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UniProtKB/Swiss-Prot entry P12530


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

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Entry information
Entry name LOX15_RABIT
Primary accession number P12530
Secondary accession numbers None
Integrated into Swiss-Prot on October 1, 1989
Sequence was last modified on January 23, 2007 (Sequence version 3)
Annotations were last modified on    July 22, 2008 (Entry version 82)
Name and origin of the protein
Protein name Arachidonate 15-lipoxygenase
Synonyms EC 1.13.11.33
Omega-6 lipoxygenase
Erythroid cell-specific 15-lipoxygenase
15-LOX
Gene name
Name: ALOX15
From
Oryctolagus cuniculus (Rabbit) [TaxID: 9986] 
Taxonomy Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Glires; Lagomorpha; Leporidae; Oryctolagus.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
DOI=10.1016/0378-1119(89)90526-X; PubMed=2612916 [NCBI, ExPASy, EBI, Israel, Japan]
O'Prey J., Chester J., Thiele B.J., Janetzki S., Prehn S., Fleming J., Harrison P.R.;
"The promoter structure and complete sequence of the gene encoding the rabbit erythroid cell-specific 15-lipoxygenase.";
Gene 84:493-499(1989).
[2]
NUCLEOTIDE SEQUENCE [MRNA], AND PROTEIN SEQUENCE OF 2-31.
DOI=10.1016/0378-1119(89)90103-0; PubMed=2777088 [NCBI, ExPASy, EBI, Israel, Japan]
Fleming J., Thiele B.J., Chester J., O'Prey J., Janetzki S., Aitken A., Anton I.A., Rapoport S.M., Harrison P.R.;
"The complete sequence of the rabbit erythroid cell-specific 15-lipoxygenase mRNA: comparison of the predicted amino acid sequence of the erythrocyte lipoxygenase with other lipoxygenases.";
Gene 79:181-188(1989).
[3]
NUCLEOTIDE SEQUENCE [MRNA] OF 1-31.
DOI=10.1016/0378-1119(87)90182-X; PubMed=3123326 [NCBI, ExPASy, EBI, Israel, Japan]
Thiele B.J., Fleming J., Kasturi K., O'Prey J., Black E., Chester J., Rapoport S.M., Harrison P.R.;
"Cloning of a rabbit erythroid-cell-specific lipoxygenase mRNA.";
Gene 57:111-119(1987).
[4]
NUCLEOTIDE SEQUENCE, AND GENE STRUCTURE.
PubMed=2386503 [NCBI, ExPASy, EBI, Israel, Japan]
Thiele B.J., Fleming J., Chester J., O'Prey J., Prehn S., Janetzki S., Rapoport S.M., Harrison P.R.;
"Structure of the mRNA and of the gene coding for the rabbit erythroid 15-lipoxygenase.";
Biomed. Biochim. Acta 49:S17-S24(1990).
[5]
X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) IN COMPLEX WITH IRON AND SUBSTRATE ANALOG.
DOI=10.1038/nsb1297-1003; PubMed=9406550 [NCBI, ExPASy, EBI, Israel, Japan]
Gillmor S.A., Villasenor A., Fletterick R., Sigal E., Browner M.F.;
"The structure of mammalian 15-lipoxygenase reveals similarity to the lipases and the determinants of substrate specificity.";
Nat. Struct. Biol. 4:1003-1009(1997).
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
M33291; AAA75014.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
M27214; AAB86978.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
M22617; AAA31385.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR JQ0018; JQ0018.
RefSeq NP_001075751.1; -.
UniGene Ocu.2185
3D structure databases
PDB
1LOX; X-ray; 2.40 A; A=1-663.[ExPASy / RCSB / EBI]
2P0M; X-ray; 2.40 A; A/B=2-663.[ExPASy / RCSB / EBI]
Detailed list of linked structures.
PDBsum 1LOX; -.
2P0M; -.
ModBase P12530.
Ontologies
GO
GO:0050473; Molecular function: arachidonate 15-lipoxygenase activity (inferred from electronic annotation from EC).
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 P12530.
Genome annotation databases
GeneID 100009114; -.
Phylogenomic databases
HOVERGEN P12530; -.
Other
ProtoNet P12530.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
3D-structure; Cytoplasm; Dioxygenase; Direct protein sequencing; 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 15-lipoxygenase. PRO_0000220699
DOMAIN   2   115  114     PLAT. 
METAL   361   361        Iron (catalytic). 
METAL   366   366        Iron (catalytic). 
METAL   541   541        Iron (catalytic). 
METAL   545   545        Iron (catalytic). 
METAL   663   663        Iron (via carboxylate) (catalytic). 
CONFLICT   190   190        N -> D (in Ref. 2; AAB86978). 
CONFLICT   194   194        I -> V (in Ref. 2; AAB86978). 
STRAND   3    10  8      
STRAND   12    15  4      
STRAND   19    30  12      
STRAND   32    39  8      
STRAND   46    52  7      
STRAND   59    68  10      
STRAND   70    72  3      
STRAND   76    89  14      
STRAND   93   101  9      
STRAND   103   105  3      
STRAND   107   110  4      
HELIX   126   139  14      
STRAND   152   154  3      
HELIX   158   160  3      
HELIX   163   165  3      
HELIX   169   191  23      
HELIX   192   195  4      
HELIX   201   203  3      
HELIX   204   207  4      
HELIX   214   221  8      
STRAND   222   224  3      
HELIX   226   235  10      
HELIX   260   271  12      
STRAND   274   278  5      
HELIX   280   282  3      
STRAND   301   307  7      
TURN   308   310  3      
STRAND   311   318  8      
HELIX   338   358  21      
HELIX   359   365  7      
HELIX   366   379  14      
HELIX   385   390  6      
HELIX   391   394  4      
HELIX   397   404  8      
TURN   405   408  4      
HELIX   414   418  5      
TURN   422   424  3      
HELIX   425   431  7      
HELIX   432   434  3      
HELIX   439   442  4      
HELIX   444   451  8      
HELIX   460   483  24      
HELIX   487   491  5      
HELIX   494   504  11      
TURN   505   509  5      
TURN   511   515  5      
HELIX   523   536  14      
HELIX   539   545  7      
HELIX   548   551  4      
STRAND   552   554  3      
HELIX   555   557  3      
STRAND   568   570  3      
HELIX   574   580  7      
HELIX   584   597  14      
HELIX   618   644  27      
TURN   654   656  3      
STRAND   657   660  4      
Sequence information
Length: 663 AA [This is the length of the unprocessed precursor] Molecular weight: 75310 Da [This is the MW of the unprocessed precursor] CRC64: C3391E1E6E7930BF [This is a checksum on the sequence]
        10         20         30         40         50         60 
MGVYRVCVST GASIYAGSKN KVELWLVGQH GEVELGSCLR PTRNKEEEFK VNVSKYLGSL 

        70         80         90        100        110        120 
LFVRLRKKHF LKEDAWFCNW ISVQALGAAE DKYWFPCYRW VVGDGVQSLP VGTGCTTVGD 

       130        140        150        160        170        180 
PQGLFQKHRE QELEERRKLY QWGSWKEGLI LNVAGSKLTD LPVDERFLED KKIDFEASLA 

       190        200        210        220        230        240 
WGLAELALKN SLNILAPWKT LDDFNRIFWC GRSKLARRVR DSWQEDSLFG YQFLNGANPM 

       250        260        270        280        290        300 
LLRRSVQLPA RLVFPPGMEE LQAQLEKELK AGTLFEADFA LLDNIKANVI LYCQQYLAAP 

       310        320        330        340        350        360 
LVMLKLQPDG KLMPMVIQLH LPKIGSSPPP LFLPTDPPMV WLLAKCWVRS SDFQVHELNS 

       370        380        390        400        410        420 
HLLRGHLMAE VFTVATMRCL PSIHPVFKLI VPHLRYTLEI NVRARNGLVS DFGIFDQIMS 

       430        440        450        460        470        480 
TGGGGHVQLL QQAGAFLTYR SFCPPDDLAD RGLLGVESSF YAQDALRLWE IISRYVQGIM 

       490        500        510        520        530        540 
GLYYKTDEAV RDDLELQSWC REITEIGLQG AQKQGFPTSL QSVAQACHFV TMCIFTCTGQ 

       550        560        570        580        590        600 
HSSIHLGQLD WFTWVPNAPC TMRLPPPTTK DATLETVMAT LPNLHQSSLQ MSIVWQLGRD 

       610        620        630        640        650        660 
QPIMVPLGQH QEEYFSGPEP RAVLEKFREE LAIMDKEIEV RNEKLDIPYE YLRPSIVENS 


VAI 

P12530 in FASTA format

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