005737;	Cellular component: cytoplasm (traceable author statement from ProtInc).
GO:0005887;	Cellular component: integral to plasma membrane (traceable author statement from ProtInc).
GO:0003779;	Molecular function: actin binding (inferred from direct assay from UniProtKB).
GO:0016493;	Molecular function: C-C chemokine receptor activity (inferred from electronic annotation from InterPro).
GO:0016494;	Molecular function: C-X-C chemokine receptor activity (non-traceable author statement from UniProtKB).
GO:0015026;	Molecular function: coreceptor activity (traceable author statement from ProtInc).
GO:0032027;	Molecular function: myosin light chain binding (inferred from direct assay from UniProtKB).
GO:0000187;	Biological process: activation of MAPK activity (traceable author statement from ProtInc).
GO:0006915;	Biological process: apoptosis (traceable author statement from ProtInc).
GO:0006935;	Biological process: chemotaxis (traceable author statement from ProtInc).
GO:0007204;	Biological process: elevation of cytosolic calcium ion concentration (traceable author statement from ProtInc).
GO:0007186;	Biological process: G-protein coupled receptor protein signaling pathway (traceable author statement from ProtInc).
GO:0006955;	Biological process: immune response (traceable author statement from ProtInc).
GO:0006954;	Biological process: inflammatory response (traceable author statement from ProtInc).
GO:0019059;	Biological process: initiation of viral infection (inferred from experiment from Reactome).
GO:0044419;	Biological process: interspecies interaction between organisms (inferred from electronic annotation from UniProtKB-KW).
GO:0001666;	Biological process: response to hypoxia (inferred from expression pattern from UniProtKB).
GO:0009615;	Biological process: response to virus (traceable author statement from ProtInc).
QuickGo view.

Family and domain databases

InterPro

IPR000276; 7TM_GPCR_Rhodpsn.
IPR000355; Chmkine_rcpt.
IPR001277; CXC_4_rcpt.
IPR017452; GPCR_Rhodpsn_supfam.
Graphical view of domain structure.

Pfam

PF00001; 7tm_1; 1.
Pfam graphical view of domain structure.

PRINTS

PR00657; CCCHEMOKINER.
PR00645; CXCCHMKINER4.
PR00237; GPCRRHODOPSN.

PROSITE

PS00237; G_PROTEIN_RECEP_F1_1; 1.
PS50262; G_PROTEIN_RECEP_F1_2; 1.
PROSITE graphical view of domain structure (profiles).

Proteomic databases

PRIDE

P61073; -.

Genome annotation databases

Ensembl

ENSG00000121966; Homo sapiens. [Contig view]

GeneID

7852; -.

KEGG

hsa:7852; -.

Phylogenomic databases

HOGENOM

P61073; -.

HOVERGEN

P61073; -.

OMA

P61073; FNRIFLP.

Other

DB00452; Framycetin.

30286; -.

P61073; -.

CXCR4; Homo sapiens.

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

3D-structure; Alternative splicing; Cell membrane; Disulfide bond; G-protein coupled receptor; Glycoprotein; Host-virus interaction; Membrane; Phosphoprotein; Proteoglycan; Receptor; Sulfation; Transducer; Transmembrane.

