ID VTC4_SCHPO Reviewed; 721 AA. AC P78810; Q1L850; DT 10-FEB-2009, integrated into UniProtKB/Swiss-Prot. DT 01-JUN-2000, sequence version 2. DT 27-MAR-2024, entry version 127. DE RecName: Full=Vacuolar transporter chaperone complex subunit 4; DE AltName: Full=Polyphosphate kinase; DE AltName: Full=SPX-dependent polyphosphate polymerase VTC subunit 4; DE AltName: Full=Vacuolar membrane polyphosphate polymerase catalytic subunit; DE Short=PolyP polymerase; DE EC=2.7.4.1 {ECO:0000250|UniProtKB:P47075}; GN Name=vtc4; ORFNames=SPCC1322.14c; OS Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast). OC Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina; OC Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae; OC Schizosaccharomyces. OX NCBI_TaxID=284812; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=972 / ATCC 24843; RX PubMed=11859360; DOI=10.1038/nature724; RA Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A., RA Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S., RA Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M., RA Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S., RA Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S., RA Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D., RA Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P., RA Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K., RA O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M., RA Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N., RA Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A., RA Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R., RA Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M., RA Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A., RA Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A., RA Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H., RA Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S., RA Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C., RA Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A., RA Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M., RA del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S., RA Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R., RA Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G., RA Nurse P.; RT "The genome sequence of Schizosaccharomyces pombe."; RL Nature 415:871-880(2002). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA] OF 192-721. RC STRAIN=PR745; RX PubMed=9501991; DOI=10.1093/dnares/4.6.363; RA Yoshioka S., Kato K., Nakai K., Okayama H., Nojima H.; RT "Identification of open reading frames in Schizosaccharomyces pombe RT cDNAs."; RL DNA Res. 4:363-369(1997). RN [3] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-495; THR-497; SER-501; RP THR-534 AND SER-546, AND IDENTIFICATION BY MASS SPECTROMETRY. RX PubMed=18257517; DOI=10.1021/pr7006335; RA Wilson-Grady J.T., Villen J., Gygi S.P.; RT "Phosphoproteome analysis of fission yeast."; RL J. Proteome Res. 7:1088-1097(2008). CC -!- FUNCTION: Catalytic subunit of the vacuolar transporter chaperone (VTC) CC complex. The VTC complex acts as a vacuolar polyphosphate polymerase CC that catalyzes the synthesis of inorganic polyphosphate (polyP) via CC transfer of phosphate from ATP to a growing polyP chain, releasing ADP. CC VTC exposes its catalytic domain vtc4 to the cytosol, where the growing CC polyP chain winds through a tunnel-shaped pocket, integrating CC cytoplasmic polymer synthesis with polyP membrane translocation. The CC VTC complex carries 9 vacuolar transmembrane domains, which are likely CC to constitute the translocation channel into the organelle lumen. PolyP CC synthesis is tightly coupled to its transport into the vacuole lumen, CC in order to avoid otherwise toxic intermediates in the cytosol, and it CC depends on the proton gradient across the membrane, formed by V-ATPase. CC The VTC complex also plays a role in vacuolar membrane fusion. CC {ECO:0000250|UniProtKB:P47075}. CC -!- CATALYTIC ACTIVITY: CC Reaction=[phosphate](n) + ATP = [phosphate](n+1) + ADP; CC Xref=Rhea:RHEA:19573, Rhea:RHEA-COMP:9859, Rhea:RHEA-COMP:14280, CC ChEBI:CHEBI:16838, ChEBI:CHEBI:30616, ChEBI:CHEBI:456216; EC=2.7.4.1; CC Evidence={ECO:0000250|UniProtKB:P47075}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:19574; CC Evidence={ECO:0000250|UniProtKB:P47075}; CC -!- COFACTOR: CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035; CC Evidence={ECO:0000250|UniProtKB:P47075}; CC -!- ACTIVITY REGULATION: Activity of the enzyme is Mn(2+)-dependent and CC enhanced in the presence of pyrophosphate (PPi). CC {ECO:0000250|UniProtKB:P47075}. CC -!- SUBUNIT: The VTC core complex is an integral membrane heterooligomer CC composed of at least the catalytic subunit vtc4 and the accessory CC subunits vtc1 and vtc2. vtc1 is a small membrane protein without CC hydrophilic domain. Vtc2 and vtc4 are related and have 2 hydrophilic CC domains that face the cytosol, an N-terminal SPX domain and the central CC core domain. The central core in vtc4 is the catalytic domain. CC {ECO:0000250|UniProtKB:P47075}. CC -!- SUBCELLULAR LOCATION: Vacuole membrane {ECO:0000250|UniProtKB:P47075}; CC Multi-pass membrane protein {ECO:0000255}. CC -!- DOMAIN: The SPX domain has very high affinity for inositol CC polyphosphates. SPX domains may integrate inositol pyrophosphates (PP- CC InsP)-dependent signaling to adapt cytosolic phosphate concentrations CC to different metabolic situations. {ECO:0000250|UniProtKB:P47075}. CC -!- SIMILARITY: Belongs to the VTC4 family. {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; CU329672; CAA22867.1; -; Genomic_DNA. DR EMBL; D89159; BAA13821.1; -; mRNA. DR PIR; T40945; T40945. DR PIR; T42520; T42520. DR RefSeq; NP_588142.1; NM_001023132.2. DR AlphaFoldDB; P78810; -. DR SMR; P78810; -. DR BioGRID; 275369; 8. DR STRING; 284812.P78810; -. DR iPTMnet; P78810; -. DR MaxQB; P78810; -. DR PaxDb; 4896-SPCC1322-14c-1; -. DR EnsemblFungi; SPCC1322.14c.1; SPCC1322.14c.1:pep; SPCC1322.14c. DR GeneID; 2538788; -. DR KEGG; spo:SPCC1322.14c; -. DR PomBase; SPCC1322.14c; vtc4. DR VEuPathDB; FungiDB:SPCC1322.14c; -. DR eggNOG; KOG1161; Eukaryota. DR eggNOG; KOG4580; Eukaryota. DR HOGENOM; CLU_009308_0_0_1; -. DR InParanoid; P78810; -. DR OMA; AGGKQQN; -. DR PhylomeDB; P78810; -. DR PRO; PR:P78810; -. DR Proteomes; UP000002485; Chromosome III. DR GO; GO:0000329; C:fungal-type vacuole membrane; IBA:GO_Central. DR GO; GO:0033254; C:vacuolar transporter chaperone complex; IBA:GO_Central. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW. DR GO; GO:0006112; P:energy reserve metabolic process; IC:PomBase. DR GO; GO:0016237; P:microautophagy; IBA:GO_Central. DR GO; GO:0006799; P:polyphosphate biosynthetic process; ISO:PomBase. DR GO; GO:0006797; P:polyphosphate metabolic process; IBA:GO_Central. DR GO; GO:0007034; P:vacuolar transport; IBA:GO_Central. DR GO; GO:0042144; P:vacuole fusion, non-autophagic; IBA:GO_Central. DR CDD; cd07751; PolyPPase_VTC4_like; 1. DR CDD; cd14480; SPX_VTC2_like; 1. DR Gene3D; 3.20.100.30; VTC, catalytic tunnel domain; 1. DR InterPro; IPR003807; DUF202. DR InterPro; IPR004331; SPX_dom. DR InterPro; IPR018966; VTC_domain. DR InterPro; IPR042267; VTC_sf. DR PANTHER; PTHR46140; VACUOLAR TRANSPORTER CHAPERONE 1-RELATED; 1. DR PANTHER; PTHR46140:SF1; VACUOLAR TRANSPORTER CHAPERONE 4; 1. DR Pfam; PF02656; DUF202; 1. DR Pfam; PF09359; VTC; 1. DR PROSITE; PS51382; SPX; 1. PE 1: Evidence at protein level; KW ATP-binding; Chaperone; Manganese; Membrane; Metal-binding; KW Nucleotide-binding; Phosphoprotein; Reference proteome; Transferase; KW Transmembrane; Transmembrane helix; Vacuole. FT CHAIN 1..721 FT /note="Vacuolar transporter chaperone complex subunit 4" FT /id="PRO_0000363396" FT TOPO_DOM 1..631 FT /note="Cytoplasmic" FT /evidence="ECO:0000250|UniProtKB:P47075" FT TRANSMEM 632..652 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 653..657 FT /note="Vacuolar" FT /evidence="ECO:0000250|UniProtKB:P47075" FT TRANSMEM 658..678 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 679..697 FT /note="Cytoplasmic" FT /evidence="ECO:0000250|UniProtKB:P47075" FT TRANSMEM 698..718 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 719..721 FT /note="Vacuolar" FT /evidence="ECO:0000250|UniProtKB:P47075" FT DOMAIN 1..146 FT /note="SPX" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00714" FT REGION 490..547 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 490..515 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 526..547 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT ACT_SITE 453 FT /evidence="ECO:0000250|UniProtKB:P47075" FT BINDING 198 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000250|UniProtKB:P47075" FT BINDING 262 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000250|UniProtKB:P47075" FT BINDING 264 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000250|UniProtKB:P47075" FT BINDING 279 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000250|UniProtKB:P47075" FT BINDING 292 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000250|UniProtKB:P47075" FT BINDING 357 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000250|UniProtKB:P47075" FT BINDING 359 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000250|UniProtKB:P47075" FT BINDING 421 FT /ligand="Mn(2+)" FT /ligand_id="ChEBI:CHEBI:29035" FT /evidence="ECO:0000250|UniProtKB:P47075" FT MOD_RES 495 FT /note="Phosphoserine" FT /evidence="ECO:0000269|PubMed:18257517" FT MOD_RES 497 FT /note="Phosphothreonine" FT /evidence="ECO:0000269|PubMed:18257517" FT MOD_RES 501 FT /note="Phosphoserine" FT /evidence="ECO:0000269|PubMed:18257517" FT MOD_RES 534 FT /note="Phosphothreonine" FT /evidence="ECO:0000269|PubMed:18257517" FT MOD_RES 546 FT /note="Phosphoserine" FT /evidence="ECO:0000269|PubMed:18257517" FT CONFLICT 580 FT /note="K -> R (in Ref. 2; BAA13821)" FT /evidence="ECO:0000305" FT CONFLICT 714 FT /note="N -> Y (in Ref. 2; BAA13821)" FT /evidence="ECO:0000305" SQ SEQUENCE 721 AA; 83635 MW; DF4471E8FC0A6BCF CRC64; MKFGQLLKET LMYEYKYSYV NYDKLKKEIK RRNDQGGWSE EDESDFVELL EKELDKVYSF QKNKSAEVME RIRFCEEQTD EVVRRLDSDN PPNENDFAIL ETELTDIMAT VHDLAKFSEL NYTAFYKIIK KHDKHTGWIL KPVFAARLNA KPFFKEQYDL LVVKLSKLYD FVRTRGSPIK GDSAAGGTQQ NFVRQTTKYW VHPNNVTELK IYILKHLPVL VFNPNKEFAR EDAAITSIYY DNDDLDFYLG RLEKREGAEA IRLRWYGNMD NNNIFVERKT HREDWTGEKS VKARFPLKEK YVNAFLRGDY TVEEAFAKMR KDGKKSLKEI ESLERLAKEV QYTVLSRGMK PYVRSFYERT AFQLPGDARV RISLDTNLSL IREDGPSRAG NNWRRMDIGI DYPFDQLPDE DIVRFPYAIL EVKLQTQFGQ DPPEWVNNLV NSHLVEAVPK FSKFIHGVST LFYDRVTLLP YWFPQMDIDI RKPATHTFIQ GRSQSGTHSS SVSANVLTDS ENTPIHADGD NYVDEESRIG SSSTRNDNST FQTSDSFQEL DERTNLLDIS KRKGRDSFVA ALNSRLKDIK DSFFLETVPK FEEPTEPTVI YEQKYVSPPG KRIYVPVRVE PKTYFALERT YLDYLRYSIL MGSIGITLFS FAKTRSGILG AASFTLVALF AIFYSTFLYL WRAVNIAKHN AVRYDDRFGP TAICVITFAA ISANVILNFN A //