ID S5A2_PIG Reviewed; 254 AA. AC O18765; DT 16-APR-2002, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-2001, sequence version 2. DT 27-MAR-2024, entry version 129. DE RecName: Full=3-oxo-5-alpha-steroid 4-dehydrogenase 2; DE EC=1.3.1.22 {ECO:0000250|UniProtKB:P31213}; DE AltName: Full=5 alpha-SR2; DE AltName: Full=SR type 2; DE AltName: Full=Steroid 5-alpha-reductase 2; DE Short=S5AR 2; GN Name=SRD5A2; Synonyms=ST5AR2; OS Sus scrofa (Pig). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus. OX NCBI_TaxID=9823; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RC TISSUE=Epididymis; RA Lacroix D.A., Men T., Houde A., Murphy B.D.; RL Submitted (AUG-2000) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Converts testosterone (T) into 5-alpha-dihydrotestosterone CC (DHT) and progesterone or corticosterone into their corresponding 5- CC alpha-3-oxosteroids. It plays a central role in sexual differentiation CC and androgen physiology (By similarity). CC {ECO:0000250|UniProtKB:P31213}. 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:P31213}; 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:P31213}; CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:50822; CC Evidence={ECO:0000250|UniProtKB:P31213}; 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:P31213}; CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:21954; CC Evidence={ECO:0000250|UniProtKB:P31213}; 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; AF008440; AAB69279.2; -; mRNA. DR RefSeq; NP_999153.1; NM_213988.1. DR AlphaFoldDB; O18765; -. DR SMR; O18765; -. DR STRING; 9823.ENSSSCP00000009087; -. DR PaxDb; 9823-ENSSSCP00000009087; -. DR PeptideAtlas; O18765; -. DR Ensembl; ENSSSCT00000009325.5; ENSSSCP00000009087.5; ENSSSCG00000008521.5. DR Ensembl; ENSSSCT00030046625.1; ENSSSCP00030021001.1; ENSSSCG00030033689.1. DR Ensembl; ENSSSCT00040065105.1; ENSSSCP00040027543.1; ENSSSCG00040048320.1. DR Ensembl; ENSSSCT00045015342.1; ENSSSCP00045010660.1; ENSSSCG00045009063.1. DR Ensembl; ENSSSCT00055036688.1; ENSSSCP00055029157.1; ENSSSCG00055018745.1. DR Ensembl; ENSSSCT00060032689.1; ENSSSCP00060014019.1; ENSSSCG00060024102.1. DR GeneID; 397048; -. DR KEGG; ssc:397048; -. DR CTD; 6716; -. DR VGNC; VGNC:93449; SRD5A2. DR eggNOG; KOG1638; Eukaryota. DR GeneTree; ENSGT00950000182886; -. DR HOGENOM; CLU_065395_3_0_1; -. DR InParanoid; O18765; -. DR OMA; SYGKHTE; -. DR OrthoDB; 152402at2759; -. DR Reactome; R-SSC-193048; Androgen biosynthesis. DR Proteomes; UP000008227; Chromosome 3. DR Proteomes; UP000314985; Unplaced. DR Proteomes; UP000694570; Unplaced. DR Proteomes; UP000694571; Unplaced. DR Proteomes; UP000694720; Unplaced. DR Proteomes; UP000694722; Unplaced. DR Proteomes; UP000694723; Unplaced. DR Proteomes; UP000694724; Unplaced. DR Proteomes; UP000694725; Unplaced. DR Proteomes; UP000694726; Unplaced. DR Proteomes; UP000694727; Unplaced. DR Proteomes; UP000694728; Unplaced. DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell. DR GO; GO:0003865; F:3-oxo-5-alpha-steroid 4-dehydrogenase activity; IBA:GO_Central. DR GO; GO:0047751; F:3-oxo-5alpha-steroid 4-dehydrogenase (NADP+); IEA:UniProtKB-EC. DR GO; GO:0009917; F:sterol 5-alpha reductase activity; IEA:Ensembl. DR GO; GO:0030283; F:testosterone dehydrogenase [NAD(P)] activity; ISS:UniProtKB. DR GO; GO:0006702; P:androgen biosynthetic process; IEA:Ensembl. DR GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW. DR GO; GO:0030539; P:male genitalia development; IEA:Ensembl. DR GO; GO:0008584; P:male gonad development; IEA:Ensembl. DR GO; GO:0006694; P:steroid biosynthetic process; IBA:GO_Central. DR GO; GO:0061370; P:testosterone biosynthetic process; ISS:UniProtKB. 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:SF43; 3-OXO-5-ALPHA-STEROID 4-DEHYDROGENASE 2; 1. DR Pfam; PF02544; Steroid_dh; 1. DR PIRSF; PIRSF015596; 5_alpha-SR2; 1. DR PROSITE; PS50244; S5A_REDUCTASE; 1. DR Genevisible; O18765; SS. 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..254 FT /note="3-oxo-5-alpha-steroid 4-dehydrogenase 2" FT /id="PRO_0000213679" FT TRANSMEM 8..28 FT /note="Helical" FT /evidence="ECO:0000255" FT TRANSMEM 72..92 FT /note="Helical" FT /evidence="ECO:0000255" FT TRANSMEM 146..166 FT /note="Helical" FT /evidence="ECO:0000255" FT TRANSMEM 206..226 FT /note="Helical" FT /evidence="ECO:0000255" SQ SEQUENCE 254 AA; 28536 MW; F647B3D46AB98A29 CRC64; MPVRCQQSPV LAGSATLAAL GALALYFAEP SGYGKYTESL TPAAIRLPAR AAWFLQELPS FVVPAGILAG QPRSLFGPPA TVLLGLFCAH YFHRTFVYSL LTRGRPFPVV FLFRGFVFCM GNGLLQGYYL VYCAEYPAEW YTDIRFSLGV FLFILGMGIN IHSDYILRQL RKPGEVIYKI PQGGLFTYVS GANFLGEIIE WIGYALATWS LPALAFAFFS LCFLGLRAFH HHRFYVKMFE DYPKSRKALI PFIF //