Steroid 21-hydroxylase - Canis lupus (Gray wolf)

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Q2LCM1 (CP21A_CANLU) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 43. History...

Clusters with 100%, 90%, 50% identity |

Documents (1) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

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

Organism

Canis lupus (Gray wolf)

Taxonomic identifier

9612 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Laurasiatheria › Carnivora › Caniformia › Canidae › Canis

Protein attributes

Sequence length	492 AA.
Sequence status	Complete.
Protein existence	Inferred from homology

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
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 – 492

492

Steroid 21-hydroxylase

PRO_0000269709

Regions

Region

340 – 356

Steroid-binding By similarity

Sites

Metal binding

426

Iron (heme axial ligand) By similarity

Sequences

Sequence

Length

Mass (Da)

Tools

Q2LCM1 [UniParc].

Last modified February 21, 2006. Version 1.
Checksum: 8151F79FF0484A54
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FASTA

492

55,366

        10         20         30         40         50         60 
MLLLGVLLLT VLAGARLLWG KWKLRGLHLP PLVPGCLHLL QPDLPLHLLG LTQKLGPIYR 

        70         80         90        100        110        120 
LRLGLQDVVV LNSKRTIEEA MVRKWVDFAG RPQTPSYKLV SLHHQDLSLG DYSLLWKAHK 

       130        140        150        160        170        180 
KLTRSALLLG IRSSMEPLVE QLTQEFCERM RAQAGTPVAI QKEFSLLTCA IICHLTFGDK 

       190        200        210        220        230        240 
EDTLVHTFHD CVQDLMRTWE HWSIQMLDII PFLRFFPNPG LWRLKRALEN RDHIVEKQLR 

       250        260        270        280        290        300 
QHKESMVAGQ WRDMTDYMLQ RVGRLRAEEG CGQLLEGHVH MSVVDLFIGG TETTATTLSW 

       310        320        330        340        350        360 
AVAFLLHHPE IQQRLQEELD RELGPGASGS RIPYRDPTRL PLLSATVAEV LRLRPVVPLA 

       370        380        390        400        410        420 
LPHCTTRPSS ISGYDIPEGM VVIPNLQGAH LDETVWERPQ EFRPDRFLVP GASPRVLAFG 

       430        440        450        460        470        480 
CGARVCLGEP LARLELLVVL AQLLRAFTLM PAAGTLPSLR PRARCGVNLS MQPFQVQLQP 

       490 
RGAGVLGRGQ HP

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References

[1]

"Phylogenetic analysis of a steroid 21-hydroxylase gene in some species of animals and a man."
Kosowska B., Brzezinska K., Dobosz T., Moska M., Strzala T., Marszalek B., Schmidt K.
Submitted (DEC-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Tissue: Muscle.

Cross-references

Sequence databases
EMBL GenBank DDBJ	DQ336566 Genomic DNA. Translation: ABC67289.1.
3D structure databases
ProteinModelPortal	Q2LCM1.
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Phylogenomic databases
HOVERGEN	HBG106944.
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...

Entry information

Entry name

CP21A_CANLU

Accession

Primary (citable) accession number: Q2LCM1

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 9, 2007
Last sequence update:	February 21, 2006
Last modified:	May 1, 2013
This is version 43 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections