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UniProtKB/Swiss-Prot entry P09917


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name LOX5_HUMAN
Primary accession number P09917
Secondary accession number Q5JQ14
Integrated into Swiss-Prot on July 1, 1989
Sequence was last modified on January 23, 2007 (Sequence version 2)
Annotations were last modified on    September 2, 2008 (Entry version 101)
Name and origin of the protein
Protein name Arachidonate 5-lipoxygenase
Synonyms 5-lipoxygenase
5-LO
EC 1.13.11.34
Gene name
Name: ALOX5
Synonyms: LOG5
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], AND PARTIAL PROTEIN SEQUENCE.
PubMed=3422434 [NCBI, ExPASy, EBI, Israel, Japan]
Dixon R.A.F., Jones R.E., Diehl R.E., Bennett C.D., Kargman S., Rouzer C.A.;
"Cloning of the cDNA for human 5-lipoxygenase.";
Proc. Natl. Acad. Sci. U.S.A. 85:416-420(1988).
[2]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=2829172 [NCBI, ExPASy, EBI, Israel, Japan]
Matsumoto T., Funk C.D., Raadmark O., Hoeoeg J.-O., Joernvall H., Samuelsson B.;
"Molecular cloning and amino acid sequence of human 5-lipoxygenase.";
Proc. Natl. Acad. Sci. U.S.A. 85:26-30(1988).
[3]
ERRATUM.
Matsumoto T., Funk C.D., Raadmark O., Hoeoeg J.-O., Joernvall H., Samuelsson B.;
Proc. Natl. Acad. Sci. U.S.A. 85:3406-3406(1988).
[4]
NUCLEOTIDE SEQUENCE, AND PARTIAL PROTEIN SEQUENCE.
PubMed=2526519 [NCBI, ExPASy, EBI, Israel, Japan]
Matsumoto T., Funk C.D., Raadmark O., Hoeoeg J.-O., Joernvall H., Samuelsson B.;
"Molecular cloning and amino acid sequence of human 5-lipoxygenase.";
Adv. Prostaglandin Thromboxane Leukotriene Res. 19:466-469(1989).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
DOI=10.1038/nature02462; PubMed=15164054 [NCBI, ExPASy, EBI, Israel, Japan]
Deloukas P., Earthrowl M.E., Grafham D.V., Rubenfield M., French L., Steward C.A., Sims S.K., Jones M.C., Searle S., Scott C., Howe K., Hunt S.E., Andrews T.D., Gilbert J.G.R., Swarbreck D., Ashurst J.L., Taylor A., Battles J., Bird C.P., Ainscough R., Almeida J.P., Ashwell R.I.S., Ambrose K.D., Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Bates K., Beasley H., Bray-Allen S., Brown A.J., Brown J.Y., Burford D.C., Burrill W., Burton J., Cahill P., Camire D., Carter N.P., Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S., Corby N., Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L., Frankish A., Frankland J.A., Garner P., Garnett J., Gribble S., Griffiths C., Grocock R., Gustafson E., Hammond S., Harley J.L., Hart E., Heath P.D., Ho T.P., Hopkins B., Horne J., Howden P.J., Huckle E., Hynds C., Johnson C., Johnson D., Kana A., Kay M., Kimberley A.M., Kershaw J.K., Kokkinaki M., Laird G.K., Lawlor S., Lee H.M., Leongamornlert D.A., Laird G., Lloyd C., Lloyd D.M., Loveland J., Lovell J., McLaren S., McLay K.E., McMurray A., Mashreghi-Mohammadi M., Matthews L., Milne S., Nickerson T., Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V., Peck A.I., Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A., Ross M.T., Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M., Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W., Tracey A., Tromans A., Tsolas J., Wall M., Walsh J., Wang H., Weinstock K., West A.P., Willey D.L., Whitehead S.L., Wilming L., Wray P.W., Young L., Chen Y., Lovering R.C., Moschonas N.K., Siebert R., Fechtel K., Bentley D., Durbin R.M., Hubbard T., Doucette-Stamm L., Beck S., Smith D.R., Rogers J.;
"The DNA sequence and comparative analysis of human chromosome 10.";
Nature 429:375-381(2004).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Brain;
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).
[7]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-50.
PubMed=2565035 [NCBI, ExPASy, EBI, Israel, Japan]
