PGK2_PIG
ID PGK2_PIG Reviewed; 417 AA.
AC Q6RI85; Q6RFZ5;
DT 12-APR-2005, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 91.
DE RecName: Full=Phosphoglycerate kinase 2;
DE EC=2.7.2.3;
DE AltName: Full=Phosphoglycerate kinase, testis specific;
GN Name=PGK2 {ECO:0000312|EMBL:AAR89550.1};
OS Sus scrofa (Pig).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX NCBI_TaxID=9823;
RN [1] {ECO:0000305, ECO:0000312|EMBL:AAR89550.1}
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], TISSUE SPECIFICITY, DEVELOPMENTAL
RP STAGE, AND VARIANTS PRO-102 AND LYS-264.
RX PubMed=15599558; DOI=10.1007/s00335-004-2405-1;
RA Chen K., Knorr C., Moser G., Gatphayak K., Brenig B.;
RT "Molecular characterization of the porcine testis-specific phosphoglycerate
RT kinase 2 (PGK2) gene and its association with male fertility.";
RL Mamm. Genome 15:996-1006(2004).
CC -!- FUNCTION: Essential for sperm motility and male fertility but is not
CC required for the completion of spermatogenesis.
CC {ECO:0000250|UniProtKB:P09041}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(2R)-3-phosphoglycerate + ATP = (2R)-3-phospho-glyceroyl
CC phosphate + ADP; Xref=Rhea:RHEA:14801, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:57604, ChEBI:CHEBI:58272, ChEBI:CHEBI:456216; EC=2.7.2.3;
CC Evidence={ECO:0000305};
CC -!- PATHWAY: Carbohydrate degradation; glycolysis; pyruvate from D-
CC glyceraldehyde 3-phosphate: step 2/5.
CC -!- SUBUNIT: Monomer. {ECO:0000250|UniProtKB:P09041}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Testis specific. {ECO:0000269|PubMed:15599558}.
CC -!- DEVELOPMENTAL STAGE: Expression is highest in the adult, lower in a 10
CC month old and very weak in an 8 week old.
CC {ECO:0000269|PubMed:15599558}.
CC -!- POLYMORPHISM: Contains at least 10 polymorphisms. Those that lead to
CC amino acid substitutions may alter protein secondary structures and may
CC influence male fertility. {ECO:0000269|PubMed:15599558}.
CC -!- SIMILARITY: Belongs to the phosphoglycerate kinase family.
CC {ECO:0000255}.
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DR EMBL; AY496962; AAR88362.1; -; mRNA.
DR EMBL; AY500132; AAR89550.1; -; Genomic_DNA.
DR RefSeq; NP_998947.1; NM_213782.1.
DR AlphaFoldDB; Q6RI85; -.
DR SMR; Q6RI85; -.
DR IntAct; Q6RI85; 1.
DR PeptideAtlas; Q6RI85; -.
DR PRIDE; Q6RI85; -.
DR Ensembl; ENSSSCT00000001943; ENSSSCP00000045543; ENSSSCG00000001738.
DR Ensembl; ENSSSCT00005008811; ENSSSCP00005005203; ENSSSCG00005005823.
DR Ensembl; ENSSSCT00030039845; ENSSSCP00030018351; ENSSSCG00030028466.
DR Ensembl; ENSSSCT00040037149; ENSSSCP00040015448; ENSSSCG00040027666.
DR Ensembl; ENSSSCT00050004221; ENSSSCP00050001635; ENSSSCG00050003199.
DR Ensembl; ENSSSCT00055011631; ENSSSCP00055009207; ENSSSCG00055005986.
DR Ensembl; ENSSSCT00060065813; ENSSSCP00060028173; ENSSSCG00060048462.
DR Ensembl; ENSSSCT00065007143; ENSSSCP00065003084; ENSSSCG00065005263.
DR Ensembl; ENSSSCT00070040987; ENSSSCP00070034394; ENSSSCG00070020628.
DR GeneID; 396673; -.
DR KEGG; ssc:396673; -.
DR CTD; 5232; -.
DR VGNC; VGNC:91351; PGK2.
DR GeneTree; ENSGT00390000008820; -.
DR InParanoid; Q6RI85; -.
DR OMA; DMIFDIG; -.
DR OrthoDB; 838642at2759; -.
DR BRENDA; 2.7.2.3; 6170.
DR UniPathway; UPA00109; UER00185.
DR Proteomes; UP000008227; Chromosome 7.
DR Proteomes; UP000314985; Chromosome 7.
DR Bgee; ENSSSCG00000001738; Expressed in testis and 4 other tissues.
DR ExpressionAtlas; Q6RI85; differential.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0035686; C:sperm fibrous sheath; IBA:GO_Central.
DR GO; GO:0043531; F:ADP binding; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; ISS:UniProtKB.
DR GO; GO:0004618; F:phosphoglycerate kinase activity; ISS:UniProtKB.
DR GO; GO:0006094; P:gluconeogenesis; IBA:GO_Central.
DR GO; GO:0006096; P:glycolytic process; IBA:GO_Central.
DR GO; GO:0016310; P:phosphorylation; ISS:UniProtKB.
DR CDD; cd00318; Phosphoglycerate_kinase; 1.
DR Gene3D; 3.40.50.1260; -; 3.
DR HAMAP; MF_00145; Phosphoglyc_kinase; 1.
DR InterPro; IPR001576; Phosphoglycerate_kinase.
DR InterPro; IPR015911; Phosphoglycerate_kinase_CS.
DR InterPro; IPR015824; Phosphoglycerate_kinase_N.
DR InterPro; IPR036043; Phosphoglycerate_kinase_sf.
DR PANTHER; PTHR11406; PTHR11406; 1.
DR Pfam; PF00162; PGK; 1.
DR PIRSF; PIRSF000724; Pgk; 1.
DR PRINTS; PR00477; PHGLYCKINASE.
DR SUPFAM; SSF53748; SSF53748; 1.
DR PROSITE; PS00111; PGLYCERATE_KINASE; 1.
PE 2: Evidence at transcript level;
KW Acetylation; ATP-binding; Cytoplasm; Glycolysis; Kinase;
KW Nucleotide-binding; Phosphoprotein; Reference proteome; Transferase.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:P00558"
FT CHAIN 2..417
FT /note="Phosphoglycerate kinase 2"
FT /id="PRO_0000145838"
FT BINDING 24..26
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 39
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 63..66
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 123
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 171
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 220
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 344
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 373..376
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0000250|UniProtKB:P00558"
FT MOD_RES 2
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P00558"
FT MOD_RES 4
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P00558"
FT MOD_RES 11
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P00558"
FT MOD_RES 75
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P00558"
FT MOD_RES 86
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P00558"
FT MOD_RES 97
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P00558"
FT MOD_RES 131
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P00558"
FT MOD_RES 146
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P00558"
FT MOD_RES 196
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:P00558"
FT MOD_RES 199
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P00558"
FT MOD_RES 267
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P00558"
FT MOD_RES 291
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P00558"
FT VARIANT 102
FT /note="S -> P (in SNP-A; possible loss of CK2
FT phosphorylation site)"
FT /evidence="ECO:0000269|PubMed:15599558"
FT VARIANT 264
FT /note="T -> K (in SNP-B; increased semen volume in
FT ejaculate)"
FT /evidence="ECO:0000269|PubMed:15599558"
FT CONFLICT 324
FT /note="Y -> N (in Ref. 1; AAR89550)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 417 AA; 44895 MW; 1DB0048021528BA0 CRC64;
MSLSKKLTLD KLDVKGKRVI MRVDFNVPMK RNQVTNNQRI KASLPSIRYC LDNGARSVVL
MSHLGRPDGV AMPDKYSLEP VAAELKSLLG KDVLFLKDCV GSEAEQACAN PPAGSVILLE
NLRFHVEEEG KGQDPSGNKL KAEPDKVEAF RASLSKLGDV YVNDAFGTAH RAHSSMVGVN
LPQKASGFLM KKELDYFAKA LENPERPFLA ILGGAKVADK IQLIKNMLDK VNEMIIGGGM
AFTFLKVLNN MEIGASLFDK EGATIVKEIM AKAEKNRVNI TFPVDFVIAD KFEENAKVGQ
ATVASGIPAG WVALDCGPET NKKYAQVVAR AKLIVWNGPL GVFEWDAFAN GTKALMDEIV
KATSKGCITI IGGGDTATCC AKWNTEDKVS HVSTGGGASL ELLEGKVLPG VEALSNL
