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Glyceraldehyde-3-phosphate dehydrogenase, testis-specific (EC 1.2.1.12) (Spermatogenic cell-specific glyceraldehyde 3-phosphate dehydrogenase 2) (GAPDH-2) (Spermatogenic glyceraldehyde-3-phosphate dehydrogenase)

 G3PT_RAT                Reviewed;         432 AA.
Q9ESV6;
28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
01-MAR-2001, sequence version 1.
12-SEP-2018, entry version 115.
RecName: Full=Glyceraldehyde-3-phosphate dehydrogenase, testis-specific;
EC=1.2.1.12;
AltName: Full=Spermatogenic cell-specific glyceraldehyde 3-phosphate dehydrogenase 2;
Short=GAPDH-2;
AltName: Full=Spermatogenic glyceraldehyde-3-phosphate dehydrogenase;
Name=Gapdhs; Synonyms=Gapd-s, Gapds;
Rattus norvegicus (Rat).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Rattus.
NCBI_TaxID=10116;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
STRAIN=Wistar; TISSUE=Testis;
McLaughlin E.A., Hall L.;
"Nucleotide sequence of rat testis-specific glyceraldehyde-3-phosphate
dehydrogenase (GAPDH-2) cDNA.";
Submitted (AUG-2000) to the EMBL/GenBank/DDBJ databases.
[2]
IDENTIFICATION BY MASS SPECTROMETRY, AND TISSUE SPECIFICITY.
PubMed=19423663; DOI=10.1530/REP-09-0052;
Khan S.A., Suryawanshi A.R., Ranpura S.A., Jadhav S.V., Khole V.V.;
"Identification of novel immunodominant epididymal sperm proteins
using combinatorial approach.";
Reproduction 138:81-93(2009).
[3]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-350, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22673903; DOI=10.1038/ncomms1871;
Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A.,
Lundby C., Olsen J.V.;
"Quantitative maps of protein phosphorylation sites across 14
different rat organs and tissues.";
Nat. Commun. 3:876-876(2012).
[4]
X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 102-432 IN TETRAMER WITH
E.COLI GAPDH.
PubMed=19542219; DOI=10.1074/jbc.M109.004648;
Frayne J., Taylor A., Cameron G., Hadfield A.T.;
"Structure of insoluble rat sperm glyceraldehyde-3-phosphate
dehydrogenase (GAPDH) via heterotetramer formation with Escherichia
coli GAPDH reveals target for contraceptive design.";
J. Biol. Chem. 284:22703-22712(2009).
-!- FUNCTION: May play an important role in regulating the switch
between different pathways for energy production during
spermiogenesis and in the spermatozoon. Required for sperm
motility and male fertility (By similarity). {ECO:0000250}.
-!- CATALYTIC ACTIVITY: D-glyceraldehyde 3-phosphate + phosphate +
NAD(+) = 3-phospho-D-glyceroyl phosphate + NADH.
{ECO:0000255|PROSITE-ProRule:PRU10009}.
-!- PATHWAY: Carbohydrate degradation; glycolysis; pyruvate from D-
glyceraldehyde 3-phosphate: step 1/5.
-!- SUBUNIT: Homotetramer. {ECO:0000250}.
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
-!- TISSUE SPECIFICITY: Expressed in both head and flagellum of
epididymal sperm. {ECO:0000269|PubMed:19423663}.
-!- DOMAIN: The testis-specific N-terminal extension mediates tight
association with the cytoskeletal fibrous sheath of the
spermatozoa flagellum, possibly via interchain disulfide-bonding
of Cys-33 with sheath components. {ECO:0000250}.
-!- SIMILARITY: Belongs to the glyceraldehyde-3-phosphate
dehydrogenase family. {ECO:0000305}.
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EMBL; AJ297631; CAC05399.1; -; mRNA.
RefSeq; NP_076454.1; NM_023964.1.
UniGene; Rn.64496; -.
PDB; 2VYN; X-ray; 2.20 A; D=102-432.
PDB; 2VYV; X-ray; 2.38 A; D=102-432.
PDBsum; 2VYN; -.
PDBsum; 2VYV; -.
ProteinModelPortal; Q9ESV6; -.
SMR; Q9ESV6; -.
STRING; 10116.ENSRNOP00000028518; -.
iPTMnet; Q9ESV6; -.
PhosphoSitePlus; Q9ESV6; -.
SwissPalm; Q9ESV6; -.
PaxDb; Q9ESV6; -.
PRIDE; Q9ESV6; -.
Ensembl; ENSRNOT00000028518; ENSRNOP00000028518; ENSRNOG00000021009.
GeneID; 66020; -.
KEGG; rno:66020; -.
UCSC; RGD:620150; rat.
CTD; 26330; -.
RGD; 620150; Gapdhs.
eggNOG; KOG0657; Eukaryota.
eggNOG; COG0057; LUCA.
GeneTree; ENSGT00760000119172; -.
HOGENOM; HOG000071678; -.
InParanoid; Q9ESV6; -.
KO; K10705; -.
PhylomeDB; Q9ESV6; -.
TreeFam; TF300533; -.
BRENDA; 1.2.1.12; 5301.
Reactome; R-RNO-70171; Glycolysis.
Reactome; R-RNO-70263; Gluconeogenesis.
UniPathway; UPA00109; UER00184.
EvolutionaryTrace; Q9ESV6; -.
PRO; PR:Q9ESV6; -.
Proteomes; UP000002494; Chromosome 1.
Bgee; ENSRNOG00000021009; Expressed in 9 organ(s), highest expression level in testis.
ExpressionAtlas; Q9ESV6; baseline and differential.
Genevisible; Q9ESV6; RN.
GO; GO:0001669; C:acrosomal vesicle; TAS:RGD.
GO; GO:0005737; C:cytoplasm; IDA:RGD.
GO; GO:0031514; C:motile cilium; IDA:RGD.
GO; GO:0004365; F:glyceraldehyde-3-phosphate dehydrogenase (NAD+) (phosphorylating) activity; IEA:UniProtKB-EC.
GO; GO:0051287; F:NAD binding; IEA:InterPro.
GO; GO:0050661; F:NADP binding; IEA:InterPro.
GO; GO:0006006; P:glucose metabolic process; IEA:InterPro.
GO; GO:0006096; P:glycolytic process; TAS:RGD.
GO; GO:0007286; P:spermatid development; IEP:RGD.
InterPro; IPR020831; GlycerAld/Erythrose_P_DH.
InterPro; IPR020830; GlycerAld_3-P_DH_AS.
InterPro; IPR020829; GlycerAld_3-P_DH_cat.
InterPro; IPR020828; GlycerAld_3-P_DH_NAD(P)-bd.
InterPro; IPR006424; Glyceraldehyde-3-P_DH_1.
InterPro; IPR036291; NAD(P)-bd_dom_sf.
PANTHER; PTHR10836; PTHR10836; 1.
Pfam; PF02800; Gp_dh_C; 1.
Pfam; PF00044; Gp_dh_N; 1.
PRINTS; PR00078; G3PDHDRGNASE.
SMART; SM00846; Gp_dh_N; 1.
SUPFAM; SSF51735; SSF51735; 1.
TIGRFAMs; TIGR01534; GAPDH-I; 1.
PROSITE; PS00071; GAPDH; 1.
1: Evidence at protein level;
3D-structure; Complete proteome; Cytoplasm; Glycolysis; NAD;
Oxidoreductase; Phosphoprotein; Reference proteome.
CHAIN 1 432 Glyceraldehyde-3-phosphate dehydrogenase,
testis-specific.
/FTId=PRO_0000380245.
NP_BIND 109 110 NAD. {ECO:0000250}.
REGION 1 97 Testis-specific N-terminal extension.
{ECO:0000250}.
REGION 247 249 Glyceraldehyde 3-phosphate binding.
{ECO:0000250}.
REGION 307 308 Glyceraldehyde 3-phosphate binding.
{ECO:0000250}.
COMPBIAS 20 34 Cys/Pro-rich.
COMPBIAS 55 65 Poly-Pro.
COMPBIAS 76 96 Poly-Pro.
ACT_SITE 248 248 Nucleophile. {ECO:0000255|PROSITE-
ProRule:PRU10009}.
BINDING 130 130 NAD. {ECO:0000250}.
BINDING 175 175 NAD; via carbonyl oxygen. {ECO:0000250}.
BINDING 197 197 NAD. {ECO:0000250}.
BINDING 217 217 NAD. {ECO:0000250}.
BINDING 278 278 Glyceraldehyde 3-phosphate.
{ECO:0000250}.
