Steroid 21-hydroxylase - Sus scrofa (Pig)

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Reviewed, UniProtKB/Swiss-Prot P15540 (CP21A_PIG)

Last modified October 13, 2009. Version 74. History...

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Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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Names and origin

Protein names

Recommended name:
    Steroid 21-hydroxylase
    EC=1.14.99.10
Alternative name(s):
    Cytochrome P450 21
    Cytochrome P450 XXI
    21-OHase
    P450-C21
    P-450c21

Gene names

Name:	CYP21
Synonyms:	CYP21A1, CYP21A3

Organism

Sus scrofa (Pig)

Taxonomic identifier

9823 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Laurasiatheria › Cetartiodactyla › Suina › Suidae › Sus

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Protein attributes

Sequence length	492 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

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General annotation (Comments)

Function	Specifically catalyzes the 21-hydroxylation of steroids. Required for the adrenal synthesis of mineralocorticoids and glucocorticoids.
Catalytic activity	A steroid + AH₂ + O₂ = a 21-hydroxysteroid + A + H₂O.
Cofactor	Heme group By similarity.
Subcellular location	Endoplasmic reticulum membrane; Peripheral membrane protein. Microsome membrane; Peripheral membrane protein.
Domain	The leucine-rich hydrophobic amino acid N-terminal region probably helps to anchor the protein to the microsomal membrane.
Sequence similarities	Belongs to the cytochrome P450 family.

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Ontologies

Keywords
Biological process	Steroidogenesis
Cellular component	Endoplasmic reticulum Membrane Microsome
Ligand	Heme Iron Lipid-binding Metal-binding Steroid-binding
Molecular function	Monooxygenase Oxidoreductase
Technical term	Direct protein sequencing
Gene Ontology (GO)
Biological process	oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW steroid biosynthetic process Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	endoplasmic reticulum Inferred from electronic annotation. Source: UniProtKB-KW extrinsic to membrane Inferred from electronic annotation. Source: UniProtKB-SubCell microsome Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	electron carrier activity Inferred from electronic annotation. Source: InterPro heme binding Inferred from electronic annotation. Source: InterPro steroid 21-monooxygenase activity Inferred from electronic annotation. Source: EC steroid binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

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Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 492

492

Steroid 21-hydroxylase

PRO_0000051978

Regions

Region

341 – 357

Steroid-binding Potential

Sites

Metal binding

427

Iron (heme axial ligand) By similarity

Experimental info

Sequence conflict

L → T AA sequence Ref.1

Sequence conflict

L → K AA sequence Ref.1

Sequence conflict

R → K AA sequence Ref.1

Sequence conflict

141

E → C AA sequence Ref.1

Sequence conflict

201

E → D AA sequence Ref.1

Sequence conflict

391

H → I AA sequence Ref.1

Sequence conflict

463 – 465

HPH → VPY AA sequence Ref.1

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Sequences

Sequence

Length

Mass (Da)

Tools

P15540-1 [UniParc].

Last modified April 26, 2005. Version 2.
Checksum: 1FD5FFBFCA5A9E02
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FASTA

492

55,620

        10         20         30         40         50         60 
MVLVWLLLLL TLLAGARLLW GQWKLRNLHL PPLVPGFLHL LQPNLPIYLL GLTQRLGPIY 

        70         80         90        100        110        120 
RLRLGLQDVV VLNSKRTIEE ALVRKWVDFA GRPQIPSYKL ASQHCPDISL GDYSLFWKAH 

       130        140        150        160        170        180 
KKLTRSALLL GVRSSMEPRV EQLTQEFCER MRAQAGTPVT IQKEFSVLTC SIICCLTFGD 

       190        200        210        220        230        240 
KEDTLVHALH DCVQDLMKTW EHWSIQILDM VPFLRFFPSP GLRRLKQAIE NRDHLVEKQL 

       250        260        270        280        290        300 
RRHKESMVAG QWRDMLDYML QEAGRQRVEE GQGQLLEGHV HMSVVDLFIG GTETTANTLS 

       310        320        330        340        350        360 
WAVVYLLHHP EIQWRLQEEL DRELGPGAAG SRVPYKDRAR LPLLNATIAE VLRLRPVVPL 

       370        380        390        400        410        420 
ALPHRATRPS SIFGYDIPEG TVVIPNLQGA HLDETVWEQP HEFRPDRFLA PGANPSALAF 

       430        440        450        460        470        480 
GCGARVCLGE PLARLELFVV LVQLLQAFTL LPPEGALPSL QPHPHSGINL KVQPFQVRLQ 

       490 
PRGGRGEGPG PR

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References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Complete amino acid sequence of 21-hydroxylase cytochrome P-450 from porcine adrenal microsomes." Haniu M., Yanagibashi K., Hall P.F., Shively J.E. Arch. Biochem. Biophys. 254:380-384(1987) [PubMed: 3495238] [Abstract] Cited for: PROTEIN SEQUENCE. Tissue: Adrenal gland.
[2]	"Sequences of the swine 21-hydroxylase gene (CYP21) and a portion of the opposite-strand overlapping gene of unknown function previously described in human." Burghelle-Mayeur C., Geffrotin C., Vaiman M. Biochim. Biophys. Acta 1171:153-161(1992) [PubMed: 1482677] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[3]	"Detection of quantitative trait loci for fat androstenone levels in pigs." Quintanilla R., Demeure O., Bidanel J.P., Milan D., Iannuccelli N., Amigues Y., Gruand J., Renard C., Chevalet C., Bonneau M. J. Anim. Sci. 81:385-394(2003) [PubMed: 12643481] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: Meishan.
[4]	Porcine genome sequencing project Submitted (MAY-2007) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: Duroc.
[5]	"The swine steroid 21-hydroxylase gene (CYP21): cloning and mapping within the swine leucocyte antigen complex." Geffrotin C., Chardon P., de Andres-Cara D.F., Feil R., Renard C., Vaiman M. Anim. Genet. 21:1-13(1990) [PubMed: 2109953] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-99.

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Cross-references

Sequence databases
	M83939 Genomic DNA. Translation: AAA31080.1. AF490410 Genomic DNA. Translation: AAM11646.1. AL773560 Genomic DNA. Translation: CAN59658.1.
PIR	A32525. S28169.
RefSeq	NP_999598.1.
UniGene	Ssc.52818
3D structure databases
HSSP	HSSP built from PDB template 1DT6 based on UniProtKB P00179.
ModBase	Search...
Genome annotation databases
GeneID	403337.
KEGG	ssc:403337.
Organism-specific databases
CTD	403337.
Phylogenomic databases
HOVERGEN	P15540.
Enzyme and pathway databases
BRENDA	1.14.99.10. 249.
Family and domain databases
InterPro	IPR001128. Cyt_P450. IPR017973. Cyt_P450_C. IPR017972. Cyt_P450_CS. IPR002401. Cyt_P450_E_grp-I. [Graphical view]
Gene3D	G3DSA:1.10.630.10. Cyt_P450. 1 hit.
PANTHER	PTHR19383. Cyt_P450. 1 hit.
Pfam	PF00067. p450. 1 hit. [Graphical view]
PRINTS	PR00463. EP450I. PR00385. P450.
PROSITE	PS00086. CYTOCHROME_P450. 1 hit. [Graphical view]
ProtoNet	Search...

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Entry information

Entry name

CP21A_PIG

Accession

Primary (citable) accession number: P15540
Secondary accession number(s): A5A8W6, Q02390

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 1, 1990
Last sequence update:	April 26, 2005
Last modified:	October 13, 2009
This is version 74 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)

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Relevant documents

SIMILARITY comments

Index of protein domains and families

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Regions

Sites

Experimental info

Sequences

References

Cross-references

Sequence databases

3D structure databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Family and domain databases

Entry information

Relevant documents