GenomeNet

Database: UniProt
Entry: H3AV07_LATCH
LinkDB: H3AV07_LATCH
Original site: H3AV07_LATCH 
ID   H3AV07_LATCH            Unreviewed;       363 AA.
AC   H3AV07;
DT   18-APR-2012, integrated into UniProtKB/TrEMBL.
DT   18-APR-2012, sequence version 1.
DT   27-MAR-2024, entry version 48.
DE   SubName: Full=C-terminal binding protein 2 {ECO:0000313|Ensembl:ENSLACP00000013478.1};
GN   Name=CTBP2 {ECO:0000313|Ensembl:ENSLACP00000013478.1};
OS   Latimeria chalumnae (Coelacanth).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Coelacanthiformes; Coelacanthidae; Latimeria.
OX   NCBI_TaxID=7897 {ECO:0000313|Ensembl:ENSLACP00000013478.1, ECO:0000313|Proteomes:UP000008672};
RN   [1] {ECO:0000313|Proteomes:UP000008672}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Wild caught {ECO:0000313|Proteomes:UP000008672};
RA   Di Palma F., Alfoldi J., Johnson J., Berlin A., Gnerre S., Jaffe D.,
RA   MacCallum I., Young S., Walker B.J., Lander E., Lindblad-Toh K.;
RT   "The draft genome of Latimeria chalumnae.";
RL   Submitted (AUG-2011) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Ensembl:ENSLACP00000013478.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (NOV-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   EMBL; AFYH01057521; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AFYH01057522; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AFYH01057523; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AFYH01057524; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AFYH01057525; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AFYH01057526; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AFYH01057527; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AFYH01057528; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AFYH01057529; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AFYH01057530; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   AlphaFoldDB; H3AV07; -.
DR   Ensembl; ENSLACT00000013574.1; ENSLACP00000013478.1; ENSLACG00000011865.2.
DR   GeneTree; ENSGT00940000154430; -.
DR   HOGENOM; CLU_019796_1_3_1; -.
DR   Proteomes; UP000008672; Unassembled WGS sequence.
DR   Bgee; ENSLACG00000011865; Expressed in pectoral fin and 5 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|ARBA:ARBA00023002,
KW   ECO:0000256|RuleBase:RU003719};
KW   Reference proteome {ECO:0000313|Proteomes:UP000008672}.
FT   DOMAIN          19..333
FT                   /note="D-isomer specific 2-hydroxyacid dehydrogenase
FT                   catalytic"
FT                   /evidence="ECO:0000259|Pfam:PF00389"
FT   DOMAIN          116..298
FT                   /note="D-isomer specific 2-hydroxyacid dehydrogenase NAD-
FT                   binding"
FT                   /evidence="ECO:0000259|Pfam:PF02826"
SQ   SEQUENCE   363 AA;  40277 MW;  D1FE4B62592F5340 CRC64;
     MNGPMHPRPL VALLDGRDCT VEMPILKDLA TVAFCDAQST QEIHEKVLNE AVGAMMYHTI
     TLTREDLEKF KALRVIVRIG SGYDNIDIKA AGDLGIAVCN IPSAAVEETA DSTTCHILNL
     YRRNTWLYQA LREGTRVPSV EQIREVASGA ARIRGETLGL IGFGRTGQAV AVRAKAFGFN
     VIFYDPYLQD GIERSLGVQR VYTLQDLLYQ SDCVSLHCNL NEHNHHLIND FTIKQMRQGA
     FLVNTARGGL VDEKALAQAL KEGRIRGAAL DVHESEPFSF TQGPLKEAPN LICTPHAAWY
     SEQASLEMRE AAATEIRRAI TGRIPDSLRN CVNKEFFVTT ATWSVMDQQT VHPELNGATY
     RMC
//
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