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P00191

- CP21A_BOVIN

UniProt

P00191 - CP21A_BOVIN

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Protein
Steroid 21-hydroxylase
Gene
CYP21, CYP21A1, CYP21A2
Organism
Bos taurus (Bovine)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

Specifically catalyzes the 21-hydroxylation of steroids. Required for the adrenal synthesis of mineralocorticoids and glucocorticoids.1 Publication

Catalytic activityi

A C(21) steroid + (reduced NADPH--hemoprotein reductase) + O2 = a 21-hydroxy-C(21)-steroid + (oxidized NADPH--hemoprotein reductase) + H2O.1 Publication

Cofactori

Heme group.1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi427 – 4271Iron (heme axial ligand)

GO - Molecular functioni

  1. heme binding Source: InterPro
  2. iron ion binding Source: InterPro
  3. steroid 21-monooxygenase activity Source: UniProtKB-EC
  4. steroid binding Source: UniProtKB-KW
Complete GO annotation...

GO - Biological processi

  1. steroid biosynthetic process Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Monooxygenase, Oxidoreductase

Keywords - Biological processi

Steroidogenesis

Keywords - Ligandi

Heme, Iron, Lipid-binding, Metal-binding, Steroid-binding

Enzyme and pathway databases

BRENDAi1.14.99.10. 908.

Names & Taxonomyi

Protein namesi
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 namesi
Name:CYP21
Synonyms:CYP21A1, CYP21A2
OrganismiBos taurus (Bovine)
Taxonomic identifieri9913 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaRuminantiaPecoraBovidaeBovinaeBos
ProteomesiUP000009136: Unplaced

Subcellular locationi

GO - Cellular componenti

  1. endoplasmic reticulum membrane Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Endoplasmic reticulum, Membrane, Microsome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 496496Steroid 21-hydroxylase
PRO_0000051974Add
BLAST

Proteomic databases

PRIDEiP00191.

Interactioni

Protein-protein interaction databases

STRINGi9913.ENSBTAP00000007353.

Structurei

Secondary structure

Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi41 – 433
Helixi45 – 517
Helixi52 – 543
Beta strandi58 – 625
Beta strandi64 – 674
Beta strandi69 – 724
Helixi77 – 804
Turni81 – 844
Turni96 – 1005
Beta strandi108 – 1114
Helixi115 – 12915
Helixi137 – 15216
Helixi160 – 1656
Helixi167 – 1726
Turni173 – 1764
Helixi183 – 19412
Turni195 – 2006
Helixi203 – 2108
Helixi212 – 2143
Helixi220 – 24526
Beta strandi253 – 2553
Helixi256 – 2594
Helixi278 – 30831
Helixi310 – 32415
Beta strandi326 – 3316
Helixi337 – 3393
Helixi342 – 35413
Beta strandi357 – 3604
Beta strandi373 – 3775
Beta strandi382 – 3854
Helixi387 – 3904
Turni394 – 3963
Beta strandi397 – 3993
Beta strandi423 – 4264
Helixi430 – 44718

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3QZ1X-ray3.00A/B/C/D1-496[»]
ProteinModelPortaliP00191.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni341 – 35717Steroid-binding By similarity
Add
BLAST

Domaini

The leucine-rich hydrophobic amino acid N-terminal region probably helps to anchor the protein to the microsomal membrane.

Sequence similaritiesi

Belongs to the cytochrome P450 family.

Phylogenomic databases

eggNOGiCOG2124.
HOGENOMiHOG000036991.
HOVERGENiHBG106944.
InParanoidiP00191.
KOiK00513.

Family and domain databases

Gene3Di1.10.630.10. 1 hit.
InterProiIPR001128. Cyt_P450.
IPR017972. Cyt_P450_CS.
IPR002401. Cyt_P450_E_grp-I.
[Graphical view]
PfamiPF00067. p450. 1 hit.
[Graphical view]
PRINTSiPR00463. EP450I.
PR00385. P450.
SUPFAMiSSF48264. SSF48264. 1 hit.
PROSITEiPS00086. CYTOCHROME_P450. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P00191-1 [UniParc]FASTAAdd to Basket

