ID A0A3B1J5Y1_ASTMX Unreviewed; 405 AA.
AC A0A3B1J5Y1;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 24-JAN-2024, entry version 19.
DE SubName: Full=C-terminal-binding protein 2-like {ECO:0000313|Ensembl:ENSAMXP00000036744.1};
OS Astyanax mexicanus (Blind cave fish) (Astyanax fasciatus mexicanus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Characiformes;
OC Characoidei; Characidae; Astyanax.
OX NCBI_TaxID=7994 {ECO:0000313|Ensembl:ENSAMXP00000036744.1, ECO:0000313|Proteomes:UP000018467};
RN [1] {ECO:0000313|Proteomes:UP000018467}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=female {ECO:0000313|Proteomes:UP000018467};
RA Jeffery W., Warren W., Wilson R.K.;
RL Submitted (MAR-2013) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Proteomes:UP000018467}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=female {ECO:0000313|Proteomes:UP000018467};
RX PubMed=25329095; DOI=10.1038/ncomms6307;
RA McGaugh S.E., Gross J.B., Aken B., Blin M., Borowsky R., Chalopin D.,
RA Hinaux H., Jeffery W.R., Keene A., Ma L., Minx P., Murphy D., O'Quin K.E.,
RA Retaux S., Rohner N., Searle S.M., Stahl B.A., Tabin C., Volff J.N.,
RA Yoshizawa M., Warren W.C.;
RT "The cavefish genome reveals candidate genes for eye loss.";
RL Nat. Commun. 5:5307-5307(2014).
RN [3] {ECO:0000313|Ensembl:ENSAMXP00000036744.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (JUL-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_007251995.1; XM_007251933.2.
DR AlphaFoldDB; A0A3B1J5Y1; -.
DR Ensembl; ENSAMXT00000037920.1; ENSAMXP00000036744.1; ENSAMXG00000000443.2.
DR GeneID; 103037620; -.
DR CTD; 65230; -.
DR GeneTree; ENSGT00940000171352; -.
DR OrthoDB; 4204864at2759; -.
DR Proteomes; UP000018467; Unassembled WGS sequence.
DR Bgee; ENSAMXG00000000443; Expressed in brain and 14 other cell types or tissues.
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:SF3; C-TERMINAL-BINDING PROTEIN 2; 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|RuleBase:RU003719};
KW Reference proteome {ECO:0000313|Proteomes:UP000018467}.
FT DOMAIN 44..358
FT /note="D-isomer specific 2-hydroxyacid dehydrogenase
FT catalytic"
FT /evidence="ECO:0000259|Pfam:PF00389"
FT DOMAIN 140..323
FT /note="D-isomer specific 2-hydroxyacid dehydrogenase NAD-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02826"
SQ SEQUENCE 405 AA; 45009 MW; CB4F70963F3D2392 CRC64;
MALIDKHKVK RQRIDRICEG IRPQIMNGPM HPRPLVALLD GRDCTVEMPI LKDLATVAFC
DAQSTQEIHE KVLNEAVGAM MYHTITLTRE DLEKFKALRI IIRIGSGYDN IDIKAAGEMG
IAVCNIPSAA VEETADSTLC HVLNLYRRNT WLYQALREGS RVQSVEQIRE LASGAARIRG
ETLGLIGFGR SGQAVAVRAK AFGFNVIFYD PYLQDGLERS LGVQRVYTLQ DLLYQSDCVS
LHCNLNEHNH HLINDFTIKQ MRQGAFLVNC ARGGLVDEKA LAQALKEGRI RGAALDVHES
EPFSFTQGPL KDAPNLICTP HTAWYSEQAS LEMREAAATE IRRAITGRIP DSLRNCVNKE
FFVPSAPWGV VEQQQVHAEL NGGAYRVAQP LPAISPGGMQ DKMYT
//