ID   CLH_CAEEL               Reviewed;        1681 AA.
AC   P34574;
DT   01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1994, sequence version 1.
DT   03-AUG-2022, entry version 159.
DE   RecName: Full=Probable clathrin heavy chain 1;
GN   Name=chc-1; ORFNames=T20G5.1;
OS   Caenorhabditis elegans.
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC   Caenorhabditis.
OX   NCBI_TaxID=6239;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Bristol N2;
RX   PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG   The C. elegans sequencing consortium;
RT   "Genome sequence of the nematode C. elegans: a platform for investigating
RT   biology.";
RL   Science 282:2012-2018(1998).
RN   [2]
RP   INTERACTION WITH ARR-1.
RX   PubMed=15878875; DOI=10.1074/jbc.m502637200;
RA   Palmitessa A., Hess H.A., Bany I.A., Kim Y.M., Koelle M.R., Benovic J.L.;
RT   "Caenorhabditus elegans arrestin regulates neural G protein signaling and
RT   olfactory adaptation and recovery.";
RL   J. Biol. Chem. 280:24649-24662(2005).
RN   [3]
RP   FUNCTION, AND DISRUPTION PHENOTYPE.
RX   PubMed=19798448; DOI=10.1371/journal.pgen.1000675;
RA   Giuliani C., Troglio F., Bai Z., Patel F.B., Zucconi A., Malabarba M.G.,
RA   Disanza A., Stradal T.B., Cassata G., Confalonieri S., Hardin J.D.,
RA   Soto M.C., Grant B.D., Scita G.;
RT   "Requirements for F-BAR proteins TOCA-1 and TOCA-2 in actin dynamics and
RT   membrane trafficking during Caenorhabditis elegans oocyte growth and
RT   embryonic epidermal morphogenesis.";
RL   PLoS Genet. 5:E1000675-E1000675(2009).
CC   -!- FUNCTION: Clathrin is the major protein of the polyhedral coat of
CC       coated pits and vesicles (By similarity). May play a role in yolk
CC       protein clatherin-mediated endocytosis by oocytes during oogenesis
CC       (PubMed:19798448). {ECO:0000250, ECO:0000269|PubMed:19798448}.
CC   -!- SUBUNIT: Clathrin triskelions, composed of 3 heavy chains and 3 light
CC       chains, are the basic subunits of the clathrin coat (By similarity).
CC       May interact with beta arrestin arr-1 (PubMed:15878875).
CC       {ECO:0000250|UniProtKB:Q00610, ECO:0000269|PubMed:15878875}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasmic vesicle membrane {ECO:0000250};
CC       Peripheral membrane protein {ECO:0000250}; Cytoplasmic side
CC       {ECO:0000250}. Membrane, coated pit {ECO:0000250}; Peripheral membrane
CC       protein {ECO:0000250}; Cytoplasmic side {ECO:0000250}. Note=Cytoplasmic
CC       face of coated pits and vesicles. {ECO:0000250}.
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   -!- DISRUPTION PHENOTYPE: RNAi-mediated knockdown results in defective
CC       endocytosis by oocytes characterized by an accumulation of aggregated
CC       yolk protein in the pseudocoelomatic space.
CC       {ECO:0000269|PubMed:19798448}.
CC   -!- SIMILARITY: Belongs to the clathrin heavy chain family. {ECO:0000305}.
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DR   EMBL; Z30423; CAA83003.1; -; Genomic_DNA.
DR   PIR; S42369; S42369.
DR   RefSeq; NP_499260.1; NM_066859.4.
DR   AlphaFoldDB; P34574; -.
DR   SMR; P34574; -.
DR   BioGRID; 41628; 45.
DR   DIP; DIP-25251N; -.
DR   IntAct; P34574; 20.
DR   MINT; P34574; -.
DR   STRING; 6239.T20G5.1; -.
DR   EPD; P34574; -.
DR   PaxDb; P34574; -.
DR   PeptideAtlas; P34574; -.
DR   PRIDE; P34574; -.
DR   EnsemblMetazoa; T20G5.1.1; T20G5.1.1; WBGene00011867.
DR   GeneID; 176434; -.
DR   KEGG; cel:CELE_T20G5.1; -.
DR   UCSC; T20G5.1; c. elegans.
DR   CTD; 176434; -.
DR   WormBase; T20G5.1; CE00480; WBGene00011867; chc-1.
DR   eggNOG; KOG0985; Eukaryota.
DR   GeneTree; ENSGT00950000183166; -.
