CLAH2_ARATH
ID CLAH2_ARATH Reviewed; 1703 AA.
AC Q0WLB5; Q8L3R8; Q9C6U0; Q9CA00;
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 2;
GN Name=CHC2; Synonyms=CHC1; OrderedLocusNames=At3g08530;
GN ORFNames=F17O14.1, T8G24.1;
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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 973-1703.
RC STRAIN=cv. Columbia;
RX PubMed=14593172; DOI=10.1126/science.1088305;
RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA Ecker J.R.;
RT "Empirical analysis of transcriptional activity in the Arabidopsis
RT genome.";
RL Science 302:842-846(2003).
RN [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=cv. Landsberg erecta;
RX PubMed=17272265; DOI=10.1074/mcp.m600408-mcp200;
RA Maor R., Jones A., Nuehse T.S., Studholme D.J., Peck S.C., Shirasu K.;
RT "Multidimensional protein identification technology (MudPIT) analysis of
RT ubiquitinated proteins in plants.";
RL Mol. Cell. Proteomics 6:601-610(2007).
RN [6]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
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 [7]
RP INTERACTION WITH CLC2 AND TPLATE.
RX PubMed=21187379; DOI=10.1073/pnas.1017890108;
RA Van Damme D., Gadeyne A., Vanstraelen M., Inze D., Van Montagu M.C.,
RA De Jaeger G., Russinova E., Geelen D.;
RT "Adaptin-like protein TPLATE and clathrin recruitment during plant somatic
RT cytokinesis occurs via two distinct pathways.";
RL Proc. Natl. Acad. Sci. U.S.A. 108:615-620(2011).
RN [8]
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 [9]
RP INTERACTION WITH EDR4.
RC STRAIN=cv. Columbia;
RX PubMed=25747881; DOI=10.1105/tpc.114.134668;
RA Wu G., Liu S., Zhao Y., Wang W., Kong Z., Tang D.;
RT "ENHANCED DISEASE RESISTANCE4 associates with CLATHRIN HEAVY CHAIN2 and
RT modulates plant immunity by regulating relocation of EDR1 in Arabidopsis.";
RL Plant Cell 27:857-873(2015).
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, 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 CLC2 and TPLATE. Interacts with EDR4 (PubMed:25747881).
CC {ECO:0000250, ECO:0000269|PubMed:21187379,
CC ECO:0000269|PubMed:25747881}.
CC -!- INTERACTION:
CC Q0WLB5; Q0WLB5: CHC2; NbExp=2; IntAct=EBI-4412194, EBI-4412194;
CC Q0WLB5; O04209: CLC2; NbExp=3; IntAct=EBI-4412194, EBI-4406025;
CC Q0WLB5; Q5ICL9: NPR4; NbExp=3; IntAct=EBI-4412194, EBI-1392093;
CC Q0WLB5; F4J8D3: TPLATE; NbExp=2; IntAct=EBI-4412194, EBI-4412119;
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: Defective in bulk endocytosis as well as in
CC internalization of prominent plasma membrane proteins. Defects in
CC constitutive endocytic recycling of PIN auxin transporters and their
CC polar distribution in embryos and roots leading to altered auxin
CC distribution patterns and associated auxin transport-related
CC phenotypes. Defective in embryonic and postembryonic development.
CC {ECO:0000269|PubMed:21551390}.
CC -!- SIMILARITY: Belongs to the clathrin heavy chain family. {ECO:0000305}.
CC -!- CAUTION: Was assigned to CHC1 in PubMed:21187379. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAG50828.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=AAG51341.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=AAM19776.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AC012562; AAG51341.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AC074395; AAG50828.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002686; AEE74644.1; -; Genomic_DNA.
DR EMBL; AK230290; BAF02092.1; -; mRNA.
DR EMBL; AY094397; AAM19776.1; ALT_INIT; mRNA.
DR EMBL; AY125528; AAM78038.1; -; mRNA.
DR RefSeq; NP_187466.4; NM_111688.7.
DR AlphaFoldDB; Q0WLB5; -.
DR SMR; Q0WLB5; -.
DR BioGRID; 5336; 99.
DR DIP; DIP-59590N; -.
DR IntAct; Q0WLB5; 54.
DR MINT; Q0WLB5; -.
DR STRING; 3702.AT3G08530.1; -.
DR iPTMnet; Q0WLB5; -.
DR PaxDb; Q0WLB5; -.
DR PRIDE; Q0WLB5; -.
DR ProteomicsDB; 246814; -.
DR EnsemblPlants; AT3G08530.1; AT3G08530.1; AT3G08530.
DR GeneID; 820001; -.
DR Gramene; AT3G08530.1; AT3G08530.1; AT3G08530.
DR KEGG; ath:AT3G08530; -.
DR Araport; AT3G08530; -.
DR TAIR; locus:2103442; AT3G08530.
DR eggNOG; KOG0985; Eukaryota.
DR HOGENOM; CLU_002136_0_0_1; -.
DR InParanoid; Q0WLB5; -.
DR OMA; QKMKSHQ; -.
DR OrthoDB; 17940at2759; -.
DR PhylomeDB; Q0WLB5; -.
DR PRO; PR:Q0WLB5; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q0WLB5; baseline and differential.
DR Genevisible; Q0WLB5; AT.
DR GO; GO:0009507; C:chloroplast; HDA:TAIR.
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:0005794; C:Golgi apparatus; HDA:TAIR.
DR GO; GO:0005886; C:plasma membrane; HDA:TAIR.
DR GO; GO:0009506; C:plasmodesma; HDA:TAIR.
DR GO; GO:0032051; F:clathrin light chain binding; IBA:GO_Central.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0003729; F:mRNA binding; IDA:TAIR.
DR GO; GO:0005198; F:structural molecule activity; IEA:InterPro.
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:0016192; P:vesicle-mediated transport; IDA:TAIR.
DR Gene3D; 1.25.40.10; -; 2.
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..1703
FT /note="Clathrin heavy chain 2"
FT /id="PRO_0000413950"
FT REPEAT 551..697
FT /note="CHCR 1"
FT REPEAT 700..842
FT /note="CHCR 2"
FT REPEAT 847..986
FT /note="CHCR 3"
FT REPEAT 993..1138
FT /note="CHCR 4"
FT REPEAT 1142..1283
FT /note="CHCR 5"
FT REPEAT 1288..1434
FT /note="CHCR 6"
FT REPEAT 1437..1580
FT /note="CHCR 7"
FT REGION 2..492
FT /note="Globular terminal domain"
FT /evidence="ECO:0000250"
FT REGION 25..67
FT /note="WD40-like repeat 1"
FT REGION 68..113
FT /note="WD40-like repeat 2"
FT REGION 114..155
FT /note="WD40-like repeat 3"
FT REGION 156..205
FT /note="WD40-like repeat 4"
FT REGION 206..270
FT /note="WD40-like repeat 5"
FT REGION 271..314
FT /note="WD40-like repeat 6"
FT REGION 315..343
FT /note="WD40-like repeat 7"
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..1703
FT /note="Heavy chain arm"
FT /evidence="ECO:0000250"
FT REGION 537..648
FT /note="Distal segment"
FT /evidence="ECO:0000250"
FT REGION 653..1703
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..1703
FT /note="Trimerization"
FT /evidence="ECO:0000250"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0007744|PubMed:22223895"
SQ SEQUENCE 1703 AA; 193271 MW; 6A91D665A841F504 CRC64;
MAAANAPITM KEVLTLPSIG INQQFITFTN VTMESDKYIC VRETSPQNSV VIIDMNMPMQ
PLRRPITADS ALMNPNSKIL ALKAQVPGTT QDHLQIFNIE AKAKLKSHQM PEQVVFWKWI
TPKMLGLVTQ NSVYHWSIEG DSEPVKMFDR TANLANNQII NYKCSPNEKW LVLIGIAPGS
PERQQLVKGN 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 VGYTPDYLFL LQTILRTDPQ
GAVNFALMMS QMEGGSPVDY NTITDLFLQR NLIREATSFL LDVLKPNLPE HAFLQTKVLE
INLVTFPNVA DAVLANGMFT HYDRPRIAQL CEKAGLYIQS LKHYSELPDI KRVIVNTHAI
EPQALVEFFG TLSSEWAMEC MKDLLLVNLR GNLQIIVQAC KEYCEQLGVD ACIKLFEQFK
SYEGLYFFLG SYLSMSEDPE IHFKYIEAAA KTGQIKEVER VTRESNFYDA EKTKNFLMEA
KLPDARPLIN VCDRFSFVPD LTHYLYTNNM LRYIEGYVQK VNPGNAPLVV GQLLDDECPE
DFIKGLILSV RSLLPVEPLV EECEKRNRLR LLTQFLEHLV SEGSQDVHVH NALGKIIIDS
NNNPEHFLTT NPYYDSKVVG KYCEKRDPTL AVVAYRRGQC DEELINVTNK NSLFKLQARY
VVERMDGDLW DKVLDENNDY RRQLIDQVVS TALPESKSPE QVSAAVKAFM TADLPHELIE
LLEKIVLQNS AFSGNFNLQN LLILTAIKAD PSRVMDYINR LDNFDGPAVG EVAVEAQLYE
EAFAIFKKFN LNVQAVNVLL DNVRSIERAV EFAFRVEEDS VWSQVAKAQL REGLVSDAIE
SFIRADDATH FLEVIRVSED TDVYDDLVKY LLMVRQKVKE PKVDSELIYA YAKIDRLGEI
EEFILMPNVA NLQHVGDRLY DEALYEAAKI IYAFISNWGK LAVTLVKLQQ FQGAVDAARK
ANSAKTWKEV CFACVDAEEF RLAQICGLNI IIQVDDLEEV SEYYQNRGCF NELISLMESG
LGLERAHMGI FTELGVLYAR YRYEKLMEHI KLFSTRLNIP KLIRACDEQQ HWQELTYLYI
QYDEFDNAAT TVMNHSPEAW EHMQFKDIVA KVANVELYYK AVHFYLQEHP DIINDLLNVL
ALRLDHTRVV DIMRKAGHLR LIKPYMIAVQ SNNVSAVNEA LNEIYVEEED YDRLRESIDL
HDSFDQIGLA QKIEKHELVE MRRVAAYIYK KAGRWKQSIA LSKKDNMYKD CMETASQSGE
HELAEQLLVY FIEQGKKECF ATCLFVCYDL IRPDVALELA WINNMMDFAF PYLLQFIREY
SGKVDELIKD KLEAQKEVKA KEQEEKDVIS QQNMYAQMLP LALPAPPMPG MGGGGGYGPP
PQMGGMPGMP PMPPYGMPPM GGY