« Hide

MVLAGLLLLL TLLAGAHLLW GRWKLRNLHL PPLVPGFLHL LQPNLPIHLL    50
SLTQKLGPVY RLRLGLQEVV VLNSKRTIEE AMIRKWVDFA GRPQIPSYKL 100
VSQRCQDISL GDYSLLWKAH KKLTRSALLL GTRSSMEPWV DQLTQEFCER 150
MRVQAGAPVT IQKEFSLLTC SIICYLTFGN KEDTLVHAFH DCVQDLMKTW 200
DHWSIQILDM VPFLRFFPNP GLWRLKQAIE NRDHMVEKQL TRHKESMVAG 250
QWRDMTDYML QGVGRQRVEE GPGQLLEGHV HMSVVDLFIG GTETTASTLS 300
WAVAFLLHHP EIQRRLQEEL DRELGPGASC SRVTYKDRAR LPLLNATIAE 350
VLRLRPVVPL ALPHRTTRPS SIFGYDIPEG MVVIPNLQGA HLDETVWEQP 400
HEFRPDRFLE PGANPSALAF GCGARVCLGE SLARLELFVV LLRLLQAFTL 450
LPPPVGALPS LQPDPYCGVN LKVQPFQVRL QPRGVEAGAW ESASAQ 496
Length:496
Mass (Da):56,077
Last modified:November 1, 1990 - v2
Checksum:i2E87C829A7E66B31
GO

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti13 – 131L → K AA sequence 1 Publication
Sequence conflicti14 – 141A → S in AAA30487. 1 Publication
Sequence conflicti401 – 4011H → Y in AAA30487. 1 Publication
Sequence conflicti431 – 4311S → C in AAA30486. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
M11267 Genomic DNA. Translation: AAA83247.1.
M12918 mRNA. Translation: AAA30487.1.
K01333 mRNA. Translation: AAA30486.1.
PIRiA27555. O4BOC2.
RefSeqiNP_001013614.1. NM_001013596.1.
NP_777064.1. NM_174639.1.
UniGeneiBt.1964.

Genome annotation databases

GeneIDi281741.
282425.
KEGGibta:281741.
bta:282425.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
M11267 Genomic DNA. Translation: AAA83247.1 .
M12918 mRNA. Translation: AAA30487.1 .
K01333 mRNA. Translation: AAA30486.1 .
PIRi A27555. O4BOC2.
RefSeqi NP_001013614.1. NM_001013596.1.
NP_777064.1. NM_174639.1.
UniGenei Bt.1964.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
3QZ1 X-ray 3.00 A/B/C/D 1-496 [» ]
ProteinModelPortali P00191.
ModBasei Search...

Protein-protein interaction databases

STRINGi 9913.ENSBTAP00000007353.

Proteomic databases

PRIDEi P00191.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

GeneIDi 281741.
282425.
KEGGi bta:281741.
bta:282425.

Organism-specific databases

CTDi 1589.
281741.

Phylogenomic databases

eggNOGi COG2124.
HOGENOMi HOG000036991.
HOVERGENi HBG106944.
InParanoidi P00191.
KOi K00513.

Enzyme and pathway databases

BRENDAi 1.14.99.10. 908.

Miscellaneous databases

NextBioi 20805661.

Family and domain databases

Gene3Di 1.10.630.10. 1 hit.
InterProi IPR001128. Cyt_P450.
IPR017972. Cyt_P450_CS.
IPR002401. Cyt_P450_E_grp-I.
[Graphical view ]
Pfami PF00067. p450. 1 hit.
[Graphical view ]
PRINTSi PR00463. EP450I.
PR00385. P450.
SUPFAMi SSF48264. SSF48264. 1 hit.
PROSITEi PS00086. CYTOCHROME_P450. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  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. 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.
  5. "Three-dimensional structure of steroid 21-hydroxylase (cytochrome P450 21A2) with two substrates reveals locations of disease-associated variants."
    Zhao B., Lei L., Kagawa N., Sundaramoorthy M., Banerjee S., Nagy L.D., Guengerich F.P., Waterman M.R.
    J. Biol. Chem. 287:10613-10622(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS) IN COMPLEX WITH HEME AND 17-HYDROXYPROGESTERONE, FUNCTION, COFACTOR, CATALYTIC ACTIVITY.

Entry informationi

Entry nameiCP21A_BOVIN
AccessioniPrimary (citable) accession number: P00191
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: November 1, 1990
Last modified: January 22, 2014
This is version 114 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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