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Suppressor of yeast profilin deletion

 SYP1_YEAST              Reviewed;         870 AA.
P25623; D6VR40; P25622; Q96VH0;
01-MAY-1992, integrated into UniProtKB/Swiss-Prot.
24-OCT-2003, sequence version 3.
22-NOV-2017, entry version 145.
RecName: Full=Suppressor of yeast profilin deletion;
Name=SYP1; OrderedLocusNames=YCR030C; ORFNames=YCR30C/YCR29C;
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina;
Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Saccharomyces.
NCBI_TaxID=559292;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 204508 / S288c;
PubMed=1574125; DOI=10.1038/357038a0;
Oliver S.G., van der Aart Q.J.M., Agostoni-Carbone M.L., Aigle M.,
Alberghina L., Alexandraki D., Antoine G., Anwar R., Ballesta J.P.G.,
Benit P., Berben G., Bergantino E., Biteau N., Bolle P.-A.,
Bolotin-Fukuhara M., Brown A., Brown A.J.P., Buhler J.-M., Carcano C.,
Carignani G., Cederberg H., Chanet R., Contreras R., Crouzet M.,
Daignan-Fornier B., Defoor E., Delgado M.D., Demolder J., Doira C.,
Dubois E., Dujon B., Duesterhoeft A., Erdmann D., Esteban M.,
Fabre F., Fairhead C., Faye G., Feldmann H., Fiers W.,
Francingues-Gaillard M.-C., Franco L., Frontali L., Fukuhara H.,
Fuller L.J., Galland P., Gent M.E., Gigot D., Gilliquet V.,
Glansdorff N., Goffeau A., Grenson M., Grisanti P., Grivell L.A.,
de Haan M., Haasemann M., Hatat D., Hoenicka J., Hegemann J.H.,
Herbert C.J., Hilger F., Hohmann S., Hollenberg C.P., Huse K.,
Iborra F., Indge K.J., Isono K., Jacq C., Jacquet M., James C.M.,
Jauniaux J.-C., Jia Y., Jimenez A., Kelly A., Kleinhans U., Kreisl P.,
Lanfranchi G., Lewis C., van der Linden C.G., Lucchini G.,
Lutzenkirchen K., Maat M.J., Mallet L., Mannhaupt G., Martegani E.,
Mathieu A., Maurer C.T.C., McConnell D., McKee R.A., Messenguy F.,
Mewes H.-W., Molemans F., Montague M.A., Muzi Falconi M., Navas L.,
Newlon C.S., Noone D., Pallier C., Panzeri L., Pearson B.M., Perea J.,
Philippsen P., Pierard A., Planta R.J., Plevani P., Poetsch B.,
Pohl F.M., Purnelle B., Ramezani Rad M., Rasmussen S.W., Raynal A.,
Remacha M.A., Richterich P., Roberts A.B., Rodriguez F., Sanz E.,
Schaaff-Gerstenschlaeger I., Scherens B., Schweitzer B., Shu Y.,
Skala J., Slonimski P.P., Sor F., Soustelle C., Spiegelberg R.,
Stateva L.I., Steensma H.Y., Steiner S., Thierry A., Thireos G.,
Tzermia M., Urrestarazu L.A., Valle G., Vetter I.,
van Vliet-Reedijk J.C., Voet M., Volckaert G., Vreken P., Wang H.,
Warmington J.R., von Wettstein D., Wicksteed B.L., Wilson C.,
Wurst H., Xu G., Yoshikawa A., Zimmermann F.K., Sgouros J.G.;
"The complete DNA sequence of yeast chromosome III.";
Nature 357:38-46(1992).
[2]
SEQUENCE REVISION.
Gromadka R.;
Submitted (JAN-1996) to the EMBL/GenBank/DDBJ databases.
[3]
SEQUENCE REVISION TO 824 AND 831.
Valles G., Volckaerts G.;
Submitted (JUN-2001) to the EMBL/GenBank/DDBJ databases.
[4]
GENOME REANNOTATION.
STRAIN=ATCC 204508 / S288c;
PubMed=24374639; DOI=10.1534/g3.113.008995;
Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M.,
Cherry J.M.;
"The reference genome sequence of Saccharomyces cerevisiae: Then and
now.";
G3 (Bethesda) 4:389-398(2014).
[5]
FUNCTION, AND SUBCELLULAR LOCATION.
PubMed=11014808;
Marcoux N., Cloutier S., Zakrzewska E., Charest P.-M., Bourbonnais Y.,
Pallotta D.;
"Suppression of the profilin-deficient phenotype by the RHO2 signaling
pathway in Saccharomyces cerevisiae.";
Genetics 156:579-592(2000).
[6]
LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
PubMed=14562106; DOI=10.1038/nature02046;
Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A.,
Dephoure N., O'Shea E.K., Weissman J.S.;
"Global analysis of protein expression in yeast.";
Nature 425:737-741(2003).
[7]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-264; SER-496 AND
SER-500, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
STRAIN=ADR376;
PubMed=17330950; DOI=10.1021/pr060559j;
Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J.,
Elias J.E., Gygi S.P.;
"Large-scale phosphorylation analysis of alpha-factor-arrested
Saccharomyces cerevisiae.";
J. Proteome Res. 6:1190-1197(2007).
[8]
FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH CDC3; CDC10;
CDC11 AND CDC12.
PubMed=18791237; DOI=10.1534/genetics.108.091900;
Qiu W., Neo S.P., Yu X., Cai M.;
"A novel septin-associated protein, Syp1p, is required for normal cell
cycle-dependent septin cytoskeleton dynamics in yeast.";
Genetics 180:1445-1457(2008).
[9]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-577, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=18407956; DOI=10.1074/mcp.M700468-MCP200;
Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
"A multidimensional chromatography technology for in-depth
phosphoproteome analysis.";
Mol. Cell. Proteomics 7:1389-1396(2008).
[10]
SUBCELLULAR LOCATION, AND FUNCTION.
PubMed=19776351; DOI=10.1091/mbc.E09-05-0429;
Stimpson H.E., Toret C.P., Cheng A.T., Pauly B.S., Drubin D.G.;
"Early-arriving Syp1p and Ede1p function in endocytic site placement
and formation in budding yeast.";
Mol. Biol. Cell 20:4640-4651(2009).
[11]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-264; SER-331; THR-416
AND SER-496, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
PubMed=19779198; DOI=10.1126/science.1172867;
Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.;
"Global analysis of Cdk1 substrate phosphorylation sites provides
insights into evolution.";
Science 325:1682-1686(2009).
[12]
UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-256, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22106047; DOI=10.1002/pmic.201100166;
Starita L.M., Lo R.S., Eng J.K., von Haller P.D., Fields S.;
"Sites of ubiquitin attachment in Saccharomyces cerevisiae.";
Proteomics 12:236-240(2012).
[13]
X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF 1-264 AND 566-870,
INTERACTION WITH EDE1, SUBCELLULAR LOCATION, AND FUNCTION.
PubMed=19713939; DOI=10.1038/emboj.2009.248;
Reider A., Barker S.L., Mishra S.K., Im Y.J., Maldonado-Baez L.,
Hurley J.H., Traub L.M., Wendland B.;
"Syp1 is a conserved endocytic adaptor that contains domains involved
in cargo selection and membrane tubulation.";
EMBO J. 28:3103-3116(2009).
-!- FUNCTION: Multi-functional protein that contributes to the
endocytic process, but also to events that occur at the neck
during budding and/or cytokinesis. Plays a role as an endocytic
adapters with membrane-tubulation activity that associates with
transmembrane cargo proteins and initiates the formation of
endocytic sites. Contributes to the stabilization of the nascent
clathrin-coated pit. Plays also a role in late endocytosis by
mediating vesiculation. Involved in the regulation of cell cycle-
dependent dynamics of the septin cytoskeleton by promoting septin
turnover in different cell cycle stages. May act through the RHO2
signaling pathway to repolarize cortical actin patches in
profilin-deficient cells. {ECO:0000269|PubMed:11014808,
ECO:0000269|PubMed:18791237, ECO:0000269|PubMed:19713939,
ECO:0000269|PubMed:19776351}.
-!- SUBUNIT: Interacts with CDC3, CDC10, CDC11, CDC12, EDE1 and EPS15.
{ECO:0000269|PubMed:18791237, ECO:0000269|PubMed:19713939}.
-!- INTERACTION:
Self; NbExp=2; IntAct=EBI-21900, EBI-21900;
P34216:EDE1; NbExp=6; IntAct=EBI-21900, EBI-21243;
P36027:MID2; NbExp=2; IntAct=EBI-21900, EBI-10901;
-!- SUBCELLULAR LOCATION: Bud neck {ECO:0000269|PubMed:11014808,
ECO:0000269|PubMed:18791237, ECO:0000269|PubMed:19713939,
ECO:0000269|PubMed:19776351}. Note=Concentrates at the mother-bud
neck and at the tip of the forming bud. As the bud grows, abundant
in the mother-bud neck and in the bud. At cytokinesis, found
predominantly at the junction between the mother cell and the bud.
Present at the base of shmoo projections.
-!- MISCELLANEOUS: Present with 4280 molecules/cell in log phase SD
medium. {ECO:0000269|PubMed:14562106}.
-!- SIMILARITY: Belongs to the SYP1 family. {ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; X59720; CAC42980.1; -; Genomic_DNA.
EMBL; BK006937; DAA07509.1; -; Genomic_DNA.
PIR; S74291; S74291.
RefSeq; NP_009959.2; NM_001178744.1.
PDB; 3G9G; X-ray; 2.40 A; A=1-264.
PDB; 3G9H; X-ray; 2.80 A; A=566-870.
PDBsum; 3G9G; -.
PDBsum; 3G9H; -.
ProteinModelPortal; P25623; -.
SMR; P25623; -.
BioGrid; 31013; 79.
DIP; DIP-1758N; -.
IntAct; P25623; 36.
MINT; MINT-402640; -.
STRING; 4932.YCR030C; -.
iPTMnet; P25623; -.
MaxQB; P25623; -.
PRIDE; P25623; -.
EnsemblFungi; YCR030C; YCR030C; YCR030C.
GeneID; 850396; -.
KEGG; sce:YCR030C; -.
EuPathDB; FungiDB:YCR030C; -.
SGD; S000000626; SYP1.
HOGENOM; HOG000057127; -.
InParanoid; P25623; -.
KO; K20042; -.
OMA; KHLVYWR; -.
OrthoDB; EOG092C13HH; -.
BioCyc; YEAST:G3O-29344-MONOMER; -.
EvolutionaryTrace; P25623; -.
PRO; PR:P25623; -.
Proteomes; UP000002311; Chromosome III.
GO; GO:0005935; C:cellular bud neck; IDA:UniProtKB.
GO; GO:0000144; C:cellular bud neck septin ring; IDA:SGD.
GO; GO:0005934; C:cellular bud tip; IDA:UniProtKB.
GO; GO:0061645; C:endocytic patch; IDA:SGD.
GO; GO:0001400; C:mating projection base; IDA:UniProtKB.
GO; GO:0004857; F:enzyme inhibitor activity; IDA:SGD.
GO; GO:0042802; F:identical protein binding; IPI:IntAct.
GO; GO:0000147; P:actin cortical patch assembly; IMP:SGD.
GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
GO; GO:0006897; P:endocytosis; IEA:UniProtKB-KW.
GO; GO:0043086; P:negative regulation of catalytic activity; IDA:SGD.
GO; GO:0032185; P:septin cytoskeleton organization; IMP:SGD.
InterPro; IPR027267; AH/BAR_dom_sf.
InterPro; IPR028565; MHD.
InterPro; IPR018808; Muniscin_C.
Pfam; PF10291; muHD; 1.
SUPFAM; SSF103657; SSF103657; 1.
PROSITE; PS51072; MHD; 1.
1: Evidence at protein level;
3D-structure; Cell cycle; Complete proteome; Endocytosis;
Isopeptide bond; Phosphoprotein; Reference proteome; Ubl conjugation.
CHAIN 1 870 Suppressor of yeast profilin deletion.
/FTId=PRO_0000072390.
DOMAIN 609 869 MHD. {ECO:0000255|PROSITE-
ProRule:PRU00404}.
COMPBIAS 308 405 Ser-rich.
COMPBIAS 417 528 Pro-rich.
MOD_RES 264 264 Phosphoserine.
{ECO:0000244|PubMed:17330950,
ECO:0000244|PubMed:19779198}.
MOD_RES 331 331 Phosphoserine.
{ECO:0000244|PubMed:19779198}.
MOD_RES 416 416 Phosphothreonine.
{ECO:0000244|PubMed:19779198}.
MOD_RES 496 496 Phosphoserine.
{ECO:0000244|PubMed:17330950,
ECO:0000244|PubMed:19779198}.
MOD_RES 500 500 Phosphoserine.
{ECO:0000244|PubMed:17330950}.
MOD_RES 577 577 Phosphothreonine.
{ECO:0000244|PubMed:18407956}.
CROSSLNK 256 256 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in ubiquitin).
{ECO:0000244|PubMed:22106047}.
HELIX 7 11 {ECO:0000244|PDB:3G9G}.
TURN 12 15 {ECO:0000244|PDB:3G9G}.
HELIX 18 64 {ECO:0000244|PDB:3G9G}.
HELIX 67 77 {ECO:0000244|PDB:3G9G}.
HELIX 83 88 {ECO:0000244|PDB:3G9G}.
HELIX 97 125 {ECO:0000244|PDB:3G9G}.
HELIX 127 131 {ECO:0000244|PDB:3G9G}.
STRAND 133 136 {ECO:0000244|PDB:3G9G}.
HELIX 138 159 {ECO:0000244|PDB:3G9G}.
HELIX 168 230 {ECO:0000244|PDB:3G9G}.
HELIX 233 246 {ECO:0000244|PDB:3G9G}.
STRAND 611 625 {ECO:0000244|PDB:3G9H}.
STRAND 628 643 {ECO:0000244|PDB:3G9H}.
STRAND 646 648 {ECO:0000244|PDB:3G9H}.
STRAND 654 661 {ECO:0000244|PDB:3G9H}.
HELIX 663 665 {ECO:0000244|PDB:3G9H}.
STRAND 666 671 {ECO:0000244|PDB:3G9H}.
TURN 673 675 {ECO:0000244|PDB:3G9H}.
STRAND 676 680 {ECO:0000244|PDB:3G9H}.
STRAND 683 686 {ECO:0000244|PDB:3G9H}.
TURN 688 691 {ECO:0000244|PDB:3G9H}.
STRAND 695 705 {ECO:0000244|PDB:3G9H}.
STRAND 709 718 {ECO:0000244|PDB:3G9H}.
STRAND 720 731 {ECO:0000244|PDB:3G9H}.
STRAND 741 753 {ECO:0000244|PDB:3G9H}.
STRAND 758 766 {ECO:0000244|PDB:3G9H}.
STRAND 771 773 {ECO:0000244|PDB:3G9H}.
STRAND 775 779 {ECO:0000244|PDB:3G9H}.
STRAND 784 787 {ECO:0000244|PDB:3G9H}.
STRAND 793 803 {ECO:0000244|PDB:3G9H}.
STRAND 812 818 {ECO:0000244|PDB:3G9H}.
TURN 827 830 {ECO:0000244|PDB:3G9H}.
STRAND 836 845 {ECO:0000244|PDB:3G9H}.
STRAND 856 869 {ECO:0000244|PDB:3G9H}.
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


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