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UniProtKB/Swiss-Prot entry Q02928


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

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Entry information
Entry name CP4AB_HUMAN
Primary accession number Q02928
Secondary accession numbers Q06766 Q16865 Q16866 Q5VSP8 Q86SU6 Q8IWY5
Integrated into Swiss-Prot on November 1, 1997
Sequence was last modified on November 1, 1997 (Sequence version 1)
Annotations were last modified on    November 25, 2008 (Entry version 78)
Name and origin of the protein
Protein name Cytochrome P450 4A11 [Precursor]
Synonyms EC 1.14.15.3
CYPIVA11
Fatty acid omega-hydroxylase
P-450 HK omega
Lauric acid omega-hydroxylase
CYP4AII
P450-HL-omega
20-hydroxyeicosatetraenoic acid synthase
20-HETE synthase
Gene name
Name: CYP4A11
Synonyms: CYP4A2
From
Homo sapiens (Human) [TaxID: 9606] 
Taxonomy Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; Homo.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND CHARACTERIZATION.
TISSUE=Kidney;
PubMed=7679927 [NCBI, ExPASy, EBI, Israel, Japan]
Palmer C.N.A., Richardson T.H., Griffin K.J., Hsu M.-H., Muerhoff A.S., Clark J.E., Johnson E.F.;
"Characterization of a cDNA encoding a human kidney, cytochrome P-450 4A fatty acid omega-hydroxylase and the cognate enzyme expressed in Escherichia coli.";
Biochim. Biophys. Acta 1172:161-166(1993).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), PROTEIN SEQUENCE OF 5-24, AND CHARACTERIZATION.
TISSUE=Liver;
PubMed=7798189 [NCBI, ExPASy, EBI, Israel, Japan]
Kawashima H., Kusunose E., Kikuta Y., Kinoshita H., Tanaka S., Yamamoto S., Kishimoto T., Kusunose M.;
"Purification and cDNA cloning of human liver CYP4A fatty acid omega-hydroxylase.";
J. Biochem. 116:74-80(1994).
[3]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), VARIANT SER-434, AND CHARACTERIZATION.
TISSUE=Kidney;
PubMed=8274222 [NCBI, ExPASy, EBI, Israel, Japan]
Imaoka S., Ogawa H., Kimura S., Gonzalez F.J.;
"Complete cDNA sequence and cDNA-directed expression of CYP4A11, a fatty acid omega-hydroxylase expressed in human kidney.";
DNA Cell Biol. 12:893-899(1993).
[4]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
DOI=10.1016/S0003-9861(02)00545-3; PubMed=12464262 [NCBI, ExPASy, EBI, Israel, Japan]
Bellamine A., Wang Y., Waterman M.R., Gainer J.V. III, Dawson E.P., Brown N.J., Capdevila J.H.;
"Characterization of the CYP4A11 gene, a second CYP4A gene in humans.";
Arch. Biochem. Biophys. 409:221-227(2003).
[5]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM 1), AND VARIANT SER-434.
SeattleSNPs program for genomic applications;
Submitted (AUG-2003) to the EMBL/GenBank/DDBJ databases.
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
DOI=10.1038/nature04727; PubMed=16710414 [NCBI, ExPASy, EBI, Israel, Japan]
Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K., Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.;
"The DNA sequence and biological annotation of human chromosome 1.";
Nature 441:315-321(2006).
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
TISSUE=Colon;
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).
[8]
PARTIAL PROTEIN SEQUENCE OF 5-39, AND CHARACTERIZATION.
TISSUE=Kidney;
DOI=10.1016/0005-2760(92)90106-6; PubMed=1739747 [NCBI, ExPASy, EBI, Israel, Japan]
Kawashima H., Kusunose E., Kubota I., Maekawa M., Kusunose M.;
"Purification and NH2-terminal amino acid sequences of human and rat kidney fatty acid omega-hydroxylases.";
Biochim. Biophys. Acta 1123:156-162(1992).
[9]
NUCLEOTIDE SEQUENCE [MRNA] OF 317-457, AND VARIANTS GLY-353 AND SER-434.
TISSUE=Liver;
PubMed=8363569 [NCBI, ExPASy, EBI, Israel, Japan]
Bell D.R., Plant N.J., Rider C.G., Na L., Brown S., Ateitalla I., Acharya S.K., Davies M.H., Elias E.E., Jenkins N.A., Gilbert D.J., Copeland N.G., Elcombe C.R.;
"Species-specific induction of cytochrome P-450 4A RNAs: PCR cloning of partial guinea-pig, human and mouse CYP4A cDNAs.";
Biochem. J. 294:173-180(1993).
[10]
COVALENT HEME ATTACHMENT.
DOI=10.1074/jbc.M009969200; PubMed=11139583 [NCBI, ExPASy, EBI, Israel, Japan]
Hoch U., Ortiz de Montellano P.R.;
"Covalently linked heme in cytochrome P4504A fatty acid hydroxylases.";
J. Biol. Chem. 276:11339-11346(2001).
[11]
COVALENT HEME ATTACHMENT, AND MUTAGENESIS OF GLU-321.
DOI=10.1074/jbc.M112155200; PubMed=11821421 [NCBI, ExPASy, EBI, Israel, Japan]
LeBrun L.A., Hoch U., Ortiz de Montellano P.R.;
"Autocatalytic mechanism and consequences of covalent heme attachment in the cytochrome P4504A family.";
J. Biol. Chem. 277:12755-12761(2002).
[12]
FUNCTION, MUTAGENESIS OF GYL-130, AND VARIANT SER-434.
DOI=10.1161/01.CIR.0000151309.82473.59; PubMed=15611369 [NCBI, ExPASy, EBI, Israel, Japan]
Gainer J.V., Bellamine A., Dawson E.P., Womble K.E., Grant S.W., Wang Y., Cupples L.A., Guo C.-Y., Demissie S., O'Donnell C.J., Brown N.J., Waterman M.R., Capdevila J.H.;
"Functional variant of CYP4A11 20-hydroxyeicosatetraenoic acid synthase is associated with essential hypertension.";
Circulation 111:63-69(2005).
[13]