DR   HOGENOM; CLU_002136_0_0_1; -.
DR   InParanoid; P34574; -.
DR   OMA; QVNEACV; -.
DR   OrthoDB; 17940at2759; -.
DR   PhylomeDB; P34574; -.
DR   Reactome; R-CEL-190873; Gap junction degradation.
DR   Reactome; R-CEL-196025; Formation of annular gap junctions.
DR   Reactome; R-CEL-432720; Lysosome Vesicle Biogenesis.
DR   Reactome; R-CEL-432722; Golgi Associated Vesicle Biogenesis.
DR   Reactome; R-CEL-437239; Recycling pathway of L1.
DR   Reactome; R-CEL-5099900; WNT5A-dependent internalization of FZD4.
DR   Reactome; R-CEL-5140745; WNT5A-dependent internalization of FZD2, FZD5 and ROR2.
DR   Reactome; R-CEL-8856825; Cargo recognition for clathrin-mediated endocytosis.
DR   Reactome; R-CEL-8856828; Clathrin-mediated endocytosis.
DR   Reactome; R-CEL-8866427; VLDLR internalisation and degradation.
DR   Reactome; R-CEL-8964038; LDL clearance.
DR   Reactome; R-CEL-9013420; RHOU GTPase cycle.
DR   Reactome; R-CEL-9013424; RHOV GTPase cycle.
DR   SignaLink; P34574; -.
DR   PRO; PR:P34574; -.
DR   Proteomes; UP000001940; Chromosome III.
DR   Bgee; WBGene00011867; Expressed in pharyngeal muscle cell (C elegans) and 4 other tissues.
DR   GO; GO:0016324; C:apical plasma membrane; IDA:WormBase.
DR   GO; GO:0005938; C:cell cortex; IDA:WormBase.
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; IBA:GO_Central.
DR   GO; GO:0045334; C:clathrin-coated endocytic vesicle; IDA:WormBase.
DR   GO; GO:0005737; C:cytoplasm; IDA:WormBase.
DR   GO; GO:0009898; C:cytoplasmic side of plasma membrane; IDA:WormBase.
DR   GO; GO:0031410; C:cytoplasmic vesicle; IDA:WormBase.
DR   GO; GO:0030139; C:endocytic vesicle; IDA:WormBase.
DR   GO; GO:0072686; C:mitotic spindle; IDA:WormBase.
DR   GO; GO:0005886; C:plasma membrane; IDA:WormBase.
DR   GO; GO:0032051; F:clathrin light chain binding; IBA:GO_Central.
DR   GO; GO:0005198; F:structural molecule activity; IEA:InterPro.
DR   GO; GO:0045176; P:apical protein localization; IMP:WormBase.
DR   GO; GO:0030866; P:cortical actin cytoskeleton organization; IMP:WormBase.
DR   GO; GO:0008340; P:determination of adult lifespan; IGI:UniProtKB.
DR   GO; GO:0009792; P:embryo development ending in birth or egg hatching; IMP:WormBase.
DR   GO; GO:0006886; P:intracellular protein transport; IEA:InterPro.
DR   GO; GO:2000370; P:positive regulation of clathrin-dependent endocytosis; IMP:UniProtKB.
DR   GO; GO:0008104; P:protein localization; IMP:WormBase.
DR   GO; GO:0006898; P:receptor-mediated endocytosis; IMP:WormBase.
DR   Gene3D; 1.25.40.10; -; 3.
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; 4.
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; Membrane; Reference proteome; Repeat.
FT   CHAIN           1..1681
FT                   /note="Probable clathrin heavy chain 1"
FT                   /id="PRO_0000205781"
FT   REPEAT          539..685
FT                   /note="CHCR 1"
FT   REPEAT          688..830
FT                   /note="CHCR 2"
FT   REPEAT          835..974
FT                   /note="CHCR 3"
FT   REPEAT          981..1126
FT                   /note="CHCR 4"
FT   REPEAT          1130..1271
FT                   /note="CHCR 5"
FT   REPEAT          1276..1422
FT                   /note="CHCR 6"
FT   REPEAT          1425..1568
FT                   /note="CHCR 7"
FT   REGION          22..65
FT                   /note="WD40-like repeat 1"
FT   REGION          66..105
FT                   /note="WD40-like repeat 2"
FT   REGION          106..147
FT                   /note="WD40-like repeat 3"
FT   REGION          148..193
FT                   /note="WD40-like repeat 4"
FT   REGION          194..255
FT                   /note="WD40-like repeat 5"
FT   REGION          256..299
FT                   /note="WD40-like repeat 6"
FT   REGION          300..328
FT                   /note="WD40-like repeat 7"
FT   REGION          1616..1635
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1681 AA;  191542 MW;  44D15C61339009D9 CRC64;
     MALPIKFHEH LQLPNAGIRV PNITFSNVTM ESDKNIVVRE MIGDQQQVVI IDLADTANPT
     RRPISADSVI MHPTAKILAL KSGKTLQIFN IELKAKVKAH QNVEDVVYWK WISEKTIALV
     SDTAVYHWSI EGDAAPVKMF DRHQSLAGTQ IINYRADAEN KWLVLIGISA KDSRVVGSMQ
     LYSTERKVSQ PIEGHAACFV RFKVDGNQNP SNLFCFSVKT DNGGKLHVIE VGTPAAGNTP
     FQKKNVDVPY TADTAGDFPV SMQVSAKQGI IYLVTKQGYV HLYDVESGTR IYSNRISTDT
     VFVTCEYTAT GGIMGINRKG QVLSVSIDEA NLVPFVTNQL QNPDLALKLA VRCDLPGAEE
     LFVRKFNLLF SNGQFGESAK VAASAPQGIL RTPATIQKFQ QCPSTGPGPS PLLQYFGILL
     DQGKLNKYET LELCRPVLAQ GRKELITKWL NDQKLECCEE LGDLIKPHDV NTALSVYLRG
     NVPHKVVQSF AETGQFDKIV MYAKRVGFQP DYLFQLRQIL RNSNPDHGAK FAQLLVSESE
     NGEPLADLSQ IIDCFMEVQA VQPCTSFLLE VLKGDKPEEG HLQTRLLEMN LLAAPAVADA
     ILANKMFSHY DRAAIGQLCE KAGLLQRALE HFTDLYDIKR TVVHTHLLKP DWLVGYFGSL
     SVEDSVECLK AMLTQNIRQN LQVVVQIASK YHEQLGADKL IEMFENHKSY EGLFYFLGSI
     VNFSQDPEVH FKYIQAATRT GQIKEVERIC RESQCYDAER VKNFLKEAKL NDQLPLIIVC
     DRHNMVHDLV LYLYRNQLQK YIEVFVQKVN AARLPIVVGA LLDVDCSEDA IKQLIINTRG
     KFDIDELVEE VEKRNRLKLL NHWLESKIQE GATDAATHNA MAKIYIDSNN NPERFLKENP
     YYDSKVVGKY CEKRDPHYAF LSYERGQCDA ELINVCNENS LFKNLARYLV KRRDFTLWEQ
     VLNEENVHRR QLIDQVVQTA LSETQDPEDI SVTVKAFMAA DLPNELIELL EKIVLDNSAF
     SEHRNLQNLL ILTAMRADRT RVMEYIQKLD NYDAPDIANI AITSELYEEA FAIFKKFDVN
     SSAINVLIEN VNNLDRAYEF AEKCNQSDVW ASLAKAQLQQ NLVKEAVDSF IKADDPGAYM
     EVVNKCSQTE HWEDLVRYLQ MARKKSRESY IETELVFALA KTGRLTELEE FIAGPNHAQI
     GQIGDRCFDN GMFDSAKILF NNVSNFAKLS VTLVRLGEYQ GAVDAARKAN STKTWKQVCF
     SCVENGEFRL AQMCGLHIVV HADELEELIN FYQDRGHFEE LIALLEAALG LERAHMGMFT
     ELAILYSKYK PEKMREHLEL FWSRVNIPKV LRAAEQAHLW SELVFLYDKY EEYDNAALTM
     MQHPTESWRE QHFKEVIAKV ANVELYYKAM QFYLDYKPLL LNDLLTVLSP RLDHSRTVLF
     FNKLKQIPLV KPYLRQVQNL NNKAINEALN QLLIDEEDHA GLRSSIEAQD NFDNITLAQQ
     LEKHPLVEFR RISAYLFKGN NRWKQSIELC KKDKLYKDAM EYAAESRNGE LAEELLSFFL
     DEKLYDCFAA SLYHCYDLLH PDVIMELAWK HKIMDYAMPY MIQVMRDYQT RLEKLERSEH
     ERKEEKAEQQ QNNGMTMEPQ LMLTYGAPAP QMTYPGTTGG YGGQPAYGQP GQPGYNAPGF
     M