G3PT_MOUSE
ID G3PT_MOUSE Reviewed; 440 AA.
AC Q64467; Q60650;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 178.
DE RecName: Full=Glyceraldehyde-3-phosphate dehydrogenase, testis-specific;
DE EC=1.2.1.12;
DE AltName: Full=Spermatogenic cell-specific glyceraldehyde 3-phosphate dehydrogenase 2;
DE Short=GAPDH-2;
DE AltName: Full=Spermatogenic glyceraldehyde-3-phosphate dehydrogenase;
GN Name=Gapdhs; Synonyms=Gapd-s, Gapds;
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 [MRNA].
RC STRAIN=CD-1; TISSUE=Testis;
RX PubMed=1375514; DOI=10.1095/biolreprod46.5.869;
RA Welch J.E., Schatte E.C., O'Brien D.A., Eddy E.M.;
RT "Expression of a glyceraldehyde 3-phosphate dehydrogenase gene specific to
RT mouse spermatogenic cells.";
RL Biol. Reprod. 46:869-878(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ICR X Swiss Webster; TISSUE=Testis;
RX PubMed=7736666; DOI=10.1002/dvg.1020160210;
RA Welch J.E., Brown P.R., O'Brien D.A., Eddy E.M.;
RT "Genomic organization of a mouse glyceraldehyde 3-phosphate dehydrogenase
RT gene (Gapd-s) expressed in post-meiotic spermatogenic cells.";
RL Dev. Genet. 16:179-189(1995).
RN [3]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=15546993; DOI=10.1073/pnas.0407708101;
RA Miki K., Qu W., Goulding E.H., Willis W.D., Bunch D.O., Strader L.F.,
RA Perreault S.D., Eddy E.M., O'Brien D.A.;
RT "Glyceraldehyde 3-phosphate dehydrogenase-S, a sperm-specific glycolytic
RT enzyme, is required for sperm motility and male fertility.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:16501-16506(2004).
RN [4]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=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: 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.
CC {ECO:0000269|PubMed:15546993}.
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 -!- TISSUE SPECIFICITY: Testis specific.
CC -!- DEVELOPMENTAL STAGE: First expressed at day 20 in post-meiotic germ
CC cells. Levels increase until day 24 and then remain constant during
CC maturity.
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-33 with
CC sheath components. {ECO:0000250}.
CC -!- DISRUPTION PHENOTYPE: Mice display greatly reduced ATP levels in sperm,
CC severely impaired sperm motility and are infertile.
CC {ECO:0000269|PubMed:15546993}.
CC -!- SIMILARITY: Belongs to the glyceraldehyde-3-phosphate dehydrogenase
CC family. {ECO:0000305}.
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DR EMBL; M60978; AAA53033.1; -; mRNA.
DR EMBL; U09964; AAA80276.1; -; Genomic_DNA.
DR CCDS; CCDS71933.1; -.
DR PIR; I49681; I49681.
DR RefSeq; NP_032111.1; NM_008085.2.
DR PDB; 5C7I; X-ray; 2.01 A; O/R=107-439.
DR PDBsum; 5C7I; -.
DR AlphaFoldDB; Q64467; -.
DR SMR; Q64467; -.
DR BioGRID; 199830; 7.
DR IntAct; Q64467; 1.
DR STRING; 10090.ENSMUSP00000074317; -.
DR iPTMnet; Q64467; -.
DR PhosphoSitePlus; Q64467; -.
DR SwissPalm; Q64467; -.
DR EPD; Q64467; -.
DR jPOST; Q64467; -.
DR MaxQB; Q64467; -.
DR PaxDb; Q64467; -.
DR PeptideAtlas; Q64467; -.
DR PRIDE; Q64467; -.
DR ProteomicsDB; 271624; -.
DR DNASU; 14447; -.
DR GeneID; 14447; -.
DR KEGG; mmu:14447; -.
DR CTD; 26330; -.
DR MGI; MGI:95653; Gapdhs.
DR eggNOG; KOG0657; Eukaryota.
DR InParanoid; Q64467; -.
DR OrthoDB; 945145at2759; -.
