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Clathrin heavy chain 2

 CLAH2_ARATH             Reviewed;        1703 AA.
Q0WLB5; Q8L3R8; Q9C6U0; Q9CA00;
16-NOV-2011, integrated into UniProtKB/Swiss-Prot.
05-SEP-2006, sequence version 1.
28-MAR-2018, entry version 99.
RecName: Full=Clathrin heavy chain 2;
Name=CHC2; Synonyms=CHC1; OrderedLocusNames=At3g08530;
ORFNames=F17O14.1, T8G24.1;
Arabidopsis thaliana (Mouse-ear cress).
Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
Spermatophyta; Magnoliophyta; eudicotyledons; Gunneridae;
Pentapetalae; rosids; malvids; Brassicales; Brassicaceae; Camelineae;
Arabidopsis.
NCBI_TaxID=3702;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=cv. Columbia;
PubMed=11130713; DOI=10.1038/35048706;
Salanoubat M., Lemcke K., Rieger M., Ansorge W., Unseld M.,
Fartmann B., Valle G., Bloecker H., Perez-Alonso M., Obermaier B.,
Delseny M., Boutry M., Grivell L.A., Mache R., Puigdomenech P.,
De Simone V., Choisne N., Artiguenave F., Robert C., Brottier P.,
Wincker P., Cattolico L., Weissenbach J., Saurin W., Quetier F.,
Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Benes V.,
Wurmbach E., Drzonek H., Erfle H., Jordan N., Bangert S.,
Wiedelmann R., Kranz H., Voss H., Holland R., Brandt P., Nyakatura G.,
Vezzi A., D'Angelo M., Pallavicini A., Toppo S., Simionati B.,
Conrad A., Hornischer K., Kauer G., Loehnert T.-H., Nordsiek G.,
Reichelt J., Scharfe M., Schoen O., Bargues M., Terol J., Climent J.,
Navarro P., Collado C., Perez-Perez A., Ottenwaelder B., Duchemin D.,
Cooke R., Laudie M., Berger-Llauro C., Purnelle B., Masuy D.,
de Haan M., Maarse A.C., Alcaraz J.-P., Cottet A., Casacuberta E.,
Monfort A., Argiriou A., Flores M., Liguori R., Vitale D.,
Mannhaupt G., Haase D., Schoof H., Rudd S., Zaccaria P., Mewes H.-W.,
Mayer K.F.X., Kaul S., Town C.D., Koo H.L., Tallon L.J., Jenkins J.,
Rooney T., Rizzo M., Walts A., Utterback T., Fujii C.Y., Shea T.P.,
Creasy T.H., Haas B., Maiti R., Wu D., Peterson J., Van Aken S.,
Pai G., Militscher J., Sellers P., Gill J.E., Feldblyum T.V.,
Preuss D., Lin X., Nierman W.C., Salzberg S.L., White O., Venter J.C.,
Fraser C.M., Kaneko T., Nakamura Y., Sato S., Kato T., Asamizu E.,
Sasamoto S., Kimura T., Idesawa K., Kawashima K., Kishida Y.,
Kiyokawa C., Kohara M., Matsumoto M., Matsuno A., Muraki A.,
Nakayama S., Nakazaki N., Shinpo S., Takeuchi C., Wada T.,
Watanabe A., Yamada M., Yasuda M., Tabata S.;
"Sequence and analysis of chromosome 3 of the plant Arabidopsis
thaliana.";
Nature 408:820-822(2000).
[2]
GENOME REANNOTATION.
STRAIN=cv. Columbia;
The Arabidopsis Information Portal (Araport);
Submitted (MAY-2016) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=cv. Columbia;
Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A.,
Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y.,
Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.,
Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J.,
Hayashizaki Y., Shinozaki K.;
"Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 973-1703.
STRAIN=cv. Columbia;
PubMed=14593172; DOI=10.1126/science.1088305;
Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J.,
Southwick A.M., Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F.,
Karlin-Newmann G., Liu S.X., Lam B., Sakano H., Wu T., Yu G.,
Miranda M., Quach H.L., Tripp M., Chang C.H., Lee J.M., Toriumi M.J.,
Chan M.M., Tang C.C., Onodera C.S., Deng J.M., Akiyama K., Ansari Y.,
Arakawa T., Banh J., Banno F., Bowser L., Brooks S.Y., Carninci P.,
Chao Q., Choy N., Enju A., Goldsmith A.D., Gurjal M., Hansen N.F.,
Hayashizaki Y., Johnson-Hopson C., Hsuan V.W., Iida K., Karnes M.,
Khan S., Koesema E., Ishida J., Jiang P.X., Jones T., Kawai J.,
Kamiya A., Meyers C., Nakajima M., Narusaka M., Seki M., Sakurai T.,
Satou M., Tamse R., Vaysberg M., Wallender E.K., Wong C., Yamamura Y.,
Yuan S., Shinozaki K., Davis R.W., Theologis A., Ecker J.R.;
"Empirical analysis of transcriptional activity in the Arabidopsis
genome.";
Science 302:842-846(2003).
[5]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
STRAIN=cv. Landsberg erecta;
PubMed=17272265; DOI=10.1074/mcp.M600408-MCP200;
Maor R., Jones A., Nuehse T.S., Studholme D.J., Peck S.C., Shirasu K.;
"Multidimensional protein identification technology (MudPIT) analysis
of ubiquitinated proteins in plants.";
Mol. Cell. Proteomics 6:601-610(2007).
[6]
FUNCTION, AND DISRUPTION PHENOTYPE.
PubMed=21551390; DOI=10.1105/tpc.111.083030;
Kitakura S., Vanneste S., Robert S., Loefke C., Teichmann T.,
Tanaka H., Friml J.;
"Clathrin mediates endocytosis and polar distribution of PIN auxin
transporters in Arabidopsis.";
Plant Cell 23:1920-1931(2011).
[7]
INTERACTION WITH CLC2 AND TPLATE.
PubMed=21187379; DOI=10.1073/pnas.1017890108;
Van Damme D., Gadeyne A., Vanstraelen M., Inze D., Van Montagu M.C.,
De Jaeger G., Russinova E., Geelen D.;
"Adaptin-like protein TPLATE and clathrin recruitment during plant
somatic cytokinesis occurs via two distinct pathways.";
Proc. Natl. Acad. Sci. U.S.A. 108:615-620(2011).
[8]
ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22223895; DOI=10.1074/mcp.M111.015131;
Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C.,
Meinnel T., Giglione C.;
"Comparative large-scale characterisation of plant vs. mammal proteins
reveals similar and idiosyncratic N-alpha acetylation features.";
Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
[9]
INTERACTION WITH EDR4.
STRAIN=cv. Columbia;
PubMed=25747881; DOI=10.1105/tpc.114.134668;
Wu G., Liu S., Zhao Y., Wang W., Kong Z., Tang D.;
"ENHANCED DISEASE RESISTANCE4 associates with CLATHRIN HEAVY CHAIN2
and modulates plant immunity by regulating relocation of EDR1 in
Arabidopsis.";
Plant Cell 27:857-873(2015).
-!- FUNCTION: Clathrin is the major protein of the polyhedral coat of
coated pits and vesicles (By similarity). Mediates endocytosis and
is required for a correct polar distribution of PIN auxin
transporters. {ECO:0000250, ECO:0000269|PubMed:21551390}.
-!- SUBUNIT: Clathrin triskelions, composed of 3 heavy chains and 3
light chains, are the basic subunits of the clathrin coat (By
similarity). Interacts with CLC2 and TPLATE. Interacts with EDR4
(PubMed:25747881). {ECO:0000250, ECO:0000269|PubMed:21187379,
ECO:0000269|PubMed:25747881}.
-!- INTERACTION:
Self; NbExp=2; IntAct=EBI-4412194, EBI-4412194;
O04209:CLC2; NbExp=3; IntAct=EBI-4412194, EBI-4406025;
F4J8D3:TPLATE; NbExp=2; IntAct=EBI-4412194, EBI-4412119;
-!- SUBCELLULAR LOCATION: Cytoplasmic vesicle membrane {ECO:0000250};
Peripheral membrane protein {ECO:0000250}; Cytoplasmic side
{ECO:0000250}. Membrane, coated pit {ECO:0000250}; Peripheral
membrane protein {ECO:0000250}; Cytoplasmic side {ECO:0000250}.
Note=Cytoplasmic face of coated pits and vesicles. {ECO:0000250}.
-!- DOMAIN: The C-terminal third of the heavy chains forms the hub of
the triskelion. This region contains the trimerization domain and
the light-chain binding domain involved in the assembly of the
clathrin lattice.
-!- DOMAIN: The N-terminal seven-bladed beta-propeller is formed by
WD40-like repeats, and projects inward from the polyhedral outer
clathrin coat. It constitutes a major protein-protein interaction
node (By similarity). {ECO:0000250}.
-!- DISRUPTION PHENOTYPE: Defective in bulk endocytosis as well as in
internalization of prominent plasma membrane proteins. Defects in
constitutive endocytic recycling of PIN auxin transporters and
their polar distribution in embryos and roots leading to altered
auxin distribution patterns and associated auxin transport-related
phenotypes. Defective in embryonic and postembryonic development.
{ECO:0000269|PubMed:21551390}.
-!- SIMILARITY: Belongs to the clathrin heavy chain family.
{ECO:0000305}.
-!- CAUTION: Was assigned to CHC1 in PubMed:21187379. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=AAG50828.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
Sequence=AAG51341.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
Sequence=AAM19776.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305};
-----------------------------------------------------------------------
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Distributed under the Creative Commons Attribution-NoDerivs License
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EMBL; AC012562; AAG51341.1; ALT_SEQ; Genomic_DNA.
EMBL; AC074395; AAG50828.1; ALT_SEQ; Genomic_DNA.
EMBL; CP002686; AEE74644.1; -; Genomic_DNA.
EMBL; AK230290; BAF02092.1; -; mRNA.
EMBL; AY094397; AAM19776.1; ALT_INIT; mRNA.
EMBL; AY125528; AAM78038.1; -; mRNA.
RefSeq; NP_187466.4; NM_111688.7.
UniGene; At.17332; -.
UniGene; At.26828; -.
ProteinModelPortal; Q0WLB5; -.
SMR; Q0WLB5; -.
BioGrid; 5336; 50.
DIP; DIP-59590N; -.
IntAct; Q0WLB5; 53.
MINT; Q0WLB5; -.
STRING; 3702.AT3G08530.1; -.
iPTMnet; Q0WLB5; -.
PaxDb; Q0WLB5; -.
PRIDE; Q0WLB5; -.
EnsemblPlants; AT3G08530.1; AT3G08530.1; AT3G08530.
GeneID; 820001; -.
Gramene; AT3G08530.1; AT3G08530.1; AT3G08530.
KEGG; ath:AT3G08530; -.
Araport; AT3G08530; -.
TAIR; locus:2103442; AT3G08530.
eggNOG; KOG0985; Eukaryota.
eggNOG; ENOG410XPH1; LUCA.
HOGENOM; HOG000188877; -.
InParanoid; Q0WLB5; -.
KO; K04646; -.
OMA; RCYDDKM; -.
OrthoDB; EOG0936004P; -.
PhylomeDB; Q0WLB5; -.
Reactome; R-ATH-8856828; Clathrin-mediated endocytosis.
PRO; PR:Q0WLB5; -.
Proteomes; UP000006548; Chromosome 3.
ExpressionAtlas; Q0WLB5; baseline and differential.
Genevisible; Q0WLB5; AT.
GO; GO:0009507; C:chloroplast; IDA:TAIR.
GO; GO:0030132; C:clathrin coat of coated pit; IEA:InterPro.
GO; GO:0030130; C:clathrin coat of trans-Golgi network vesicle; IEA:InterPro.
GO; GO:0071439; C:clathrin complex; IEA:InterPro.
GO; GO:0005829; C:cytosol; IDA:TAIR.
GO; GO:0005794; C:Golgi apparatus; IDA:TAIR.
GO; GO:0016020; C:membrane; IDA:TAIR.
GO; GO:0005886; C:plasma membrane; IDA:TAIR.
GO; GO:0009506; C:plasmodesma; IDA:TAIR.
GO; GO:0032051; F:clathrin light chain binding; IEA:InterPro.
GO; GO:0042802; F:identical protein binding; IPI:IntAct.
GO; GO:0005198; F:structural molecule activity; IEA:InterPro.
GO; GO:0048268; P:clathrin coat assembly; IEA:InterPro.
GO; GO:0006897; P:endocytosis; IMP:TAIR.
GO; GO:0006886; P:intracellular protein transport; IEA:InterPro.
GO; GO:0016192; P:vesicle-mediated transport; IDA:TAIR.
Gene3D; 1.25.40.10; -; 3.
InterPro; IPR016024; ARM-type_fold.
InterPro; IPR000547; Clathrin_H-chain/VPS_repeat.
InterPro; IPR015348; Clathrin_H-chain_linker_core.
InterPro; IPR022365; Clathrin_H-chain_propeller_rpt.
InterPro; IPR016341; Clathrin_heavy_chain.
InterPro; IPR011990; TPR-like_helical_dom_sf.
Pfam; PF00637; Clathrin; 7.
Pfam; PF09268; Clathrin-link; 1.
Pfam; PF01394; Clathrin_propel; 2.
PIRSF; PIRSF002290; Clathrin_H_chain; 1.
SMART; SM00299; CLH; 7.
SUPFAM; SSF48371; SSF48371; 5.
PROSITE; PS50236; CHCR; 7.
1: Evidence at protein level;
Acetylation; Coated pit; Complete proteome; Cytoplasmic vesicle;
Endocytosis; Membrane; Reference proteome; Repeat.
INIT_MET 1 1 Removed. {ECO:0000244|PubMed:22223895}.
CHAIN 2 1703 Clathrin heavy chain 2.
/FTId=PRO_0000413950.
REPEAT 551 697 CHCR 1.
REPEAT 700 842 CHCR 2.
REPEAT 847 986 CHCR 3.
REPEAT 993 1138 CHCR 4.
REPEAT 1142 1283 CHCR 5.
REPEAT 1288 1434 CHCR 6.
REPEAT 1437 1580 CHCR 7.
REGION 2 492 Globular terminal domain. {ECO:0000250}.
REGION 25 67 WD40-like repeat 1.
REGION 68 113 WD40-like repeat 2.
REGION 114 155 WD40-like repeat 3.
REGION 156 205 WD40-like repeat 4.
REGION 206 270 WD40-like repeat 5.
REGION 271 314 WD40-like repeat 6.
REGION 315 343 WD40-like repeat 7.
REGION 462 478 Binding site for the uncoating ATPase,
involved in lattice disassembly.
{ECO:0000250}.
REGION 493 536 Flexible linker. {ECO:0000250}.
REGION 537 1703 Heavy chain arm. {ECO:0000250}.
REGION 537 648 Distal segment. {ECO:0000250}.
REGION 653 1703 Proximal segment. {ECO:0000250}.
REGION 1227 1536 Involved in binding clathrin light chain.
{ECO:0000250}.
REGION 1564 1703 Trimerization. {ECO:0000250}.
MOD_RES 2 2 N-acetylalanine.
{ECO:0000244|PubMed:22223895}.
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


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