ID PGK2_MOUSE Reviewed; 417 AA. AC P09041; Q5RKV3; Q6P8V2; DT 01-NOV-1988, integrated into UniProtKB/Swiss-Prot. DT 27-JUL-2011, sequence version 4. DT 24-JAN-2024, entry version 176. DE RecName: Full=Phosphoglycerate kinase 2; DE EC=2.7.2.3 {ECO:0000269|PubMed:2823118}; DE AltName: Full=Phosphoglycerate kinase, testis specific; GN Name=Pgk2; Synonyms=Pgk-2; 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 [GENOMIC DNA / MRNA], CATALYTIC ACTIVITY, AND TISSUE RP SPECIFICITY. RX PubMed=2823118; DOI=10.1128/mcb.7.9.3107-3112.1987; RA Boer P.H., Adra C.N., Lau Y.-F.C., McBurney M.W.; RT "The testis-specific phosphoglycerate kinase gene pgk-2 is a recruited RT retroposon."; RL Mol. Cell. Biol. 7:3107-3112(1987). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=C57BL/6J; TISSUE=Testis; RX PubMed=16141072; DOI=10.1126/science.1112014; RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J., RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.; RT "The transcriptional landscape of the mammalian genome."; RL Science 309:1559-1563(2005). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.; RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases. RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Testis; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA project: RT the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [5] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-6. RX PubMed=2166582; DOI=10.1016/0167-4781(90)90106-c; RA Tamaru M., Nagao Y., Taira M., Tatibana M., Masamune Y., Nakanishi Y.; RT "Selective activation of testis-specific genes in cultured rat RT spermatogenic cells."; RL Biochim. Biophys. Acta 1049:331-338(1990). RN [6] RP TISSUE SPECIFICITY. RX PubMed=3453121; DOI=10.1038/326501a0; RA McCarrey J.R., Thomas K.; RT "Human testis-specific PGK gene lacks introns and possesses characteristics RT of a processed gene."; RL Nature 326:501-504(1987). RN [7] RP FUNCTION, DISRUPTION PHENOTYPE, AND TISSUE SPECIFICITY. RX PubMed=19759366; DOI=10.1095/biolreprod.109.079699; RA Danshina P.V., Geyer C.B., Dai Q., Goulding E.H., Willis W.D., Kitto G.B., RA McCarrey J.R., Eddy E.M., O'Brien D.A.; RT "Phosphoglycerate kinase 2 (PGK2) is essential for sperm function and male RT fertility in mice."; RL Biol. Reprod. 82:136-145(2010). RN [8] 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). RN [9] RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 2-417 ALONE AND IN COMPLEX WITH RP PHOSPHOGLYCERATE AND ATP, SUBUNIT, AND SUBSTRATE-BINDING SITES. RX PubMed=18004764; DOI=10.1002/prot.21801; RA Sawyer G.M., Monzingo A.F., Poteet E.C., O'Brien D.A., Robertus J.D.; RT "X-ray analysis of phosphoglycerate kinase 2, a sperm-specific isoform from RT Mus musculus."; RL Proteins 71:1134-1144(2008). CC -!- FUNCTION: Essential for sperm motility and male fertility but is not CC required for the completion of spermatogenesis (PubMed:19759366). CC {ECO:0000269|PubMed:19759366}. 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|PubMed:2823118}; CC -!- PATHWAY: Carbohydrate degradation; glycolysis; pyruvate from D- CC glyceraldehyde 3-phosphate: step 2/5. CC -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:18004764}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. CC -!- TISSUE SPECIFICITY: Testis and sperm. Localized on the principle piece CC in the sperm (at protein level). Testis-specific. CC {ECO:0000269|PubMed:19759366, ECO:0000269|PubMed:3453121}. CC -!- DISRUPTION PHENOTYPE: Mice display greatly reduced ATP levels in sperm, CC severely impaired sperm motility and are infertile. No alteration in CC testis histology, sperm counts, or sperm ultrastructure seen. CC {ECO:0000269|PubMed:19759366}. CC -!- SIMILARITY: Belongs to the phosphoglycerate kinase family. CC {ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; M17299; AAA39920.1; -; Genomic_DNA. DR EMBL; M18654; AAA39921.1; -; mRNA. DR EMBL; AK133436; BAE21656.1; -; mRNA. DR EMBL; CH466559; EDL23381.1; -; Genomic_DNA. DR EMBL; BC052343; AAH52343.1; -; mRNA. DR EMBL; BC061054; AAH61054.1; -; mRNA. DR EMBL; X55310; CAA39014.1; -; Genomic_DNA. DR CCDS; CCDS28782.1; -. DR PIR; A27775; A27775. DR RefSeq; NP_112467.2; NM_031190.2. DR PDB; 2P9Q; X-ray; 2.70 A; A/B=2-417. DR PDB; 2P9T; X-ray; 2.00 A; A=2-417. DR PDB; 2PAA; X-ray; 2.70 A; A/B=2-417. DR PDBsum; 2P9Q; -. DR PDBsum; 2P9T; -. DR PDBsum; 2PAA; -. DR AlphaFoldDB; P09041; -. DR SMR; P09041; -. DR BioGRID; 202135; 14. DR IntAct; P09041; 1. DR STRING; 10090.ENSMUSP00000033585; -. DR GlyGen; P09041; 1 site, 1 O-linked glycan (1 site). DR iPTMnet; P09041; -. DR PhosphoSitePlus; P09041; -. DR SwissPalm; P09041; -. DR REPRODUCTION-2DPAGE; IPI00555060; -. DR REPRODUCTION-2DPAGE; P09041; -. DR EPD; P09041; -. DR jPOST; P09041; -. DR MaxQB; P09041; -. DR PaxDb; 10090-ENSMUSP00000033585; -. DR PeptideAtlas; P09041; -. DR ProteomicsDB; 288106; -. DR Pumba; P09041; -. DR Antibodypedia; 30847; 269 antibodies from 29 providers. DR DNASU; 18663; -. DR Ensembl; ENSMUST00000033585.7; ENSMUSP00000033585.5; ENSMUSG00000031233.7. DR GeneID; 18663; -. DR KEGG; mmu:18663; -. DR UCSC; uc008cof.2; mouse. DR AGR; MGI:97563; -. DR CTD; 5232; -. DR MGI; MGI:97563; Pgk2. DR VEuPathDB; HostDB:ENSMUSG00000031233; -. DR eggNOG; KOG1367; Eukaryota. DR GeneTree; ENSGT00390000008820; -. DR HOGENOM; CLU_025427_0_0_1; -. DR InParanoid; P09041; -. DR OMA; SCKFAFG; -. DR OrthoDB; 5477183at2759; -. DR PhylomeDB; P09041; -. DR TreeFam; TF300489; -. DR BRENDA; 2.7.2.3; 3474. DR Reactome; R-MMU-70171; Glycolysis. DR Reactome; R-MMU-70263; Gluconeogenesis. DR SABIO-RK; P09041; -. DR UniPathway; UPA00109; UER00185. DR BioGRID-ORCS; 18663; 2 hits in 76 CRISPR screens. DR EvolutionaryTrace; P09041; -. DR PRO; PR:P09041; -. DR Proteomes; UP000000589; Chromosome 17. DR RNAct; P09041; Protein. DR Bgee; ENSMUSG00000031233; Expressed in spermatid and 10 other cell types or tissues. DR GO; GO:0005929; C:cilium; IDA:MGI. DR GO; GO:0005829; C:cytosol; IBA:GO_Central. DR GO; GO:0035686; C:sperm fibrous sheath; IDA:MGI. 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; IDA:MGI. DR GO; GO:0030317; P:flagellated sperm motility; IMP:MGI. DR GO; GO:0006094; P:gluconeogenesis; IBA:GO_Central. DR GO; GO:0006096; P:glycolytic process; IMP:MGI. DR GO; GO:0016310; P:phosphorylation; ISS:UniProtKB. DR CDD; cd00318; Phosphoglycerate_kinase; 1. DR DisProt; DP02749; -. DR Gene3D; 3.40.50.1260; Phosphoglycerate kinase, N-terminal domain; 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; PHOSPHOGLYCERATE KINASE; 1. DR PANTHER; PTHR11406:SF10; PHOSPHOGLYCERATE KINASE 2; 1. DR Pfam; PF00162; PGK; 1. DR PIRSF; PIRSF000724; Pgk; 1. DR PRINTS; PR00477; PHGLYCKINASE. DR SUPFAM; SSF53748; Phosphoglycerate kinase; 1. DR PROSITE; PS00111; PGLYCERATE_KINASE; 1. DR Genevisible; P09041; MM. PE 1: Evidence at protein level; KW 3D-structure; Acetylation; ATP-binding; Cytoplasm; Glycolysis; Kinase; KW Nucleotide-binding; Phosphoprotein; Reference proteome; Transferase. FT CHAIN 1..417 FT /note="Phosphoglycerate kinase 2" FT /id="PRO_0000145836" FT BINDING 24..26 FT /ligand="substrate" FT BINDING 39 FT /ligand="substrate" FT BINDING 63..66 FT /ligand="substrate" FT BINDING 123 FT /ligand="substrate" FT BINDING 171 FT /ligand="substrate" FT BINDING 220 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000269|PubMed:18004764" FT BINDING 313 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000269|PubMed:18004764" FT BINDING 344 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000269|PubMed:18004764" FT BINDING 373..376 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000269|PubMed:18004764" 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 48 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 CONFLICT 151 FT /note="Q -> R (in Ref. 1; AAA39920)" FT /evidence="ECO:0000305" FT CONFLICT 176 FT /note="T -> M (in Ref. 1; AAA39920/AAA39921)" FT /evidence="ECO:0000305" FT HELIX 9..11 FT /evidence="ECO:0007829|PDB:2P9T" FT STRAND 18..22 FT /evidence="ECO:0007829|PDB:2P9T" FT STRAND 29..32 FT /evidence="ECO:0007829|PDB:2P9Q" FT STRAND 33..35 FT /evidence="ECO:0007829|PDB:2P9T" FT HELIX 38..52 FT /evidence="ECO:0007829|PDB:2P9T" FT STRAND 56..61 FT /evidence="ECO:0007829|PDB:2P9T" FT HELIX 73..76 FT /evidence="ECO:0007829|PDB:2P9T" FT HELIX 79..89 FT /evidence="ECO:0007829|PDB:2P9T" FT STRAND 93..95 FT /evidence="ECO:0007829|PDB:2P9Q" FT STRAND 99..101 FT /evidence="ECO:0007829|PDB:2P9T" FT HELIX 102..109 FT /evidence="ECO:0007829|PDB:2P9T" FT STRAND 115..118 FT /evidence="ECO:0007829|PDB:2P9T" FT HELIX 122..124 FT /evidence="ECO:0007829|PDB:2P9T" FT TURN 126..130 FT /evidence="ECO:0007829|PDB:2P9T" FT STRAND 131..133 FT /evidence="ECO:0007829|PDB:2P9T" FT STRAND 139..141 FT /evidence="ECO:0007829|PDB:2P9T" FT HELIX 144..155 FT /evidence="ECO:0007829|PDB:2P9T" FT STRAND 159..163 FT /evidence="ECO:0007829|PDB:2P9T" FT HELIX 166..168 FT /evidence="ECO:0007829|PDB:2P9T" FT HELIX 174..177 FT /evidence="ECO:0007829|PDB:2P9T" FT STRAND 184..186 FT /evidence="ECO:0007829|PDB:2P9T" FT HELIX 188..202 FT /evidence="ECO:0007829|PDB:2P9T" FT STRAND 206..213 FT /evidence="ECO:0007829|PDB:2P9T" FT HELIX 218..220 FT /evidence="ECO:0007829|PDB:2P9T" FT HELIX 221..227 FT /evidence="ECO:0007829|PDB:2P9T" FT TURN 228..230 FT /evidence="ECO:0007829|PDB:2P9T" FT STRAND 232..237 FT /evidence="ECO:0007829|PDB:2P9T" FT HELIX 240..249 FT /evidence="ECO:0007829|PDB:2P9T" FT STRAND 253..256 FT /evidence="ECO:0007829|PDB:2P9Q" FT HELIX 260..263 FT /evidence="ECO:0007829|PDB:2P9T" FT HELIX 266..275 FT /evidence="ECO:0007829|PDB:2P9T" FT STRAND 279..281 FT /evidence="ECO:0007829|PDB:2P9T" FT STRAND 284..293 FT /evidence="ECO:0007829|PDB:2P9T" FT STRAND 298..302 FT /evidence="ECO:0007829|PDB:2P9T" FT TURN 303..305 FT /evidence="ECO:0007829|PDB:2P9T" FT STRAND 312..316 FT /evidence="ECO:0007829|PDB:2P9T" FT HELIX 318..329 FT /evidence="ECO:0007829|PDB:2P9T" FT STRAND 332..338 FT /evidence="ECO:0007829|PDB:2P9T" FT HELIX 346..348 FT /evidence="ECO:0007829|PDB:2P9T" FT HELIX 350..364 FT /evidence="ECO:0007829|PDB:2P9T" FT STRAND 368..371 FT /evidence="ECO:0007829|PDB:2P9T" FT HELIX 375..382 FT /evidence="ECO:0007829|PDB:2P9T" FT TURN 386..388 FT /evidence="ECO:0007829|PDB:2P9T" FT STRAND 389..392 FT /evidence="ECO:0007829|PDB:2P9T" FT HELIX 396..402 FT /evidence="ECO:0007829|PDB:2P9T" FT TURN 403..405 FT /evidence="ECO:0007829|PDB:2P9T" FT HELIX 409..412 FT /evidence="ECO:0007829|PDB:2P9T" SQ SEQUENCE 417 AA; 44853 MW; BC3FACE559798B53 CRC64; MALSAKLTLD KVDLKGKRVI MRVDFNVPMK NNQITNNQRI KAAIPSIKHC LDNGAKSVVL MSHLGRPDGI PMPDKYSLEP VADELKSLLN KDVIFLKDCV GPEVEQACAN PDNGSIILLE NLRFHVEEEG KGKDSSGKKI SADPAKVEAF QASLSKLGDV YVNDAFGTAH RAHSSTVGVN LPQKASGFLM KKELDYFSKA LEKPERPFLA ILGGAKVKDK IQLIKNMLDK VNFMIIGGGM AYTFLKELKN MQIGASLFDE EGATIVKEIM EKAEKNGVKI VFPVDFVTGD KFDENAKVGQ ATIESGIPSG WMGLDCGPES IKINAQIVAQ AKLIVWNGPI GVFEWDAFAK GTKALMDEVV KATSNGCVTI IGGGDTATCC AKWGTEDKVS HVSTGGGASL ELLEGKILPG VEALSNM //