BINDING 330 330 Glyceraldehyde 3-phosphate.
{ECO:0000250}.
BINDING 412 412 NAD. {ECO:0000250}.
SITE 275 275 Activates thiol group during catalysis.
{ECO:0000250}.
MOD_RES 350 350 Phosphoserine.
{ECO:0000244|PubMed:22673903}.
STRAND 101 105 {ECO:0000244|PDB:2VYN}.
HELIX 109 121 {ECO:0000244|PDB:2VYN}.
STRAND 124 129 {ECO:0000244|PDB:2VYN}.
HELIX 135 143 {ECO:0000244|PDB:2VYN}.
TURN 146 148 {ECO:0000244|PDB:2VYN}.
STRAND 155 158 {ECO:0000244|PDB:2VYN}.
STRAND 161 164 {ECO:0000244|PDB:2VYN}.
STRAND 167 172 {ECO:0000244|PDB:2VYN}.
HELIX 177 179 {ECO:0000244|PDB:2VYN}.
HELIX 182 185 {ECO:0000244|PDB:2VYN}.
STRAND 189 192 {ECO:0000244|PDB:2VYN}.
STRAND 194 196 {ECO:0000244|PDB:2VYN}.
HELIX 200 203 {ECO:0000244|PDB:2VYN}.
HELIX 205 208 {ECO:0000244|PDB:2VYN}.
STRAND 214 218 {ECO:0000244|PDB:2VYN}.
STRAND 221 223 {ECO:0000244|PDB:2VYN}.
TURN 228 230 {ECO:0000244|PDB:2VYN}.
HELIX 232 234 {ECO:0000244|PDB:2VYN}.
TURN 237 239 {ECO:0000244|PDB:2VYN}.
STRAND 241 244 {ECO:0000244|PDB:2VYN}.
HELIX 248 264 {ECO:0000244|PDB:2VYN}.
STRAND 266 276 {ECO:0000244|PDB:2VYN}.
STRAND 281 285 {ECO:0000244|PDB:2VYN}.
HELIX 293 295 {ECO:0000244|PDB:2VYN}.
TURN 298 300 {ECO:0000244|PDB:2VYN}.
STRAND 303 305 {ECO:0000244|PDB:2VYN}.
HELIX 309 316 {ECO:0000244|PDB:2VYN}.
HELIX 318 320 {ECO:0000244|PDB:2VYN}.
STRAND 323 332 {ECO:0000244|PDB:2VYN}.
STRAND 337 347 {ECO:0000244|PDB:2VYN}.
HELIX 351 363 {ECO:0000244|PDB:2VYN}.
TURN 364 369 {ECO:0000244|PDB:2VYN}.
STRAND 370 373 {ECO:0000244|PDB:2VYN}.
HELIX 379 382 {ECO:0000244|PDB:2VYN}.
STRAND 388 392 {ECO:0000244|PDB:2VYN}.
TURN 393 395 {ECO:0000244|PDB:2VYN}.
STRAND 397 400 {ECO:0000244|PDB:2VYN}.
STRAND 403 410 {ECO:0000244|PDB:2VYN}.
HELIX 414 429 {ECO:0000244|PDB:2VYN}.
SEQUENCE 432 AA; 46708 MW; EC5F08F31DC8D35C CRC64;
MSRRDVVLTN VTVVQLRRDP CPCPCPCPCP CPCPVIRPPP PPPKVEEPPP PKEEPPPPPP
PPPPPQIEPE EPKEAPPPPP PPPPPPPPPP PPPPKPAKEL TVGINGFGRI GRLVLRVCME
KGVRVVAVND PFIDPEYMVY MFKYDSTHGR YKGTVEHKNG RLVVDNLEIN VFQCKEPKEI
PWSSVGNPYV VEATGVYLSI EAASGHISSG ARRVIVTAPS PDAPMLVMGV NEKDYNPGSM
TVVSNASCTT NCLAPLAKVI HERFGIVEGL MTTVHAYTAT QKTVDGPSKK DWRGGRGAHQ
NIIPSSTGAA KAVGKVIPEL NGKLTGMAFR VPTPNVSVVD LTCRLAQPAS YTAIKEAVKA
AAKGPMAGIL AYTEDQVVST DFNGDSHSSI FDAKAGIALN DNFVKLVSWY DNEYGYSHRV
VDLLRYMFSR EK


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