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Database: UniProt
Entry: A0A096MX00_PAPAN
LinkDB: A0A096MX00_PAPAN
Original site: A0A096MX00_PAPAN 
ID   A0A096MX00_PAPAN        Unreviewed;       387 AA.
AC   A0A096MX00;
DT   26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT   25-MAY-2022, sequence version 2.
DT   24-JAN-2024, entry version 52.
DE   RecName: Full=Glycerol-3-phosphate dehydrogenase [NAD(+)] {ECO:0000256|RuleBase:RU361243};
DE            EC=1.1.1.8 {ECO:0000256|RuleBase:RU361243};
GN   Name=GPD1L {ECO:0000313|Ensembl:ENSPANP00000004409.2};
OS   Papio anubis (Olive baboon).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC   Cercopithecidae; Cercopithecinae; Papio.
OX   NCBI_TaxID=9555 {ECO:0000313|Ensembl:ENSPANP00000004409.2, ECO:0000313|Proteomes:UP000028761};
RN   [1] {ECO:0000313|Ensembl:ENSPANP00000004409.2, ECO:0000313|Proteomes:UP000028761}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Liu Y.L., Abraham K.A., Akbar H.A., Ali S.A., Anosike U.A., Aqrawi P.A.,
RA   Arias F.A., Attaway T.A., Awwad R.A., Babu C.B., Bandaranaike D.B.,
RA   Battles P.B., Bell A.B., Beltran B.B., Berhane-Mersha D.B., Bess C.B.,
RA   Bickham C.B., Bolden T.B., Carter K.C., Chau D.C., Chavez A.C.,
RA   Clerc-Blankenburg K.C., Coyle M.C., Dao M.D., Davila M.L.D.,
RA   Davy-Carroll L.D., Denson S.D., Dinh H.D., Fernandez S.F., Fernando P.F.,
RA   Forbes L.F., Francis C.F., Francisco L.F., Fu Q.F., Garcia-Iii R.G.,
RA   Garrett T.G., Gross S.G., Gubbala S.G., Hirani K.H., Hogues M.H.,
RA   Hollins B.H., Jackson L.J., Javaid M.J., Jhangiani S.J., Johnson A.J.,
RA   Johnson B.J., Jones J.J., Joshi V.J., Kalu J.K., Khan N.K., Korchina V.K.,
RA   Kovar C.K., Lago L.L., Lara F.L., Le T.-K.L., Lee S.L., Legall-Iii F.L.,
RA   Lemon S.L., Liu J.L., Liu Y.-S.L., Liyanage D.L., Lopez J.L.,
RA   Lorensuhewa L.L., Mata R.M., Mathew T.M., Mercado C.M., Mercado I.M.,
RA   Morales K.M., Morgan M.M., Munidasa M.M., Ngo D.N., Nguyen L.N.,
RA   Nguyen T.N., Nguyen N.N., Obregon M.O., Okwuonu G.O., Ongeri F.O.,
RA   Onwere C.O., Osifeso I.O., Parra A.P., Patil S.P., Perez A.P., Perez Y.P.,
RA   Pham C.P., Pu L.-L.P., Puazo M.P., Quiroz J.Q., Rouhana J.R., Ruiz M.R.,
RA   Ruiz S.-J.R., Saada N.S., Santibanez J.S., Scheel M.S., Schneider B.S.,
RA   Simmons D.S., Sisson I.S., Tang L.-Y.T., Thornton R.T., Tisius J.T.,
RA   Toledanes G.T., Trejos Z.T., Usmani K.U., Varghese R.V., Vattathil S.V.,
RA   Vee V.V., Walker D.W., Weissenberger G.W., White C.W., Williams A.W.,
RA   Woodworth J.W., Wright R.W., Zhu Y.Z., Han Y.H., Newsham I.N.,
RA   Nazareth L.N., Worley K.W., Muzny D.M., Rogers J.R., Gibbs R.G.;
RT   "Whole Genome Assembly of Papio anubis.";
RL   Submitted (MAR-2012) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Ensembl:ENSPANP00000004409.2}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (SEP-2023) to UniProtKB.
