VRP1_YEAST
ID VRP1_YEAST Reviewed; 817 AA.
AC P37370; D6VYX7; Q06133;
DT 01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 2.
DT 03-AUG-2022, entry version 172.
DE RecName: Full=Verprolin;
GN Name=VRP1; Synonyms=END5, MDP2; OrderedLocusNames=YLR337C;
GN ORFNames=L8300.13;
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 [GENOMIC DNA].
RC STRAIN=A364;
RX PubMed=7968536; DOI=10.1111/j.1365-2958.1993.tb00930.x;
RA Donnelly S.F.H., Pocklington M.J., Pallota D., Orr E.;
RT "A proline-rich protein, verprolin, involved in cytoskeletal organization
RT and cellular growth in the yeast Saccharomyces cerevisiae.";
RL Mol. Microbiol. 10:585-596(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169871;
RA Johnston M., Hillier L.W., Riles L., Albermann K., Andre B., Ansorge W.,
RA Benes V., Brueckner M., Delius H., Dubois E., Duesterhoeft A.,
RA Entian K.-D., Floeth M., Goffeau A., Hebling U., Heumann K.,
RA Heuss-Neitzel D., Hilbert H., Hilger F., Kleine K., Koetter P., Louis E.J.,
RA Messenguy F., Mewes H.-W., Miosga T., Moestl D., Mueller-Auer S.,
RA Nentwich U., Obermaier B., Piravandi E., Pohl T.M., Portetelle D.,
RA Purnelle B., Rechmann S., Rieger M., Rinke M., Rose M., Scharfe M.,
RA Scherens B., Scholler P., Schwager C., Schwarz S., Underwood A.P.,
RA Urrestarazu L.A., Vandenbol M., Verhasselt P., Vierendeels F., Voet M.,
RA Volckaert G., Voss H., Wambutt R., Wedler E., Wedler H., Zimmermann F.K.,
RA Zollner A., Hani J., Hoheisel J.D.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XII.";
RL Nature 387:87-90(1997).
RN [3]
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 [4]
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 [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-519 AND SER-762, 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 [6]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS].
RX PubMed=19756047; DOI=10.1038/msb.2009.64;
RA Kung L.A., Tao S.-C., Qian J., Smith M.G., Snyder M., Zhu H.;
RT "Global analysis of the glycoproteome in Saccharomyces cerevisiae reveals
RT new roles for protein glycosylation in eukaryotes.";
RL Mol. Syst. Biol. 5:308-308(2009).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-762, AND IDENTIFICATION BY
RP 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: Involved in cytoskeletal organization and cellular growth.
CC May exert its effects on the cytoskeleton directly, or indirectly via
CC proline-binding proteins (e.g. profilin) or proteins possessing SH3
CC domains.
CC -!- INTERACTION:
CC P37370; Q05080: HOF1; NbExp=4; IntAct=EBI-20502, EBI-5412;
CC P37370; Q12446: LAS17; NbExp=6; IntAct=EBI-20502, EBI-10022;
CC P37370; P36006: MYO3; NbExp=11; IntAct=EBI-20502, EBI-11670;
CC P37370; Q04439: MYO5; NbExp=19; IntAct=EBI-20502, EBI-11687;
CC P37370; P39743: RVS167; NbExp=3; IntAct=EBI-20502, EBI-14500;
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton
CC {ECO:0000305|PubMed:14562095}.
CC -!- PTM: N-glycosylated. {ECO:0000269|PubMed:19756047}.
CC -!- SIMILARITY: Belongs to the verprolin family. {ECO:0000305}.
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DR EMBL; Z26645; CAA81388.1; -; Genomic_DNA.
DR EMBL; U19028; AAB67263.1; -; Genomic_DNA.
DR EMBL; BK006945; DAA09643.1; -; Genomic_DNA.
DR PIR; S51342; S51342.
DR RefSeq; NP_013441.1; NM_001182226.1.
DR AlphaFoldDB; P37370; -.
DR BioGRID; 31601; 643.
DR DIP; DIP-860N; -.
DR ELM; P37370; -.
DR IntAct; P37370; 25.
DR MINT; P37370; -.
DR STRING; 4932.YLR337C; -.
DR MoonDB; P37370; Predicted.
DR iPTMnet; P37370; -.
DR MaxQB; P37370; -.
DR PaxDb; P37370; -.
DR PRIDE; P37370; -.
DR EnsemblFungi; YLR337C_mRNA; YLR337C; YLR337C.
DR GeneID; 851051; -.
DR KEGG; sce:YLR337C; -.
DR SGD; S000004329; VRP1.
DR VEuPathDB; FungiDB:YLR337C; -.
DR eggNOG; KOG4462; Eukaryota.
DR GeneTree; ENSGT00940000171387; -.
DR HOGENOM; CLU_386454_0_0_1; -.
DR InParanoid; P37370; -.
DR OMA; GSFTQMF; -.
DR BioCyc; YEAST:G3O-32416-MON; -.
DR PRO; PR:P37370; -.
DR Proteomes; UP000002311; Chromosome XII.
DR RNAct; P37370; protein.
DR GO; GO:0030479; C:actin cortical patch; IDA:SGD.
DR GO; GO:0005935; C:cellular bud neck; IDA:SGD.
DR GO; GO:0000131; C:incipient cellular bud site; IDA:SGD.
DR GO; GO:0043332; C:mating projection tip; HDA:SGD.
DR GO; GO:0003779; F:actin binding; IPI:SGD.
DR GO; GO:0051666; P:actin cortical patch localization; IMP:SGD.
DR GO; GO:0007121; P:bipolar cellular bud site selection; IMP:SGD.
DR GO; GO:0006897; P:endocytosis; IMP:SGD.
DR GO; GO:2000601; P:positive regulation of Arp2/3 complex-mediated actin nucleation; IDA:SGD.
DR GO; GO:0032465; P:regulation of cytokinesis; IMP:SGD.
DR InterPro; IPR003124; WH2_dom.
DR Pfam; PF02205; WH2; 2.
DR SMART; SM00246; WH2; 2.
DR PROSITE; PS51082; WH2; 2.
PE 1: Evidence at protein level;
KW Cytoplasm; Cytoskeleton; Glycoprotein; Phosphoprotein; Reference proteome;
KW Repeat.
FT CHAIN 1..817
FT /note="Verprolin"
FT /id="PRO_0000065929"
FT DOMAIN 30..47
FT /note="WH2 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00406"
FT DOMAIN 87..106
FT /note="WH2 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00406"
FT REGION 1..752
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 786..806
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..19
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 36..50
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 62..78
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 117..184
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 208..232
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 233..247
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 250..264
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 291..307
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 308..338
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 373..409
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 421..449
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 450..472
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 515..539
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 561..582
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 646..665
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 713..743
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 519
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956"
FT MOD_RES 762
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956,
FT ECO:0007744|PubMed:19779198"
FT CARBOHYD 109
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 212
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 337
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 383
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 784
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 796
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CONFLICT 308
FT /note="P -> R (in Ref. 1; CAA81388)"
FT /evidence="ECO:0000305"
FT CONFLICT 350
FT /note="A -> R (in Ref. 1; CAA81388)"
FT /evidence="ECO:0000305"
FT CONFLICT 689
FT /note="V -> E (in Ref. 1; CAA81388)"
FT /evidence="ECO:0000305"
FT CONFLICT 710..817
FT /note="PSTMDTGTSNSPSKNLKQRLFSTGGSTLQHKHNTHTNQPDVDVGRYTIGGSN
FT SIVGAKSGNERIVIDDSRFKWTNVSQMPKPRPFQNKTKLYPSGKGSSVPLDLTLFT ->
FT HLRWIPVPLIAPVKTLNNGYFLQVDRRCNTSIIRIQINQMLM (in Ref. 1)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 817 AA; 82594 MW; 24C7522D5B1CA1C8 CRC64;
MAGAPAPPPP PPPPALGGSA PKPAKSVMQG RDALLGDIRK GMKLKKAETN DRSAPIVGGG
VVSSASGSSG TVSSKGPSMS APPIPGMGAP QLGDILAGGI PKLKHINNNA STKPSPSASA
PPIPGAVPSV AAPPIPNAPL SPAPAVPSIP SSSAPPIPDI PSSAAPPIPI VPSSPAPPLP
LSGASAPKVP QNRPHMPSVR PAHRSHQRKS SNISLPSVSA PPLPSASLPT HVSNPPQAPP
PPPTPTIGLD SKNIKPTDNA VSPPSSEVPA GGLPFLAEIN ARRSERGAVE GVSSTKIQTE
NHKSPSQPPL PSSAPPIPTS HAPPLPPTAP PPPSLPNVTS APKKATSAPA PPPPPLPAAM
SSASTNSVKA TPVPPTLAPP LPNTTSVPPN KASSMPAPPP PPPPPPGAFS TSSALSASSI
PLAPLPPPPP PSVATSVPSA PPPPPTLTTN KPSASSKQSK ISSSSSSSAV TPGGPLPFLA
EIQKKRDDRF VVGGDTGYTT QDKQEDVIGS SKDDNVRPSP ISPSINPPKQ SSQNGMSFLD
EIESKLHKQT SSNAFNAPPP HTDAMAPPLP PSAPPPPITS LPTPTASGDD HTNDKSETVL
GMKKAKAPAL PGHVPPPPVP PVLSDDSKNN VPAASLLHDV LPSSNLEKPP SPPVAAAPPL
PTFSAPSLPQ QSVSTSIPSP PPVAPTLSVR TETESISKNP TKSPPPPPSP STMDTGTSNS
PSKNLKQRLF STGGSTLQHK HNTHTNQPDV DVGRYTIGGS NSIVGAKSGN ERIVIDDSRF
KWTNVSQMPK PRPFQNKTKL YPSGKGSSVP LDLTLFT
