ID   CLAH1_ARATH             Reviewed;        1705 AA.
AC   Q0WNJ6; Q0WM81; Q9SRM1;
DT   16-NOV-2011, integrated into UniProtKB/Swiss-Prot.
DT   05-SEP-2006, sequence version 1.
DT   27-MAR-2024, entry version 126.
DE   RecName: Full=Clathrin heavy chain 1 {ECO:0000303|PubMed:21551390};
GN   Name=CHC1 {ECO:0000303|PubMed:21551390};
GN   OrderedLocusNames=At3g11130 {ECO:0000312|Araport:AT3G11130};
GN   ORFNames=F11B9.30 {ECO:0000312|EMBL:AAG50967.1}, F9F8.6
GN   {ECO:0000312|EMBL:AAF01510.1};
OS   Arabidopsis thaliana (Mouse-ear cress).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX   NCBI_TaxID=3702;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Columbia;
RX   PubMed=11130713; DOI=10.1038/35048706;
RA   Salanoubat M., Lemcke K., Rieger M., Ansorge W., Unseld M., Fartmann B.,
RA   Valle G., Bloecker H., Perez-Alonso M., Obermaier B., Delseny M.,
RA   Boutry M., Grivell L.A., Mache R., Puigdomenech P., De Simone V.,
RA   Choisne N., Artiguenave F., Robert C., Brottier P., Wincker P.,
RA   Cattolico L., Weissenbach J., Saurin W., Quetier F., Schaefer M.,
RA   Mueller-Auer S., Gabel C., Fuchs M., Benes V., Wurmbach E., Drzonek H.,
RA   Erfle H., Jordan N., Bangert S., Wiedelmann R., Kranz H., Voss H.,
RA   Holland R., Brandt P., Nyakatura G., Vezzi A., D'Angelo M., Pallavicini A.,
RA   Toppo S., Simionati B., Conrad A., Hornischer K., Kauer G., Loehnert T.-H.,
RA   Nordsiek G., Reichelt J., Scharfe M., Schoen O., Bargues M., Terol J.,
RA   Climent J., Navarro P., Collado C., Perez-Perez A., Ottenwaelder B.,
RA   Duchemin D., Cooke R., Laudie M., Berger-Llauro C., Purnelle B., Masuy D.,
RA   de Haan M., Maarse A.C., Alcaraz J.-P., Cottet A., Casacuberta E.,
RA   Monfort A., Argiriou A., Flores M., Liguori R., Vitale D., Mannhaupt G.,
RA   Haase D., Schoof H., Rudd S., Zaccaria P., Mewes H.-W., Mayer K.F.X.,
RA   Kaul S., Town C.D., Koo H.L., Tallon L.J., Jenkins J., Rooney T., Rizzo M.,
RA   Walts A., Utterback T., Fujii C.Y., Shea T.P., Creasy T.H., Haas B.,
RA   Maiti R., Wu D., Peterson J., Van Aken S., Pai G., Militscher J.,
RA   Sellers P., Gill J.E., Feldblyum T.V., Preuss D., Lin X., Nierman W.C.,
RA   Salzberg S.L., White O., Venter J.C., Fraser C.M., Kaneko T., Nakamura Y.,
RA   Sato S., Kato T., Asamizu E., Sasamoto S., Kimura T., Idesawa K.,
RA   Kawashima K., Kishida Y., Kiyokawa C., Kohara M., Matsumoto M., Matsuno A.,
RA   Muraki A., Nakayama S., Nakazaki N., Shinpo S., Takeuchi C., Wada T.,
RA   Watanabe A., Yamada M., Yasuda M., Tabata S.;
RT   "Sequence and analysis of chromosome 3 of the plant Arabidopsis thaliana.";
RL   Nature 408:820-822(2000).
RN   [2]
RP   GENOME REANNOTATION.
RC   STRAIN=cv. Columbia;
RX   PubMed=27862469; DOI=10.1111/tpj.13415;
RA   Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA   Town C.D.;
RT   "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT   genome.";
RL   Plant J. 89:789-804(2017).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=cv. Columbia;
RA   Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A.,
RA   Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y.,
RA   Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.,
RA   Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y.,
RA   Shinozaki K.;
RT   "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
RL   Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   FUNCTION.
RX   PubMed=21551390; DOI=10.1105/tpc.111.083030;
RA   Kitakura S., Vanneste S., Robert S., Loefke C., Teichmann T., Tanaka H.,
RA   Friml J.;
RT   "Clathrin mediates endocytosis and polar distribution of PIN auxin
RT   transporters in Arabidopsis.";
RL   Plant Cell 23:1920-1931(2011).
RN   [5]
RP   ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
RP   METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP   [LARGE SCALE ANALYSIS].
RX   PubMed=22223895; DOI=10.1074/mcp.m111.015131;
RA   Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T.,
RA   Giglione C.;
RT   "Comparative large-scale characterisation of plant vs. mammal proteins
RT   reveals similar and idiosyncratic N-alpha acetylation features.";
RL   Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
RN   [6]
RP   INTERACTION WITH SCYL2B.
RC   STRAIN=cv. Columbia;
RX   PubMed=28751315; DOI=10.1104/pp.17.00824;
RA   Jung J.-Y., Lee D.W., Ryu S.B., Hwang I., Schachtman D.P.;
RT   "SCYL2 genes are involved in clathrin-mediated vesicle trafficking and
RT   essential for plant growth.";
RL   Plant Physiol. 175:194-209(2017).
CC   -!- FUNCTION: Clathrin is the major protein of the polyhedral coat of
CC       coated pits and vesicles (By similarity). Mediates endocytosis and is
CC       required for a correct polar distribution of PIN auxin transporters.
CC       {ECO:0000250|UniProtKB:P25870, ECO:0000269|PubMed:21551390}.
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       Interacts with SCYL2B (PubMed:28751315). {ECO:0000250|UniProtKB:Q00610,
CC       ECO:0000269|PubMed:28751315}.
CC   -!- INTERACTION:
CC       Q0WNJ6; Q8VY07: EPSIN1; NbExp=3; IntAct=EBI-1162845, EBI-1162785;
CC   -!- SUBCELLULAR LOCATION: Cytoplasmic vesicle membrane
CC       {ECO:0000250|UniProtKB:P25870}; Peripheral membrane protein
CC       {ECO:0000250|UniProtKB:P25870}; Cytoplasmic side
CC       {ECO:0000250|UniProtKB:P25870}. Membrane, coated pit
CC       {ECO:0000250|UniProtKB:P25870}; Peripheral membrane protein
CC       {ECO:0000250|UniProtKB:P25870}; Cytoplasmic side
CC       {ECO:0000250|UniProtKB:P25870}. Note=Cytoplasmic face of coated pits
CC       and vesicles. {ECO:0000250|UniProtKB:P25870}.
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   -!- SIMILARITY: Belongs to the clathrin heavy chain family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAF01510.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC       Sequence=AAG50967.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AC009991; AAF01510.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; AC073395; AAG50967.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; CP002686; AEE75005.1; -; Genomic_DNA.
DR   EMBL; AK229443; BAF01303.1; -; mRNA.
DR   EMBL; AK229949; BAF01775.1; -; mRNA.
DR   RefSeq; NP_187724.2; NM_111950.3.
DR   AlphaFoldDB; Q0WNJ6; -.
DR   SMR; Q0WNJ6; -.
DR   BioGRID; 5618; 60.
DR   IntAct; Q0WNJ6; 7.
DR   MINT; Q0WNJ6; -.
DR   STRING; 3702.Q0WNJ6; -.
DR   iPTMnet; Q0WNJ6; -.
DR   PaxDb; 3702-AT3G11130-1; -.
DR   ProteomicsDB; 246876; -.
DR   EnsemblPlants; AT3G11130.1; AT3G11130.1; AT3G11130.
DR   GeneID; 820284; -.
DR   Gramene; AT3G11130.1; AT3G11130.1; AT3G11130.
DR   KEGG; ath:AT3G11130; -.
DR   Araport; AT3G11130; -.
DR   TAIR; AT3G11130; CHC1.
DR   eggNOG; KOG0985; Eukaryota.
DR   HOGENOM; CLU_002136_0_0_1; -.
DR   InParanoid; Q0WNJ6; -.
DR   OMA; HCYDLLH; -.
DR   OrthoDB; 5474327at2759; -.
DR   PhylomeDB; Q0WNJ6; -.
DR   PRO; PR:Q0WNJ6; -.
DR   Proteomes; UP000006548; Chromosome 3.
DR   ExpressionAtlas; Q0WNJ6; baseline and differential.
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; IEA:InterPro.
DR   GO; GO:0005829; C:cytosol; HDA:TAIR.
DR   GO; GO:0005794; C:Golgi apparatus; HDA:TAIR.
DR   GO; GO:0000325; C:plant-type vacuole; HDA:TAIR.
DR   GO; GO:0005886; C:plasma membrane; HDA:TAIR.
DR   GO; GO:0009506; C:plasmodesma; HDA:TAIR.
DR   GO; GO:0005773; C:vacuole; HDA:TAIR.
DR   GO; GO:0032051; F:clathrin light chain binding; IEA:InterPro.
DR   GO; GO:0005198; F:structural molecule activity; IEA:InterPro.
DR   GO; GO:0072583; P:clathrin-dependent endocytosis; IMP:TAIR.
DR   GO; GO:0006897; P:endocytosis; IMP:TAIR.
DR   GO; GO:0006886; P:intracellular protein transport; IEA:InterPro.
DR   GO; GO:0009414; P:response to water deprivation; IMP:TAIR.
DR   GO; GO:0010118; P:stomatal movement; IMP:TAIR.
DR   GO; GO:0016192; P:vesicle-mediated transport; IDA:TAIR.
DR   Gene3D; 1.25.40.730; -; 1.
DR   Gene3D; 2.130.10.110; Clathrin heavy-chain terminal domain; 1.
DR   Gene3D; 1.25.40.10; Tetratricopeptide repeat domain; 3.
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   PANTHER; PTHR10292:SF34; CLATHRIN HEAVY CHAIN 1-RELATED; 1.
DR   PANTHER; PTHR10292; CLATHRIN HEAVY CHAIN RELATED; 1.
DR   Pfam; PF00637; Clathrin; 7.
DR   Pfam; PF09268; Clathrin-link; 1.
DR   Pfam; PF13838; Clathrin_H_link; 1.
DR   Pfam; PF01394; Clathrin_propel; 2.
DR   PIRSF; PIRSF002290; Clathrin_H_chain; 1.
DR   SMART; SM00299; CLH; 7.
DR   SUPFAM; SSF48371; ARM repeat; 5.
DR   SUPFAM; SSF50989; Clathrin heavy-chain terminal domain; 1.
DR   PROSITE; PS50236; CHCR; 7.
DR   Genevisible; Q0WNJ6; AT.
PE   1: Evidence at protein level;
KW   Acetylation; Coated pit; Cytoplasmic vesicle; Endocytosis; Membrane;
KW   Reference proteome; Repeat.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0007744|PubMed:22223895"
FT   CHAIN           2..1705
FT                   /note="Clathrin heavy chain 1"
FT                   /id="PRO_0000413949"
FT   REPEAT          551..697
FT                   /note="CHCR 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01006"
FT   REPEAT          700..842
FT                   /note="CHCR 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01006"
FT   REPEAT          847..986
FT                   /note="CHCR 3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01006"
FT   REPEAT          993..1138
FT                   /note="CHCR 4"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01006"
FT   REPEAT          1142..1283
FT                   /note="CHCR 5"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01006"
FT   REPEAT          1288..1434
FT                   /note="CHCR 6"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01006"
FT   REPEAT          1437..1580
FT                   /note="CHCR 7"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01006"
FT   REGION          2..492
FT                   /note="Globular terminal domain"
FT                   /evidence="ECO:0000250"
FT   REGION          25..67
FT                   /note="WD40-like repeat 1"
FT                   /evidence="ECO:0000255"
FT   REGION          68..113
FT                   /note="WD40-like repeat 2"
FT                   /evidence="ECO:0000255"
FT   REGION          114..155
FT                   /note="WD40-like repeat 3"
FT                   /evidence="ECO:0000255"
FT   REGION          156..205
FT                   /note="WD40-like repeat 4"
FT                   /evidence="ECO:0000255"
FT   REGION          206..270
FT                   /note="WD40-like repeat 5"
FT                   /evidence="ECO:0000255"
FT   REGION          271..314
FT                   /note="WD40-like repeat 6"
FT                   /evidence="ECO:0000255"
FT   REGION          315..343
FT                   /note="WD40-like repeat 7"
FT                   /evidence="ECO:0000255"
FT   REGION          462..478
FT                   /note="Binding site for the uncoating ATPase, involved in
FT                   lattice disassembly"
FT                   /evidence="ECO:0000250"
FT   REGION          493..536
FT                   /note="Flexible linker"
FT                   /evidence="ECO:0000250"
FT   REGION          537..1705
FT                   /note="Heavy chain arm"
FT                   /evidence="ECO:0000250"
FT   REGION          537..648
FT                   /note="Distal segment"
FT                   /evidence="ECO:0000250"
FT   REGION          653..1705
FT                   /note="Proximal segment"
FT                   /evidence="ECO:0000250"
FT   REGION          1227..1536
FT                   /note="Involved in binding clathrin light chain"
FT                   /evidence="ECO:0000250"
FT   REGION          1564..1705
FT                   /note="Trimerization"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         2
FT                   /note="N-acetylalanine"
FT                   /evidence="ECO:0007744|PubMed:22223895"
SQ   SEQUENCE   1705 AA;  193245 MW;  0850CAE77FE17616 CRC64;
     MAAANAPIIM KEVLTLPSVG IGQQFITFTN VTMESDKYIC VRETAPQNSV VIIDMNMPMQ
     PLRRPITADS ALMNPNSRIL ALKAQVPGTT QDHLQIFNIE AKAKLKSHQM PEQVAFWKWI
     TPKMLGLVTQ TSVYHWSIEG DSEPVKMFDR TANLANNQII NYKCSPNEKW LVLIGIAPGS
     PERPQLVKGN MQLFSVDQQR SQALEAHAAS FAQFKVPGNE NPSILISFAS KSFNAGQITS
     KLHVIELGAQ PGKPSFTKKQ ADLFFPPDFA DDFPVAMQVS HKFNLIYVIT KLGLLFVYDL
     ETASAIYRNR ISPDPIFLTS EASSVGGFYA INRRGQVLLA TVNEATIIPF ISGQLNNLEL
     AVNLAKRGNL PGAENLVVQR FQELFAQTKY KEAAELAAES PQGILRTPDT VAKFQSVPVQ
     AGQTPPLLQY FGTLLTRGKL NSYESLELSR LVVNQNKKNL LENWLAEDKL ECSEELGDLV
     KTVDNDLALK IYIKARATPK VVAAFAERRE FDKILIYSKQ VGYTPDYMFL LQTILRTDPQ
     GAVNFALMMS QMEGGCPVDY NTITDLFLQR NLIREATAFL LDVLKPNLPE HAFLQTKVLE
     INLVTFPNVA DAILANGMFS HYDRPRVAQL CEKAGLYIQS LKHYSELPDI KRVIVNTHAI
     EPQALVEFFG TLSSEWAMEC MKDLLLVNLR GNLQIIVQAC KEYCEQLGVD ACIKLFEQFK
     SYEGLYFFLG SYLSMSEDPE IHFKYIEAAA KTGQIKEVER VTRESNFYDA EKTKNFLMEA
     KLPDARPLIN VCDRFGFVPD LTHYLYTNNM LRYIEGYVQK VNPGNAPLVV GQLLDDECPE
     DFIKGLILSV RSLLPVEPLV AECEKRNRLR LLTQFLEHLV SEGSQDVHVH NALGKIIIDS
     NNNPEHFLTT NPYYDSKVVG KYCEKRDPTL AVVAYRRGQC DEELINVTNK NSLFKLQARY
     VVERMDGDLW EKVLTEENEY RRQLIDQVVS TALPESKSPE QVSAAVKAFM TADLPHELIE
     LLEKIVLQNS AFSGNFNLQN LLILTAIKAD PSRVMDYINR LDNFDGPAVG EVAVDAQLYE
     EAFAIFKKFN LNVQAVNVLL DNVRSIERAV EFAFRVEEDA VWSQVAKAQL REGLVSDAIE
     SFIRADDTTQ FLEVIRASED TNVYDDLVRY LLMVRQKVKE PKVDSELIYA YAKIERLGEI
     EEFILMPNVA NLQHVGDRLY DEALYEAAKI IYAFISNWAK LAVTLVKLQQ FQGAVDAARK
     ANSAKTWKEV CFACVDAEEF RLAQICGLNI IIQVDDLEEV SEYYQNRGCF NELISLMESG
     LGLERAHMGI FTELGVLYAR YRYEKLMEHI KLFSTRLNIP KLIRACDEQQ HWQELTYLYI
     QYDEFDNAAT TVMNHSPEAW EHMQFKDIVA KVANVELYYK AVHFYLQEHP DIINDLLNVL
     ALRLDHTRVV DIMRKAGHLR LIKPYMVAVQ SNNVSAVNEA LNEIYAEEED YDRLRESIDL
     HDSFDQIGLA QKIEKHELVE MRRVAAYIYK KAGRWKQSIA LSKKDNMYKD CMETASQSGD
     HDLAEQLLVY FIEQGKKECF ATCLFVCYDL IRPDVALELA WINNMIDFAF PYLLQFIREY
     SGKVDELIKD KLEAQKEVKA KEQEEKDVMS QQNMYAQLLP LALPAPPMPG MGGGGYGPPP
     QMGGMPGMSG MPPMPPYGMP PMGGY
//