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Database: UniProt
Entry: A0A3L6SFQ4_PANMI
LinkDB: A0A3L6SFQ4_PANMI
Original site: A0A3L6SFQ4_PANMI 
ID   A0A3L6SFQ4_PANMI        Unreviewed;       391 AA.
AC   A0A3L6SFQ4;
DT   13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT   13-FEB-2019, sequence version 1.
DT   27-MAR-2024, entry version 16.
DE   RecName: Full=11-beta-hydroxysteroid dehydrogenase 1B-like {ECO:0008006|Google:ProtNLM};
GN   ORFNames=C2845_PM02G08420 {ECO:0000313|EMBL:RLN19818.1};
OS   Panicum miliaceum (Proso millet) (Broomcorn millet).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; PACMAD clade;
OC   Panicoideae; Panicodae; Paniceae; Panicinae; Panicum.
OX   NCBI_TaxID=4540 {ECO:0000313|EMBL:RLN19818.1, ECO:0000313|Proteomes:UP000275267};
RN   [1] {ECO:0000313|Proteomes:UP000275267}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=30683860; DOI=10.1038/s41467-019-08409-5;
RA   Zou C., Miki D., Li D., Tang Q., Xiao L., Rajput S., Deng P., Jia W.,
RA   Huang R., Zhang M., Sun Y., Hu J., Fu X., Schnable P.S., Li F., Zhang H.,
RA   Feng B., Zhu X., Liu R., Schnable J.C., Zhu J.-K., Zhang H.;
RT   "The genome of broomcorn millet.";
RL   Nat. Commun. 10:436-436(2019).
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004606}; Single-
CC       pass type II membrane protein {ECO:0000256|ARBA:ARBA00004606}.
CC   -!- SIMILARITY: Belongs to the short-chain dehydrogenases/reductases (SDR)
CC       family. {ECO:0000256|ARBA:ARBA00006484}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:RLN19818.1}.
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DR   EMBL; PQIB02000005; RLN19818.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A3L6SFQ4; -.
DR   STRING; 4540.A0A3L6SFQ4; -.
DR   Proteomes; UP000275267; Chromosome 2.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR   Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   InterPro; IPR002347; SDR_fam.
DR   PANTHER; PTHR43391:SF76; 11-BETA-HYDROXYSTEROID DEHYDROGENASE-LIKE 6; 1.
DR   PANTHER; PTHR43391; RETINOL DEHYDROGENASE-RELATED; 1.
DR   Pfam; PF00106; adh_short; 1.
DR   PRINTS; PR00081; GDHRDH.
DR   SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
PE   3: Inferred from homology;
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW   Reference proteome {ECO:0000313|Proteomes:UP000275267};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        46..67
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   REGION          1..36
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..20
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   391 AA;  42373 MW;  ADB7A54B651F6983 CRC64;
     MKENEGGQGQ TSNAGRSGDS QYNCRRRPVA SIGRRRSQAG TRAMELYLLL HSVVMHAIAA
     LVILVYIPVC VPARLLARAL VRPRRKEDLR GKVVLITGAS SGIGEELAYQ YAREGAYLAL
     VARRKQALKS VAAAALERGA PDVLVLPADV ADPEQSRRAV EETVAHFGKL NHLVANAGIW
     SSCSFDQVTN IAAFTKLMDV NFWGSVYPTY YALPHLKASR GKLVVSCSAA GTVATSRMAF
     YNASKAAQLR FYETLRTELG SEVGITILTA GYVESEITKG KGVQKGGEVA VDEDARDAQI
     GVFPVGRVET LCEVALDAVR SGDWYVTWPS MYRPMQLVAC LAPEVLSWVS YALYKEEAAK
     GSRPLGQRIL EATGAKTLFP PSLLHPVVKT D
//
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