G3PT_BOVIN
ID G3PT_BOVIN Reviewed; 395 AA.
AC Q2KJE5;
DT 01-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 07-MAR-2006, sequence version 1.
DT 03-AUG-2022, entry version 112.
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;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Hereford; TISSUE=Testis;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (SEP-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; BC105381; AAI05382.1; -; mRNA.
DR RefSeq; NP_001035642.1; NM_001040552.2.
DR AlphaFoldDB; Q2KJE5; -.
DR SMR; Q2KJE5; -.
DR STRING; 9913.ENSBTAP00000021166; -.
DR PaxDb; Q2KJE5; -.
DR PeptideAtlas; Q2KJE5; -.
DR PRIDE; Q2KJE5; -.
DR Ensembl; ENSBTAT00000021166; ENSBTAP00000021166; ENSBTAG00000015917.
DR GeneID; 532231; -.
DR KEGG; bta:532231; -.
DR CTD; 26330; -.
DR VEuPathDB; HostDB:ENSBTAG00000015917; -.
DR VGNC; VGNC:29248; GAPDHS.
DR eggNOG; KOG0657; Eukaryota.
DR GeneTree; ENSGT00940000160272; -.
DR HOGENOM; CLU_030140_0_3_1; -.
DR InParanoid; Q2KJE5; -.
DR OMA; NAKVLAW; -.
DR OrthoDB; 945145at2759; -.
DR TreeFam; TF300533; -.
DR BRENDA; 1.2.1.12; 908.
DR Reactome; R-BTA-70171; Glycolysis.
DR Reactome; R-BTA-70263; Gluconeogenesis.
DR UniPathway; UPA00109; UER00184.
DR Proteomes; UP000009136; Chromosome 18.
DR Bgee; ENSBTAG00000015917; Expressed in spermatid and 106 other tissues.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0004365; F:glyceraldehyde-3-phosphate dehydrogenase (NAD+) (phosphorylating) activity; IBA:GO_Central.
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; IBA:GO_Central.
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 PIRSF; PIRSF000149; GAP_DH; 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..395
FT /note="Glyceraldehyde-3-phosphate dehydrogenase, testis-
FT specific"
FT /id="PRO_0000286175"
FT REGION 1..60
FT /note="Testis-specific N-terminal extension"
FT /evidence="ECO:0000250"
FT REGION 19..59
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 26..59
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 211
FT /note="Nucleophile"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10009"
FT BINDING 72..73
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 93
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 210..212
FT /ligand="D-glyceraldehyde 3-phosphate"
FT /ligand_id="ChEBI:CHEBI:59776"
FT /evidence="ECO:0000250"
FT BINDING 241
FT /ligand="D-glyceraldehyde 3-phosphate"
FT /ligand_id="ChEBI:CHEBI:59776"
FT /evidence="ECO:0000250"
FT BINDING 270..271
FT /ligand="D-glyceraldehyde 3-phosphate"
FT /ligand_id="ChEBI:CHEBI:59776"
FT /evidence="ECO:0000250"
FT BINDING 293
FT /ligand="D-glyceraldehyde 3-phosphate"
FT /ligand_id="ChEBI:CHEBI:59776"
FT /evidence="ECO:0000250"
FT BINDING 375
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT SITE 238
FT /note="Activates thiol group during catalysis"
FT /evidence="ECO:0000250"
SQ SEQUENCE 395 AA; 43288 MW; 8DF90EBDAB156160 CRC64;
MSKRDIVLTN VTVVQLLRQP CPEPRVEAEP EPPAQPQPQP EPIKEEVPPP PPPPPAPKKV
RELIVGINGF GRIGRLVLRA CMEKGVKVVA VNDPFIDLEY MVYMFKYDST HGRYKGNVEH
KKGQLVVDNN EISVFQCKQP KEIPWKSVGS PFVVEATGVY LSLEETKAHI EAGAQRVVIC
APSPDAPMFV MGVNEKEYNP SSMKIVSNAS CTTNCLAPLA KVIHERFGIL EGLMTTVHSY
TATQKTVDGP SKKAWRDGRG AHQNIIPAST GAAKAVGKVI PDLKGKLTGM AFRVPTPDVS
VVDLTCRLAQ PTPYSAIKDA IKAAAKGPMA GILAYTEDEV VSTDFLSDTH SSIFDAKAGI
ALNDNFVKLI SWYDNEYGYS NRVVDLVRYM FSRDK