VARIANTS GLY-353 AND SER-434.
DOI=10.1007/s10038-005-0245-9; PubMed=15895287 [NCBI, ExPASy, EBI, Israel, Japan]
Cho B.H., Park B.L., Kim L.H., Chung H.S., Shin H.D.;
"Highly polymorphic human CYP4A11 gene.";
J. Hum. Genet. 50:259-263(2005).
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
L04751; AAA58436.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
D26481; BAA05491.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
S67580; AAB29502.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
S67581; AAB29503.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF525488; AAO16078.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AY369778; AAQ56847.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AL731892; CAH72778.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AL731892; CAH72779.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC041158; AAH41158.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
X71480; CAA50586.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR A56859; A56859.
I53015; I53015.
I65981; I65981.
JX0331; JX0331.
RefSeq NP_000769.2; -.
UniGene Hs.1645
3D structure databases
HSSP P14779; 1JPZ. [HSSP ENTRY / PDB]
ModBase Q02928.
PTM databases
PhosphoSite Q02928; -.
Enzyme and pathway databases
Reactome REACT_2063; Metabolism of xenobiotics.
Organism-specific databases
H-InvDB HIX0023641; -.
HIX0028676; -.
HGNC HGNC:2642; CYP4A11.
GenAtlas CYP4A11.
MIM 601310; gene. [NCBI / EBI]
PharmGKB PA27118; -.
GeneCards Q02928.
Gene expression databases
CleanEx HS_CYP4A11; -.
GermOnline ENSG00000187048; Homo sapiens.
Ontologies
GO
GO:0005789; Cellular component: endoplasmic reticulum membrane (inferred from electronic annotation from UniProtKB-SubCell).
GO:0005792; Cellular component: microsome (traceable author statement from ProtInc).
GO:0018685; Molecular function: alkane 1-monooxygenase activity (inferred from electronic annotation from EC).
GO:0009055; Molecular function: electron carrier activity (inferred from electronic annotation from InterPro).
GO:0008393; Molecular function: fatty acid (omega-1)-hydroxylase activity (traceable author statement from ProtInc).
GO:0020037; Molecular function: heme binding (inferred from electronic annotation from InterPro).
GO:0005506; Molecular function: iron ion binding (inferred from electronic annotation from InterPro).
GO:0019825; Molecular function: oxygen binding (inferred from experiment from Reactome).
GO:0006631; Biological process: fatty acid metabolic process (traceable author statement from ProtInc).
GO:0055114; Biological process: oxidation reduction (inferred from electronic annotation from UniProtKB-KW).
QuickGo view.
Family and domain databases
InterPro IPR001128; Cyt_P450.
IPR002401; Cyt_P450_E_grp-I.
Graphical view of domain structure.
Gene3D G3DSA:1.10.630.10; Cyt_P450; 1.
PANTHER PTHR19383; Cyt_P450; 1.
Pfam PF00067; p450; 1.
Pfam graphical view of domain structure.
PRINTS PR00463; EP450I.
PR00385; P450.
PROSITE PS00086; CYTOCHROME_P450; 1.
ProtoNet Q02928.
Genome annotation databases
Ensembl ENSG00000187048; Homo sapiens. [Contig view]
GeneID 1579; -.
KEGG hsa:1579; -.
Phylogenomic databases
HOVERGEN Q02928; -.
Other
DrugBank DB00157; NADH.
NextBio 6485; -.
SOURCE CYP4A11; Homo sapiens.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
Alternative splicing; Direct protein sequencing; Endoplasmic reticulum; Heme; Iron; Membrane; Metal-binding; Microsome; Monooxygenase; Oxidoreductase; Polymorphism.
Features
SEVIEWER logo Feature table viewer FT aligner logo Feature aligner
KeyFrom   To Length Description FTId
PROPEP   1     4  4      PRO_0000003579
CHAIN   5   519  515     Cytochrome P450 4A11. PRO_0000003580
COMPBIAS   24    31  8     Poly-Leu. 
COMPBIAS   131   134  4     Poly-Leu. 
METAL   457   457        Iron (heme axial ligand). 
BINDING   321   321        Heme (covalent; via 1 link). 
VAR_SEQ   356   519        Missing (in isoform 2). VSP_034595
VARIANT   353   353  1     S -> G. VAR_044377 
VARIANT   434   434  1     F -> S (associated with hypertension; significantly reduced arachidonic acid and lauric acid metabolizing activity; dbSNP:rs1126742 [NCBI]). VAR_019160 
VARIANT   500   519  20     NGIHLRLRRLPNPCEDKDQL -> MESTCVSGGSLTLVKTRTSFEGLHLPSCLPDPRFCPLPVC PYPVFCLPTFPSSHLPAVPQSACPSLSHLSPGLPTCLSTC LLPTCISCWEKS (in CYP4A11V). VAR_001257
MUTAGEN   130   130        G->S: Loss of activity. 
MUTAGEN   321   321        E->A: Loss of covalent heme binding. 
CONFLICT   5     5        V -> A (in Ref. 8; AA sequence). 
CONFLICT   383   383        Y -> F (in Ref. 4; AAO16078). 
CONFLICT   390   390        G -> S (in Ref. 9; CAA50586). 
CONFLICT   410   412        MVL -> TVM (in Ref. 9; CAA50586). 
Sequence information
Length: 519 AA [This is the length of the unprocessed precursor] Molecular weight: 59348 Da [This is the MW of the unprocessed precursor] CRC64: A8D3073EEFF48AE9 [This is a checksum on the sequence]
        10         20         30         40         50         60 
MSVSVLSPSR LLGDVSGILQ AASLLILLLL LIKAVQLYLH RQWLLKALQQ FPCPPSHWLF 

