GPD1L_MOUSE
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 03-AUG-2022, entry version 133.
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, Pancreas,
RC 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; 2.
DR STRING; 10090.ENSMUSP00000117509; -.
DR iPTMnet; Q3ULJ0; -.
DR PhosphoSitePlus; Q3ULJ0; -.
DR SwissPalm; Q3ULJ0; -.
DR EPD; Q3ULJ0; -.
DR jPOST; Q3ULJ0; -.
DR MaxQB; Q3ULJ0; -.
DR PaxDb; Q3ULJ0; -.
DR PeptideAtlas; Q3ULJ0; -.
DR PRIDE; Q3ULJ0; -.
DR ProteomicsDB; 271437; -. [Q3ULJ0-1]
DR ProteomicsDB; 271438; -. [Q3ULJ0-2]
DR Antibodypedia; 27707; 166 antibodies from 25 providers.
DR DNASU; 333433; -.
DR Ensembl; ENSMUST00000084853; ENSMUSP00000081913; ENSMUSG00000050627. [Q3ULJ0-2]
DR Ensembl; ENSMUST00000146623; ENSMUSP00000117509; ENSMUSG00000050627. [Q3ULJ0-1]
DR GeneID; 333433; -.
DR KEGG; mmu:333433; -.
DR UCSC; uc009ryj.2; mouse. [Q3ULJ0-1]
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; FIHKVCD; -.
DR PhylomeDB; Q3ULJ0; -.
DR TreeFam; TF300836; -.
DR Reactome; R-MMU-1483166; Synthesis of PA.
DR BioGRID-ORCS; 333433; 3 hits in 74 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 227 other tissues.
DR ExpressionAtlas; Q3ULJ0; baseline and differential.
DR Genevisible; Q3ULJ0; MM.
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: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: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:2000649; P:regulation of sodium ion transmembrane transporter activity; 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; 1.10.1040.10; -; 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 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; SSF48179; 1.
DR SUPFAM; SSF51735; SSF51735; 1.
DR TIGRFAMs; TIGR03376; glycerol3P_DH; 1.
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
