[1]	NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM 1), FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, AND VARIANTS ARG-121 AND ILE-491. DOI=10.1006/abbi.2000.1831; PubMed=10860550 [NCBI, ExPASy, EBI, Israel, Japan] Kawashima H., Naganuma T., Kusunose E., Kono T., Yasumoto R., Sugimura K., Kishimoto T.; "Human fatty acid omega-hydroxylase, CYP4A11: determination of complete genomic sequence and characterization of purified recombinant protein."; Arch. Biochem. Biophys. 378:333-339(2000).
[2]	NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, AND VARIANTS TRP-126; SER-130; TYR-152; ASN-226; SER-230; ARG-231; PRO-428 AND PHE-509. TISSUE=Kidney, and Liver; 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).
[3]	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).
[4]	NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). 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).
[5]	VARIANTS CYS-11; TRP-126; SER-130; TYR-152; PHE-185; ARG-231; THR-276; PRO-428 AND PHE-509. DOI=10.1016/j.mrfmmm.2006.02.008; PubMed=16806293 [NCBI, ExPASy, EBI, Israel, Japan] Hiratsuka M., Nozawa H., Katsumoto Y., Moteki T., Sasaki T., Konno Y., Mizugaki M.; "Genetic polymorphisms and haplotype structures of the CYP4A22 gene in a Japanese population."; Mutat. Res. 599:98-104(2006).

Comments

FUNCTION: Catalyzes the omega- and (omega-1)-hydroxylation of various fatty acids such as laurate and palmitate. Shows no activity towards arachidonic acid and prostaglandin A1. Lacks functional activity in the kidney and does not contribute to renal 20-hydroxyeicosatetraenoic acid (20-HETE) biosynthesis.
CATALYTIC ACTIVITY: Octane + reduced rubredoxin + O₂ = 1-octanol + oxidized rubredoxin + H₂O.
BIOPHYSICOCHEMICAL PROPERTIES:

Kinetic parameters: K_M=56.7 µM for laurate;
Note=V_max:15.2 µmol/min/µmol enzyme;
SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Peripheral membrane protein (By similarity). Microsome membrane; Peripheral membrane protein (By similarity).
ALTERNATIVE PRODUCTS: 2 named isoforms [FASTA] produced by alternative splicing.

Name 1

Isoform ID Q5TCH4-1

This is the isoform sequence displayed in this entry.

Name 2

Isoform ID Q5TCH4-2

Features which should be applied to build the isoform sequence: VSP_034584.
SIMILARITY: Belongs to the cytochrome P450 family.
CAUTION: Was originally (PubMed:10860550) termed CYP4A11.
WEB RESOURCE: Name=Cytochrome P450 Allele Nomenclature Committee; Note=CYP4A22 alleles; URL="http://www.cypalleles.ki.se/cyp4a22.htm";.

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

AF208532; AAF76722.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AY280371; AAQ21367.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AY280372; AAQ21368.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AL135960; CAI19737.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AL135960; CAI19738.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
BC148248; AAI48249.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

RefSeq

NP_001010969.2; -.

UniGene

Hs.567807

3D structure databases

ModBase

Q5TCH4.

Organism-specific databases

HGNC:20575; CYP4A22.

PA134979692; -.

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.

BLOCKS

Q5TCH4.

Genome annotation databases

Ensembl

ENSG00000162365; Homo sapiens. [Contig view]

GeneID

284541; -.

KEGG

hsa:284541; -.

Phylogenomic databases

HOGENOM

Q5TCH4; -.

HOVERGEN

Q5TCH4; -.

Other

ProtoNet

Q5TCH4.

UniRef

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

Alternative splicing; Endoplasmic reticulum; Heme; Iron; Membrane; Metal-binding; Microsome; Monooxygenase; Oxidoreductase; Polymorphism.

