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UniProtKB/Swiss-Prot entry P39654


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

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Entry information
Entry name LX12L_MOUSE
Primary accession number P39654
Secondary accession numbers Q4FJY9 Q5F2E3 Q6PHB2
Integrated into Swiss-Prot on February 1, 1995
Sequence was last modified on September 11, 2007 (Sequence version 4)
Annotations were last modified on    November 25, 2008 (Entry version 78)
Name and origin of the protein
Protein name Arachidonate 12-lipoxygenase, leukocyte-type
Synonyms 12-LOX
EC 1.13.11.31
Gene name
Name: Alox12l
Synonyms: Alox15
From
Mus musculus (Mouse) [TaxID: 10090] 
Taxonomy Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; Muroidea; Muridae; Murinae; Mus.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [MRNA], AND CHARACTERIZATION.
STRAIN=C57BL/6, and ICR;
TISSUE=Spleen;
PubMed=8188678 [NCBI, ExPASy, EBI, Israel, Japan]
Chen X.-S., Kurre U., Jenkins N.A., Copeland N.G., Funk C.D.;
"cDNA cloning, expression, mutagenesis of C-terminal isoleucine, genomic structure, and chromosomal localizations of murine 12-lipoxygenases.";
J. Biol. Chem. 269:13979-13987(1994).
[2]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Macrophage;
DOI=10.1016/0005-2760(94)00199-9; PubMed=7811740 [NCBI, ExPASy, EBI, Israel, Japan]
Freire-Moar J., Alavi-Nassab A., Ng M., Mulkins M., Sigal E.;
"Cloning and characterization of a murine macrophage lipoxygenase.";
Biochim. Biophys. Acta 1254:112-116(1995).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=C57BL/6J;
TISSUE=Lung;
DOI=10.1126/science.1112014; PubMed=16141072 [NCBI, ExPASy, EBI, Israel, Japan]
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J., Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
"The transcriptional landscape of the mammalian genome.";
Science 309:1559-1563(2005).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Ebert L., Muenstermann E., Schatten R., Henze S., Bohn E., Mollenhauer J., Wiemann S., Schick M., Korn B.;
"Cloning of mouse full open reading frames in Gateway(R) system entry vector (pDONR201).";
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=C57BL/6J;
The mouse genome sequencing consortium;
Submitted (FEB-2005) to the EMBL/GenBank/DDBJ databases.
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=FVB/N, and FVB/N-3;
TISSUE=Mammary tumor;
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).
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
U04331; AAA20658.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
L34570; AAA64930.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AK142371; BAE25045.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
CT010263; CAJ18471.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AL596096; CAI51979.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC056625; AAH56625.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC081546; AAH81546.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR B54075; B54075.
RefSeq NP_033790.3; -.
UniGene Mm.4584
3D structure databases
HSSP P12530; 1LOX. [HSSP ENTRY / PDB]
SMR P39654; 2-663.
ModBase P39654.
PTM databases
PhosphoSite P39654; -.
Organism-specific databases
MGI MGI:87997; Alox15.
Gene expression databases
ArrayExpress P39654; -.
CleanEx MM_ALOX15; -.
GermOnline ENSMUSG00000018924; Mus musculus.
Ontologies
GO
GO:0004052; Molecular function: arachidonate 12-lipoxygenase activity (inferred from electronic annotation from EC).
GO:0005506; Molecular function: iron ion binding (inferred from electronic annotation from InterPro).
GO:0016165; Molecular function: lipoxygenase activity (inferred from electronic annotation from InterPro).
GO:0030282; Biological process: bone mineralization (inferred from mutant phenotype from MGI).
GO:0019370; Biological process: leukotriene biosynthetic process (inferred from electronic annotation from UniProtKB-KW).
GO:0055114; Biological process: oxidation reduction (inferred from electronic annotation from UniProtKB-KW).
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).
ProtoNet P39654.
Genome annotation databases
Ensembl ENSMUSG00000018924; Mus musculus. [Contig view]
GeneID 11687; -.
KEGG mmu:11687; -.
Phylogenomic databases
HOGENOM P39654; -.
HOVERGEN P39654; -.
Other
NextBio 279331; -.
SOURCE Alox12l; Mus musculus.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
Cytoplasm; Dioxygenase; Iron; Leukotriene biosynthesis; Metal-binding; Oxidoreductase.
Features
SEVIEWER logo Feature table viewer FT aligner logo Feature aligner
KeyFrom   To Length Description FTId
INIT_MET   1     1        Removed (By similarity). 
CHAIN   2   663  662     Arachidonate 12-lipoxygenase, leukocyte-type. PRO_0000220686
DOMAIN   2   115  114     PLAT. 
DOMAIN   116   663  548     Lipoxygenase. 
METAL   361   361        Iron; catalytic (By similarity). 
METAL   366   366        Iron; catalytic (By similarity). 
METAL   541   541        Iron; catalytic (By similarity). 
METAL   663   663        Iron; via carboxylate; catalytic (By similarity). 
CONFLICT   37    37        K -> N (in Ref. 2; AAA64930). 
CONFLICT   119   119        E -> Q (in Ref. 2; AAA64930). 
CONFLICT   397   397        T -> N (in Ref. 2; AAA64930). 
CONFLICT   568   568        K -> T (in Ref. 4; CAJ18471 and 6; AAH56625/AAH81546). 
Sequence information
Length: 663 AA [This is the length of the unprocessed precursor] Molecular weight: 75445 Da [This is the MW of the unprocessed precursor] CRC64: 0D5412B4502B5799 [This is a checksum on the sequence]
        10         20         30         40         50         60 
MGVYRIRVST GDSVYAGSNN EVYLWLIGQH GEASLGKLFR PCRNSEAEFK VDVSEYLGPL 

        70         80         90        100        110        120 
LFVRVQKWHY LKEDAWFCNW ISVKGPGDQG SEYTFPCYRW VQGTSILNLP EGTGCTVVED 

       130        140        150        160        170        180 
SQGLFRNHRE EELEERRSLY RWGNWKDGTI LNVAATSISD LPVDQRFRED KRLEFEASQV 

       190        200        210        220        230        240 
LGTMDTVINF PKNTVTCWKS LDDFNYVFKS GHTKMAERVR NSWKEDAFFG YQFLNGANPM 

       250        260        270        280        290        300 
VLKRSTCLPA RLVFPPGMEK LQAQLDEELK KGTLFEADFF LLDGIKANVI LCSQQYLAAP 

       310        320        330        340        350        360 
LVMLKLQPDG QLLPIAIQLE LPKTGSTPPP IFTPLDPPMD WLLAKCWVRS SDLQLHELQA 

       370        380        390        400        410        420 
HLLRGHLVAE VFAVATMRCL PSVHPVFKLL VPHLLYTMEI NVRARSDLIS ERGFFDKVMS 

       430        440        450        460        470        480 
TGGGGHLDLL KQAGAFLTYS SLCPPDDLAE RGLLDIDTCF YAKDALQLWQ VMNRYVVGMF 

       490        500        510        520        530        540 
DLYYKTDQAV QDDYELQSWC QEITEIGLQG AQDRGFPTSL QSRAQACHFI TMCIFTCTAQ 

       550        560        570        580        590        600 
HSSIHLGQLD WFYWVPNAPC TMRLPPPKTK DATMEKLMAT LPNPNQSTLQ INVVWLLGRR 

       610        620        630        640        650        660 
QAVMVPLGQH SEEHFPNPEA KAVLKKFREE LAALDKEIEI RNKSLDIPYE YLRPSLVENS 


VAI 

P39654 in FASTA format

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