ID S5A1_BOVIN Reviewed; 257 AA. AC A5PJS2; DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot. DT 10-JUL-2007, sequence version 1. DT 27-MAR-2024, entry version 96. DE RecName: Full=3-oxo-5-alpha-steroid 4-dehydrogenase 1; DE EC=1.3.1.22 {ECO:0000250|UniProtKB:P18405}; DE AltName: Full=SR type 1; DE AltName: Full=Steroid 5-alpha-reductase 1; DE Short=S5AR 1; GN Name=SRD5A1; OS Bos taurus (Bovine). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae; OC Bovinae; Bos. OX NCBI_TaxID=9913; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=Hereford; TISSUE=Fetal skin; RG NIH - Mammalian Gene Collection (MGC) project; RL Submitted (JUN-2007) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Converts testosterone into 5-alpha-dihydrotestosterone and CC progesterone or corticosterone into their corresponding 5-alpha-3- CC oxosteroids. It plays a central role in sexual differentiation and CC androgen physiology. {ECO:0000250|UniProtKB:P24008}. CC -!- CATALYTIC ACTIVITY: CC Reaction=a 3-oxo-5alpha-steroid + NADP(+) = a 3-oxo-Delta(4)-steroid + CC H(+) + NADPH; Xref=Rhea:RHEA:54384, ChEBI:CHEBI:13601, CC ChEBI:CHEBI:15378, ChEBI:CHEBI:47909, ChEBI:CHEBI:57783, CC ChEBI:CHEBI:58349; EC=1.3.1.22; CC Evidence={ECO:0000250|UniProtKB:P24008}; CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:54386; CC Evidence={ECO:0000250|UniProtKB:P24008}; CC -!- CATALYTIC ACTIVITY: CC Reaction=5alpha-pregnane-3,20-dione + NADP(+) = H(+) + NADPH + CC progesterone; Xref=Rhea:RHEA:21952, ChEBI:CHEBI:15378, CC ChEBI:CHEBI:17026, ChEBI:CHEBI:28952, ChEBI:CHEBI:57783, CC ChEBI:CHEBI:58349; EC=1.3.1.22; CC Evidence={ECO:0000250|UniProtKB:P24008}; CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:21954; CC Evidence={ECO:0000250|UniProtKB:P24008}; CC -!- CATALYTIC ACTIVITY: CC Reaction=17beta-hydroxy-5alpha-androstan-3-one + NADP(+) = H(+) + NADPH CC + testosterone; Xref=Rhea:RHEA:50820, ChEBI:CHEBI:15378, CC ChEBI:CHEBI:16330, ChEBI:CHEBI:17347, ChEBI:CHEBI:57783, CC ChEBI:CHEBI:58349; EC=1.3.1.22; CC Evidence={ECO:0000250|UniProtKB:P24008}; CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:50822; CC Evidence={ECO:0000250|UniProtKB:P24008}; CC -!- CATALYTIC ACTIVITY: CC Reaction=androst-4-ene-3,17-dione + H(+) + NADPH = 5alpha- CC androstan-3,17-dione + NADP(+); Xref=Rhea:RHEA:50816, CC ChEBI:CHEBI:15378, ChEBI:CHEBI:15994, ChEBI:CHEBI:16422, CC ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; CC Evidence={ECO:0000250|UniProtKB:P24008}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:50817; CC Evidence={ECO:0000250|UniProtKB:P24008}; CC -!- SUBCELLULAR LOCATION: Microsome membrane {ECO:0000250}; Multi-pass CC membrane protein {ECO:0000250}. Endoplasmic reticulum membrane CC {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. CC -!- SIMILARITY: Belongs to the steroid 5-alpha reductase family. CC {ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; BC142219; AAI42220.1; -; mRNA. DR RefSeq; NP_001092607.1; NM_001099137.1. DR RefSeq; XP_015314613.1; XM_015459127.1. DR AlphaFoldDB; A5PJS2; -. DR SMR; A5PJS2; -. DR STRING; 9913.ENSBTAP00000020570; -. DR PaxDb; 9913-ENSBTAP00000020570; -. DR Ensembl; ENSBTAT00000020570.5; ENSBTAP00000020570.4; ENSBTAG00000015478.5. DR GeneID; 614612; -. DR KEGG; bta:614612; -. DR CTD; 6715; -. DR VEuPathDB; HostDB:ENSBTAG00000015478; -. DR VGNC; VGNC:35271; SRD5A1. DR eggNOG; KOG1638; Eukaryota. DR GeneTree; ENSGT00950000182886; -. DR HOGENOM; CLU_065395_1_1_1; -. DR InParanoid; A5PJS2; -. DR OMA; PHYALEW; -. DR OrthoDB; 152402at2759; -. DR TreeFam; TF314668; -. DR Reactome; R-BTA-193048; Androgen biosynthesis. DR Proteomes; UP000009136; Chromosome 20. DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell. DR GO; GO:0003865; F:3-oxo-5-alpha-steroid 4-dehydrogenase activity; ISS:UniProtKB. DR GO; GO:0047751; F:3-oxo-5alpha-steroid 4-dehydrogenase (NADP+); IEA:UniProtKB-EC. DR GO; GO:0006702; P:androgen biosynthetic process; IEA:UniProt. DR GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW. DR GO; GO:0007548; P:sex differentiation; IEA:UniProtKB-KW. DR GO; GO:0006694; P:steroid biosynthetic process; IBA:GO_Central. DR Gene3D; 1.20.120.1630; -; 1. DR InterPro; IPR016636; 3-oxo-5-alpha-steroid_4-DH. DR InterPro; IPR001104; 3-oxo-5_a-steroid_4-DH_C. DR InterPro; IPR039357; SRD5A/TECR. DR PANTHER; PTHR10556; 3-OXO-5-ALPHA-STEROID 4-DEHYDROGENASE; 1. DR PANTHER; PTHR10556:SF57; 3-OXO-5-ALPHA-STEROID 4-DEHYDROGENASE 1; 1. DR Pfam; PF02544; Steroid_dh; 1. DR PIRSF; PIRSF015596; 5_alpha-SR2; 1. DR PROSITE; PS50244; S5A_REDUCTASE; 1. PE 2: Evidence at transcript level; KW Differentiation; Endoplasmic reticulum; Lipid metabolism; Membrane; KW Microsome; NADP; Oxidoreductase; Reference proteome; KW Sexual differentiation; Transmembrane; Transmembrane helix. FT CHAIN 1..257 FT /note="3-oxo-5-alpha-steroid 4-dehydrogenase 1" FT /id="PRO_0000317710" FT TRANSMEM 7..27 FT /note="Helical" FT /evidence="ECO:0000255" FT TRANSMEM 50..70 FT /note="Helical" FT /evidence="ECO:0000255" FT TRANSMEM 84..104 FT /note="Helical" FT /evidence="ECO:0000255" FT TRANSMEM 109..129 FT /note="Helical" FT /evidence="ECO:0000255" FT TRANSMEM 149..169 FT /note="Helical" FT /evidence="ECO:0000255" FT TRANSMEM 208..228 FT /note="Helical" FT /evidence="ECO:0000255" SQ SEQUENCE 257 AA; 29186 MW; 2A49937DFB45FFB0 CRC64; MELAERFLLD ALAYLECALG VVCYVLLKLV GSPYGRYASS GSAFGLPARA AWTVQELPSL ALPLLACAGA GAPAERLNRW PNCILLAMFL VHYAQRSLVF PFLIRGGKPM PLYAFLLAFI FCTYNGYLQS RYLSQYAVYA DDWLSDPRFL TGSALWLIGM LINIHSDHVL RNLRKPGETG YKIPRGGLFE YISAANYFGE VVEWCGYALA SWSIQGWAFA VFTFCVLFTR AQQHHKWYHE KFEDYPKFRK IMIPFLV //