ID A0A3B3VQ51_9TELE Unreviewed; 442 AA.
AC A0A3B3VQ51;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE SubName: Full=C-terminal binding protein 1 {ECO:0000313|Ensembl:ENSPLAP00000027012.1};
OS Poecilia latipinna (sailfin molly).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Atherinomorphae; Cyprinodontiformes; Poeciliidae; Poeciliinae;
OC Poecilia.
OX NCBI_TaxID=48699 {ECO:0000313|Ensembl:ENSPLAP00000027012.1, ECO:0000313|Proteomes:UP000261500};
RN [1] {ECO:0000313|Ensembl:ENSPLAP00000027012.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
CC -!- SIMILARITY: Belongs to the D-isomer specific 2-hydroxyacid
CC dehydrogenase family. {ECO:0000256|RuleBase:RU003719}.
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DR RefSeq; XP_014902561.1; XM_015047075.1.
DR AlphaFoldDB; A0A3B3VQ51; -.
DR STRING; 48699.ENSPLAP00000027012; -.
DR Ensembl; ENSPLAT00000019624.1; ENSPLAP00000027012.1; ENSPLAG00000015265.1.
DR GeneID; 106956309; -.
DR KEGG; plai:106956309; -.
DR CTD; 1487; -.
DR GeneTree; ENSGT00940000157061; -.
DR OrthoDB; 4204864at2759; -.
DR Proteomes; UP000261500; Unplaced.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0051287; F:NAD binding; IEA:InterPro.
DR GO; GO:0016616; F:oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor; IEA:InterPro.
DR GO; GO:0003714; F:transcription corepressor activity; IEA:InterPro.
DR CDD; cd05299; CtBP_dh; 1.
DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 2.
DR InterPro; IPR043322; CtBP.
DR InterPro; IPR006139; D-isomer_2_OHA_DH_cat_dom.
DR InterPro; IPR029753; D-isomer_DH_CS.
DR InterPro; IPR006140; D-isomer_DH_NAD-bd.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR PANTHER; PTHR46029; C-TERMINAL-BINDING PROTEIN; 1.
DR PANTHER; PTHR46029:SF2; C-TERMINAL-BINDING PROTEIN 1; 1.
DR Pfam; PF00389; 2-Hacid_dh; 1.
DR Pfam; PF02826; 2-Hacid_dh_C; 1.
DR SUPFAM; SSF52283; Formate/glycerate dehydrogenase catalytic domain-like; 1.
DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
DR PROSITE; PS00671; D_2_HYDROXYACID_DH_3; 1.
PE 3: Inferred from homology;
KW Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000256|RuleBase:RU003719}.
FT DOMAIN 38..351
FT /note="D-isomer specific 2-hydroxyacid dehydrogenase
FT catalytic"
FT /evidence="ECO:0000259|Pfam:PF00389"
FT DOMAIN 134..317
FT /note="D-isomer specific 2-hydroxyacid dehydrogenase NAD-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02826"
FT REGION 407..442
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 410..424
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 442 AA; 48106 MW; F38C6FEEA5DE3E7D CRC64;
MGSSHLLNKG MPLGIRPPIM NGPMHPRPLV ALLDGRDCTV EMPILKDVAT VAFCDAQSTQ
EIHEKVLNEA VGALMYHTIT LMREDLEKFK ALRIIVRIGS GYDNIDIKSA GELGIAVCNM
PAASVEETAD STLCHILTLY RRTTWLHQAL REGTRVQSVE QIREVASGAA RIRGETLGLI
GLGRVGQAVA LRAKAFGFNV IFYDPYLADG VERSLGLQRV TTLQDLLFHS DCVSLHCSLN
EHNHHLINDF TIKQMRQGAF LVNTARGGLV DEKALAQALK EGRIRGAALD VHEAEPFSFS
QGPLKDAPNL ICTPHAAWYS EQASLEMREE AAREIRRAVT GRIPDSLKNC VNKEFLSPNN
HWAVDPAAVH PELNGAYRYP PGVVSLPAGG LPPPVEGIVP SAVPITHTLP PAAAHPPHAP
SPGQNTVKPP EGDREQHPND QL
//
