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Q5TCH4 (CP4AM_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 88. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Cytochrome P450 4A22
Alternative name(s):
CYPIVA22
Fatty acid omega-hydroxylase
Lauric acid omega-hydroxylase
EC=1.14.15.3
Gene names
Name:CYP4A22
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length519 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (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. Ref.1 Ref.2

Catalytic activity

Octane + reduced rubredoxin + O2 = 1-octanol + oxidized rubredoxin + H2O.

Subcellular location

Endoplasmic reticulum membrane; Peripheral membrane protein By similarity. Microsome membrane; Peripheral membrane protein By similarity.

Sequence similarities

Belongs to the cytochrome P450 family.

Caution

Was originally (Ref.1) termed CYP4A11.

Biophysicochemical properties

Kinetic parameters:

Vmax:15.2 µmol/min/µmol enzyme.

KM=56.7 µM for laurate Ref.1

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q5TCH4-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform 2 (identifier: Q5TCH4-2)

The sequence of this isoform differs from the canonical sequence as follows:
     356-519: Missing.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Propeptide1 – 44 By similarity
PRO_0000343408
Chain5 – 519515Cytochrome P450 4A22
PRO_0000343409

Regions

Compositional bias24 – 318Poly-Leu
Compositional bias131 – 1344Poly-Leu

Sites

Metal binding4571Iron (heme axial ligand) By similarity
Binding site3211Heme (covalent; via 1 link) By similarity

Natural variations

Alternative sequence356 – 519164Missing in isoform 2.
VSP_034584
Natural variant111R → C in allele CYP4A22*2 and CYP4A22*3. Ref.5
Corresponds to variant rs76011927 [ dbSNP | Ensembl ].
VAR_044349
Natural variant1041Y → F.
Corresponds to variant rs61507155 [ dbSNP | Ensembl ].
VAR_061045
Natural variant1211K → R. Ref.1
Corresponds to variant rs2758717 [ dbSNP | Ensembl ].
VAR_044350
Natural variant1261R → W in allele CYP4A22*8, allele CYP4A22*9, allele CYP4A22*11, allele CYP4A22*12, allele CYP4A22*13, allele CYP4A22*14 and allele CYP4A22*15. Ref.2 Ref.5
Corresponds to variant rs12564525 [ dbSNP | Ensembl ].
VAR_044351
Natural variant1301G → S in allele CYP4A22*4, allele CYP4A22*10, allele CYP4A22*12, allele CYP4A22*13, allele CYP4A22*14 and allele CYP4A22*15. Ref.2 Ref.5
Corresponds to variant rs2056900 [ dbSNP | Ensembl ].
VAR_044352
Natural variant1521N → Y in allele CYP4A22*2, allele CYP4A22*3, allele CYP4A22*4, allele CYP4A22*5, allele CYP4A22*6, allele CYP4A22*7, allele CYP4A22*8, allele CYP4A22*9, allele CYP4A22*10, allele CYP4A22*11, allele CYP4A22*12, allele CYP4A22*13, allele CYP4A22*14 and allele CYP4A22*15. Ref.2 Ref.5
Corresponds to variant rs2056899 [ dbSNP | Ensembl ].
VAR_044353
Natural variant1851V → F in allele CYP4A22*10, allele CYP4A22*11, allele CYP4A22*12, allele CYP4A22*13, allele CYP4A22*14 and allele CYP4A22*15. Ref.5
Corresponds to variant rs113777592 [ dbSNP | Ensembl ].
VAR_044354
Natural variant2261S → N. Ref.2
Corresponds to variant rs35202523 [ dbSNP | Ensembl ].
VAR_044355
Natural variant2301C → S. Ref.2
Corresponds to variant rs35156123 [ dbSNP | Ensembl ].
VAR_044356
Natural variant2311C → R Allele CYP4A22*2, allele CYP4A22*3, allele CYP4A22*4, allele CYP4A22*5, allele CYP4A22*6, allele CYP4A22*7, allele CYP4A22*8, allele CYP4A22*9, allele CYP4A22*10, allele CYP4A22*11, allele CYP4A22*12, allele CYP4A22*13, allele CYP4A22*14 and allele CYP4A22*15. Ref.2 Ref.5
Corresponds to variant rs10789501 [ dbSNP | Ensembl ].
VAR_044357
Natural variant2761K → T in allele CYP4A22*8, allele CYP4A22*11, allele CYP4A22*14 and allele CYP4A22*15. Ref.5
Corresponds to variant rs149718343 [ dbSNP | Ensembl ].
VAR_044358
Natural variant4281L → P in allele CYP4A22*6, allele CYP4A22*9, allele CYP4A22*10, allele CYP4A22*12, allele CYP4A22*13 and allele CYP4A22*15. Ref.2 Ref.5
Corresponds to variant rs2405599 [ dbSNP | Ensembl ].
VAR_044359
Natural variant4911M → I. Ref.1
Corresponds to variant rs2758714 [ dbSNP | Ensembl ].
VAR_044360
Natural variant5091L → F in allele CYP4A22*7, allele CYP4A22*10, allele CYP4A22*11, allele CYP4A22*13, allele CYP4A22*14 and allele CYP4A22*15. Ref.2 Ref.5
Corresponds to variant rs4926600 [ dbSNP | Ensembl ].
VAR_044361

Experimental info

Sequence conflict21S → A in AAQ21368. Ref.2
Sequence conflict1141P → S in AAQ21368. Ref.2
Sequence conflict2251N → S in AAQ21368. Ref.2
Sequence conflict2321M → V in AAQ21367. Ref.2
Sequence conflict2381E → Q in AAQ21367. Ref.2
Sequence conflict2411T → A in AAQ21368. Ref.2
Sequence conflict3531G → S in AAQ21367. Ref.2
Sequence conflict4341S → F in AAQ21367. Ref.2
Sequence conflict4871I → T in AAQ21367. Ref.2

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified December 21, 2004. Version 1.
Checksum: AA96444A38EE79BC

FASTA51959,246
        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 

« Hide

Isoform 2 [UniParc].

Checksum: 392C812A7C120920
Show »

FASTA35540,922

References

« Hide 'large scale' references
[1]"Human fatty acid omega-hydroxylase, CYP4A11: determination of complete genomic sequence and characterization of purified recombinant protein."
Kawashima H., Naganuma T., Kusunose E., Kono T., Yasumoto R., Sugimura K., Kishimoto T.
Arch. Biochem. Biophys. 378:333-339(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM 1), FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, VARIANTS ARG-121 AND ILE-491.
[2]"Functional variant of CYP4A11 20-hydroxyeicosatetraenoic acid synthase is associated with essential hypertension."
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.
Circulation 111:63-69(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, VARIANTS TRP-126; SER-130; TYR-152; ASN-226; SER-230; ARG-231; PRO-428 AND PHE-509.
Tissue: Kidney and Liver.
[3]"The DNA sequence and biological annotation of human chromosome 1."
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. expand/collapse author list , 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.
Nature 441:315-321(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[4]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
[5]"Genetic polymorphisms and haplotype structures of the CYP4A22 gene in a Japanese population."
Hiratsuka M., Nozawa H., Katsumoto Y., Moteki T., Sasaki T., Konno Y., Mizugaki M.
Mutat. Res. 599:98-104(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS CYS-11; TRP-126; SER-130; TYR-152; PHE-185; ARG-231; THR-276; PRO-428 AND PHE-509.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF208532 Genomic DNA. Translation: AAF76722.1.
AY280371 mRNA. Translation: AAQ21367.1.
AY280372 mRNA. Translation: AAQ21368.1.
AL135960 Genomic DNA. Translation: CAI19737.1.
AL135960 Genomic DNA. Translation: CAI19738.1.
BC148248 mRNA. Translation: AAI48249.1.
RefSeqNP_001010969.2. NM_001010969.2.
UniGeneHs.726474.

3D structure databases

ProteinModelPortalQ5TCH4.
SMRQ5TCH4. Positions 71-509.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING9606.ENSP00000360958.

PTM databases

PhosphoSiteQ5TCH4.

Polymorphism databases

DMDM74746067.

Proteomic databases

PaxDbQ5TCH4.
PRIDEQ5TCH4.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000294337; ENSP00000294337; ENSG00000162365.
ENST00000371891; ENSP00000360958; ENSG00000162365. [Q5TCH4-1]
GeneID284541.
KEGGhsa:284541.
UCSCuc001cqv.1. human. [Q5TCH4-1]

Organism-specific databases

CTD284541.
GeneCardsGC01P047603.
H-InvDBHIX0028676.
HGNCHGNC:20575. CYP4A22.
MIM615341. gene.
neXtProtNX_Q5TCH4.
PharmGKBPA134979692.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG2124.
HOGENOMHOG000233833.
HOVERGENHBG000182.
InParanoidQ5TCH4.
KOK17688.
OMAKSAFSHQ.
PhylomeDBQ5TCH4.
TreeFamTF105088.

Enzyme and pathway databases

ReactomeREACT_111217. Metabolism.

Gene expression databases

BgeeQ5TCH4.
GenevestigatorQ5TCH4.

Family and domain databases

Gene3D1.10.630.10. 1 hit.
InterProIPR001128. Cyt_P450.
IPR017972. Cyt_P450_CS.
IPR002401. Cyt_P450_E_grp-I.
[Graphical view]
PfamPF00067. p450. 1 hit.
[Graphical view]
PRINTSPR00463. EP450I.
PR00385. P450.
SUPFAMSSF48264. SSF48264. 1 hit.
PROSITEPS00086. CYTOCHROME_P450. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

GeneWikiCYP4A22.
GenomeRNAi284541.
NextBio94950.
PROQ5TCH4.
SOURCESearch...

Entry information

Entry nameCP4AM_HUMAN
AccessionPrimary (citable) accession number: Q5TCH4
Secondary accession number(s): Q5TCH3 expand/collapse secondary AC list , Q6JXK7, Q6JXK8, Q9NRM4
Entry history
Integrated into UniProtKB/Swiss-Prot: July 1, 2008
Last sequence update: December 21, 2004
Last modified: April 16, 2014
This is version 88 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 1

Human chromosome 1: entries, gene names and cross-references to MIM