P00191 (CP21A_BOVIN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Steroid 21-hydroxylase
EC=1.14.99.10

Alternative name(s):
21-OHase
Cytochrome P-450c21
Cytochrome P450 21
Cytochrome P450 XXI
Cytochrome P450-C21

Gene names

Name:	CYP21
Synonyms:	CYP21A1

Organism

Bos taurus (Bovine) [Reference proteome]

Taxonomic identifier

9913 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Laurasiatheria › Cetartiodactyla › Ruminantia › Pecora › Bovidae › Bovinae › Bos

Protein attributes

Sequence length	496 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Specifically catalyzes the 21-hydroxylation of steroids. Required for the adrenal synthesis of mineralocorticoids and glucocorticoids.
Catalytic activity	A C21 steroid + (reduced NADPH--hemoprotein reductase) + O2 = a 21-hydroxy-C(21)-steroid + (oxidized NADPH--hemoprotein reductase) + 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.

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	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	steroid biosynthetic process Inferred from electronic annotation. Source: UniProtKB-KW
Cellular_component	endoplasmic reticulum membrane Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	electron carrier activity Inferred from electronic annotation. Source: InterPro heme binding Inferred from electronic annotation. Source: InterPro iron ion 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...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 496

496

Steroid 21-hydroxylase

PRO_0000051974

Regions

Region

341 – 357

17

Steroid-binding By similarity

Sites

Metal binding

427

1

Iron (heme axial ligand)

Experimental info

Sequence conflict

13

1

L → K AA sequence Ref.4

Sequence conflict

14

1

A → S in AAA30487. Ref.2

Sequence conflict

401

1

H → Y in AAA30487. Ref.2

Sequence conflict

431

1

S → C in AAA30486. Ref.3

Secondary structure

1

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496

Helix Strand Turn

Details...

Beta strand

41 – 43

3

Helix

45 – 51

7

Helix

52 – 54

3

Beta strand

58 – 62

5

Beta strand

64 – 67

4

Beta strand

69 – 72

4

Helix

77 – 80

4

Turn

81 – 84

4

Turn

96 – 100

5

Beta strand

108 – 111

4

Helix

115 – 129

15

Helix

137 – 152

16

Helix

160 – 165

6

Helix

167 – 172

6

Turn

173 – 176

4

Helix

183 – 194

12

Turn

195 – 200

6

Helix

203 – 210

8

Helix

212 – 214

3

Helix

220 – 245

26

Beta strand

253 – 255

3

Helix

256 – 259

4

Helix

278 – 308

31

Helix

310 – 324

15

Beta strand

326 – 331

6

Helix

337 – 339

3

Helix

342 – 354

13

Beta strand

357 – 360

4

Beta strand

373 – 377

5

Beta strand

382 – 385

4

Helix

387 – 390

4

Turn

394 – 396

3

Beta strand

397 – 399

3

Beta strand

423 – 426

4

Helix

430 – 447

18

Sequences

	Sequence		Length	Mass (Da)
	P00191 [UniParc]. Last modified November 1, 1990. Version 2. Checksum: 2E87C829A7E66B31	FASTA	496	56,077
	10 20 30 40 50 60 MVLAGLLLLL TLLAGAHLLW GRWKLRNLHL PPLVPGFLHL LQPNLPIHLL SLTQKLGPVY 70 80 90 100 110 120 RLRLGLQEVV VLNSKRTIEE AMIRKWVDFA GRPQIPSYKL VSQRCQDISL GDYSLLWKAH 130 140 150 160 170 180 KKLTRSALLL GTRSSMEPWV DQLTQEFCER MRVQAGAPVT IQKEFSLLTC SIICYLTFGN 190 200 210 220 230 240 KEDTLVHAFH DCVQDLMKTW DHWSIQILDM VPFLRFFPNP GLWRLKQAIE NRDHMVEKQL 250 260 270 280 290 300 TRHKESMVAG QWRDMTDYML QGVGRQRVEE GPGQLLEGHV HMSVVDLFIG GTETTASTLS 310 320 330 340 350 360 WAVAFLLHHP EIQRRLQEEL DRELGPGASC SRVTYKDRAR LPLLNATIAE VLRLRPVVPL 370 380 390 400 410 420 ALPHRTTRPS SIFGYDIPEG MVVIPNLQGA HLDETVWEQP HEFRPDRFLE PGANPSALAF 430 440 450 460 470 480 GCGARVCLGE SLARLELFVV LLRLLQAFTL LPPPVGALPS LQPDPYCGVN LKVQPFQVRL 490 QPRGVEAGAW ESASAQ

References

[1]	"Structure of a bovine gene for P-450c21 (steroid 21-hydroxylase) defines a novel cytochrome P-450 gene family." Chung B., Matteson K.J., Miller W.L. Proc. Natl. Acad. Sci. U.S.A. 83:4243-4247(1986) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]	"Structural analysis of cloned cDNA for mRNA of microsomal cytochrome P-450(C21) which catalyzes steroid 21-hydroxylation in bovine adrenal cortex." Yoshioka H., Morohashi K., Sogawa K., Yamane M., Kominami S., Takemori S., Okada Y., Omura T., Fujii-Kuriyama Y. J. Biol. Chem. 261:4106-4109(1986) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[3]	"Bovine steroid 21-hydroxylase: regulation of biosynthesis." John M.E., Okamura T., Dee A., Adler B., John M.C., White P.C., Simpson E.R., Waterman M.R. Biochemistry 25:2846-2853(1986) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 121-496.
[4]	"Partial amino acid sequences of two mitochondrial and two microsomal cytochrome P-450's from adrenal cortex." Ogishima T., Okada Y., Kominami S., Takemori S., Omura T. J. Biochem. 94:1711-1714(1983) [PubMed] [Europe PMC] [Abstract] Cited for: PROTEIN SEQUENCE OF 1-15.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

M11267 Genomic DNA. Translation: AAA83247.1.
M12918 mRNA. Translation: AAA30487.1.
K01333 mRNA. Translation: AAA30486.1.

IPI

IPI00703155.

PIR

O4BOC2. A27555.

RefSeq

NP_001013614.1. NM_001013596.1.
NP_777064.1. NM_174639.1.

UniGene

Bt.1964.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
3QZ1	X-ray	3.00	A/B/C/D	1-496	[»]

ProteinModelPortal

P00191.

ModBase

Search...

Protein-protein interaction databases

STRING

9913.ENSBTAP00000007353.

Proteomic databases

PRIDE

P00191.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

GeneID

281741.
282425.

KEGG

bta:281741.
bta:282425.

Organism-specific databases

CTD

1589.
281741.

Phylogenomic databases

eggNOG

COG2124.

HOGENOM

HOG000036991.

HOVERGEN

HBG106944.

InParanoid

P00191.

KO

K00513.

OrthoDB

EOG4TB4B5.

Enzyme and pathway databases

BRENDA

1.14.99.10. 908.

Family and domain databases

Gene3D

1.10.630.10. 1 hit.

InterPro

IPR001128. Cyt_P450.
IPR017972. Cyt_P450_CS.
IPR002401. Cyt_P450_E_grp-I.
[Graphical view]

Pfam

PF00067. p450. 1 hit.
[Graphical view]

PRINTS

PR00463. EP450I.
PR00385. P450.

SUPFAM

SSF48264. Cytochrome_P450. 1 hit.

PROSITE

PS00086. CYTOCHROME_P450. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

NextBio

20805661.

Entry information

Entry name

CP21A_BOVIN

Accession

Primary (citable) accession number: P00191

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 21, 1986
Last sequence update:	November 1, 1990
Last modified:	May 1, 2013
This is version 109 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program