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UniProtKB/Swiss-Prot entry Q02759

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

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Entry information
Entry name LX12L_RAT
Primary accession number Q02759
Secondary accession numbers None
Integrated into Swiss-Prot on July 1, 1993
Sequence was last modified on January 23, 2007 (Sequence version 2)
Annotations were last modified on    July 22, 2008 (Entry version 73)
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: Alox12, Alox15
From
Rattus norvegicus (Rat) [TaxID: 10116] 
Taxonomy Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; Muroidea; Muridae; Murinae; Rattus.
Protein existence 2: Evidence at transcript level;
References
[1]
 NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND TISSUE SPECIFICITY.
STRAIN=Sprague-Dawley;
TISSUE=Brain;
PubMed=8444196 [NCBI, ExPASy, EBI, Israel, Japan]
Watanabe T., Medina J.F., Haeggstroem J.Z., Raadmark O.P., Samuelsson B.;
"Molecular cloning of a 12-lipoxygenase cDNA from rat brain.";
Eur. J. Biochem. 212:605-612(1993).
[2]
 NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND SUBCELLULAR LOCATION.
TISSUE=Pineal gland;
DOI=10.1016/0005-2760(94)90272-0; PubMed=8117750 [NCBI, ExPASy, EBI, Israel, Japan]
Hada T., Hagiya H., Suzuki H., Arakawa T., Nakamura M., Matsuda S., Yoshimoto T., Yamamoto S., Azekawa T., Morita Y., Ishimura K., Kim H.Y.;
"Arachidonate 12-lipoxygenase of rat pineal glands: catalytic properties and primary structure deduced from its cDNA.";
Biochim. Biophys. Acta 1211:221-228(1994).
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
L06040; AAA41532.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
S69383; AAB30132.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR I52462; I52462.
S30051; S30051.
RefSeq NP_112272.2; -.
UniGene Rn.11318
3D structure databases
HSSP P12530; 1LOX. [HSSP ENTRY / PDB]
SMR Q02759; 2-663.
ModBase Q02759.
Organism-specific databases
RGD 70493; Alox15.
Gene expression databases
ArrayExpress Q02759; -.
GermOnline ENSRNOG00000019183; Rattus norvegicus.
Ontologies
GO
GO:0005829; Cellular component: cytosol (inferred from direct assay from UniProtKB).
GO:0042383; Cellular component: sarcolemma (inferred from sequence or structural similarity from UniProtKB).
GO:0047977; Molecular function: hepoxilin-epoxide hydrolase activity (inferred from direct assay from UniProtKB).
GO:0019870; Molecular function: potassium channel inhibitor activity (traceable author statement from UniProtKB).
GO:0006916; Biological process: anti-apoptosis (inferred from sequence or structural similarity from UniProtKB).
GO:0019369; Biological process: arachidonic acid metabolic process (non-traceable author statement from UniProtKB).
GO:0019395; Biological process: fatty acid oxidation (inferred from sequence or structural similarity from UniProtKB).
GO:0046456; Biological process: icosanoid biosynthetic process (non-traceable author statement from UniProtKB).
GO:0045794; Biological process: negative regulation of cell volume (traceable author statement from UniProtKB).
GO:0030307; Biological process: positive regulation of cell growth (inferred from sequence or structural similarity from UniProtKB).
GO:0008284; Biological process: positive regulation of cell proliferation (inferred from sequence or structural similarity from UniProtKB).
GO:0042391; Biological process: regulation of membrane potential (traceable author statement from UniProtKB).
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.
PS50095; PLAT; 1.
PROSITE graphical view of domain structure (profiles).
BLOCKS Q02759.
Genome annotation databases
Ensembl ENSRNOG00000019183; Rattus norvegicus. [Contig view]
GeneID 81639; -.
KEGG rno:81639; -.
Phylogenomic databases
HOVERGEN Q02759; -.
Other
ProtoNet Q02759.
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. 
CHAIN   2   663  662     Arachidonate 12-lipoxygenase, leukocyte-type. PRO_0000220687
DOMAIN   2   115  114     PLAT. 
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   55    55        E -> G (in Ref. 2; AAB30132). 
CONFLICT   371   371        L -> V (in Ref. 2; AAB30132). 
Sequence information
Length: 663 AA [This is the length of the unprocessed precursor] Molecular weight: 75392 Da [This is the MW of the unprocessed precursor] CRC64: 91D8FB4547A3948D [This is a checksum on the sequence] 
        10         20         30         40         50         60 
MGVYRIRVST GDSKYAGSNN EVYLWLVGQH GEASLGKLLR PCRDSEAEFK VDVSEYLGPL 

        70         80         90        100        110        120 
LFVRVQKWHY LTDDAWFCNW ISVKGPGDQG SEYMFPCYRW VQGRSILSLP EGTGCTVVED 

       130        140        150        160        170        180 
SQGLFRKHRE EELEERRSLY RWGNWKDGSI LNVAAASISD LPVDQRFRED KRIEFEASQV 

       190        200        210        220        230        240 
IGVMDTVVNF PINTVTCWKS LDDFNCVFKS GHTKMAERVR NSWKEDAFFG YQFLNGANPM 

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

       310        320        330        340        350        360 
LVMLKLMPDG QLLPIAIQLE LPKTGSTPPP IFTPSDPPMD WLLAKCWVRS SDLQLHELQA 

       370        380        390        400        410        420 
HLLRGHLMAE LFAVATMRCL PSVHPVFKLL VPHLLYTMEI NVRARSDLIS ERGFFDKAMS 

       430        440        450        460        470        480 
TGGGGHLDLL KQAGAFLTYC SLCPPDDLAE RGLLDIETCF YAKDALRLWQ IMNRYVVGMF 

       490        500        510        520        530        540 
NLHYKTDKAV QDDYELQSWC REITDIGLQG AQDRGFPTSL QSRAQACYFI TMCIFTCTAQ 

       550        560        570        580        590        600 
HSSVHLGQLD WFYWVPNAPC TMRLPPPTTK EATMEKLMAT LPNPNQSTLQ INVVWLLGRR 

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


VAI
Q02759 in FASTA format

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