Funk C.D., Hoshiko S., Matsumoto T., Raadmark O., Samuelsson B.;
"Characterization of the human 5-lipoxygenase gene.";
Proc. Natl. Acad. Sci. U.S.A. 86:2587-2591(1989).
[8]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-11.
PubMed=2251250 [NCBI, ExPASy, EBI, Israel, Japan]
Hoshiko S., Raadmark O., Samuelsson B.;
"Characterization of the human 5-lipoxygenase gene promoter.";
Proc. Natl. Acad. Sci. U.S.A. 87:9073-9077(1990).
[9]
SUBCELLULAR LOCATION.
PubMed=3118366 [NCBI, ExPASy, EBI, Israel, Japan]
Rouzer C.A., Samuelsson B.;
"Reversible, calcium-dependent membrane association of human leukocyte 5-lipoxygenase.";
Proc. Natl. Acad. Sci. U.S.A. 84:7393-7397(1987).
[10]
MUTAGENESIS OF SOME HISTIDINE RESIDUES.
PubMed=1939225 [NCBI, ExPASy, EBI, Israel, Japan]
Nguyen T., Falgueyret J.-P., Abramowitz M., Riendeau D.;
"Evaluation of the role of conserved His and Met residues among lipoxygenases by site-directed mutagenesis of recombinant human 5-lipoxygenase.";
J. Biol. Chem. 266:22057-22062(1991).
[11]
MUTAGENESIS OF SOME RESIDUES.
DOI=10.1016/0006-291X(92)91901-2; PubMed=1540191 [NCBI, ExPASy, EBI, Israel, Japan]
Ishii S., Noguchi M., Miyano M., Matsumoto T., Noma M.;
"Mutagenesis studies on the amino acid residues involved in the iron-binding and the activity of human 5-lipoxygenase.";
Biochem. Biophys. Res. Commun. 182:1482-1490(1992).
[12]
PHOSPHORYLATION AT SER-272.
DOI=10.1074/jbc.M111945200; PubMed=11844797 [NCBI, ExPASy, EBI, Israel, Japan]
Werz O., Szellas D., Steinhilber D., Radmark O.;
"Arachidonic acid promotes phosphorylation of 5-lipoxygenase at Ser-271 by MAPK-activated protein kinase 2 (MK2).";
J. Biol. Chem. 277:14793-14800(2002).
[13]
PHOSPHORYLATION AT SER-524, AND MUTAGENESIS OF SER-524.
DOI=10.1074/jbc.M312568200; PubMed=15280375 [NCBI, ExPASy, EBI, Israel, Japan]
Luo M., Jones S.M., Phare S.M., Coffey M.J., Peters-Golden M., Brock T.G.;
"Protein kinase A inhibits leukotriene synthesis by phosphorylation of 5-lipoxygenase on serine 523.";
J. Biol. Chem. 279:41512-41520(2004).
[14]
VARIANT LYS-254.
DOI=10.1093/carcin/bgh260; PubMed=15308583 [NCBI, ExPASy, EBI, Israel, Japan]
Goodman J.E., Bowman E.D., Chanock S.J., Alberg A.J., Harris C.C.;
"Arachidonate lipoxygenase (ALOX) and cyclooxygenase (COX) polymorphisms and colon cancer risk.";
Carcinogenesis 25:2467-2472(2004).
Comments
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
J03600; AAA36183.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
J03571; AAA65450.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
J04520; AAA59522.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AL731567; CAI41243.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC130332; AAI30333.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC132677; AAI32678.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
M38191; AAA63212.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR A28117; DAHUAL.
RefSeq NP_000689.1; -.
UniGene Hs.89499
3D structure databases
PDB
2ABV; Model; -; A=2-674.[ExPASy / RCSB / EBI]
PDBsum 2ABV; -.
ModBase P09917.
Protein-protein interaction databases
IntAct P09917; -.
PTM databases
PhosphoSite P09917; -.
Organism-specific databases
H-InvDB HIX0035390; -.
HGNC HGNC:435; ALOX5.
GenAtlas ALOX5.
HPA CAB005066; -.
MIM 152390; gene. [NCBI / EBI]
PharmGKB PA46; -.
GeneCards P09917.
Gene expression databases
CleanEx HS_ALOX5; -.
GermOnline ENSG00000012779; Homo sapiens.
Ontologies
GO
GO:0004051; Molecular function: arachidonate 5-lipoxygenase activity (traceable author statement from ProtInc).
GO:0005515; Molecular function: protein binding (inferred from physical interaction from UniProtKB).
GO:0006691; Biological process: leukotriene metabolic process (traceable author statement from ProtInc).
QuickGo view.
Family and domain databases
InterPro IPR000907; LipOase.
IPR013819; LipOase_C.
IPR001024; LipOase_LH2.
IPR001885; LipOase_mml.
Graphical view of domain structure.
Gene3D G3DSA:2.60.60.20; Lipase_LipOase; 1.
PANTHER PTHR11771; LipOase; 1.
Pfam PF00305; Lipoxygenase; 1.
PF01477; PLAT; 1.
Pfam graphical view of domain structure.
PRINTS PR00087; LIPOXYGENASE.
PR00467; MAMLPOXGNASE.
SMART SM00308; LH2; 1.
SMART graphical view of domain structure.
PROSITE PS00711; LIPOXYGENASE_1; 1.
PS00081; LIPOXYGENASE_2; 1.
PS51393; LIPOXYGENASE_3; 1.
PS50095; PLAT; 1.
PROSITE graphical view of domain structure (profiles).
BLOCKS P09917.
Genome annotation databases
Ensembl ENSG00000012779; Homo sapiens. [Contig view]
GeneID 240; -.
KEGG hsa:240; -.
NMPDR fig|9606.3.peg.3842; -.
Phylogenomic databases
HOGENOM P09917; -.
HOVERGEN P09917; -.
Other
DrugBank DB00711; Diethylcarbamazine.
DB00741; Hydrocortisone.
DB01097; Leflunomide.
DB00179; Masoprocol.
DB00939; Meclofenamic acid.
DB01017; Minocycline.
DB00471; Montelukast.
DB01103; Quinacrine.
DB00163; Vitamin E.
DB00744; Zileuton.
SOURCE ALOX5; Homo sapiens.
ProtoNet P09917.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
3D-structure; Calcium; Cytoplasm; Dioxygenase; Direct protein sequencing; Iron; Leukotriene biosynthesis; Membrane; Metal-binding; Oxidoreductase; Phosphoprotein; Polymorphism.
Features
SEVIEWER logo Feature table viewer FT aligner logo Feature aligner
KeyFrom   To Length Description FTId
INIT_MET   1     1        Removed. 
CHAIN   2   674  673     Arachidonate 5-lipoxygenase. PRO_0000220693
DOMAIN   2   118  117     PLAT. 
DOMAIN   119   674  556     Lipoxygenase. 
METAL   17    17        Calcium 1; via carbonyl oxygen; structural (By similarity). 
METAL   18    18        Calcium 2; via carbonyl oxygen; structural (By similarity). 
METAL   19    19        Calcium 2; structural (By similarity). 
METAL   44    44        Calcium 2; structural (By similarity). 
METAL   45    45        Calcium 2; via carbonyl oxygen; structural (By similarity). 
METAL   47    47        Calcium 2; structural (By similarity). 
METAL   79    79        Calcium 1; via carbonyl oxygen; structural (By similarity). 
METAL   80    80        Calcium 1; via carbonyl oxygen; structural (By similarity). 
METAL   368   368        Iron; catalytic (By similarity). 
METAL   373   373        Iron; catalytic (By similarity). 
METAL   551   551        Iron; catalytic (By similarity). 
METAL   555   555        Iron; catalytic (By similarity). 
METAL   674   674        Iron; via carboxylate; catalytic (By similarity). 
MOD_RES   272   272        Phosphoserine; by MAPKAPK2. 
MOD_RES   524   524        Phosphoserine; by PKA. 
VARIANT   254   254  1     E -> K. VAR_028018 
MUTAGEN   359   359        D->N: No loss of activity. 
MUTAGEN   363   363        H->S,N: Still some substantial activity. 
MUTAGEN   368   368        H->S,N,A: No activity. 
MUTAGEN   373   373        H->S,N: No activity. 
MUTAGEN   377   377        E->Q: No activity. 
MUTAGEN   391   391        H->A: No activity. 
MUTAGEN   391   391        H->S,N: Still some substantial activity. 
MUTAGEN   400   400        H->A: No activity. 
MUTAGEN   400   400        H->S,N: Still some substantial activity. 
MUTAGEN   433   433        H->N,A: Almost no loss of activity. 
MUTAGEN   524   524        S->A: Prevents phosphorylation by PKA. 
MUTAGEN   551   551        H->N,A: No activity. 
Sequence information
Length: 674 AA [This is the length of the unprocessed precursor] Molecular weight: 77983 Da [This is the MW of the unprocessed precursor] CRC64: 36F38C0A9E86BB21 [This is a checksum on the sequence]
        10         20         30         40         50         60 
MPSYTVTVAT GSQWFAGTDD YIYLSLVGSA GCSEKHLLDK PFYNDFERGA VDSYDVTVDE 

