ID   GPD1L_PONAB             Reviewed;         351 AA.
AC   Q5R5V3;
DT   15-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT   21-DEC-2004, sequence version 1.
DT   24-JAN-2024, entry version 90.
DE   RecName: Full=Glycerol-3-phosphate dehydrogenase 1-like protein;
DE            EC=1.1.1.8 {ECO:0000250|UniProtKB:Q8N335};
GN   Name=GPD1L;
OS   Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Pongo.
OX   NCBI_TaxID=9601;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Brain cortex;
RG   The German cDNA consortium;
RL   Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Plays a role in regulating cardiac sodium current; decreased
CC       enzymatic activity with resulting increased levels of glycerol 3-
CC       phosphate activating the DPD1L-dependent SCN5A phosphorylation pathway,
CC       may ultimately lead to decreased sodium current; cardiac sodium current
CC       may also be reduced due to alterations of NAD(H) balance induced by
CC       DPD1L. {ECO:0000250|UniProtKB:Q8N335}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=NAD(+) + sn-glycerol 3-phosphate = dihydroxyacetone phosphate
CC         + H(+) + NADH; Xref=Rhea:RHEA:11092, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:57540, ChEBI:CHEBI:57597, ChEBI:CHEBI:57642,
CC         ChEBI:CHEBI:57945; EC=1.1.1.8;
CC         Evidence={ECO:0000250|UniProtKB:Q8N335};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:11093;
CC         Evidence={ECO:0000250|UniProtKB:Q8N335};
CC   -!- SUBUNIT: Interacts with SCN5A. {ECO:0000250|UniProtKB:Q8N335}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the NAD-dependent glycerol-3-phosphate
CC       dehydrogenase family. {ECO:0000305}.
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DR   EMBL; CR860749; CAH92863.1; -; mRNA.
DR   RefSeq; NP_001126675.1; NM_001133203.1.
DR   AlphaFoldDB; Q5R5V3; -.
DR   SMR; Q5R5V3; -.
DR   STRING; 9601.ENSPPYP00000015713; -.
DR   GeneID; 100173675; -.
DR   KEGG; pon:100173675; -.
DR   CTD; 23171; -.
DR   InParanoid; Q5R5V3; -.
DR   OrthoDB; 3675564at2759; -.
DR   Proteomes; UP000001595; Unplaced.
DR   GO; GO:0009331; C:glycerol-3-phosphate dehydrogenase complex; IEA:InterPro.
DR   GO; GO:0047952; F:glycerol-3-phosphate dehydrogenase [NAD(P)+] activity; IEA:UniProtKB-EC.
DR   GO; GO:0051287; F:NAD binding; IEA:InterPro.
DR   GO; GO:0042803; F:protein homodimerization activity; IEA:InterPro.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR   GO; GO:0046168; P:glycerol-3-phosphate catabolic process; IEA:InterPro.
DR   Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR   InterPro; IPR008927; 6-PGluconate_DH-like_C_sf.
DR   InterPro; IPR013328; 6PGD_dom2.
DR   InterPro; IPR006168; G3P_DH_NAD-dep.
DR   InterPro; IPR006109; G3P_DH_NAD-dep_C.
DR   InterPro; IPR017751; G3P_DH_NAD-dep_euk.
DR   InterPro; IPR011128; G3P_DH_NAD-dep_N.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   NCBIfam; TIGR03376; glycerol3P_DH; 1.
DR   PANTHER; PTHR11728; GLYCEROL-3-PHOSPHATE DEHYDROGENASE; 1.
DR   PANTHER; PTHR11728:SF7; GLYCEROL-3-PHOSPHATE DEHYDROGENASE 1-LIKE PROTEIN; 1.
DR   Pfam; PF07479; NAD_Gly3P_dh_C; 1.
DR   Pfam; PF01210; NAD_Gly3P_dh_N; 1.
DR   PIRSF; PIRSF000114; Glycerol-3-P_dh; 1.
DR   PRINTS; PR00077; GPDHDRGNASE.
DR   SUPFAM; SSF48179; 6-phosphogluconate dehydrogenase C-terminal domain-like; 1.
DR   SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
PE   2: Evidence at transcript level;
KW   Cytoplasm; NAD; Oxidoreductase; Reference proteome.
FT   CHAIN           1..351
FT                   /note="Glycerol-3-phosphate dehydrogenase 1-like protein"
FT                   /id="PRO_0000286513"
FT   ACT_SITE        206
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000250"
FT   BINDING         12..17
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250|UniProtKB:Q8N335"
FT   BINDING         122
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         155
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250|UniProtKB:Q8N335"
FT   BINDING         271..272
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         271
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250"
FT   BINDING         298
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250|UniProtKB:Q8N335"
FT   BINDING         300
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   351 AA;  38329 MW;  74C273D429C8F30D CRC64;
     MAAAPLKVCI VGSGNWGSAV AKIIGNNVKK LQKFASTVKM WVFEETVNGR KLTDIINNDH
     ENVKYLPGHK LPENVVAISN LSEAVQDADL LVFVIPHQFI HRICDEITGR VPKKALGITL
     IKGIDEGPEG LKLISDIIRE KMGIDISVLM GANIANEVAA EKFCETTIGS KVMENGLLFK
     ELLQTPNFRI TVVDDADTVE LCGALKNIVA VGAGFCDGLR CGDNTKAAVI RLGLMEMIAF
     ARIFCKGQVS TATFLESCGV ADLITTCYGG RNRRVAEAFA RTGKTIEELE KEMLNGQKLQ
     GPQTSAEVYR ILKQKGLLDK FPLFTAVYQI CYESRPVQGM LSCLQSHPEH T
//