CLC1_YEAST
ID CLC1_YEAST Reviewed; 233 AA.
AC P17891; D6VUV0;
DT 01-NOV-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1990, sequence version 1.
DT 03-AUG-2022, entry version 182.
DE RecName: Full=Clathrin light chain;
DE Short=CLC;
GN Name=CLC1; OrderedLocusNames=YGR167W;
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], AND PROTEIN SEQUENCE OF 31-39.
RX PubMed=2211819; DOI=10.1083/jcb.111.4.1437;
RA Silveira L.A., Wong D.H., Masiarz F.R., Schekman R.;
RT "Yeast clathrin has a distinctive light chain that is important for cell
RT growth.";
RL J. Cell Biol. 111:1437-1449(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9290212;
RX DOI=10.1002/(sici)1097-0061(19970915)13:11<1077::aid-yea152>3.0.co;2-y;
RA Rieger M., Brueckner M., Schaefer M., Mueller-Auer S.;
RT "Sequence analysis of 203 kilobases from Saccharomyces cerevisiae
RT chromosome VII.";
RL Yeast 13:1077-1090(1997).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169869;
RA Tettelin H., Agostoni-Carbone M.L., Albermann K., Albers M., Arroyo J.,
RA Backes U., Barreiros T., Bertani I., Bjourson A.J., Brueckner M.,
RA Bruschi C.V., Carignani G., Castagnoli L., Cerdan E., Clemente M.L.,
RA Coblenz A., Coglievina M., Coissac E., Defoor E., Del Bino S., Delius H.,
RA Delneri D., de Wergifosse P., Dujon B., Durand P., Entian K.-D., Eraso P.,
RA Escribano V., Fabiani L., Fartmann B., Feroli F., Feuermann M.,
RA Frontali L., Garcia-Gonzalez M., Garcia-Saez M.I., Goffeau A.,
RA Guerreiro P., Hani J., Hansen M., Hebling U., Hernandez K., Heumann K.,
RA Hilger F., Hofmann B., Indge K.J., James C.M., Klima R., Koetter P.,
RA Kramer B., Kramer W., Lauquin G., Leuther H., Louis E.J., Maillier E.,
RA Marconi A., Martegani E., Mazon M.J., Mazzoni C., McReynolds A.D.K.,
RA Melchioretto P., Mewes H.-W., Minenkova O., Mueller-Auer S., Nawrocki A.,
RA Netter P., Neu R., Nombela C., Oliver S.G., Panzeri L., Paoluzi S.,
RA Plevani P., Portetelle D., Portillo F., Potier S., Purnelle B., Rieger M.,
RA Riles L., Rinaldi T., Robben J., Rodrigues-Pousada C.,
RA Rodriguez-Belmonte E., Rodriguez-Torres A.M., Rose M., Ruzzi M.,
RA Saliola M., Sanchez-Perez M., Schaefer B., Schaefer M., Scharfe M.,
RA Schmidheini T., Schreer A., Skala J., Souciet J.-L., Steensma H.Y.,
RA Talla E., Thierry A., Vandenbol M., van der Aart Q.J.M., Van Dyck L.,
RA Vanoni M., Verhasselt P., Voet M., Volckaert G., Wambutt R., Watson M.D.,
RA Weber N., Wedler E., Wedler H., Wipfli P., Wolf K., Wright L.F.,
RA Zaccaria P., Zimmermann M., Zollner A., Kleine K.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome VII.";
RL Nature 387:81-84(1997).
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 NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=17322287; DOI=10.1101/gr.6037607;
RA Hu Y., Rolfs A., Bhullar B., Murthy T.V.S., Zhu C., Berger M.F.,
RA Camargo A.A., Kelley F., McCarron S., Jepson D., Richardson A., Raphael J.,
RA Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F., Williamson J.,
RA Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G., Kolodner R.D.,
RA LaBaer J.;
RT "Approaching a complete repository of sequence-verified protein-encoding
RT clones for Saccharomyces cerevisiae.";
RL Genome Res. 17:536-543(2007).
RN [6]
RP INTERACTION WITH SWA2.
RX PubMed=11084334; DOI=10.1016/s0960-9822(00)00771-5;
RA Gall W.E., Higginbotham M.A., Chen C.-Y., Ingram M.F., Cyr D.M.,
RA Graham T.R.;
RT "The auxilin-like phosphoprotein Swa2p is required for clathrin function in
RT yeast.";
RL Curr. Biol. 10:1349-1358(2000).
RN [7]
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 [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-49 AND SER-52, 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 [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-52, 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).
CC -!- FUNCTION: Clathrin is the major protein of the polyhedral coat of
CC coated pits and vesicles. In yeast, it is involved in the retention of
CC proteins in an intracellular membrane compartment, presumably the
CC trans-Golgi. The yeast light chain is important for cell growth. The
CC light chain may help to properly orient the assembly/ disassembly of
CC the clathrin coats.
CC -!- SUBUNIT: Clathrin coats are formed from molecules containing 3 heavy
CC chains and 3 light chains. Interacts with the auxilin-like clathrin
CC uncoating factor SWA2. {ECO:0000269|PubMed:11084334}.
CC -!- INTERACTION:
CC P17891; P22137: CHC1; NbExp=4; IntAct=EBI-4758, EBI-4766;
CC -!- SUBCELLULAR LOCATION: Cytoplasmic vesicle membrane; Peripheral membrane
CC protein; Cytoplasmic side. Membrane, coated pit; Peripheral membrane
CC protein; Cytoplasmic side. Note=Cytoplasmic face of coated pits and
CC vesicles.
CC -!- MISCELLANEOUS: CLC1 binds calcium, and calmodulin in presence of
CC calcium.
CC -!- MISCELLANEOUS: Present with 3490 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the clathrin light chain family. {ECO:0000305}.
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DR EMBL; X52272; CAA36515.1; -; Genomic_DNA.
DR EMBL; Z72952; CAA97192.1; -; Genomic_DNA.
DR EMBL; Z72953; CAA97193.1; -; Genomic_DNA.
DR EMBL; AY558272; AAS56598.1; -; Genomic_DNA.
DR EMBL; BK006941; DAA08261.1; -; Genomic_DNA.
DR PIR; A36425; A36425.
DR RefSeq; NP_011683.3; NM_001181296.3.
DR AlphaFoldDB; P17891; -.
DR SMR; P17891; -.
DR BioGRID; 33419; 410.
DR ComplexPortal; CPX-1616; Clathrin complex.
DR DIP; DIP-2280N; -.
DR IntAct; P17891; 12.
DR MINT; P17891; -.
DR STRING; 4932.YGR167W; -.
DR iPTMnet; P17891; -.
DR MaxQB; P17891; -.
DR PaxDb; P17891; -.
DR PRIDE; P17891; -.
DR EnsemblFungi; YGR167W_mRNA; YGR167W; YGR167W.
DR GeneID; 853077; -.
DR KEGG; sce:YGR167W; -.
DR SGD; S000003399; CLC1.
DR VEuPathDB; FungiDB:YGR167W; -.
DR eggNOG; KOG4031; Eukaryota.
DR HOGENOM; CLU_069856_0_1_1; -.
DR InParanoid; P17891; -.
DR OMA; FYENYNT; -.
DR BioCyc; YEAST:G3O-30865-MON; -.
DR Reactome; R-SCE-196025; Formation of annular gap junctions.
DR Reactome; R-SCE-432720; Lysosome Vesicle Biogenesis.
DR Reactome; R-SCE-437239; Recycling pathway of L1.
DR Reactome; R-SCE-8856828; Clathrin-mediated endocytosis.
DR Reactome; R-SCE-8866427; VLDLR internalisation and degradation.
DR Reactome; R-SCE-8964038; LDL clearance.
DR PRO; PR:P17891; -.
DR Proteomes; UP000002311; Chromosome VII.
DR RNAct; P17891; protein.
DR GO; GO:0030132; C:clathrin coat of coated pit; IEA:InterPro.
DR GO; GO:0030130; C:clathrin coat of trans-Golgi network vesicle; IEA:InterPro.
DR GO; GO:0071439; C:clathrin complex; IPI:ComplexPortal.
DR GO; GO:0030125; C:clathrin vesicle coat; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0005802; C:trans-Golgi network; IDA:SGD.
DR GO; GO:0005516; F:calmodulin binding; IEA:UniProtKB-KW.
DR GO; GO:0032050; F:clathrin heavy chain binding; IBA:GO_Central.
DR GO; GO:0005198; F:structural molecule activity; TAS:SGD.
DR GO; GO:0048268; P:clathrin coat assembly; IC:ComplexPortal.
DR GO; GO:0072583; P:clathrin-dependent endocytosis; IBA:GO_Central.
DR GO; GO:0006897; P:endocytosis; IDA:SGD.
DR GO; GO:0006886; P:intracellular protein transport; IEA:InterPro.
DR GO; GO:0045807; P:positive regulation of endocytosis; IMP:SGD.
DR GO; GO:0065003; P:protein-containing complex assembly; IMP:SGD.
DR InterPro; IPR000996; Clathrin_L-chain.
DR PANTHER; PTHR10639; PTHR10639; 1.
DR Pfam; PF01086; Clathrin_lg_ch; 1.
DR PROSITE; PS00581; CLATHRIN_LIGHT_CHN_2; 1.
PE 1: Evidence at protein level;
KW Calcium; Calmodulin-binding; Coated pit; Coiled coil; Cytoplasmic vesicle;
KW Direct protein sequencing; Membrane; Phosphoprotein; Reference proteome.
FT CHAIN 1..233
FT /note="Clathrin light chain"
FT /id="PRO_0000205776"
FT REGION 1..124
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 144..204
FT /note="Involved in binding clathrin heavy chain"
FT /evidence="ECO:0000255"
FT COILED 125..186
FT /evidence="ECO:0000255"
FT COMPBIAS 14..61
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 71..109
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 110..124
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 49
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:17330950"
FT MOD_RES 52
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17330950,
FT ECO:0007744|PubMed:18407956"
SQ SEQUENCE 233 AA; 26532 MW; 27BAB175780EC8B3 CRC64;
MSEKFPPLED QNIDFTPNDK KDDDTDFLKR EAEILGDEFK TEQDDILETE ASPAKDDDEI
RDFEEQFPDI NSANGAVSSD QNGSATVSSG NDNGEADDDF STFEGANQST ESVKEDRSEV
VDQWKQRRAV EIHEKDLKDE ELKKELQDEA IKHIDDFYDS YNKKKEQQLE DAAKEAEAFL
KKRDEFFGQD NTTWDRALQL INQDDADIIG GRDRSKLKEI LLRLKGNAKA PGA