DR PhylomeDB; Q64467; -.
DR TreeFam; TF300533; -.
DR BRENDA; 1.2.1.12; 3474.
DR Reactome; R-MMU-70171; Glycolysis.
DR Reactome; R-MMU-70263; Gluconeogenesis.
DR UniPathway; UPA00109; UER00184.
DR BioGRID-ORCS; 14447; 3 hits in 73 CRISPR screens.
DR ChiTaRS; Gapdhs; mouse.
DR PRO; PR:Q64467; -.
DR Proteomes; UP000000589; Unplaced.
DR RNAct; Q64467; protein.
DR GO; GO:0005929; C:cilium; IDA:MGI.
DR GO; GO:0005737; C:cytoplasm; ISO:MGI.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0031514; C:motile cilium; IDA:MGI.
DR GO; GO:0035686; C:sperm fibrous sheath; IDA:MGI.
DR GO; GO:0097228; C:sperm principal piece; IDA:MGI.
DR GO; GO:0004365; F:glyceraldehyde-3-phosphate dehydrogenase (NAD+) (phosphorylating) activity; IDA:MGI.
DR GO; GO:0051287; F:NAD binding; IEA:InterPro.
DR GO; GO:0050661; F:NADP binding; IEA:InterPro.
DR GO; GO:0030317; P:flagellated sperm motility; IDA:UniProtKB.
DR GO; GO:0006006; P:glucose metabolic process; IEA:InterPro.
DR GO; GO:0006096; P:glycolytic process; IMP:MGI.
DR GO; GO:0045821; P:positive regulation of glycolytic process; TAS:UniProtKB.
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 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; Glycolysis; NAD; Oxidoreductase; Phosphoprotein;
KW Reference proteome.
FT CHAIN 1..440
FT /note="Glyceraldehyde-3-phosphate dehydrogenase, testis-
FT specific"
FT /id="PRO_0000145504"
FT REGION 1..105
FT /note="Testis-specific N-terminal extension"
FT /evidence="ECO:0000250"
FT REGION 40..106
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 40..104
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 256
FT /note="Nucleophile"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10009"
FT BINDING 117..118
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 138
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 183
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 205
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 225
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 255..257
FT /ligand="D-glyceraldehyde 3-phosphate"
FT /ligand_id="ChEBI:CHEBI:59776"
FT /evidence="ECO:0000250"
FT BINDING 286
FT /ligand="D-glyceraldehyde 3-phosphate"
FT /ligand_id="ChEBI:CHEBI:59776"
FT /evidence="ECO:0000250"
FT BINDING 315..316
FT /ligand="D-glyceraldehyde 3-phosphate"
FT /ligand_id="ChEBI:CHEBI:59776"
FT /evidence="ECO:0000250"
FT BINDING 338
FT /ligand="D-glyceraldehyde 3-phosphate"
FT /ligand_id="ChEBI:CHEBI:59776"
FT /evidence="ECO:0000250"
FT BINDING 420
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT SITE 283
FT /note="Activates thiol group during catalysis"
FT /evidence="ECO:0000250"
FT MOD_RES 358
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9ESV6"
FT CONFLICT 33..34
FT /note="Missing (in Ref. 2; AAA80276)"
FT /evidence="ECO:0000305"