Features

Feature table viewer

Feature aligner

`Key`	`From To`	`Length`	`Description`	`FTId`
`PROPEP`	`1 4`	`4`	`By similarity.`	`PRO_0000343408`
`CHAIN`	`5 519`	`515`	`Cytochrome P450 4A22.`	`PRO_0000343409`
`COMPBIAS`	`24 31`	`8`	`Poly-Leu.`
`COMPBIAS`	`131 134`	`4`	`Poly-Leu.`
`METAL`	`457 457`		`Iron (heme axial ligand) (By similarity).`
`BINDING`	`321 321`		`Heme (covalent; via 1 link) (By similarity).`
`VAR_SEQ`	`356 519`		`Missing (in isoform 2).`	`VSP_034584`
`VARIANT`	`11 11`	`1`	`R -> C (in allele CYP4A222 and CYP4A223).`	`VAR_044349`
`VARIANT`	`121 121`	`1`	`K -> R (in dbSNP:rs2758717 [NCBI]).`	`VAR_044350`
`VARIANT`	`126 126`	`1`	`R -> W (in allele CYP4A228, allele CYP4A229, allele CYP4A2211, allele CYP4A2212, allele CYP4A2213, allele CYP4A2214 and allele CYP4A22*15; dbSNP:rs12564525 [NCBI]).`	`VAR_044351`
`VARIANT`	`130 130`	`1`	`G -> S (in allele CYP4A224, allele CYP4A2210, allele CYP4A2212, allele CYP4A2213, allele CYP4A2214 and allele CYP4A2215; dbSNP:rs2056900 [NCBI]).`	`VAR_044352`
`VARIANT`	`152 152`	`1`	`N -> Y (in allele CYP4A222, allele CYP4A223, allele CYP4A224, allele CYP4A225, allele CYP4A226, allele CYP4A227, allele CYP4A228, allele CYP4A229, allele CYP4A2210, allele CYP4A2211, allele CYP4A2212, allele CYP4A2213, allele CYP4A2214 and allele CYP4A2215; dbSNP:rs2056899 [NCBI]).`	`VAR_044353`
`VARIANT`	`185 185`	`1`	`V -> F (in allele CYP4A2210, allele CYP4A2211, allele CYP4A2212, allele CYP4A2213, allele CYP4A2214 and allele CYP4A2215).`	`VAR_044354`
`VARIANT`	`226 226`	`1`	`S -> N (in dbSNP:rs35202523 [NCBI]).`	`VAR_044355`
`VARIANT`	`230 230`	`1`	`C -> S (in dbSNP:rs35156123 [NCBI]).`	`VAR_044356`
`VARIANT`	`231 231`	`1`	`C -> R (allele CYP4A222, allele CYP4A223, allele CYP4A224, allele CYP4A225, allele CYP4A226, allele CYP4A227, allele CYP4A228, allele CYP4A229, allele CYP4A2210, allele CYP4A2211, allele CYP4A2212, allele CYP4A2213, allele CYP4A2214 and allele CYP4A2215; dbSNP:rs10789501 [NCBI]).`	`VAR_044357`
`VARIANT`	`276 276`	`1`	`K -> T (in allele CYP4A228, allele CYP4A2211, allele CYP4A2214 and allele CYP4A2215).`	`VAR_044358`
`VARIANT`	`428 428`	`1`	`L -> P (in allele CYP4A226, allele CYP4A229, allele CYP4A2210, allele CYP4A2212, allele CYP4A2213 and allele CYP4A2215; dbSNP:rs2405599 [NCBI]).`	`VAR_044359`
`VARIANT`	`491 491`	`1`	`M -> I (in dbSNP:rs2758714 [NCBI]).`	`VAR_044360`
`VARIANT`	`509 509`	`1`	`L -> F (in allele CYP4A227, allele CYP4A2210, allele CYP4A2211, allele CYP4A2213, allele CYP4A2214 and allele CYP4A2215; dbSNP:rs4926600 [NCBI]).`	`VAR_044361`
`CONFLICT`	`2 2`		`S -> A (in Ref. 2; AAQ21368).`
`CONFLICT`	`114 114`		`P -> S (in Ref. 2; AAQ21368).`
`CONFLICT`	`225 225`		`N -> S (in Ref. 2; AAQ21368).`
`CONFLICT`	`232 232`		`M -> V (in Ref. 2; AAQ21367).`
`CONFLICT`	`238 238`		`E -> Q (in Ref. 2; AAQ21367).`
`CONFLICT`	`241 241`		`T -> A (in Ref. 2; AAQ21368).`
`CONFLICT`	`353 353`		`G -> S (in Ref. 2; AAQ21367).`
`CONFLICT`	`434 434`		`S -> F (in Ref. 2; AAQ21367).`
`CONFLICT`	`487 487`		`I -> T (in Ref. 2; AAQ21367).`

Sequence information

Length: 519 AA [This is the length of the unprocessed precursor]

Molecular weight: 59246 Da [This is the MW of the unprocessed precursor]

CRC64: AA96444A38EE79BC [This is a checksum on the sequence]

        10         20         30         40         50         60 
MSVSVLSPSR RLGGVSGILQ VTSLLILLLL LIKAAQLYLH RQWLLKALQQ FPCPPSHWLF 

        70         80         90        100        110        120 
GHIQEFQHDQ ELQRIQERVK TFPSACPYWI WGGKVRVQLY DPDYMKVILG RSDPKSHGSY 

       130        140        150        160        170        180 
KFLAPRIGYG LLLLNGQTWF QHRRMLTPAF HNDILKPYVG LMADSVRVML DKWEELLGQD 

       190        200        210        220        230        240 
SPLEVFQHVS LMTLDTIMKS AFSHQGSIQV DRNSQSYIQA ISDLNSLVFC CMRNAFHEND 

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

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

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

       430        440        450        460        470        480 
NPKVWPNLEV FDPSRFAPGS AQHSHAFLPF SGGSRNCIGK QFAMNQLKVA RALTLLRFEL 

       490        500        510 
LPDPTRIPIP MARLVLKSKN GIHLRLRRLP NPCEDKDQL

Q5TCH4 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools