VBA4_YEAST
ID VBA4_YEAST Reviewed; 768 AA.
AC Q04602; D6VSA4;
DT 03-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 140.
DE RecName: Full=Vacuolar basic amino acid transporter 4;
GN Name=VBA4; OrderedLocusNames=YDR119W;
OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=559292;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169867;
RA Jacq C., Alt-Moerbe J., Andre B., Arnold W., Bahr A., Ballesta J.P.G.,
RA Bargues M., Baron L., Becker A., Biteau N., Bloecker H., Blugeon C.,
RA Boskovic J., Brandt P., Brueckner M., Buitrago M.J., Coster F.,
RA Delaveau T., del Rey F., Dujon B., Eide L.G., Garcia-Cantalejo J.M.,
RA Goffeau A., Gomez-Peris A., Granotier C., Hanemann V., Hankeln T.,
RA Hoheisel J.D., Jaeger W., Jimenez A., Jonniaux J.-L., Kraemer C.,
RA Kuester H., Laamanen P., Legros Y., Louis E.J., Moeller-Rieker S.,
RA Monnet A., Moro M., Mueller-Auer S., Nussbaumer B., Paricio N., Paulin L.,
RA Perea J., Perez-Alonso M., Perez-Ortin J.E., Pohl T.M., Prydz H.,
RA Purnelle B., Rasmussen S.W., Remacha M.A., Revuelta J.L., Rieger M.,
RA Salom D., Saluz H.P., Saiz J.E., Saren A.-M., Schaefer M., Scharfe M.,
RA Schmidt E.R., Schneider C., Scholler P., Schwarz S., Soler-Mira A.,
RA Urrestarazu L.A., Verhasselt P., Vissers S., Voet M., Volckaert G.,
RA Wagner G., Wambutt R., Wedler E., Wedler H., Woelfl S., Harris D.E.,
RA Bowman S., Brown D., Churcher C.M., Connor R., Dedman K., Gentles S.,
RA Hamlin N., Hunt S., Jones L., McDonald S., Murphy L.D., Niblett D.,
RA Odell C., Oliver K., Rajandream M.A., Richards C., Shore L., Walsh S.V.,
RA Barrell B.G., Dietrich F.S., Mulligan J.T., Allen E., Araujo R., Aviles E.,
RA Berno A., Carpenter J., Chen E., Cherry J.M., Chung E., Duncan M.,
RA Hunicke-Smith S., Hyman R.W., Komp C., Lashkari D., Lew H., Lin D.,
RA Mosedale D., Nakahara K., Namath A., Oefner P., Oh C., Petel F.X.,
RA Roberts D., Schramm S., Schroeder M., Shogren T., Shroff N., Winant A.,
RA Yelton M.A., Botstein D., Davis R.W., Johnston M., Andrews S., Brinkman R.,
RA Cooper J., Ding H., Du Z., Favello A., Fulton L., Gattung S., Greco T.,
RA Hallsworth K., Hawkins J., Hillier L.W., Jier M., Johnson D., Johnston L.,
RA Kirsten J., Kucaba T., Langston Y., Latreille P., Le T., Mardis E.,
RA Menezes S., Miller N., Nhan M., Pauley A., Peluso D., Rifkin L., Riles L.,
RA Taich A., Trevaskis E., Vignati D., Wilcox L., Wohldman P., Vaudin M.,
RA Wilson R., Waterston R., Albermann K., Hani J., Heumann K., Kleine K.,
RA Mewes H.-W., Zollner A., Zaccaria P.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome IV.";
RL Nature 387:75-78(1997).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=24374639; DOI=10.1534/g3.113.008995;
RA Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL G3 (Bethesda) 4:389-398(2014).
RN [3]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX PubMed=14562095; DOI=10.1038/nature02026;
RA Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W.,
RA Weissman J.S., O'Shea E.K.;
RT "Global analysis of protein localization in budding yeast.";
RL Nature 425:686-691(2003).
RN [4]
RP FUNCTION PREDICTION.
RX PubMed=15572352; DOI=10.1074/jbc.m412617200;
RA Shimazu M., Sekito T., Akiyama K., Ohsumi Y., Kakinuma Y.;
RT "A family of basic amino acid transporters of the vacuolar membrane from
RT Saccharomyces cerevisiae.";
RL J. Biol. Chem. 280:4851-4857(2005).
RN [5]
RP TOPOLOGY [LARGE SCALE ANALYSIS].
RC STRAIN=ATCC 208353 / W303-1A;
RX PubMed=16847258; DOI=10.1073/pnas.0604075103;
RA Kim H., Melen K., Oesterberg M., von Heijne G.;
RT "A global topology map of the Saccharomyces cerevisiae membrane proteome.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:11142-11147(2006).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-106, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=ADR376;
RX PubMed=17330950; DOI=10.1021/pr060559j;
RA Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J.,
RA Elias J.E., Gygi S.P.;
RT "Large-scale phosphorylation analysis of alpha-factor-arrested
RT Saccharomyces cerevisiae.";
RL J. Proteome Res. 6:1190-1197(2007).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-99; SER-106 AND SER-192, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=18407956; DOI=10.1074/mcp.m700468-mcp200;
RA Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
RT "A multidimensional chromatography technology for in-depth phosphoproteome
RT analysis.";
RL Mol. Cell. Proteomics 7:1389-1396(2008).
RN [8]
RP SUBCELLULAR LOCATION, AND IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=19001347; DOI=10.1074/mcp.m800372-mcp200;
RA Wiederhold E., Gandhi T., Permentier H.P., Breitling R., Poolman B.,
RA Slotboom D.J.;
RT "The yeast vacuolar membrane proteome.";
RL Mol. Cell. Proteomics 8:380-392(2009).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-62; SER-99; SER-106 AND
RP SER-160, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19779198; DOI=10.1126/science.1172867;
RA Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.;
RT "Global analysis of Cdk1 substrate phosphorylation sites provides insights
RT into evolution.";
RL Science 325:1682-1686(2009).
CC -!- FUNCTION: Transporter required for vacuolar uptake of basic amino
CC acids. {ECO:0000269|PubMed:15572352}.
CC -!- SUBCELLULAR LOCATION: Vacuole membrane {ECO:0000269|PubMed:14562095,
CC ECO:0000269|PubMed:19001347}; Multi-pass membrane protein
CC {ECO:0000269|PubMed:14562095, ECO:0000269|PubMed:19001347}.
CC -!- SIMILARITY: Belongs to the major facilitator superfamily.
CC {ECO:0000305}.
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DR EMBL; Z48758; CAA88672.1; -; Genomic_DNA.
DR EMBL; BK006938; DAA11964.1; -; Genomic_DNA.
DR PIR; S52684; S52684.
DR RefSeq; NP_010404.1; NM_001180427.1.
DR AlphaFoldDB; Q04602; -.
DR BioGRID; 32175; 76.
DR DIP; DIP-8662N; -.
DR IntAct; Q04602; 2.
DR MINT; Q04602; -.
DR STRING; 4932.YDR119W; -.
DR MoonDB; Q04602; Predicted.
DR TCDB; 2.A.1.48.5; the major facilitator superfamily (mfs).
DR iPTMnet; Q04602; -.
DR MaxQB; Q04602; -.
DR PaxDb; Q04602; -.
DR PRIDE; Q04602; -.
DR EnsemblFungi; YDR119W_mRNA; YDR119W; YDR119W.
DR GeneID; 851697; -.
DR KEGG; sce:YDR119W; -.
DR SGD; S000002526; VBA4.
DR VEuPathDB; FungiDB:YDR119W; -.
DR eggNOG; KOG0254; Eukaryota.
DR HOGENOM; CLU_021267_0_0_1; -.
DR InParanoid; Q04602; -.
DR OMA; PMSEHEL; -.
DR BioCyc; YEAST:G3O-29719-MON; -.
DR PRO; PR:Q04602; -.
DR Proteomes; UP000002311; Chromosome IV.
DR RNAct; Q04602; protein.
DR GO; GO:0000329; C:fungal-type vacuole membrane; HDA:SGD.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0015174; F:basic amino acid transmembrane transporter activity; IBA:GO_Central.
DR GO; GO:0022857; F:transmembrane transporter activity; IBA:GO_Central.
DR GO; GO:0015802; P:basic amino acid transport; IBA:GO_Central.
DR GO; GO:0055085; P:transmembrane transport; IBA:GO_Central.
DR Gene3D; 1.20.1250.20; -; 2.
DR InterPro; IPR011701; MFS.
DR InterPro; IPR020846; MFS_dom.
DR InterPro; IPR036259; MFS_trans_sf.
DR Pfam; PF07690; MFS_1; 1.
DR SUPFAM; SSF103473; SSF103473; 1.
DR PROSITE; PS50850; MFS; 1.
PE 1: Evidence at protein level;
KW Amino-acid transport; Coiled coil; Glycoprotein; Membrane; Phosphoprotein;
KW Reference proteome; Transmembrane; Transmembrane helix; Transport; Vacuole.
FT CHAIN 1..768
FT /note="Vacuolar basic amino acid transporter 4"
FT /id="PRO_0000252272"
FT TOPO_DOM 1..252
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 253..273
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 274..282
FT /note="Vacuolar"
FT /evidence="ECO:0000255"
FT TRANSMEM 283..305
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 306..311
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 312..331
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 332..334
FT /note="Vacuolar"
FT /evidence="ECO:0000255"
FT TRANSMEM 335..357
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 358..375
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 376..396
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 397..406
FT /note="Vacuolar"
FT /evidence="ECO:0000255"
FT TRANSMEM 407..427
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 428..447
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 448..468
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 469..481
FT /note="Vacuolar"
FT /evidence="ECO:0000255"
FT TRANSMEM 482..502
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 503..522
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 523..543
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 544..562
FT /note="Vacuolar"
FT /evidence="ECO:0000255"
FT TRANSMEM 563..583
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 584..587
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 588..608
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 609..617
FT /note="Vacuolar"
FT /evidence="ECO:0000255"
FT TRANSMEM 618..638
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 639..653
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 654..674
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 675..734
FT /note="Vacuolar"
FT /evidence="ECO:0000255"
FT TRANSMEM 735..755
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 756..768
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 34..172
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 9..40
FT /evidence="ECO:0000255"
FT COMPBIAS 88..124
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 128..172
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 62
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 99
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956,
FT ECO:0007744|PubMed:19779198"
FT MOD_RES 106
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17330950,
FT ECO:0007744|PubMed:18407956, ECO:0007744|PubMed:19779198"
FT MOD_RES 160
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 192
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956"
FT CARBOHYD 480
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 553
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 768 AA; 85683 MW; 08495E43E011C099 CRC64;
MGKKDRQRKK LREFAKLKNR QRNLRKSVQT LKNEVQREAK VPRTSNQIAL GNDKIEEINE
NSPLLSAPSK QEEVSIPKAV DIDTIDAQPL HEGPKIDDSP QDEVNSIKGK PADKANEDDL
KPPSQHEACG NSALQSSITD FSDRSVSPLQ SITSCNTPMS EHELPVSSSN SFERADDMPV
VQADNQTSSS KSLHIVAPSP EVPVSGDEIT SYGYGSIPQS IGDVENGLNP PYVENTSSDE
LVHDLTRRRI FSSCMCTYLF FIAMDSSIIL VIASKIASEF HELWRLSLVI SAYLLSNAIG
QLVFLKLSLI SSVKLLLCIA QFSFILGGYL SWSSAHFWTF IFARCVTGFG GGSLIALKST
IMNRFSQKND SRYSLSASMI TFAMGVVIGP FMMNLFDSSH GSGWRNAFLI PVPFCLVNAS
IMLADMYSVK STLYGRPTPT LWKRFKNTLL SPDLYEILTL TLFLLCFVQV TSLDLTGLKN
NTMIQALLFS VIIVCGILFF LIETSDTYMN SVISMSLQGD KRLIWTMIGI SFCFAALMCI
IPFGTTYFII VLNLSTLQLA ERLSPFFFSI VLGYFSVSYF WKSKGQNFLL KFVLSGATLL
LYVALMGVSL NLPVWKQYIC LSLPFLGSSM ILTLLSNLYH EYHEQRKSPI SGSIVYCFGA
VGGTVGISLG GYVFHKTLIK LMHEKVMPFS KQGYLKKDLL KIIKHATESS DWVHESAPKF
VFQTLIECYL QACRNVFKLS TLFFTITVVA IFIFNRIHCR SQNCLSLS
