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Database: UniProt
Entry: D7MWR7_ARALL
LinkDB: D7MWR7_ARALL
Original site: D7MWR7_ARALL 
ID   D7MWR7_ARALL            Unreviewed;       123 AA.
AC   D7MWR7;
DT   10-AUG-2010, integrated into UniProtKB/TrEMBL.
DT   10-AUG-2010, sequence version 1.
DT   22-FEB-2023, entry version 38.
DE   RecName: Full=Steroid 5-alpha reductase C-terminal domain-containing protein {ECO:0000259|PROSITE:PS50244};
GN   ORFNames=ARALYDRAFT_359400 {ECO:0000313|EMBL:EFH39012.1};
OS   Arabidopsis lyrata subsp. lyrata (Lyre-leaved rock-cress).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX   NCBI_TaxID=81972 {ECO:0000313|Proteomes:UP000008694};
RN   [1] {ECO:0000313|Proteomes:UP000008694}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. MN47 {ECO:0000313|Proteomes:UP000008694};
RX   PubMed=21478890; DOI=10.1038/ng.807;
RA   Hu T.T., Pattyn P., Bakker E.G., Cao J., Cheng J.-F., Clark R.M.,
RA   Fahlgren N., Fawcett J.A., Grimwood J., Gundlach H., Haberer G.,
RA   Hollister J.D., Ossowski S., Ottilar R.P., Salamov A.A., Schneeberger K.,
RA   Spannagl M., Wang X., Yang L., Nasrallah M.E., Bergelson J.,
RA   Carrington J.C., Gaut B.S., Schmutz J., Mayer K.F.X., Van de Peer Y.,
RA   Grigoriev I.V., Nordborg M., Weigel D., Guo Y.-L.;
RT   "The Arabidopsis lyrata genome sequence and the basis of rapid genome size
RT   change.";
RL   Nat. Genet. 43:476-481(2011).
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC       pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
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DR   EMBL; GL348844; EFH39012.1; -; Genomic_DNA.
DR   RefSeq; XP_002862754.1; XM_002862708.1.
DR   AlphaFoldDB; D7MWR7; -.
DR   STRING; 81972.D7MWR7; -.
DR   EnsemblPlants; fgenesh1_pg.C_scaffold_181000001; fgenesh1_pg.C_scaffold_181000001; fgenesh1_pg.C_scaffold_181000001.
DR   GeneID; 9298834; -.
DR   Gramene; fgenesh1_pg.C_scaffold_181000001; fgenesh1_pg.C_scaffold_181000001; fgenesh1_pg.C_scaffold_181000001.
DR   KEGG; aly:9298834; -.
DR   eggNOG; KOG4650; Eukaryota.
DR   HOGENOM; CLU_043418_4_0_1; -.
DR   OrthoDB; 38588at2759; -.
DR   Proteomes; UP000008694; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0016627; F:oxidoreductase activity, acting on the CH-CH group of donors; IEA:InterPro.
DR   GO; GO:0006629; P:lipid metabolic process; IEA:InterPro.
DR   Gene3D; 1.20.120.1630; -; 1.
DR   InterPro; IPR001104; 3-oxo-5_a-steroid_4-DH_C.
DR   InterPro; IPR010721; UstE-like.
DR   PANTHER; PTHR32251; 3-OXO-5-ALPHA-STEROID 4-DEHYDROGENASE; 1.
DR   PANTHER; PTHR32251:SF23; 3-OXO-5-ALPHA-STEROID 4-DEHYDROGENASE (DUF1295); 1.
DR   Pfam; PF06966; DUF1295; 1.
DR   PROSITE; PS50244; S5A_REDUCTASE; 1.
PE   4: Predicted;
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW   Reference proteome {ECO:0000313|Proteomes:UP000008694};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        48..81
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          1..60
FT                   /note="Steroid 5-alpha reductase C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS50244"
SQ   SEQUENCE   123 AA;  14490 MW;  D33CF7015F0BFDBD CRC64;
     MAYYADTQLH EFVTGNQKLK EQGKPKIPNL DTGLWHYSRH PNYLGEQLWW WGLVIFAWNL
     GQGWTLIGAL VNTLCLVYVT ILVERRMVKQ QYRAEAYRAY QKTTSVWIPW FKSHVAATKD
     KNT
//
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