CLH_YEAST
ID CLH_YEAST Reviewed; 1653 AA.
AC P22137; D6VTU9;
DT 01-AUG-1991, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1991, sequence version 1.
DT 03-AUG-2022, entry version 192.
DE RecName: Full=Clathrin heavy chain;
GN Name=CHC1; OrderedLocusNames=YGL206C;
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].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=1898742; DOI=10.1083/jcb.112.1.65;
RA Lemmon S.K., Pellicena-Palle A., Conley K., Freund C.L.;
RT "Sequence of the clathrin heavy chain from Saccharomyces cerevisiae and
RT requirement of the COOH terminus for clathrin function.";
RL J. Cell Biol. 112:65-80(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=9153757;
RX DOI=10.1002/(sici)1097-0061(199704)13:5<475::aid-yea101>3.0.co;2-0;
RA Feuermann M., Simeonava L., Souciet J.-L., Potier S.;
RT "Analysis of 21.7 kb DNA sequence from the left arm of chromosome VII
RT reveals 11 open reading frames: two correspond to new genes.";
RL Yeast 13:475-477(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 FUNCTION, AND INTERACTION WITH INP53.
RX PubMed=12686590; DOI=10.1091/mbc.e02-10-0686;
RA Ha S.-A., Torabinejad J., DeWald D.B., Wenk M.R., Lucast L., De Camilli P.,
RA Newitt R.A., Aebersold R., Nothwehr S.F.;
RT "The synaptojanin-like protein Inp53/Sjl3 functions with clathrin in a
RT yeast TGN-to-endosome pathway distinct from the GGA protein-dependent
RT pathway.";
RL Mol. Biol. Cell 14:1319-1333(2003).
RN [6]
RP INTERACTION WITH SWA2.
RX PubMed=16687570; DOI=10.1091/mbc.e06-02-0106;
RA Xiao J., Kim L.S., Graham T.R.;
RT "Dissection of Swa2p/auxilin domain requirements for cochaperoning Hsp70
RT clathrin-uncoating activity in vivo.";
RL Mol. Biol. Cell 17:3281-3290(2006).
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 UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-1107, 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).
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. {ECO:0000269|PubMed:12686590}.
CC -!- SUBUNIT: Clathrin triskelions, composed of 3 heavy chains and 3 light
CC chains, are the basic subunits of the clathrin coat. Interacts with the
CC auxilin-like clathrin uncoating factor SWA2. Interacts with INP53.
CC {ECO:0000269|PubMed:12686590, ECO:0000269|PubMed:16687570}.
CC -!- INTERACTION:
CC P22137; P36000: APL2; NbExp=3; IntAct=EBI-4766, EBI-2206;
CC P22137; P17891: CLC1; NbExp=4; IntAct=EBI-4766, EBI-4758;
CC P22137; P32790: SLA1; NbExp=4; IntAct=EBI-4766, EBI-17313;
CC P22137; P38856: YAP1801; NbExp=2; IntAct=EBI-4766, EBI-24811;
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 -!- DOMAIN: The C-terminal third of the heavy chains forms the hub of the
CC triskelion. This region contains the trimerization domain and the
CC light-chain binding domain involved in the assembly of the clathrin
CC lattice.
CC -!- DOMAIN: The N-terminal seven-bladed beta-propeller is formed by WD40-
CC like repeats, and projects inward from the polyhedral outer clathrin
CC coat. It constitutes a major protein-protein interaction node (By
CC similarity). {ECO:0000250}.
CC -!- MISCELLANEOUS: Present with 28700 molecules/cell in log phase SD
CC medium. {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the clathrin heavy chain family. {ECO:0000305}.
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DR EMBL; X52900; CAA37082.1; -; Genomic_DNA.
DR EMBL; Z72728; CAA96919.1; -; Genomic_DNA.
DR EMBL; BK006941; DAA07910.1; -; Genomic_DNA.
DR PIR; A36349; A36349.
DR RefSeq; NP_011309.1; NM_001181071.1.
DR AlphaFoldDB; P22137; -.
DR SMR; P22137; -.
DR BioGRID; 33050; 148.
DR ComplexPortal; CPX-1616; Clathrin complex.
DR DIP; DIP-2279N; -.
DR IntAct; P22137; 104.
DR MINT; P22137; -.
DR STRING; 4932.YGL206C; -.
DR iPTMnet; P22137; -.
DR MaxQB; P22137; -.
DR PaxDb; P22137; -.
DR PRIDE; P22137; -.
DR EnsemblFungi; YGL206C_mRNA; YGL206C; YGL206C.
DR GeneID; 852666; -.
DR KEGG; sce:YGL206C; -.
DR SGD; S000003174; CHC1.
DR VEuPathDB; FungiDB:YGL206C; -.
DR eggNOG; KOG0985; Eukaryota.
DR GeneTree; ENSGT00950000183166; -.
DR HOGENOM; CLU_002136_0_0_1; -.
DR InParanoid; P22137; -.
DR OMA; QVNEACV; -.
DR BioCyc; YEAST:G3O-30683-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 Reactome; R-SCE-9013420; RHOU GTPase cycle.
DR Reactome; R-SCE-9013424; RHOV GTPase cycle.
DR PRO; PR:P22137; -.
DR Proteomes; UP000002311; Chromosome VII.
DR RNAct; P22137; protein.
DR GO; GO:0030479; C:actin cortical patch; IBA:GO_Central.
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; TAS:SGD.
DR GO; GO:0005829; C:cytosol; IEA:GOC.
DR GO; GO:0032051; F:clathrin light 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:0030866; P:cortical actin cytoskeleton organization; IMP:SGD.
DR GO; GO:0006897; P:endocytosis; IDA:SGD.
DR GO; GO:0006895; P:Golgi to endosome transport; IMP:SGD.
DR GO; GO:0006886; P:intracellular protein transport; IEA:InterPro.
DR GO; GO:0006898; P:receptor-mediated endocytosis; IBA:GO_Central.
DR Gene3D; 1.25.40.10; -; 4.
DR Gene3D; 2.130.10.110; -; 1.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR000547; Clathrin_H-chain/VPS_repeat.
DR InterPro; IPR015348; Clathrin_H-chain_linker_core.
DR InterPro; IPR016025; Clathrin_H-chain_N.
DR InterPro; IPR022365; Clathrin_H-chain_propeller_rpt.
DR InterPro; IPR016341; Clathrin_heavy_chain.
DR InterPro; IPR011990; TPR-like_helical_dom_sf.
DR Pfam; PF00637; Clathrin; 7.
DR Pfam; PF09268; Clathrin-link; 1.
DR Pfam; PF01394; Clathrin_propel; 1.
DR PIRSF; PIRSF002290; Clathrin_H_chain; 1.
DR SMART; SM00299; CLH; 7.
DR SUPFAM; SSF48371; SSF48371; 6.
DR SUPFAM; SSF50989; SSF50989; 1.
DR PROSITE; PS50236; CHCR; 7.
PE 1: Evidence at protein level;
KW Coated pit; Cytoplasmic vesicle; Isopeptide bond; Membrane;
KW Reference proteome; Repeat; Ubl conjugation.
FT CHAIN 1..1653
FT /note="Clathrin heavy chain"
FT /id="PRO_0000205785"
FT REPEAT 543..689
FT /note="CHCR 1"
FT REPEAT 692..834
FT /note="CHCR 2"
FT REPEAT 839..978
FT /note="CHCR 3"
FT REPEAT 985..1130
FT /note="CHCR 4"
FT REPEAT 1134..1275
FT /note="CHCR 5"
FT REPEAT 1280..1426
FT /note="CHCR 6"
FT REPEAT 1429..1572
FT /note="CHCR 7"
FT REGION 1..483
FT /note="Globular terminal domain"
FT REGION 23..66
FT /note="WD40-like repeat 1"
FT REGION 67..107
FT /note="WD40-like repeat 2"
FT REGION 108..152
FT /note="WD40-like repeat 3"
FT REGION 153..198
FT /note="WD40-like repeat 4"
FT REGION 199..263
FT /note="WD40-like repeat 5"
FT REGION 264..307
FT /note="WD40-like repeat 6"
FT REGION 308..336
FT /note="WD40-like repeat 7"
FT REGION 453..469
FT /note="Binding site for the uncoating ATPase, involved in
FT lattice disassembly"
FT /evidence="ECO:0000255"
FT REGION 484..527
FT /note="Flexible linker"
FT REGION 528..1653
FT /note="Heavy chain arm"
FT REGION 528..?
FT /note="Distal segment"
FT REGION 1219..1528
FT /note="Involved in binding clathrin light chain"
FT /evidence="ECO:0000250"
FT REGION ?..1653
FT /note="Proximal segment"
FT CROSSLNK 1107
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0007744|PubMed:22106047"
SQ SEQUENCE 1653 AA; 187234 MW; 622F3083DF2FE315 CRC64;
MSDLPIEFTE LVDLMSLGIS PQFLDFRSTT FESDHFVTVR ETKDGTNSVA IVDLAKGNEV
TRKNMGGDSA IMHPSQMVIS VRANGTIVQI FNLETKSKLK SFTLDEPVIF WRWLSETTLG
FVTARSILTS NVFDGNVNAK PQLLTLRHAN LNNTQIINFV ANKNLDWFAV VGILQENGRI
AGRIQLFSKQ RNISQAIDGH VAIFTNILLE GNGSTPVQVF VTGNRNATTG AGELRIIEID
HDASLPSQYQ KETTDIFFPP DATNDFPIAV QVSEKYGIIY LLTKYGFIHL YELETGTNLF
VNRITAESVF TAAPYNHENG IACINKKGQV LAVEISTSQI VPYILNKLSN VALALIVATR
GGLPGADDLF QKQFESLLLQ NDYQNAAKVA ASSTSLRNQN TINRLKNIQA PPGAISPILL
YFSTLLDKGK LNKEETIELA RPVLQQDRKQ LFEKWLKEDK LECSEELGDI VKPFDTTLAL
ACYLRAGAHA KVISCLAELQ QFEKIIPYCQ KVGYQPNFLV LISSLIRSSP DRASEFAVSL
LQNPETASQI DIEKIADLFF SQNHIQQGTS LLLDALKGDT PDQGHLQTRV LEVNLLHAPQ
VADAILGNNI FSHYDKPTIA SLSEKAGLYQ RALENYTDIK DIKRCVVHTN ALPIDWLVGY
FGKLNVEQSL ACLKALMDNN IQANIQTVVQ VATKFSDLIG PSTLIKLFED YNATEGLYYY
LASLVNLTED KDVVYKYIEA AAKMKQYREI ERIVKDNNVY DPERVKNFLK DANLEDQLPL
VIVCDRFDFV HEMILYLYKS QNLKFIETYV QQVNPSKTAQ VVGALLDMDC DEAFIQSLLQ
SVLGQVPINE LTTEVEKRNR LKILLPFLEQ SLSQGIQDQA VYNALAKIYI DSNNSPEKFL
KENDQYDTLD VGHYCEKRDP YLAYIAYEKG QNDDDLIRIT NENSMYKYQA RYLLERSDLD
LWNKVLNQEN IHRRQLIDSV ISVGIPELTD PEPVSLTVQA FMTNGLKLEL IELLEKIILE
PSPFNENVAL QGLLLLSAIK YEPTKVSSYI EKLDNYDADE IAPLCIEHDL KEEAFEIYDK
HEMYGKALKV LIEDIMSLDR AASYADKINT PELWSQIGTA QLDGLRIPDA IESYIKAEDP
SNYENVIDIA EQAGKYEELI PFLLMARKTL KEPKIDGALI LAYAELNKIH EIENLLAGSN
VANLDHVGDK LFENKEYKAA RLCYSAVSNY SKLASTLVYL GDYQAAVDTA RKASNIKVWK
LVNDACIEKK EFKLAQICGL NLIVHAEELD ELVERYESNG YFEELISLFE AGLGLERAHM
GMFTELAILY SKYEPDKTFE HLKLFWSRIN IPKVIRAVEQ AHLWSELVFL YAHYDEWDNA
ALTLIEKSTK DLDHAYFKEV VVKVSNLEIY YKAINFYVKF HPSLLVDLLT SLTPRLDIPR
TVKIFSKSDN LPLIKPFLIN VLPKNNSVVN QAYHDLMIEE EDYKALQDAV DSYDKFDQLG
LASRLESHKL IFFKKIGALL YRRNKKWAKS LSILKEEKLW KDAIETAAIS QDPKVVEALL
TYFVETGNRE GFVALLYAAY NLVRIEFVLE ISWMNSLEDY IKPFEISIKK EQNDSIKKIT
EELAKKSGSN EEHKDGQPLM LMNSAMNVQP TGF
