ID   GPD1L_MOUSE             Reviewed;         351 AA.
AC   Q3ULJ0; Q6A0D2; Q8BVZ7; Q8BWM5; Q8CFN6;
DT   15-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT   15-MAY-2007, sequence version 2.
DT   27-MAR-2024, entry version 142.
DE   RecName: Full=Glycerol-3-phosphate dehydrogenase 1-like protein;
DE            EC=1.1.1.8 {ECO:0000250|UniProtKB:Q8N335};
GN   Name=Gpd1l; Synonyms=Kiaa0089;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   TISSUE=Fetal brain;
RX   PubMed=15368895; DOI=10.1093/dnares/11.3.205;
RA   Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S.,
RA   Saga Y., Seino S., Nishimura M., Kaisho T., Hoshino K., Kitamura H.,
RA   Nagase T., Ohara O., Koga H.;
RT   "Prediction of the coding sequences of mouse homologues of KIAA gene: IV.
RT   The complete nucleotide sequences of 500 mouse KIAA-homologous cDNAs
RT   identified by screening of terminal sequences of cDNA clones randomly
RT   sampled from size-fractionated libraries.";
RL   DNA Res. 11:205-218(2004).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC   STRAIN=C57BL/6J; TISSUE=Stomach, and Thymus;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA   Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA   Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA   Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA   Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA   Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA   Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA   Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA   Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA   Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA   Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA   Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA   Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA   Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA   Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA   Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA   Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA   Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA   Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA   Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA   van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA   Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA   Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA   Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA   Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA   Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA   Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA   Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA   Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   TISSUE=Eye;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA project:
RT   the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [4]
RP   PROTEIN SEQUENCE OF 207-220, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC   TISSUE=Hippocampus;
RA   Lubec G., Klug S.;
RL   Submitted (MAR-2007) to UniProtKB.
RN   [5]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung,
RC   Pancreas, Spleen, and Testis;
RX   PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA   Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA   Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT   "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL   Cell 143:1174-1189(2010).
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   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q3ULJ0-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q3ULJ0-2; Sequence=VSP_025062;
CC   -!- SIMILARITY: Belongs to the NAD-dependent glycerol-3-phosphate
CC       dehydrogenase family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAH37729.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC       Sequence=BAD32164.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR   EMBL; AK172886; BAD32164.1; ALT_INIT; mRNA.
DR   EMBL; AK050572; BAC34327.1; -; mRNA.
DR   EMBL; AK075845; BAC36001.1; -; mRNA.
DR   EMBL; AK145475; BAE26458.1; -; mRNA.
DR   EMBL; BC037729; AAH37729.1; ALT_INIT; mRNA.
DR   CCDS; CCDS23598.1; -. [Q3ULJ0-1]
DR   RefSeq; NP_780589.3; NM_175380.5. [Q3ULJ0-1]
DR   AlphaFoldDB; Q3ULJ0; -.
DR   SMR; Q3ULJ0; -.
DR   BioGRID; 237162; 3.
DR   STRING; 10090.ENSMUSP00000117509; -.
DR   GlyGen; Q3ULJ0; 1 site, 1 O-linked glycan (1 site).
DR   iPTMnet; Q3ULJ0; -.
DR   PhosphoSitePlus; Q3ULJ0; -.
DR   SwissPalm; Q3ULJ0; -.
DR   EPD; Q3ULJ0; -.
DR   jPOST; Q3ULJ0; -.
DR   MaxQB; Q3ULJ0; -.
DR   PaxDb; 10090-ENSMUSP00000117509; -.
DR   PeptideAtlas; Q3ULJ0; -.
DR   ProteomicsDB; 271437; -. [Q3ULJ0-1]
DR   ProteomicsDB; 271438; -. [Q3ULJ0-2]
DR   Pumba; Q3ULJ0; -.
DR   Antibodypedia; 27707; 189 antibodies from 25 providers.
DR   DNASU; 333433; -.
DR   Ensembl; ENSMUST00000084853.4; ENSMUSP00000081913.4; ENSMUSG00000050627.14. [Q3ULJ0-2]
DR   Ensembl; ENSMUST00000146623.8; ENSMUSP00000117509.2; ENSMUSG00000050627.14. [Q3ULJ0-1]
DR   GeneID; 333433; -.
DR   KEGG; mmu:333433; -.
DR   UCSC; uc009ryj.2; mouse. [Q3ULJ0-1]
DR   AGR; MGI:1289257; -.
DR   CTD; 23171; -.
DR   MGI; MGI:1289257; Gpd1l.
DR   VEuPathDB; HostDB:ENSMUSG00000050627; -.
DR   eggNOG; KOG2711; Eukaryota.
DR   GeneTree; ENSGT00390000003114; -.
DR   HOGENOM; CLU_033449_2_2_1; -.
DR   InParanoid; Q3ULJ0; -.
DR   OMA; YDTPPMD; -.
DR   OrthoDB; 3675564at2759; -.
DR   PhylomeDB; Q3ULJ0; -.
DR   TreeFam; TF300836; -.
DR   Reactome; R-MMU-1483166; Synthesis of PA.
DR   BioGRID-ORCS; 333433; 3 hits in 79 CRISPR screens.
DR   ChiTaRS; Gpd1l; mouse.
DR   PRO; PR:Q3ULJ0; -.
DR   Proteomes; UP000000589; Chromosome 9.
DR   RNAct; Q3ULJ0; Protein.
DR   Bgee; ENSMUSG00000050627; Expressed in gastrula and 230 other cell types or tissues.
DR   ExpressionAtlas; Q3ULJ0; baseline and differential.
DR   GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR   GO; GO:0009331; C:glycerol-3-phosphate dehydrogenase complex; IEA:InterPro.
DR   GO; GO:0016020; C:membrane; IDA:BHF-UCL.
DR   GO; GO:0005886; C:plasma membrane; ISO:MGI.
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:0017080; F:sodium channel regulator activity; ISO:MGI.
DR   GO; GO:0044325; F:transmembrane transporter binding; ISO:MGI.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR   GO; GO:0046168; P:glycerol-3-phosphate catabolic process; IEA:InterPro.
DR   GO; GO:0019674; P:NAD metabolic process; ISO:MGI.
DR   GO; GO:0006734; P:NADH metabolic process; IMP:MGI.
DR   GO; GO:0033137; P:negative regulation of peptidyl-serine phosphorylation; ISO:MGI.
DR   GO; GO:0090038; P:negative regulation of protein kinase C signaling; ISO:MGI.
DR   GO; GO:2000010; P:positive regulation of protein localization to cell surface; ISO:MGI.
DR   GO; GO:0010765; P:positive regulation of sodium ion transport; ISO:MGI.
DR   GO; GO:0002027; P:regulation of heart rate; ISO:MGI.
DR   GO; GO:0060373; P:regulation of ventricular cardiac muscle cell membrane depolarization; ISO:MGI.
DR   GO; GO:0086005; P:ventricular cardiac muscle cell action potential; ISO:MGI.
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.
DR   Genevisible; Q3ULJ0; MM.
PE   1: Evidence at protein level;
KW   Alternative splicing; Cytoplasm; Direct protein sequencing; NAD;
KW   Oxidoreductase; Reference proteome.
FT   CHAIN           1..351
FT                   /note="Glycerol-3-phosphate dehydrogenase 1-like protein"
FT                   /id="PRO_0000286512"
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"
FT   VAR_SEQ         321..351
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:16141072"
FT                   /id="VSP_025062"
FT   CONFLICT        26
FT                   /note="S -> G (in Ref. 2; BAC36001)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        179
FT                   /note="F -> S (in Ref. 2; BAC36001)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        202
FT                   /note="C -> W (in Ref. 2; BAC36001)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        212
FT                   /note="G -> V (in Ref. 2; BAC36001)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   351 AA;  38226 MW;  BE192D41F592E577 CRC64;
     MAAAPLKVCI VGSGNWGSAV AKIIGSNVKT LQKFSSTVKM WVFEETVNGR KLTDIINNDH
     ENVKYLPGHK LPENVVAVPN LSEAVQDADL LVFVIPHQFI HKICDEITGR VPEKALGITL
     IKGIDEGPDG LKLISDIIRE KMGIDISVLM GANIASEVAA EKFCETTIGS KVMQNGLLFK
     ELLQTPNFRI TVVDDADTVE LCGALKNIVA VGAGFCDGLR CGDNTKAAVI RLGLMEMIAF
     AKIFCKGQVS TATFLESCGV ADLITTCYGG RNRRVAEAFA RTGKTIEELE KELLNGQKLQ
     GPQTSAEVYR ILRQKGLLDK FPLFTAVYQI CYEGRPVTQM LSCLQSHPEH I
//