FT CONFLICT 43
FT /note="L -> V (in Ref. 2; AAA80276)"
FT /evidence="ECO:0000305"
FT STRAND 109..113
FT /evidence="ECO:0007829|PDB:5C7I"
FT HELIX 117..129
FT /evidence="ECO:0007829|PDB:5C7I"
FT STRAND 132..137
FT /evidence="ECO:0007829|PDB:5C7I"
FT HELIX 143..151
FT /evidence="ECO:0007829|PDB:5C7I"
FT TURN 154..156
FT /evidence="ECO:0007829|PDB:5C7I"
FT STRAND 163..166
FT /evidence="ECO:0007829|PDB:5C7I"
FT STRAND 169..172
FT /evidence="ECO:0007829|PDB:5C7I"
FT STRAND 175..180
FT /evidence="ECO:0007829|PDB:5C7I"
FT HELIX 185..187
FT /evidence="ECO:0007829|PDB:5C7I"
FT HELIX 190..193
FT /evidence="ECO:0007829|PDB:5C7I"
FT STRAND 197..200
FT /evidence="ECO:0007829|PDB:5C7I"
FT STRAND 202..204
FT /evidence="ECO:0007829|PDB:5C7I"
FT HELIX 208..216
FT /evidence="ECO:0007829|PDB:5C7I"
FT STRAND 220..226
FT /evidence="ECO:0007829|PDB:5C7I"
FT STRAND 229..231
FT /evidence="ECO:0007829|PDB:5C7I"
FT TURN 236..238
FT /evidence="ECO:0007829|PDB:5C7I"
FT HELIX 240..242
FT /evidence="ECO:0007829|PDB:5C7I"
FT TURN 245..247
FT /evidence="ECO:0007829|PDB:5C7I"
FT STRAND 249..252
FT /evidence="ECO:0007829|PDB:5C7I"
FT HELIX 256..271
FT /evidence="ECO:0007829|PDB:5C7I"
FT STRAND 274..284
FT /evidence="ECO:0007829|PDB:5C7I"
FT STRAND 289..293
FT /evidence="ECO:0007829|PDB:5C7I"
FT HELIX 301..303
FT /evidence="ECO:0007829|PDB:5C7I"
FT TURN 306..308
FT /evidence="ECO:0007829|PDB:5C7I"
FT STRAND 311..314
FT /evidence="ECO:0007829|PDB:5C7I"
FT TURN 317..320
FT /evidence="ECO:0007829|PDB:5C7I"
FT HELIX 321..324
FT /evidence="ECO:0007829|PDB:5C7I"
FT HELIX 326..328
FT /evidence="ECO:0007829|PDB:5C7I"
FT TURN 329..331
FT /evidence="ECO:0007829|PDB:5C7I"
FT STRAND 332..340
FT /evidence="ECO:0007829|PDB:5C7I"
FT STRAND 345..355
FT /evidence="ECO:0007829|PDB:5C7I"
FT HELIX 359..371
FT /evidence="ECO:0007829|PDB:5C7I"
FT TURN 372..377
FT /evidence="ECO:0007829|PDB:5C7I"
FT STRAND 378..381
FT /evidence="ECO:0007829|PDB:5C7I"
FT HELIX 387..390
FT /evidence="ECO:0007829|PDB:5C7I"
FT STRAND 396..400
FT /evidence="ECO:0007829|PDB:5C7I"
FT TURN 401..403
FT /evidence="ECO:0007829|PDB:5C7I"
FT STRAND 405..408
FT /evidence="ECO:0007829|PDB:5C7I"
FT STRAND 411..418
FT /evidence="ECO:0007829|PDB:5C7I"
FT HELIX 422..437
FT /evidence="ECO:0007829|PDB:5C7I"
SQ SEQUENCE 440 AA; 47657 MW; 05FF0A093D1ABD9C CRC64;
MSRRDVVLTN VTVVQLRRDR CPCPCPCPCP CPCPVIRPPP PKLEDPPPTV EEQPPPPPPP
PPPPPPPPPP PPPQIEPDKF EEAPPPPPPP PPPPPPPPPP LQKPARELTV GINGFGRIGR
LVLRVCMEKG IRVVAVNDPF IDPEYMVYMF KYDSTHGRYK GNVEHKNGQL VVDNLEINTY
QCKDPKEIPW SSIGNPYVVE CTGVYLSIEA ASAHISSGAR RVVVTAPSPD APMFVMGVNE
KDYNPGSMTI VSNASCTTNC LAPLAKVIHE NFGIVEGLMT TVHSYTATQK TVDGPSKKDW
RGGRGAHQNI IPSSTGAAKA VGKVIPELKG KLTGMAFRVP TPNVSVVDLT CRLAKPASYS
AITEAVKAAA KGPLAGILAY TEDQVVSTDF NGNPHSSIFD AKAGIALNDN FVKLVAWYDN
EYGYSNRVVD LLRYMFSREK