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:0000256|ARBA:ARBA00001343};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:11093;
CC         Evidence={ECO:0000256|ARBA:ARBA00001343};
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
CC   -!- SIMILARITY: Belongs to the NAD-dependent glycerol-3-phosphate
CC       dehydrogenase family. {ECO:0000256|ARBA:ARBA00011009,
CC       ECO:0000256|RuleBase:RU000437}.
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DR   AlphaFoldDB; A0A096MX00; -.
DR   STRING; 9555.ENSPANP00000004409; -.
DR   Ensembl; ENSPANT00000004157.4; ENSPANP00000004409.2; ENSPANG00000009800.4.
DR   eggNOG; KOG2711; Eukaryota.
DR   GeneTree; ENSGT00390000003114; -.
DR   HOGENOM; CLU_033449_2_2_1; -.
DR   OrthoDB; 3675564at2759; -.
DR   Proteomes; UP000028761; Chromosome 2.
DR   Bgee; ENSPANG00000009800; Expressed in gastrocnemius and 67 other cell types or tissues.
DR   ExpressionAtlas; A0A096MX00; baseline.
DR   GO; GO:0009331; C:glycerol-3-phosphate dehydrogenase complex; IEA:UniProtKB-UniRule.
DR   GO; GO:0005886; C:plasma membrane; IEA:Ensembl.
DR   GO; GO:0047952; F:glycerol-3-phosphate dehydrogenase [NAD(P)+] activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0051287; F:NAD binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0042803; F:protein homodimerization activity; IEA:InterPro.
DR   GO; GO:0017080; F:sodium channel regulator activity; IEA:Ensembl.
DR   GO; GO:0044325; F:transmembrane transporter binding; IEA:Ensembl.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR   GO; GO:0046168; P:glycerol-3-phosphate catabolic process; IEA:UniProtKB-UniRule.
DR   GO; GO:0006734; P:NADH metabolic process; IEA:Ensembl.
DR   GO; GO:0033137; P:negative regulation of peptidyl-serine phosphorylation; IEA:Ensembl.
DR   GO; GO:0090038; P:negative regulation of protein kinase C signaling; IEA:Ensembl.
DR   GO; GO:2000010; P:positive regulation of protein localization to cell surface; IEA:Ensembl.
DR   GO; GO:0010765; P:positive regulation of sodium ion transport; IEA:Ensembl.
DR   GO; GO:0002027; P:regulation of heart rate; IEA:Ensembl.
DR   GO; GO:0060373; P:regulation of ventricular cardiac muscle cell membrane depolarization; IEA:Ensembl.
DR   GO; GO:0086005; P:ventricular cardiac muscle cell action potential; IEA:Ensembl.
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   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   3: Inferred from homology;
KW   NAD {ECO:0000256|RuleBase:RU000437};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW   ECO:0000256|RuleBase:RU000437};
KW   Reference proteome {ECO:0000313|Proteomes:UP000028761}.
FT   DOMAIN          110..210
FT                   /note="Glycerol-3-phosphate dehydrogenase NAD-dependent N-
FT                   terminal"
FT                   /evidence="ECO:0000259|Pfam:PF01210"
FT   DOMAIN          231..377
FT                   /note="Glycerol-3-phosphate dehydrogenase NAD-dependent C-
FT                   terminal"
FT                   /evidence="ECO:0000259|Pfam:PF07479"
FT   REGION          1..102
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   387 AA;  40837 MW;  D4C46D7A85F03727 CRC64;
     MRTTCPDVPR AGWGGAGAGP GGRPGPGVRS GSWEWRSGSS PAVSCGPRSR AGVAATIGGE
     ANGAGPPPAA AGKAEQAEVG SRPGKHGPGG YIRPGHGSGA PESVHRGLGE LVAISNLSEA
     VQDADLLVFV IPHQFIHRIC DEITGRVPKK ALGITLIKGI DEGPEGLKLI SDIIREKMGI
     DISVLMGANI ANEVAAEKFC ETTIGSKVME NGLLFKELLQ TPNFRITVVD DADTVELCGA
     LKNIVAVGAG FCDGLRCGDN TKAAVIRLGL MEMIAFARIF CKGQVSTATF LESCGVADLI
     TTCYGGRNRR VAEAFARTGK TIEELEKEML NGQKLQGPQT SAEVYRILKQ KGLVDKFPLF
     TAVYQICYES RPVQEMLSCL QSHPEHT
//
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