        70         80         90        100        110        120 
GHIQELQQDQ ELQRIQKWVE TFPSACPHWL WGGKVRVQLY DPDYMKVILG RSDPKSHGSY 

       130        140        150        160        170        180 
RFLAPWIGYG LLLLNGQTWF QHRRMLTPAF HYDILKPYVG LMADSVRVML DKWEELLGQD 

       190        200        210        220        230        240 
SPLEVFQHVS LMTLDTIMKC AFSHQGSIQV DRNSQSYIQA ISDLNNLVFS RVRNAFHQND 

       250        260        270        280        290        300 
TIYSLTSAGR WTHRACQLAH QHTDQVIQLR KAQLQKEGEL EKIKRKRHLD FLDILLLAKM 

       310        320        330        340        350        360 
ENGSILSDKD LRAEVDTFMF EGHDTTASGI SWILYALATH PKHQERCREE IHSLLGDGAS 

       370        380        390        400        410        420 
ITWNHLDQMP YTTMCIKEAL RLYPPVPGIG RELSTPVTFP DGRSLPKGIM VLLSIYGLHH 

       430        440        450        460        470        480 
NPKVWPNPEV FDPFRFAPGS AQHSHAFLPF SGGSRNCIGK QFAMNELKVA TALTLLRFEL 

       490        500        510 
LPDPTRIPIP IARLVLKSKN GIHLRLRRLP NPCEDKDQL 

Q02928 in FASTA format

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