SYP1_YEAST
ID SYP1_YEAST Reviewed; 870 AA.
AC P25623; D6VR40; P25622; Q96VH0;
DT 01-MAY-1992, integrated into UniProtKB/Swiss-Prot.
DT 24-OCT-2003, sequence version 3.
DT 03-AUG-2022, entry version 176.
DE RecName: Full=Suppressor of yeast profilin deletion;
GN Name=SYP1; OrderedLocusNames=YCR030C; ORFNames=YCR30C/YCR29C;
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=1574125; DOI=10.1038/357038a0;
RA Oliver S.G., van der Aart Q.J.M., Agostoni-Carbone M.L., Aigle M.,
RA Alberghina L., Alexandraki D., Antoine G., Anwar R., Ballesta J.P.G.,
RA Benit P., Berben G., Bergantino E., Biteau N., Bolle P.-A.,
RA Bolotin-Fukuhara M., Brown A., Brown A.J.P., Buhler J.-M., Carcano C.,
RA Carignani G., Cederberg H., Chanet R., Contreras R., Crouzet M.,
RA Daignan-Fornier B., Defoor E., Delgado M.D., Demolder J., Doira C.,
RA Dubois E., Dujon B., Duesterhoeft A., Erdmann D., Esteban M., Fabre F.,
RA Fairhead C., Faye G., Feldmann H., Fiers W., Francingues-Gaillard M.-C.,
RA Franco L., Frontali L., Fukuhara H., Fuller L.J., Galland P., Gent M.E.,
RA Gigot D., Gilliquet V., Glansdorff N., Goffeau A., Grenson M., Grisanti P.,
RA Grivell L.A., de Haan M., Haasemann M., Hatat D., Hoenicka J.,
RA Hegemann J.H., Herbert C.J., Hilger F., Hohmann S., Hollenberg C.P.,
RA Huse K., Iborra F., Indge K.J., Isono K., Jacq C., Jacquet M., James C.M.,
RA Jauniaux J.-C., Jia Y., Jimenez A., Kelly A., Kleinhans U., Kreisl P.,
RA Lanfranchi G., Lewis C., van der Linden C.G., Lucchini G.,
RA Lutzenkirchen K., Maat M.J., Mallet L., Mannhaupt G., Martegani E.,
RA Mathieu A., Maurer C.T.C., McConnell D., McKee R.A., Messenguy F.,
RA Mewes H.-W., Molemans F., Montague M.A., Muzi Falconi M., Navas L.,
RA Newlon C.S., Noone D., Pallier C., Panzeri L., Pearson B.M., Perea J.,
RA Philippsen P., Pierard A., Planta R.J., Plevani P., Poetsch B., Pohl F.M.,
RA Purnelle B., Ramezani Rad M., Rasmussen S.W., Raynal A., Remacha M.A.,
RA Richterich P., Roberts A.B., Rodriguez F., Sanz E.,
RA Schaaff-Gerstenschlaeger I., Scherens B., Schweitzer B., Shu Y., Skala J.,
RA Slonimski P.P., Sor F., Soustelle C., Spiegelberg R., Stateva L.I.,
RA Steensma H.Y., Steiner S., Thierry A., Thireos G., Tzermia M.,
RA Urrestarazu L.A., Valle G., Vetter I., van Vliet-Reedijk J.C., Voet M.,
RA Volckaert G., Vreken P., Wang H., Warmington J.R., von Wettstein D.,
RA Wicksteed B.L., Wilson C., Wurst H., Xu G., Yoshikawa A., Zimmermann F.K.,
RA Sgouros J.G.;
RT "The complete DNA sequence of yeast chromosome III.";
RL Nature 357:38-46(1992).
RN [2]
RP SEQUENCE REVISION.
RA Gromadka R.;
RL Submitted (JAN-1996) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP SEQUENCE REVISION TO 824 AND 831.
RA Valles G., Volckaerts G.;
RL Submitted (JUN-2001) to the EMBL/GenBank/DDBJ databases.
RN [4]
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 [5]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=11014808; DOI=10.1093/genetics/156.2.579;
RA Marcoux N., Cloutier S., Zakrzewska E., Charest P.-M., Bourbonnais Y.,
RA Pallotta D.;
RT "Suppression of the profilin-deficient phenotype by the RHO2 signaling
RT pathway in Saccharomyces cerevisiae.";
RL Genetics 156:579-592(2000).
RN [6]
RP LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX PubMed=14562106; DOI=10.1038/nature02046;
RA Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N.,
RA O'Shea E.K., Weissman J.S.;
RT "Global analysis of protein expression in yeast.";
RL Nature 425:737-741(2003).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-264; SER-496 AND SER-500, AND
RP IDENTIFICATION BY 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 [8]
RP FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH CDC3; CDC10; CDC11 AND
RP CDC12.
RX PubMed=18791237; DOI=10.1534/genetics.108.091900;
RA Qiu W., Neo S.P., Yu X., Cai M.;
RT "A novel septin-associated protein, Syp1p, is required for normal cell
RT cycle-dependent septin cytoskeleton dynamics in yeast.";
RL Genetics 180:1445-1457(2008).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-577, AND IDENTIFICATION BY
RP 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 [10]
RP SUBCELLULAR LOCATION, AND FUNCTION.
RX PubMed=19776351; DOI=10.1091/mbc.e09-05-0429;
RA Stimpson H.E., Toret C.P., Cheng A.T., Pauly B.S., Drubin D.G.;
RT "Early-arriving Syp1p and Ede1p function in endocytic site placement and
RT formation in budding yeast.";
RL Mol. Biol. Cell 20:4640-4651(2009).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-264; SER-331; THR-416 AND
RP SER-496, 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).
RN [12]
RP UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-256, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22106047; DOI=10.1002/pmic.201100166;
RA Starita L.M., Lo R.S., Eng J.K., von Haller P.D., Fields S.;
RT "Sites of ubiquitin attachment in Saccharomyces cerevisiae.";
RL Proteomics 12:236-240(2012).
RN [13]
RP X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF 1-264 AND 566-870, INTERACTION
RP WITH EDE1, SUBCELLULAR LOCATION, AND FUNCTION.
RX PubMed=19713939; DOI=10.1038/emboj.2009.248;
RA Reider A., Barker S.L., Mishra S.K., Im Y.J., Maldonado-Baez L.,
RA Hurley J.H., Traub L.M., Wendland B.;
RT "Syp1 is a conserved endocytic adaptor that contains domains involved in
RT cargo selection and membrane tubulation.";
RL EMBO J. 28:3103-3116(2009).
CC -!- FUNCTION: Multi-functional protein that contributes to the endocytic
CC process, but also to events that occur at the neck during budding
CC and/or cytokinesis. Plays a role as an endocytic adapters with
CC membrane-tubulation activity that associates with transmembrane cargo
CC proteins and initiates the formation of endocytic sites. Contributes to
CC the stabilization of the nascent clathrin-coated pit. Also plays a role
CC in late endocytosis by mediating vesiculation. Involved in the
CC regulation of cell cycle-dependent dynamics of the septin cytoskeleton
CC by promoting septin turnover in different cell cycle stages. May act
CC through the RHO2 signaling pathway to repolarize cortical actin patches
CC in profilin-deficient cells. {ECO:0000269|PubMed:11014808,
CC ECO:0000269|PubMed:18791237, ECO:0000269|PubMed:19713939,
CC ECO:0000269|PubMed:19776351}.
CC -!- SUBUNIT: Interacts with CDC3, CDC10, CDC11, CDC12, EDE1 and EPS15.
CC {ECO:0000269|PubMed:18791237, ECO:0000269|PubMed:19713939}.
CC -!- INTERACTION:
CC P25623; P34216: EDE1; NbExp=6; IntAct=EBI-21900, EBI-21243;
CC P25623; P36027: MID2; NbExp=2; IntAct=EBI-21900, EBI-10901;
CC P25623; P25623: SYP1; NbExp=2; IntAct=EBI-21900, EBI-21900;
CC -!- SUBCELLULAR LOCATION: Bud neck {ECO:0000269|PubMed:11014808,
CC ECO:0000269|PubMed:18791237, ECO:0000269|PubMed:19713939,
CC ECO:0000269|PubMed:19776351}. Note=Concentrates at the mother-bud neck
CC and at the tip of the forming bud. As the bud grows, abundant in the
CC mother-bud neck and in the bud. At cytokinesis, found predominantly at
CC the junction between the mother cell and the bud. Present at the base
CC of shmoo projections.
CC -!- MISCELLANEOUS: Present with 4280 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the SYP1 family. {ECO:0000305}.
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DR EMBL; X59720; CAC42980.1; -; Genomic_DNA.
DR EMBL; BK006937; DAA07509.1; -; Genomic_DNA.
DR PIR; S74291; S74291.
DR RefSeq; NP_009959.2; NM_001178744.1.
DR PDB; 3G9G; X-ray; 2.40 A; A=1-264.
DR PDB; 3G9H; X-ray; 2.80 A; A=566-870.
DR PDBsum; 3G9G; -.
DR PDBsum; 3G9H; -.
DR AlphaFoldDB; P25623; -.
DR SMR; P25623; -.
DR BioGRID; 31013; 117.
DR ComplexPortal; CPX-2146; SYP1 endocytic adapter complex.
DR DIP; DIP-1758N; -.
DR IntAct; P25623; 36.
DR MINT; P25623; -.
DR STRING; 4932.YCR030C; -.
DR iPTMnet; P25623; -.
DR MaxQB; P25623; -.
DR PaxDb; P25623; -.
DR PRIDE; P25623; -.
DR EnsemblFungi; YCR030C_mRNA; YCR030C; YCR030C.
DR GeneID; 850396; -.
DR KEGG; sce:YCR030C; -.
DR SGD; S000000626; SYP1.
DR VEuPathDB; FungiDB:YCR030C; -.
DR eggNOG; ENOG502QQAW; Eukaryota.
DR HOGENOM; CLU_017975_0_0_1; -.
DR InParanoid; P25623; -.
DR OMA; IRDQPIF; -.
DR BioCyc; YEAST:G3O-29344-MON; -.
DR Reactome; R-SCE-8856828; Clathrin-mediated endocytosis.
DR EvolutionaryTrace; P25623; -.
DR PRO; PR:P25623; -.
DR Proteomes; UP000002311; Chromosome III.
DR RNAct; P25623; protein.
DR GO; GO:0032153; C:cell division site; IBA:GO_Central.
DR GO; GO:0005935; C:cellular bud neck; IDA:UniProtKB.
DR GO; GO:0000144; C:cellular bud neck septin ring; IDA:SGD.
DR GO; GO:0005934; C:cellular bud tip; IDA:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0061645; C:endocytic patch; IDA:SGD.
DR GO; GO:0030139; C:endocytic vesicle; IBA:GO_Central.
DR GO; GO:0001400; C:mating projection base; IDA:UniProtKB.
DR GO; GO:0043332; C:mating projection tip; HDA:SGD.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0005628; C:prospore membrane; HDA:SGD.
DR GO; GO:1990252; C:Syp1 complex; IPI:ComplexPortal.
DR GO; GO:0004857; F:enzyme inhibitor activity; IDA:SGD.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0000147; P:actin cortical patch assembly; IMP:SGD.
DR GO; GO:0007117; P:budding cell bud growth; IDA:ComplexPortal.
DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0007010; P:cytoskeleton organization; IBA:GO_Central.
DR GO; GO:0006897; P:endocytosis; IEA:UniProtKB-KW.
DR GO; GO:0043086; P:negative regulation of catalytic activity; IDA:SGD.
DR GO; GO:0045807; P:positive regulation of endocytosis; IDA:ComplexPortal.
DR GO; GO:0032185; P:septin cytoskeleton organization; IMP:SGD.
DR GO; GO:0009826; P:unidimensional cell growth; IDA:ComplexPortal.
DR Gene3D; 1.20.1270.60; -; 1.
DR InterPro; IPR027267; AH/BAR_dom_sf.
DR InterPro; IPR028565; MHD.
DR InterPro; IPR018808; Muniscin_C.
DR Pfam; PF10291; muHD; 1.
DR SUPFAM; SSF103657; SSF103657; 1.
DR PROSITE; PS51072; MHD; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cell cycle; Endocytosis; Isopeptide bond; Phosphoprotein;
KW Reference proteome; Ubl conjugation.
FT CHAIN 1..870
FT /note="Suppressor of yeast profilin deletion"
FT /id="PRO_0000072390"
FT DOMAIN 609..869
FT /note="MHD"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00404"
FT REGION 252..298
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 310..574
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 252..284
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 310..413
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 442..456
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 457..483
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 498..515
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 533..574
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 264
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17330950,
FT ECO:0007744|PubMed:19779198"
FT MOD_RES 331
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 416
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 496
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17330950,
FT ECO:0007744|PubMed:19779198"
FT MOD_RES 500
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17330950"
FT MOD_RES 577
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:18407956"
FT CROSSLNK 256
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0007744|PubMed:22106047"
FT HELIX 7..11
FT /evidence="ECO:0007829|PDB:3G9G"
FT TURN 12..15
FT /evidence="ECO:0007829|PDB:3G9G"
FT HELIX 18..64
FT /evidence="ECO:0007829|PDB:3G9G"
FT HELIX 67..77
FT /evidence="ECO:0007829|PDB:3G9G"
FT HELIX 83..88
FT /evidence="ECO:0007829|PDB:3G9G"
FT HELIX 97..125
FT /evidence="ECO:0007829|PDB:3G9G"
FT HELIX 127..131
FT /evidence="ECO:0007829|PDB:3G9G"
FT STRAND 133..136
FT /evidence="ECO:0007829|PDB:3G9G"
FT HELIX 138..159
FT /evidence="ECO:0007829|PDB:3G9G"
FT HELIX 168..230
FT /evidence="ECO:0007829|PDB:3G9G"
FT HELIX 233..246
FT /evidence="ECO:0007829|PDB:3G9G"
FT STRAND 611..625
FT /evidence="ECO:0007829|PDB:3G9H"
FT STRAND 628..643
FT /evidence="ECO:0007829|PDB:3G9H"
FT STRAND 646..648
FT /evidence="ECO:0007829|PDB:3G9H"
FT STRAND 654..661
FT /evidence="ECO:0007829|PDB:3G9H"
FT HELIX 663..665
FT /evidence="ECO:0007829|PDB:3G9H"
FT STRAND 666..671
FT /evidence="ECO:0007829|PDB:3G9H"
FT TURN 673..675
FT /evidence="ECO:0007829|PDB:3G9H"
FT STRAND 676..680
FT /evidence="ECO:0007829|PDB:3G9H"
FT STRAND 683..686
FT /evidence="ECO:0007829|PDB:3G9H"
FT TURN 688..691
FT /evidence="ECO:0007829|PDB:3G9H"
FT STRAND 695..705
FT /evidence="ECO:0007829|PDB:3G9H"
FT STRAND 709..718
FT /evidence="ECO:0007829|PDB:3G9H"
FT STRAND 720..731
FT /evidence="ECO:0007829|PDB:3G9H"
FT STRAND 741..753
FT /evidence="ECO:0007829|PDB:3G9H"
FT STRAND 758..766
FT /evidence="ECO:0007829|PDB:3G9H"
FT STRAND 771..773
FT /evidence="ECO:0007829|PDB:3G9H"
FT STRAND 775..779
FT /evidence="ECO:0007829|PDB:3G9H"
FT STRAND 784..787
FT /evidence="ECO:0007829|PDB:3G9H"
FT STRAND 793..803
FT /evidence="ECO:0007829|PDB:3G9H"
FT STRAND 812..818
FT /evidence="ECO:0007829|PDB:3G9H"
FT TURN 827..830
FT /evidence="ECO:0007829|PDB:3G9H"
FT STRAND 836..845
FT /evidence="ECO:0007829|PDB:3G9H"
FT STRAND 856..869
FT /evidence="ECO:0007829|PDB:3G9H"
SQ SEQUENCE 870 AA; 96137 MW; 6F35C8F1562E41CC CRC64;
MTEQRTKYAD SILTTKSPYE ATETIRIRLS QVKLLNKDFY LLFKELANLK RNYAQQLRKI
IAENEDITKI LNAQMIESNV LTPQEMSAFR FNSLGELRNV WDTVIEELKS DLKSSTEYYN
TLDQQVVREL KESVENNTSW RESKDLHSKL SKNAASIEHY SKNNENSSHL EEARRQWDQQ
SPYLFELFET IDYNRLDTLK NCMLRFQTSF SDYLLNTTKE CETVMTKFLA FEPQSEIDRF
AKDASQYNFQ LSSSSKEVVP NNASPASATG ARPVSVSNGA ANTEREKKSP QKDKRKSAFG
NIGHRLASAS SSLTHNDLMN NEFSDSTNNS SLKSKKSSHT LRSKVGSIFG RNKTKNKRQQ
QSSSNSHIQA SITETPNNSS TRVSSTATSS IYQKQRRPTY SSSKSNNWTP GEASDTPPLP
PHATPKNVDA PVTADTPPAQ TFTPSEVPPS TPQQSSPPTA KEPDSSNLPK TVPISISQPP
LQPQSKTKPL PVEPASPSIS LPTATVDNQP SGQVDSRPLH IRAPALPPSR KQNFIHNRDS
QLYDSLPNHG SGATPTSSSL SSIPQERPVS TLSSQITGEL RELNPQATGS STSLVGQSLF
QHSSLDTSQF GLNASIAEVL NASFKDGMLQ NSQLIGEIAL NYLPNSVMNS PLPIGINLRI
NNGAKFEKVI LNQAFIERVA PEEFKVNPSF IDSRTLGAIK YSIKEPIAPI VIHPVWRFES
HQASVVLTVK MSPSLPDEIS QIVIEDLVVF VNIDGANATS ALSKPQGSFS KEKKRITWRF
KEPVVLTRNG EGQRLIARFI TDGLAHESAK GVITKFTISE TDNVALPHSG AGSGITLTCQ
ELDENNPFGG EWLDVNTKRT LTTGNYHGLA