        70         80         90        100        110        120 
ELGEIQLVRI EKRKYWLNDD WYLKYITLKT PHGDYIEFPC YRWITGDVEV VLRDGRAKLA 

       130        140        150        160        170        180 
RDDQIHILKQ HRRKELETRQ KQYRWMEWNP GFPLSIDAKC HKDLPRDIQF DSEKGVDFVL 

       190        200        210        220        230        240 
NYSKAMENLF INRFMHMFQS SWNDFADFEK IFVKISNTIS ERVMNHWQED LMFGYQFLNG 

       250        260        270        280        290        300 
CNPVLIRRCT ELPEKLPVTT EMVECSLERQ LSLEQEVQQG NIFIVDFELL DGIDANKTDP 

       310        320        330        340        350        360 
CTLQFLAAPI CLLYKNLANK IVPIAIQLNQ IPGDENPIFL PSDAKYDWLL AKIWVRSSDF 

       370        380        390        400        410        420 
HVHQTITHLL RTHLVSEVFG IAMYRQLPAV HPIFKLLVAH VRFTIAINTK AREQLICECG 

       430        440        450        460        470        480 
LFDKANATGG GGHVQMVQRA MKDLTYASLC FPEAIKARGM ESKEDIPYYF YRDDGLLVWE 

       490        500        510        520        530        540 
AIRTFTAEVV DIYYEGDQVV EEDPELQDFV NDVYVYGMRG RKSSGFPKSV KSREQLSEYL 

       550        560        570        580        590        600 
TVVIFTASAQ HAAVNFGQYD WCSWIPNAPP TMRAPPPTAK GVVTIEQIVD TLPDRGRSCW 

       610        620        630        640        650        660 
HLGAVWALSQ FQENELFLGM YPEEHFIEKP VKEAMARFRK NLEAIVSVIA ERNKKKQLPY 

       670 
YYLSPDRIPN SVAI 

P09917 in FASTA format

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