Features

Feature table viewer

Feature aligner

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 352`	`352`	`C-X-C chemokine receptor type 4.`	`PRO_0000069352`
`TOPO_DOM`	`1 39`	`39`	`Extracellular (Potential).`
`TRANSMEM`	`40 63`	`24`	`1 (Potential).`
`TOPO_DOM`	`64 79`	`16`	`Cytoplasmic (Potential).`
`TRANSMEM`	`80 99`	`20`	`2 (Potential).`
`TOPO_DOM`	`100 110`	`11`	`Extracellular (Potential).`
`TRANSMEM`	`111 132`	`22`	`3 (Potential).`
`TOPO_DOM`	`133 154`	`22`	`Cytoplasmic (Potential).`
`TRANSMEM`	`155 175`	`21`	`4 (Potential).`
`TOPO_DOM`	`176 200`	`25`	`Extracellular (Potential).`
`TRANSMEM`	`201 220`	`20`	`5 (Potential).`
`TOPO_DOM`	`221 240`	`20`	`Cytoplasmic (Potential).`
`TRANSMEM`	`241 261`	`21`	`6 (Potential).`
`TOPO_DOM`	`262 285`	`24`	`Extracellular (Potential).`
`TRANSMEM`	`286 305`	`20`	`7 (Potential).`
`TOPO_DOM`	`306 352`	`47`	`Cytoplasmic (Potential).`
`MOTIF`	`133 135`	`3`	`Important for signaling.`
`MOD_RES`	`21 21`		`Sulfotyrosine.`
`MOD_RES`	`319 319`		`Phosphoserine.`
`MOD_RES`	`348 348`		`Phosphoserine.`
`MOD_RES`	`351 351`		`Phosphoserine.`
`CARBOHYD`	`11 11`		`N-linked (GlcNAc...).`
`CARBOHYD`	`18 18`		`O-linked (Xyl...) (chondroitin sulfate).`
`CARBOHYD`	`176 176`		`N-linked (GlcNAc...) (Potential).`
`DISULFID`	`109 186`		`By similarity.`
`VAR_SEQ`	`1 5`		`MEGIS -> MSIPLPLLQ (in isoform 2).`	`VSP_001890`
`MUTAGEN`	`7 7`		`Y->F: Sulfate incorporation greatly reduced; when associated with F-12 and F-21. Moderate reduction in sulfate incorporation; when associated with F-12 and A-18. No sulfate incorporation and binding PDF1alpha greatly reduced; when associated with F-12; A-18 and F-21.`
`MUTAGEN`	`8 8`		`T->A: No effect on sulfate incorporation; when associated with A-9 and A-13.`
`MUTAGEN`	`9 9`		`S->A: No effect on sulfate incorporation; when associated with A-8 and A-13.`
`MUTAGEN`	`11 11`		`N->A: Reduced molecular weight. Enhanced coreceptor activity on R5 HIV-1 isolate Envs. Slight further enhancement of coreceptor activity; when associated with A-13.`
`MUTAGEN`	`12 12`		`Y->F: Sulfate incorporation greatly reduced; when associated with F-7 and F-21. Moderate reduction in sulfate incorporation; when associated with F-7 and A-18. No sulfate incorporation and binding PDF1alpha greatly reduced; when associated with F-7; A-18 and F-21.`
`MUTAGEN`	`13 13`		`T->A: Enhanced coreceptor activity on R5 HIV-1 isolate Envs. No effect on sulfate incorporation; when associated with A-8 and A-9.`
`MUTAGEN`	`18 18`		`S->A: Sulfate incorporation greatly reduced; when associated with F-21. Moderate reduction in sulfate incorporation; when associated with F-7 and F-12. No sulfate incorporation and binding PDF1alpha greatly reduced; when associated with F-7; F-12; and F-21.`
`MUTAGEN`	`21 21`		`Y->F: Sulfate incorporation greatly reduced; when associated with F-7 and F-12. Sulfate incorporation greatly reduced; when associated with A-18. No sulfate incorporation and binding PDF1alpha greatly reduced; when associated with F-7; F-12 and A-18.`
`MUTAGEN`	`176 176`		`N->A: Enhanced coreceptor activity on R5 HIV-1 isolate Envs; when associated with A-11.`

Sequence information

Length: 352 AA [This is the length of the unprocessed precursor]

Molecular weight: 39746 Da [This is the MW of the unprocessed precursor]

CRC64: 8C8476A186786B83 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MEGISIYTSD NYTEEMGSGD YDSMKEPCFR EENANFNKIF LPTIYSIIFL TGIVGNGLVI 

        70         80         90        100        110        120 
LVMGYQKKLR SMTDKYRLHL SVADLLFVIT LPFWAVDAVA NWYFGNFLCK AVHVIYTVNL 

       130        140        150        160        170        180 
YSSVLILAFI SLDRYLAIVH ATNSQRPRKL LAEKVVYVGV WIPALLLTIP DFIFANVSEA 

       190        200        210        220        230        240 
DDRYICDRFY PNDLWVVVFQ FQHIMVGLIL PGIVILSCYC IIISKLSHSK GHQKRKALKT 

       250        260        270        280        290        300 
TVILILAFFA CWLPYYIGIS IDSFILLEII KQGCEFENTV HKWISITEAL AFFHCCLNPI 

       310        320        330        340        350 
LYAFLGAKFK TSAQHALTSV SRGSSLKILS KGKRGGHSSV STESESSSFH SS

P61073 in FASTA format

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	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools