CLAH1_ARATH
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 25-MAY-2022, entry version 119.
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},
GN F9F8.6 {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};
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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.AT3G11130.1; -.
DR iPTMnet; Q0WNJ6; -.
DR PaxDb; Q0WNJ6; -.
DR PRIDE; Q0WNJ6; -.
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; locus:2074733; AT3G11130.
DR eggNOG; KOG0985; Eukaryota.
DR HOGENOM; CLU_002136_0_0_1; -.
DR InParanoid; Q0WNJ6; -.
DR OMA; QVNEACV; -.
DR OrthoDB; 17940at2759; -.
DR PhylomeDB; Q0WNJ6; -.
DR PRO; PR:Q0WNJ6; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q0WNJ6; baseline and differential.
DR Genevisible; Q0WNJ6; AT.
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: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; IBA:GO_Central.
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:0006898; P:receptor-mediated endocytosis; IBA:GO_Central.
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; 1.25.40.10; -; 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; 2.
DR PIRSF; PIRSF002290; Clathrin_H_chain; 1.
DR SMART; SM00299; CLH; 7.
DR SUPFAM; SSF48371; SSF48371; 5.
DR SUPFAM; SSF50989; SSF50989; 1.
DR PROSITE; PS50236; CHCR; 7.
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
