SCP1_YEAST
ID SCP1_YEAST Reviewed; 200 AA.
AC Q08873; D6W360;
DT 06-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 165.
DE RecName: Full=Transgelin;
DE AltName: Full=Calponin homolog 1;
GN Name=SCP1; OrderedLocusNames=YOR367W;
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=9169874;
RA Dujon B., Albermann K., Aldea M., Alexandraki D., Ansorge W., Arino J.,
RA Benes V., Bohn C., Bolotin-Fukuhara M., Bordonne R., Boyer J., Camasses A.,
RA Casamayor A., Casas C., Cheret G., Cziepluch C., Daignan-Fornier B.,
RA Dang V.-D., de Haan M., Delius H., Durand P., Fairhead C., Feldmann H.,
RA Gaillon L., Galisson F., Gamo F.-J., Gancedo C., Goffeau A., Goulding S.E.,
RA Grivell L.A., Habbig B., Hand N.J., Hani J., Hattenhorst U., Hebling U.,
RA Hernando Y., Herrero E., Heumann K., Hiesel R., Hilger F., Hofmann B.,
RA Hollenberg C.P., Hughes B., Jauniaux J.-C., Kalogeropoulos A.,
RA Katsoulou C., Kordes E., Lafuente M.J., Landt O., Louis E.J., Maarse A.C.,
RA Madania A., Mannhaupt G., Marck C., Martin R.P., Mewes H.-W., Michaux G.,
RA Paces V., Parle-McDermott A.G., Pearson B.M., Perrin A., Pettersson B.,
RA Poch O., Pohl T.M., Poirey R., Portetelle D., Pujol A., Purnelle B.,
RA Ramezani Rad M., Rechmann S., Schwager C., Schweizer M., Sor F., Sterky F.,
RA Tarassov I.A., Teodoru C., Tettelin H., Thierry A., Tobiasch E.,
RA Tzermia M., Uhlen M., Unseld M., Valens M., Vandenbol M., Vetter I.,
RA Vlcek C., Voet M., Volckaert G., Voss H., Wambutt R., Wedler H.,
RA Wiemann S., Winsor B., Wolfe K.H., Zollner A., Zumstein E., Kleine K.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XV.";
RL Nature 387:98-102(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 INTERACTION WITH ACTIN, AND SUBCELLULAR LOCATION.
RX PubMed=12868959; DOI=10.1042/bj20030796;
RA Winder S.J., Jess T., Ayscough K.R.;
RT "SCP1 encodes an actin-bundling protein in yeast.";
RL Biochem. J. 375:287-295(2003).
RN [5]
RP INTERACTION WITH ACTIN, SUBCELLULAR LOCATION, AND MUTAGENESIS OF SER-185.
RX PubMed=12857851; DOI=10.1091/mbc.e03-01-0028;
RA Goodman A., Goode B.L., Matsudaira P., Fink G.R.;
RT "The Saccharomyces cerevisiae calponin/transgelin homolog Scp1 functions
RT with fimbrin to regulate stability and organization of the actin
RT cytoskeleton.";
RL Mol. Biol. Cell 14:2617-2629(2003).
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 INTERACTION WITH ABP1.
RX PubMed=14737190; DOI=10.1371/journal.pbio.0020014;
RA Landgraf C., Panni S., Montecchi-Palazzi L., Castagnoli L.,
RA Schneider-Mergener J., Volkmer-Engert R., Cesareni G.;
RT "Protein interaction networks by proteome peptide scanning.";
RL PLoS Biol. 2:94-103(2004).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-11, 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 [9]
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 [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-11, 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).
RN [11]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
CC -!- FUNCTION: Has actin-binding and actin-bundling activity. Stabilizes
CC actin filaments against disassembly.
CC -!- SUBUNIT: Binds to actin. Interacts with ABP1.
CC {ECO:0000269|PubMed:12857851, ECO:0000269|PubMed:12868959,
CC ECO:0000269|PubMed:14737190}.
CC -!- INTERACTION:
CC Q08873; P15891: ABP1; NbExp=7; IntAct=EBI-33137, EBI-2036;
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, actin patch
CC {ECO:0000269|PubMed:12857851, ECO:0000269|PubMed:12868959,
CC ECO:0000269|PubMed:14562095}. Note=Cortical actin patches.
CC -!- MISCELLANEOUS: Present with 1578 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
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DR EMBL; Z75275; CAA99698.1; -; Genomic_DNA.
DR EMBL; BK006948; DAA11126.1; -; Genomic_DNA.
DR PIR; S67279; S67279.
DR RefSeq; NP_015012.3; NM_001183787.3.
DR AlphaFoldDB; Q08873; -.
DR BMRB; Q08873; -.
DR SMR; Q08873; -.
DR BioGRID; 34750; 34.
DR DIP; DIP-6340N; -.
DR IntAct; Q08873; 2.
DR MINT; Q08873; -.
DR STRING; 4932.YOR367W; -.
DR iPTMnet; Q08873; -.
DR MaxQB; Q08873; -.
DR PaxDb; Q08873; -.
DR PRIDE; Q08873; -.
DR EnsemblFungi; YOR367W_mRNA; YOR367W; YOR367W.
DR GeneID; 854549; -.
DR KEGG; sce:YOR367W; -.
DR SGD; S000005894; SCP1.
DR VEuPathDB; FungiDB:YOR367W; -.
DR eggNOG; KOG2046; Eukaryota.
DR GeneTree; ENSGT00940000174742; -.
DR HOGENOM; CLU_055232_2_1_1; -.
DR InParanoid; Q08873; -.
DR OMA; EYGYMKG; -.
DR BioCyc; YEAST:G3O-33835-MON; -.
DR PRO; PR:Q08873; -.
DR Proteomes; UP000002311; Chromosome XV.
DR RNAct; Q08873; protein.
DR GO; GO:0030479; C:actin cortical patch; IDA:SGD.
DR GO; GO:0051015; F:actin filament binding; IDA:SGD.
DR GO; GO:0030674; F:protein-macromolecule adaptor activity; IDA:SGD.
DR GO; GO:0007015; P:actin filament organization; IDA:SGD.
DR CDD; cd00014; CH; 1.
DR Gene3D; 1.10.418.10; -; 1.
DR InterPro; IPR001715; CH-domain.
DR InterPro; IPR036872; CH_dom_sf.
DR InterPro; IPR003096; SM22_calponin.
DR Pfam; PF00307; CH; 1.
DR PRINTS; PR00888; SM22CALPONIN.
DR SMART; SM00033; CH; 1.
DR SUPFAM; SSF47576; SSF47576; 1.
DR PROSITE; PS50021; CH; 1.
PE 1: Evidence at protein level;
KW Acetylation; Cytoplasm; Cytoskeleton; Phosphoprotein; Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:22814378"
FT CHAIN 2..200
FT /note="Transgelin"
FT /id="PRO_0000204795"
FT DOMAIN 26..136
FT /note="Calponin-homology (CH)"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00044"
FT REGION 144..168
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 151..164
FT /note="Interaction with SH3 domain of ABP1"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0007744|PubMed:22814378"
FT MOD_RES 11
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17330950,
FT ECO:0007744|PubMed:19779198"
FT MUTAGEN 185
FT /note="S->A: Greatly reduces actin-binding and actin-
FT bundling activity."
FT /evidence="ECO:0000269|PubMed:12857851"
FT MUTAGEN 185
FT /note="S->D: Moderately reduces actin-binding and actin-
FT bundling activity."
FT /evidence="ECO:0000269|PubMed:12857851"
SQ SEQUENCE 200 AA; 22748 MW; 6C8E7EACCFD0DE28 CRC64;
MSYDKKADVT SLDEDLRQLR ESKFSPEAIQ NIKIWVYKSV LKEIAPPGDL LECLKDGTVL
CKLANILYEA DTGEANHISW KSSKMPFVQM DQISQFLSFS RKYGVPEDEL FQTIDLFEKK
DPAIVFQTLK SLSRYANKKH TDRFPVLGPQ LSTKKPRPPV KSKPKHLQDG TGWSTFEYGY
MKGASQATEG VVLGQRRDIV
