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P39654 (LX12L_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 3, 2013. Version 115. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Arachidonate 12-lipoxygenase, leukocyte-type
Short name=12-LOX
EC=1.13.11.31
Gene names
Name:Alox12l
Synonyms:Alox15
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length663 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Oxygenase and 14,15-leukotriene A4 synthase activity. Converts arachidonic acid to 12-hydroperoxyeicosatetraenoic acid (12-HPETE) and 15-hydroperoxyeicosatetraenoic acid (15-HPETE) in a 3:1 ratio. Also converts linoleic acid to 13-hydroperoxyoctadecadienoic acid.

Catalytic activity

Arachidonate + O2 = (5Z,8Z,10E,14Z)-(12S)-12-hydroperoxyicosa-5,8,10,14-tetraenoate.

Cofactor

Binds 1 iron ion per subunit.

Pathway

Lipid metabolism; leukotriene D4 biosynthesis.

Subcellular location

Cytoplasm.

Tissue specificity

Found in pituitary and pineal glands as well as leukocytes, kidney, aorta and small intestine.

Sequence similarities

Belongs to the lipoxygenase family.

Contains 1 lipoxygenase domain.

Contains 1 PLAT domain.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed By similarity
Chain2 – 663662Arachidonate 12-lipoxygenase, leukocyte-type
PRO_0000220686

Regions

Domain2 – 115114PLAT
Domain116 – 663548Lipoxygenase

Sites

Metal binding3611Iron; catalytic By similarity
Metal binding3661Iron; catalytic By similarity
Metal binding5411Iron; catalytic By similarity
Metal binding6631Iron; via carboxylate; catalytic By similarity

Experimental info

Sequence conflict371K → N in AAA64930. Ref.2
Sequence conflict1191E → Q in AAA64930. Ref.2
Sequence conflict3971T → N in AAA64930. Ref.2
Sequence conflict5681K → T in CAJ18471. Ref.4
Sequence conflict5681K → T in AAH56625. Ref.6
Sequence conflict5681K → T in AAH81546. Ref.6

Sequences

Sequence LengthMass (Da)Tools
P39654 [UniParc].

Last modified September 11, 2007. Version 4.
Checksum: 0D5412B4502B5799

FASTA66375,445
        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

« Hide

References

« Hide 'large scale' references
[1]"cDNA cloning, expression, mutagenesis of C-terminal isoleucine, genomic structure, and chromosomal localizations of murine 12-lipoxygenases."
Chen X.-S., Kurre U., Jenkins N.A., Copeland N.G., Funk C.D.
J. Biol. Chem. 269:13979-13987(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], CHARACTERIZATION.
Strain: C57BL/6 and ICR.
Tissue: Spleen.
[2]"Cloning and characterization of a murine macrophage lipoxygenase."
Freire-Moar J., Alavi-Nassab A., Ng M., Mulkins M., Sigal E.
Biochim. Biophys. Acta 1254:112-116(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Macrophage.
[3]"The transcriptional landscape of the mammalian genome."
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. expand/collapse author list , 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.
Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: C57BL/6J.
Tissue: Lung.
[4]"Cloning of mouse full open reading frames in Gateway(R) system entry vector (pDONR201)."
Ebert L., Muenstermann E., Schatten R., Henze S., Bohn E., Mollenhauer J., Wiemann S., Schick M., Korn B.
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[5]"Lineage-specific biology revealed by a finished genome assembly of the mouse."
Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S. expand/collapse author list , Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K., Eichler E.E., Ponting C.P.
PLoS Biol. 7:E1000112-E1000112(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: C57BL/6J.
[6]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: FVB/N and FVB/N-3.
Tissue: Mammary tumor.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		U04331 mRNA. Translation: AAA20658.1.
L34570 mRNA. Translation: AAA64930.1.
AK142371 mRNA. Translation: BAE25045.1.
CT010263 mRNA. Translation: CAJ18471.1.
AL596096 Genomic DNA. Translation: CAI51979.1.
BC056625 mRNA. Translation: AAH56625.1.
BC081546 mRNA. Translation: AAH81546.1.
IPIIPI00553304.
PIRB54075.
RefSeqNP_033790.3. NM_009660.3.
UniGeneMm.4584.

3D structure databases

ProteinModelPortalP39654.
SMRP39654. Positions 2-663.
ModBaseSearch...

Protein-protein interaction databases

STRING10090.ENSMUSP00000019068.

PTM databases

PhosphoSiteP39654.

Proteomic databases

PaxDbP39654.
PRIDEP39654.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000019068; ENSMUSP00000019068; ENSMUSG00000018924.
GeneID11687.
KEGGmmu:11687.

Organism-specific databases

CTD246.
MGIMGI:87997. Alox15.

Phylogenomic databases

eggNOGNOG133298.
GeneTreeENSGT00550000074415.
HOGENOMHOG000234358.
HOVERGENHBG005150.
InParanoidP39654.
KOK00460.
OMAVGQHEEE.
OrthoDBEOG4W0XCM.

Enzyme and pathway databases

UniPathwayUPA00880.

Gene expression databases

ArrayExpressP39654.
BgeeP39654.
CleanExMM_ALOX15.
GenevestigatorP39654.
GermOnlineENSMUSG00000018924. Mus musculus.

Family and domain databases

Gene3D2.60.60.20. 1 hit.
InterProIPR008976. Lipase_LipOase.
IPR000907. LipOase.
IPR013819. LipOase_C.
IPR020834. LipOase_CS.
IPR020833. LipOase_Fe_BS.
IPR001024. LipOase_LH2.
IPR001885. LipOase_mml.
[Graphical view]
PANTHERPTHR11771. PTHR11771. 1 hit.
PfamPF00305. Lipoxygenase. 1 hit.
PF01477. PLAT. 1 hit.
[Graphical view]
PRINTSPR00087. LIPOXYGENASE.
PR00467. MAMLPOXGNASE.
SMARTSM00308. LH2. 1 hit.
[Graphical view]
SUPFAMSSF49723. Lipase_LipOase. 1 hit.
SSF48484. Lipoxygenase. 1 hit.
PROSITEPS00711. LIPOXYGENASE_1. 1 hit.
PS00081. LIPOXYGENASE_2. 1 hit.
PS51393. LIPOXYGENASE_3. 1 hit.
PS50095. PLAT. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

BindingDBP39654.
NextBio279331.
SOURCESearch...

Entry information

Entry nameLX12L_MOUSE
AccessionPrimary (citable) accession number: P39654
Secondary accession number(s): Q4FJY9, Q5F2E3, Q6PHB2
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 1995
Last sequence update: September 11, 2007
Last modified: April 3, 2013
This is version 115 of the entry and version 4 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents