CLC2_ARATH
ID CLC2_ARATH Reviewed; 258 AA.
AC O04209; Q8L9R8;
DT 16-NOV-2011, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1997, sequence version 1.
DT 03-AUG-2022, entry version 125.
DE RecName: Full=Clathrin light chain 2;
GN Name=CLC2; OrderedLocusNames=At2g40060; ORFNames=T28M21.22;
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=10617197; DOI=10.1038/45471;
RA Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D.,
RA Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V.,
RA Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L., Moffat K.S.,
RA Cronin L.A., Shen M., Pai G., Van Aken S., Umayam L., Tallon L.J.,
RA Gill J.E., Adams M.D., Carrera A.J., Creasy T.H., Goodman H.M.,
RA Somerville C.R., Copenhaver G.P., Preuss D., Nierman W.C., White O.,
RA Eisen J.A., Salzberg S.L., Fraser C.M., Venter J.C.;
RT "Sequence and analysis of chromosome 2 of the plant Arabidopsis thaliana.";
RL Nature 402:761-768(1999).
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;
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RA Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Morosawa T.,
RA Kamiya A., Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K.,
RA Kohara Y., Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K.,
RA Akiyama K., Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J.,
RA Hayashizaki Y., Shinozaki K.;
RT "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
RL Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B.,
RA Feldmann K.A.;
RT "Full-length cDNA from Arabidopsis thaliana.";
RL Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP IDENTIFICATION.
RX PubMed=11943181; DOI=10.1016/s0014-5793(02)02439-0;
RA Scheele U., Holstein S.E.;
RT "Functional evidence for the identification of an Arabidopsis clathrin
RT light chain polypeptide.";
RL FEBS Lett. 514:355-360(2002).
RN [7]
RP SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=18502847; DOI=10.1105/tpc.108.059428;
RA Konopka C.A., Backues S.K., Bednarek S.Y.;
RT "Dynamics of Arabidopsis dynamin-related protein 1C and a clathrin light
RT chain at the plasma membrane.";
RL Plant Cell 20:1363-1380(2008).
RN [8]
RP SUBCELLULAR LOCATION.
RX PubMed=20231465; DOI=10.1073/pnas.0913562107;
RA Fujimoto M., Arimura S., Ueda T., Takanashi H., Hayashi Y., Nakano A.,
RA Tsutsumi N.;
RT "Arabidopsis dynamin-related proteins DRP2B and DRP1A participate together
RT in clathrin-coated vesicle formation during endocytosis.";
RL Proc. Natl. Acad. Sci. U.S.A. 107:6094-6099(2010).
RN [9]
RP SUBCELLULAR LOCATION, AND INTERACTION WITH TPLATE AND CHC2.
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).
CC -!- FUNCTION: Clathrin is the major protein of the polyhedral coat of
CC coated pits and vesicles.
CC -!- SUBUNIT: Clathrin coats are formed from molecules containing 3 heavy
CC chains and 3 light chains (By similarity). Interacts with TPLATE and
CC CHC2. {ECO:0000250, ECO:0000269|PubMed:21187379}.
CC -!- INTERACTION:
CC O04209; Q0WLB5: CHC2; NbExp=3; IntAct=EBI-4406025, EBI-4412194;
CC O04209; O04209: CLC2; NbExp=2; IntAct=EBI-4406025, EBI-4406025;
CC O04209; F4J8D3: TPLATE; NbExp=5; IntAct=EBI-4406025, EBI-4412119;
CC -!- SUBCELLULAR LOCATION: Cell membrane. Cytoplasmic vesicle membrane
CC {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; Cytoplasmic
CC side {ECO:0000250}. Membrane, coated pit {ECO:0000250}; Peripheral
CC membrane protein {ECO:0000250}; Cytoplasmic side {ECO:0000250}.
CC Cytoplasm, cytoskeleton, phragmoplast. Note=Cytoplasmic face of coated
CC pits and vesicles (By similarity). Localized in the forming cell plate
CC and the cortical division zone (CDZ) during cytokinesis. {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Expressed in root epidermal cells and root hairs
CC (at the protein level). {ECO:0000269|PubMed:18502847}.
