CLC1_ARATH
ID CLC1_ARATH Reviewed; 338 AA.
AC Q9SKU1; Q8LG44;
DT 16-NOV-2011, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 113.
DE RecName: Full=Clathrin light chain 1;
GN OrderedLocusNames=At2g20760; ORFNames=F5H14.27;
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 Quinitio C., Chen H., Kim C.J., Shinn P., Ecker J.R.;
RT "Arabidopsis ORF clones.";
RL Submitted (JUN-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.
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. {ECO:0000250}.
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 -!- SIMILARITY: Belongs to the clathrin light chain family. {ECO:0000305}.
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DR EMBL; AC006234; AAD20919.1; -; Genomic_DNA.
DR EMBL; CP002685; AEC07067.1; -; Genomic_DNA.
DR EMBL; AY057515; AAL09756.1; -; mRNA.
DR EMBL; AY057654; AAL15285.1; -; mRNA.
DR EMBL; BT025885; ABF85787.1; -; mRNA.
DR EMBL; AY084472; AAM61043.1; -; mRNA.
DR PIR; A84593; A84593.
DR RefSeq; NP_565484.1; NM_127641.4.
DR AlphaFoldDB; Q9SKU1; -.
DR SMR; Q9SKU1; -.
DR BioGRID; 1958; 6.
DR IntAct; Q9SKU1; 1.
DR STRING; 3702.AT2G20760.1; -.
DR iPTMnet; Q9SKU1; -.
DR PaxDb; Q9SKU1; -.
DR PRIDE; Q9SKU1; -.
DR ProteomicsDB; 246877; -.
DR EnsemblPlants; AT2G20760.1; AT2G20760.1; AT2G20760.
DR GeneID; 816605; -.
DR Gramene; AT2G20760.1; AT2G20760.1; AT2G20760.
DR KEGG; ath:AT2G20760; -.
DR Araport; AT2G20760; -.
DR TAIR; locus:2051472; AT2G20760.
DR eggNOG; ENOG502QVX7; Eukaryota.
DR HOGENOM; CLU_053778_2_0_1; -.
DR InParanoid; Q9SKU1; -.
DR OMA; DPTHAYS; -.
DR OrthoDB; 1220161at2759; -.
DR PhylomeDB; Q9SKU1; -.
DR PRO; PR:Q9SKU1; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; Q9SKU1; baseline and differential.
DR Genevisible; Q9SKU1; 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:0030125; C:clathrin vesicle coat; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; HDA:TAIR.
DR GO; GO:0005739; C:mitochondrion; HDA:TAIR.
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:0005198; F:structural molecule activity; IEA:InterPro.
DR GO; GO:0072583; P:clathrin-dependent endocytosis; IPI:TAIR.
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 2: Evidence at transcript level;
KW Coated pit; Coiled coil; Cytoplasmic vesicle; Membrane; Reference proteome.
FT CHAIN 1..338
FT /note="Clathrin light chain 1"
FT /id="PRO_0000413946"
FT REGION 1..111
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 102..163
FT /note="Involved in binding clathrin heavy chain"
FT /evidence="ECO:0000250"
FT REGION 192..338
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 122..142
FT /evidence="ECO:0000255"
FT COMPBIAS 29..81
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 192..212
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 254..307
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CONFLICT 270
FT /note="T -> A (in Ref. 5; AAM61043)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 338 AA; 37225 MW; 4E9DD3F153F7E710 CRC64;
MATFDDGDFP AQTHSPSEHE DFGGYDNFSE AQQPPTQHQS GGFSSFNGDP ASPNGYGFGA
SSPNHDFSSP FESSVNDANG NGGGSGGDAI FASDGPILPD PNEMREEGFQ RREWRRLNTI
HLEEKEKKEK EMRNQIITEA EDFKKAFYEK RDKTIETNKT DNREKEKLYW ANQEKFHKEV
DKHYWKAIAE LIPREVPNIE KKRGKKDPDK KPSVNVIQGP KPGKPTDLGR MRQIFLKLKT
NPPPHMMPPP PPAKDAKDGK DAKDGKDAKT GKDGKDAKGG KDAKDLKDGK PADPKVTEEK
RPSPAKDASV ETAKPDAAAS GEGEKPVAVT EAEGTKAE
