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   27-MAR-2024, entry version 188.
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; 413.
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; 4932-YGR167W; -.
DR   PeptideAtlas; P17891; -.
DR   EnsemblFungi; YGR167W_mRNA; YGR167W; YGR167W.
DR   GeneID; 853077; -.
DR   KEGG; sce:YGR167W; -.
DR   AGR; SGD:S000003399; -.
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   OrthoDB; 1330395at2759; -.
DR   BioCyc; YEAST:G3O-30865-MONOMER; -.
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   BioGRID-ORCS; 853077; 9 hits in 10 CRISPR screens.
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; NAS: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; CLATHRIN LIGHT CHAIN; 1.
DR   PANTHER; PTHR10639:SF7; CLATHRIN LIGHT CHAIN; 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
//