G3PT_MACFA
ID G3PT_MACFA Reviewed; 409 AA.
AC Q4R3T1;
DT 10-JAN-2006, integrated into UniProtKB/Swiss-Prot.
DT 19-JUL-2005, sequence version 1.
DT 03-AUG-2022, entry version 81.
DE RecName: Full=Glyceraldehyde-3-phosphate dehydrogenase, testis-specific;
DE EC=1.2.1.12;
DE AltName: Full=Spermatogenic glyceraldehyde-3-phosphate dehydrogenase;
GN Name=GAPDHS; ORFNames=QtsA-14420;
OS Macaca fascicularis (Crab-eating macaque) (Cynomolgus monkey).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Cercopithecinae; Macaca.
OX NCBI_TaxID=9541;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Testis;
RG International consortium for macaque cDNA sequencing and analysis;
RT "DNA sequences of macaque genes expressed in brain or testis and its
RT evolutionary implications.";
RL Submitted (JUN-2005) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: May play an important role in regulating the switch between
CC different pathways for energy production during spermiogenesis and in
CC the spermatozoon. Required for sperm motility and male fertility (By
CC similarity). {ECO:0000250}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=D-glyceraldehyde 3-phosphate + NAD(+) + phosphate = (2R)-3-
CC phospho-glyceroyl phosphate + H(+) + NADH; Xref=Rhea:RHEA:10300,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:43474, ChEBI:CHEBI:57540,
CC ChEBI:CHEBI:57604, ChEBI:CHEBI:57945, ChEBI:CHEBI:59776; EC=1.2.1.12;
CC Evidence={ECO:0000255|PROSITE-ProRule:PRU10009};
CC -!- PATHWAY: Carbohydrate degradation; glycolysis; pyruvate from D-
CC glyceraldehyde 3-phosphate: step 1/5.
CC -!- SUBUNIT: Homotetramer. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC -!- DOMAIN: The testis-specific N-terminal extension mediates tight
CC association with the cytoskeletal fibrous sheath of the spermatozoa
CC flagellum, possibly via interchain disulfide-bonding of Cys-21 with
CC sheath components. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the glyceraldehyde-3-phosphate dehydrogenase
CC family. {ECO:0000305}.
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DR EMBL; AB179184; BAE02235.1; -; mRNA.
DR RefSeq; NP_001270981.1; NM_001284052.1.
DR AlphaFoldDB; Q4R3T1; -.
DR SMR; Q4R3T1; -.
DR STRING; 9541.XP_005588921.1; -.
DR Ensembl; ENSMFAT00000011229; ENSMFAP00000036979; ENSMFAG00000037754.
DR GeneID; 101866112; -.
DR CTD; 26330; -.
DR eggNOG; KOG0657; Eukaryota.
DR GeneTree; ENSGT00940000160272; -.
DR OrthoDB; 945145at2759; -.
DR UniPathway; UPA00109; UER00184.
DR Proteomes; UP000233100; Chromosome 19.
DR Bgee; ENSMFAG00000037754; Expressed in lymph node and 13 other tissues.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0004365; F:glyceraldehyde-3-phosphate dehydrogenase (NAD+) (phosphorylating) activity; IEA:UniProtKB-EC.
DR GO; GO:0051287; F:NAD binding; IEA:InterPro.
DR GO; GO:0050661; F:NADP binding; IEA:InterPro.
DR GO; GO:0006006; P:glucose metabolic process; IEA:InterPro.
DR GO; GO:0006096; P:glycolytic process; IEA:UniProtKB-UniPathway.
DR InterPro; IPR020831; GlycerAld/Erythrose_P_DH.
DR InterPro; IPR020830; GlycerAld_3-P_DH_AS.
DR InterPro; IPR020829; GlycerAld_3-P_DH_cat.
DR InterPro; IPR020828; GlycerAld_3-P_DH_NAD(P)-bd.
DR InterPro; IPR006424; Glyceraldehyde-3-P_DH_1.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR PANTHER; PTHR10836; PTHR10836; 1.
DR Pfam; PF02800; Gp_dh_C; 1.
DR Pfam; PF00044; Gp_dh_N; 1.
DR PRINTS; PR00078; G3PDHDRGNASE.
DR SMART; SM00846; Gp_dh_N; 1.
DR SUPFAM; SSF51735; SSF51735; 1.
DR TIGRFAMs; TIGR01534; GAPDH-I; 1.
DR PROSITE; PS00071; GAPDH; 1.
PE 2: Evidence at transcript level;
KW Cytoplasm; Glycolysis; NAD; Oxidoreductase; Reference proteome.
FT CHAIN 1..409
FT /note="Glyceraldehyde-3-phosphate dehydrogenase, testis-
FT specific"
FT /id="PRO_0000145503"
FT REGION 1..74
FT /note="Testis-specific N-terminal extension"
FT /evidence="ECO:0000250"
FT REGION 18..76
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 21..73
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 225
FT /note="Nucleophile"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10009"
FT BINDING 86..87
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 107
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 152
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 174
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 194
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 224..226
FT /ligand="D-glyceraldehyde 3-phosphate"
FT /ligand_id="ChEBI:CHEBI:59776"
FT /evidence="ECO:0000250"
FT BINDING 255
FT /ligand="D-glyceraldehyde 3-phosphate"
FT /ligand_id="ChEBI:CHEBI:59776"
FT /evidence="ECO:0000250"
FT BINDING 284..285
FT /ligand="D-glyceraldehyde 3-phosphate"
FT /ligand_id="ChEBI:CHEBI:59776"
FT /evidence="ECO:0000250"
FT BINDING 307
FT /ligand="D-glyceraldehyde 3-phosphate"
FT /ligand_id="ChEBI:CHEBI:59776"
FT /evidence="ECO:0000250"
FT BINDING 389
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT SITE 252
FT /note="Activates thiol group during catalysis"
FT /evidence="ECO:0000250"
SQ SEQUENCE 409 AA; 44596 MW; CFA292A510221C28 CRC64;
MSKRDIVLTN VTVVQLLRQP CPVTRPPPPP EPKVEIEPQP QPEPTPVREE IKPPPPPSPP
PRPATPPPKM GPAPRELTVG INGFGRIGRL VLRACMEKGV KVVAVNDPFI DPEYMVYMFK
YDSTHGRYKG SVEFRNGQLV VDNHEISVYQ CKEPKQIPWR DVGSPYVVES TGVYLSIEAA
SNHISAGAQR VVISAPSPDA PTFVMGVNEN NYNPGSMNIV SNASCTTNCL APLAKVIHER
FGIVEGLMTT VHSYTATQKT VDGPSKKAWR DGRGAHQNII PASTGAAKAV TKVIPELKGK
LTGMAFRVPT PDVSVVDLTC RLAQPAPYSA IKEAIKAAAK GPMAGILAYT EDEVVSTDFV
GDSHSSIFDA KAGIALNDNF VKLISWYDNE YGYSHRVVDL LRYMFSRDK