CC -!- SIMILARITY: Belongs to the clathrin light chain family. {ECO:0000305}.
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DR EMBL; AF002109; AAB95291.1; -; Genomic_DNA.
DR EMBL; CP002685; AEC09770.1; -; Genomic_DNA.
DR EMBL; AY092995; AAM12994.1; -; mRNA.
DR EMBL; AY114610; AAM47929.1; -; mRNA.
DR EMBL; AK226476; BAE98618.1; -; mRNA.
DR EMBL; AY088269; AAM65809.1; -; mRNA.
DR PIR; G84824; G84824.
DR RefSeq; NP_565921.1; NM_129564.3.
DR AlphaFoldDB; O04209; -.
DR SMR; O04209; -.
DR BioGRID; 3932; 11.
DR DIP; DIP-59589N; -.
DR IntAct; O04209; 9.
DR STRING; 3702.AT2G40060.1; -.
DR iPTMnet; O04209; -.
DR PaxDb; O04209; -.
DR PRIDE; O04209; -.
DR ProteomicsDB; 246878; -.
DR EnsemblPlants; AT2G40060.1; AT2G40060.1; AT2G40060.
DR GeneID; 818594; -.
DR Gramene; AT2G40060.1; AT2G40060.1; AT2G40060.
DR KEGG; ath:AT2G40060; -.
DR Araport; AT2G40060; -.
DR TAIR; locus:2061196; AT2G40060.
DR eggNOG; ENOG502QVX7; Eukaryota.
DR HOGENOM; CLU_053778_1_1_1; -.
DR InParanoid; O04209; -.
DR OMA; QYKEEFH; -.
DR OrthoDB; 1220161at2759; -.
DR PhylomeDB; O04209; -.
DR PRO; PR:O04209; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; O04209; baseline and differential.
DR Genevisible; O04209; AT.
DR GO; GO:0009504; C:cell plate; IDA:TAIR.
DR GO; GO:0009941; C:chloroplast envelope; 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:0030125; C:clathrin vesicle coat; IBA:GO_Central.
DR GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-KW.
DR GO; GO:0005794; C:Golgi apparatus; HDA:TAIR.
DR GO; GO:0009524; C:phragmoplast; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0032050; F:clathrin heavy chain binding; IBA:GO_Central.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0005198; F:structural molecule activity; IEA:InterPro.
DR GO; GO:0072583; P:clathrin-dependent endocytosis; IBA:GO_Central.
DR GO; GO:0006886; P:intracellular protein transport; IEA:InterPro.
DR InterPro; IPR000996; Clathrin_L-chain.
DR PANTHER; PTHR10639; PTHR10639; 1.
DR Pfam; PF01086; Clathrin_lg_ch; 1.
PE 1: Evidence at protein level;
KW Cell membrane; Coated pit; Coiled coil; Cytoplasm; Cytoplasmic vesicle;
KW Cytoskeleton; Membrane; Reference proteome.
FT CHAIN 1..258
FT /note="Clathrin light chain 2"
FT /id="PRO_0000413947"
FT REGION 61..85
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 81..143
FT /note="Involved in binding clathrin heavy chain"
FT /evidence="ECO:0000250"
FT REGION 177..258
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 91..156
FT /evidence="ECO:0000255"
FT COMPBIAS 177..192
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CONFLICT 30
FT /note="D -> E (in Ref. 5; AAM65809)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 258 AA; 28837 MW; A8E4C855D86316E7 CRC64;
MSAFEDDSFV ILNDDASESV PVSGSFDATD SFSAFDGSLQ VEDSVDDVFA APSSDYGAYS
NGDGIFGSNG DHDGPILPPP SEMESDEGFA LREWRRQNAI QLEEKEKREK ELLKQIIEEA
DQYKEEFHKK IEVTCENNKA ANREKEKLYL ENQEKFYAES SKNYWKAIAE LVPKEVPTIE
KRRGKKEQQD PKKPTVSVIQ GPKPGKPTDL TRMRQILVKL KHNPPSHLKL TSQPPSEEAA
APPKNVPETK PTEAVTAA
