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Q2KMM4 (LX12B_RAT) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 55. 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·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Arachidonate 12-lipoxygenase, 12R-type

Short name=12R-LOX
Short name=12R-lipoxygenase
EC=1.13.11.-
Alternative name(s):
Epidermis-type lipoxygenase 12
Gene names
Name:Alox12b
OrganismRattus norvegicus (Rat) [Reference proteome]
Taxonomic identifier10116 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus

Protein attributes

Sequence length701 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Non-heme iron-containing dioxygenase that catalyzes the stereo-specific peroxidation of free and esterified polyunsaturated fatty acids generating a spectrum of bioactive lipid mediators. Mainly converts arachidonic acid to (12R)-hydroperoxyeicosatetraenoic acid/(12R)-HPETE and minor stereoisomers. In the skin, acts upstream of ALOXE3 on the lineolate moiety of esterified omega-hydroxyacyl-sphingosine (EOS) ceramides to produce an epoxy-ketone derivative, a crucial step in the conjugation of omega-hydroxyceramide to membrane proteins. Therefore plays a crucial role in the synthesis of corneocytes lipid envelope and the establishment of the skin barrier to water loss. May also play a role in the regulation of the expression of airway mucins. Ref.2

Catalytic activity

Arachidonate + O2 = (5Z,8Z,10E,14Z)-(12R)-12-hydroperoxyicosa-5,8,10,14-tetraenoate. Ref.2

Cofactor

Binds 1 iron ion per subunit By similarity.

Pathway

Lipid metabolism; hydroperoxy eicosatetraenoic acid biosynthesis.

Lipid metabolism; sphingolipid metabolism.

Subcellular location

Cytoplasm By similarity.

Sequence similarities

Belongs to the lipoxygenase family.

Contains 1 lipoxygenase domain.

Contains 1 PLAT domain.

Ontologies

Keywords
   Biological processFatty acid metabolism
Lipid metabolism
   Cellular componentCytoplasm
   LigandIron
Metal-binding
   Molecular functionDioxygenase
Oxidoreductase
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processarachidonic acid metabolic process

Inferred from direct assay Ref.2. Source: UniProtKB

ceramide biosynthetic process

Inferred from sequence or structural similarity. Source: UniProtKB

establishment of skin barrier

Inferred from sequence or structural similarity. Source: UniProtKB

hepoxilin biosynthetic process

Inferred from direct assay Ref.2. Source: UniProtKB

linoleic acid metabolic process

Inferred from sequence or structural similarity. Source: UniProtKB

lipoxygenase pathway

Inferred from sequence or structural similarity. Source: UniProtKB

oxidation-reduction process

Inferred from sequence or structural similarity. Source: UniProtKB

positive regulation of MAPK cascade

Inferred from sequence or structural similarity. Source: UniProtKB

positive regulation of gene expression

Inferred from sequence or structural similarity. Source: UniProtKB

positive regulation of mucus secretion

Inferred from sequence or structural similarity. Source: UniProtKB

protein lipidation

Inferred from sequence or structural similarity. Source: UniProtKB

sphingolipid metabolic process

Inferred from sequence or structural similarity. Source: UniProtKB

   Cellular_componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionarachidonate 12-lipoxygenase activity

Inferred from sequence or structural similarity. Source: UniProtKB

iron ion binding

Inferred from electronic annotation. Source: InterPro

linoleate 9S-lipoxygenase activity

Inferred from sequence or structural similarity. Source: UniProtKB

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 701701Arachidonate 12-lipoxygenase, 12R-type
PRO_0000244486

Regions

Domain2 – 119118PLAT
Domain120 – 701582Lipoxygenase

Sites

Metal binding3981Iron; catalytic By similarity UniProtKB P12530
Metal binding4031Iron; catalytic By similarity UniProtKB P12530
Metal binding5781Iron; catalytic By similarity UniProtKB P12530
Metal binding5821Iron; catalytic By similarity
Metal binding7011Iron; via carboxylate; catalytic By similarity UniProtKB P12530

Experimental info

Sequence conflict2761H → L in AAX85362. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Q2KMM4 [UniParc].

Last modified March 7, 2006. Version 1.
Checksum: 6BE209D98DEB4DB9

FASTA70180,741
        10         20         30         40         50         60 
MATYKVKVAT GTDFFSGTLD SISLTIVGTQ GESHKQRLNH FGRDFATGAV DDYTVQCQQD 

        70         80         90        100        110        120 
LGELIIIRLH KEPHSFLPKD PWYCNYVQIC APNCRVYHFP AYQWMDGYET LSLREATGKT 

       130        140        150        160        170        180 
TADDTLPILL EHRQEEIRAK KDFYHWRVFV PGLPNYVDIP SYHPPPRRCR NPNRPEWNGY 

       190        200        210        220        230        240 
IPGFPILINI KATRFLNLNL RFSFVKTASF FYRLGPMALA FKLRGLVDRK RSWKRLKDIK 

       250        260        270        280        290        300 
NIFPATKTVV SEYVAEHWTE DSFFGYQYLN GINPGHIRRC MQIPDKFPVT DEMVAPFLGE 

       310        320        330        340        350        360 
GTCLQAELEK GNIYLADYRI LDGIPTVELN GQKQHHCAPI CLLHFGPDGN MMPIAIQLSQ 

       370        380        390        400        410        420 
TPGPDCPIFL PNDSEWDWLL AKTWVRYAEF YSHEAVAHLL ESHLIGEAFC LALLRNLPMC 

       430        440        450        460        470        480 
HPLYKLLIPH TRYNVQINSI GRALLLNKGG LSARAMSLGL EGFAQVMVRG LSELTYKSLC 

       490        500        510        520        530        540 
IPNDFVERGV QDLPGYYFRD DSLAVWYAME RYVTEIITYY YPNDAAVEGD PELQCWVQEI 

       550        560        570        580        590        600 
FKECLLERES SGFPTCLRTV PELIEYVTMV MYTCSARHAA VNTGQLEYTS WMPNFPSSMR 

       610        620        630        640        650        660 
NPPMQSKGLT TLQTFMDTLP DVKTTCIVLL VLWTLCREPD DRRPLGHFPD IHFVEEAPRR 

       670        680        690        700 
SMEAFRQNLN QISHNIRQRN KCLNLPYYYL DPVLIENSIS I 

« Hide

References

[1]"Molecular analysis of the sex hormone-binding globulin gene in the rat hypodactylous mutation (Hd)."
Liska F., Goesele C., Kren V., Huebner N., Krenova D.
Folia Biol. (Praha) 50:63-68(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Strain: Brown Norway/Cub, SHR/OlaIpcv and Wistar Hd.
Tissue: Testis.
[2]"Systematic analysis of rat 12/15-lipoxygenase enzymes reveals critical role for spinal eLOX3 hepoxilin synthase activity in inflammatory hyperalgesia."
Gregus A.M., Dumlao D.S., Wei S.C., Norris P.C., Catella L.C., Meyerstein F.G., Buczynski M.W., Steinauer J.J., Fitzsimmons B.L., Yaksh T.L., Dennis E.A.
FASEB J. 27:1939-1949(2013) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, CATALYTIC ACTIVITY.
+Additional computationally mapped references.

Web resources

Protein Spotlight

about water - Issue 153 of September 2013

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AY903231 mRNA. Translation: AAX85361.1.
AY903232 mRNA. Translation: AAX85362.1.
AY903233 mRNA. Translation: AAX85363.1.
RefSeqNP_001034466.1. NM_001039377.1.
UniGeneRn.160588.

3D structure databases

ProteinModelPortalQ2KMM4.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING10116.ENSRNOP00000033009.

Proteomic databases

PRIDEQ2KMM4.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSRNOT00000039535; ENSRNOP00000033009; ENSRNOG00000022210.
GeneID287425.
KEGGrno:287425.
UCSCRGD:1305330. rat.

Organism-specific databases

CTD242.
RGD1305330. Alox12b.

Phylogenomic databases

eggNOGNOG69653.
GeneTreeENSGT00550000074415.
HOGENOMHOG000234358.
HOVERGENHBG005150.
InParanoidQ2KMM4.
KOK08021.
OrthoDBEOG7V49XR.
PhylomeDBQ2KMM4.

Enzyme and pathway databases

UniPathwayUPA00222.
UPA00881.

Gene expression databases

GenevestigatorQ2KMM4.

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.
IPR001885. LipOase_mml.
IPR001024. PLAT/LH2_dom.
[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]
SUPFAMSSF48484. SSF48484. 1 hit.
SSF49723. SSF49723. 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

NextBio626105.
PROQ2KMM4.

Entry information

Entry nameLX12B_RAT
AccessionPrimary (citable) accession number: Q2KMM4
Secondary accession number(s): Q2KMM5
Entry history
Integrated into UniProtKB/Swiss-Prot: June 27, 2006
Last sequence update: March 7, 2006
Last modified: April 16, 2014
This is version 55 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Protein Spotlight

Protein Spotlight articles and cited UniProtKB/Swiss-Prot entries

PATHWAY comments

Index of metabolic and biosynthesis pathways