NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Adrenal gland;
DOI=10.1023/A:1022101703670; PubMed=12693981 [NCBI, ExPASy, EBI, Israel, Japan]
Gilep A.A., Estabrook R.W., Usanov S.A.;
"Molecular cloning and heterologous expression in E. coli of cytochrome P45017alpha. Comparison of structural and functional properties of substrate-specific cytochromes P450 from different species.";
Biokhimiia 68:86-98(2003).

Comments

FUNCTION: Conversion of pregnenolone and progesterone to their 17-alpha-hydroxylated products and subsequently to dehydroepiandrosterone (DHEA) and androstenedione. Catalyzes both the 17-alpha-hydroxylation and the 17,20-lyase reaction. Involved in sexual development during fetal life and at puberty (By similarity).
CATALYTIC ACTIVITY: A steroid + AH₂ + O₂ = a 17-alpha-hydroxysteroid + A + H₂O.
COFACTOR: Heme group (By similarity).
PATHWAY: Lipid metabolism; steroid biosynthesis .
SUBCELLULAR LOCATION: Membrane (Potential). Membrane; Single-pass membrane protein.
SIMILARITY: Belongs to the cytochrome P450 family.

Copyright

Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.

Cross-references

Sequence databases

EMBL

AF292565; AAG02227.1; -; mRNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

3D structure databases

HSSP

P00179; 1DT6. [HSSP ENTRY / PDB]

ModBase

Q9GMC7.

Ontologies

GO:0016020;	Cellular component: membrane (inferred from electronic annotation from UniProtKB-KW).
GO:0004508;	Molecular function: steroid 17-alpha-monooxygenase activity (inferred from electronic annotation from EC).
GO:0006700;	Biological process: C21-steroid hormone biosynthetic process (inferred from electronic annotation from UniProtKB-KW).
GO:0055114;	Biological process: oxidation reduction (inferred from electronic annotation from UniProtKB-KW).
QuickGo view.

Family and domain databases

InterPro

IPR001128; Cyt_P450.
IPR002401; Cyt_P450_E_grp-I.
Graphical view of domain structure.

Gene3D

G3DSA:1.10.630.10; Cyt_P450; 1.

PANTHER

PTHR19383; Cyt_P450; 1.

Pfam

PF00067; p450; 1.
Pfam graphical view of domain structure.

PRINTS

PR00463; EP450I.
PR00385; P450.

PROSITE

PS00086; CYTOCHROME_P450; 1.

Phylogenomic databases

HOVERGEN

Q9GMC7; -.

Other

UniRef

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

Heme; Iron; Membrane; Metal-binding; Monooxygenase; Oxidoreductase; Steroidogenesis.

Features

Feature table viewer

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 509`	`509`	`Cytochrome P450 17A1.`	`PRO_0000051925`
`METAL`	`442 442`		`Iron (heme axial ligand) (By similarity).`

Sequence information

Length: 509 AA [This is the length of the unprocessed precursor]

Molecular weight: 57247 Da [This is the MW of the unprocessed precursor]

CRC64: 434E2070528AA279 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MWLLLAVFLL TLAYLFWPKT KHSGAKYPRS LPSLPLVGSL PFLPRRGQQH KNFFKLQEKY 

        70         80         90        100        110        120 
GPIYSFRLGS KTTVMIGHHQ LAREVLLKKG KEFSGRPKVA TLDILSDNQK GIAFADHGAH 

       130        140        150        160        170        180 
WQLHRKLALN AFALFKDGNL KLEKIINQEA NVLCDFLATQ HGEAIDLSEP LSLAVTNIIS 

       190        200        210        220        230        240 
FICFNFSFKN EDPALKAIQN VNDGILEVLS KEVLLDIFPV LKIFPSKAME KMKGYVQTRN 

       250        260        270        280        290        300 
ELLNEILEKC QENFSSDSIT NLLHILIQAK VNADNNNAGP DQDSKLLSSR HMLATIGDIF 

       310        320        330        340        350        360 
GAGVETTTSV IKWIVAYLLH HPSLKKRIQD DIDQIIGFNR TPAISDRNRL VLLEATIREV 

       370        380        390        400        410        420 
LRIRPVAPTL IPHKAVIDSS IGDLTIDKGT DVVVNLWALH HSEKEWQHPD LFMPERFLDP 

       430        440        450        460        470        480 
TGTQLISPSL SYLPFGAGPR SCVGEMLARQ ELFLFMSRLL QRFNLEIPDD GKLPSLEGHA 

       490        500 
SLVLQIKPFK VKIEVRQAWK EAQAEGSTP

Q9GMC7 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools