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Reviewed, UniProtKB/Swiss-Prot Q92113 (CP17A_SQUAC)

Last modified October 13, 2009. Version 59. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data | Customize display text xml rdf/xml gff fasta
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 namesRecommended name:
    Steroid 17-alpha-hydroxylase/17,20 lyase
    EC=1.14.99.9
Alternative name(s):
    Cytochrome P450 17A1
    CYPXVII
    P450-C17
      Short name=P450c17
Gene names
Name: CYP17A1
Synonyms: CYP17
OrganismSqualus acanthias (Spiny dogfish)
Taxonomic identifier7797 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Chondrichthyes › Elasmobranchii › Squalea › Hypnosqualea › Squaliformes › Squaloidei › Squalidae › Squalus

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Protein attributes

Sequence length509 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceEvidence at transcript level.

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General annotation (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.

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.

Sequence similarities

Belongs to the cytochrome P450 family.

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Ontologies

Keywords
   Biological processSteroidogenesis
   Cellular componentMembrane
   LigandHeme
Iron
Metal-binding
   Molecular functionMonooxygenase
Oxidoreductase
Gene Ontology (GO)
   Biological processoxidation reduction

Inferred from electronic annotation. Source: UniProtKB-KW

steroid biosynthetic process

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular componentintegral to membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functionelectron carrier activity

Inferred from electronic annotation. Source: InterPro

heme binding

Inferred from electronic annotation. Source: InterPro

steroid 17-alpha-monooxygenase activity

Inferred from electronic annotation. Source: EC

Complete GO annotation...

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Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 509509Steroid 17-alpha-hydroxylase/17,20 lyase
PRO_0000051947

Sites

Metal binding4451Iron (heme axial ligand) By similarity

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Sequences

Sequence LengthMass (Da)Tools
Q92113-1 [UniParc].

Last modified November 1, 1996. Version 1.
Checksum: 9D9F1CA18050EF60

FASTA50957,208
        10         20         30         40         50         60 
MSLMLAALIL TVAFVICSLT GFTQRKLSGG RLPKCLPSFP LIGSLLSLRS DLPPHLLFQK 

        70         80         90        100        110        120 
LQKTYGNLFS LMMGPHYAVV INNHQHAKEV LLKKGKIFAG RPSMVTTDLL SRGGKDIAFG 

       130        140        150        160        170        180 
KYGPAWKFHR KLVLSALHLF GDGSAGIEKM ICQEATSMCS TFERLNNAAH DMMPDVTRAV 

       190        200        210        220        230        240 
TNVICLLCFN STYEKEDPEF QTMRKYSQGI VNTVAKDSLI DIFPWLQFFP NENLHTLKQC 

       250        260        270        280        290        300 
IATRDSILQK KFEDHKANYS SDSANDLFNI LLKAKMNAEN NNSSVHEAGL TDDHMVMTVA 

       310        320        330        340        350        360 
DIFGAGVETS STAFAWMIIY LIHHPEVQKK IQEEIDSNIG FERTPKMSDK GNMNFLNATI 

       370        380        390        400        410        420 
HEILRIQPVS PLLIPHVALA DSSIGDYTIP KGTRVIINLW AIHHDEKEWK NPDAFDPGRF 

       430        440        450        460        470        480 
LDEDGKYVCS SSESYLPFGA GTRVCLGEML ARMELFLFTS WILQRFTVQV PPGYPPPDKE 

       490        500 
GKFGIVLQPL KFKVQLKLRK AWENRGLHD

« Hide

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References

[1]"Isolation and characterization of the cDNA encoding the spiny dogfish shark (Squalus acanthias) form of cytochrome P450c17."
Trant J.M.
J. Exp. Zool. 272:25-33(1995) [PubMed: 7738515] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].

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Cross-references

Sequence databases

S77384 mRNA. Translation: AAB34256.1.
PIRI51281.

3D structure databases

HSSPHSSP built from PDB template 1DT6 based on UniProtKB P00179.
ModBaseSearch...

Phylogenomic databases

HOVERGENQ92113.

Enzyme and pathway databases

BRENDA1.14.99.9. 981.

Family and domain databases

InterProIPR001128. Cyt_P450.
IPR017973. Cyt_P450_C.
IPR017972. Cyt_P450_CS.
IPR002401. Cyt_P450_E_grp-I.
[Graphical view]
Gene3DG3DSA:1.10.630.10. Cyt_P450. 1 hit.
PANTHERPTHR19383. Cyt_P450. 1 hit.
PfamPF00067. p450. 1 hit.
[Graphical view]
PRINTSPR00463. EP450I.
PR00385. P450.
PROSITEPS00086. CYTOCHROME_P450. 1 hit.
[Graphical view]
ProtoNetSearch...

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Entry information

Entry nameCP17A_SQUAC
AccessionPrimary (citable) accession number: Q92113
Entry history
Integrated into UniProtKB/Swiss-Prot: December 15, 1998
Last sequence update: November 1, 1996
Last modified: October 13, 2009
This is version 59 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)

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Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

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