(data stored in ACNUC30567 zone)

HOGENOM: AILMEGL192668_1_2_PE2

ID   AILMEGL192668_1_2_PE2                STANDARD;      PRT;   330 AA.
AC   AILMEGL192668_1_2_PE2; D2HBV9;
DT   00-JAN-0000 (Rel. 1, Created)
DT   00-JAN-0000 (Rel. 2, Last sequence update)
DT   00-JAN-0000 (Rel. 3, Last annotation update)
DE   RecName: Full=Probable polyprenol reductase; EC=1.3.1.-;AltName:
DE   Full=3-oxo-5-alpha-steroid 4-dehydrogenase 3; EC=1.3.99 5;AltName:
DE   Full=Steroid 5-alpha-reductase 3; Short=S5AR 3; Short=SR type 3;
DE   (AILMEGL192668_1_2.PE2).
GN   Name=SRD5A3; ORFNames=PANDA_008038;
OS   AILUROPODA MELANOLEUCA.
OC   Eukaryota; Metazoa; Eumetazoa; Bilateria; Coelomata; Deuterostomia;
OC   Chordata; Craniata; Vertebrata; Gnathostomata; Teleostomi; Euteleostomi;
OC   Sarcopterygii; Tetrapoda; Amniota; Mammalia; Theria; Eutheria;
OC   Laurasiatheria; Carnivora; Caniformia; Ursidae; Ailuropoda.
OX   NCBI_TaxID=9646;
RN   [0]
RP   -.;
RG   -.;
RL   -.;
CC   -!- SEQ. DATA ORIGIN: Translated from
CC       the HOGENOM CDS AILMEGL192668_1_2.PE2.
CC       Ailuropoda melanoleuca scaffold GL192668.1 ailMel1 partial sequence
CC       1000001..1660525 annotated by Ensembl
CC   -!- ANNOTATIONS ORIGIN:PORED_AILME
CC   -!- FUNCTION: Probable polyprenol reductase. Plays a key role in early
CC       steps of protein N-linked glycosylation by being required for the
CC       conversion of polyprenol into dolichol. Dolichols are required for
CC       the synthesis of dolichol-linked monosaccharides and the
CC       oligosaccharide precursor used for N-glycosylation. Probably acts
CC       as a polyprenol reductase that promotes the reduction of the
CC       alpha-isoprene unit of polyprenols into dolichols in a NADP-
CC       dependent mechanism. Also able to convert testosterone (T) into 5-
CC       alpha-dihydrotestosterone (DHT) (By similarity).
CC   -!- CATALYTIC ACTIVITY: A 3-oxo-5-alpha-steroid + acceptor = a 3-oxo-
CC       Delta(4)-steroid + reduced acceptor.
CC   -!- PATHWAY: Protein modification; protein glycosylation.
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Multi-pass
CC       membrane protein (By similarity).
CC   -!- SIMILARITY: Belongs to the steroid 5-alpha reductase family.
CC       Polyprenol reductase subfamily.
CC   -!- GENE_FAMILY: HOG000018885 [ FAMILY / ALN / TREE ]
DR   HOGENOM:Ailuropoda_melanoleuca;ENSAMEG00000018417;ENSAMET00000020235;ENSAMEP00000019466.
DR   EMBL; GL192668; - ;
DR   UniProtKB/Swiss-Prot; D2HBV9; -.
DR   EMBL; GL192668; EFB15787.1; -; Genomic_DNA.
DR   RefSeq; XP_002919412.1; XM_002919366.1.
DR   Ensembl; ENSAMET00000020235; ENSAMEP00000019466; ENSAMEG00000018417.
DR   GeneID; 100463734; -.
DR   KEGG; aml:100463734; -.
DR   CTD; 79644; -.
DR   GeneTree; ENSGT00500000044920; -.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR   GO; GO:0003865; F:3-oxo-5-alpha-steroid 4-dehydrogenase activity; ISS:UniProtKB.
DR   GO; GO:0016628; F:oxidoreductase activity, acting on the CH-CH group of donors, NAD or NADP as acceptor; ISS:UniProDR   GO; GO:0019348; P:dolichol metabolic process; ISS:UniProtKB.
DR   GO; GO:0019348; P:dolichol metabolic process; ISS:UniProtKB.
DR   GO; GO:0006488; P:dolichol-linked oligosaccharide biosynthetic process; ISS:UniProtKB.
DR   GO; GO:0016095; P:polyprenol catabolic process; ISS:UniProtKB.
DR   InterPro; IPR001104; 3-oxo-5_a-steroid_4-DH_C.
DR   Pfam; PF02544; Steroid_dh; 1.
DR   PROSITE; PS50244; S5A_REDUCTASE; 1.
DR   HOGENOMDNA; AILMEGL192668_1_2.PE2; -.
KW   ENSAMEG00000018417; ENSAMEP00000019466; D2HBV9_AILME; GL192668;
KW   Endoplasmic reticulum; Membrane; NADP; Oxidoreductase; Transmembrane;
KW   Transmembrane helix.
SQ   SEQUENCE   330 AA;  UNKNOWN MW;  UNKNOWN CRC64;
     MAPWAAAQLW ALNPLRALWL TLAAAFLLTL LLQLVPPGLL PGCALFQDLI RYGKTKREGQ
     SRPAVCRVFD VPKRYFSHFY IISALWNGFL LWHLTQSVFL GVPFPNWLHG LLRILGASQF
     QGNKIDSKEF LTRRGELALS AFLVLVFLWL HSLRRLFECF YVSVFSNTVI HIVQYCFGLV
     YYVLTGLTVL SQVPMDGRNA YVIGKNLLMQ ARWFHILGML MFIWSSVHQY KCHVILGNLR
     KNKAGVVIHC NHRIPFGDWF EYVSSPNYLA ELMIYISMAV TFGFHNLTWW LVVTYVFFSQ
     ALSAFLSHKF YKSKFVSYPK HRKAFLPFLF
//

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