ID CLCA_HUMAN Reviewed; 248 AA. AC P09496; A8K4W3; B4DIN1; F5H6N3; Q2XPN5; Q53XZ1; DT 01-JUL-1989, integrated into UniProtKB/Swiss-Prot. DT 01-JUL-1989, sequence version 1. DT 02-SEP-2026, entry version 225. DE RecName: Full=Clathrin light chain A; DE Short=Lca; GN Name=CLTA; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; OC Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS BRAIN AND NON-BRAIN). RX PubMed=3267234; DOI=10.1016/s0021-9258(18)37445-3; RA Jackson A.P., Parham P.; RT "Structure of human clathrin light chains. Conservation of light chain RT polymorphism in three mammalian species."; RL J. Biol. Chem. 263:16688-16695(1988). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM NON-BRAIN). RA Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., RA Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., RA Phelan M., Farmer A.; RT "Cloning of human full-length CDSs in BD Creator(TM) system donor vector."; RL Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases. RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS NON-BRAIN AND 4). RC TISSUE=Hippocampus; RX PubMed=14702039; DOI=10.1038/ng1285; RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S., RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., RA Isogai T., Sugano S.; RT "Complete sequencing and characterization of 21,243 full-length human RT cDNAs."; RL Nat. Genet. 36:40-45(2004). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3). RA Lin L., Nong W., Zhou G., Ke R., Shen C., Zhong G., Zheng Z., Liang M., RA Tang Z., Huang B., Li H., Yang S.; RL Submitted (OCT-2005) to the EMBL/GenBank/DDBJ databases. RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=15164053; DOI=10.1038/nature02465; RA Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E., Howe K.L., RA Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C., Ainscough R., RA Almeida J.P., Ambrose K.D., Ashwell R.I.S., Babbage A.K., Babbage S., RA Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., RA Beasley H., Beasley O., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y., RA Burford D., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., RA Chen Y., Clarke G., Clark S.Y., Clee C.M., Clegg S., Collier R.E., RA Corby N., Crosier M., Cummings A.T., Davies J., Dhami P., Dunn M., RA Dutta I., Dyer L.W., Earthrowl M.E., Faulkner L., Fleming C.J., RA Frankish A., Frankland J.A., French L., Fricker D.G., Garner P., RA Garnett J., Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S., RA Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E., RA Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D., RA Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E., RA Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K., RA Kimberley A.M., King A., Knights A., Laird G.K., Langford C., Lawlor S., RA Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M., Lovell J., RA Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S., McLay K.E., RA McMurray A., Milne S., Nickerson T., Nisbett J., Nordsiek G., Pearce A.V., RA Peck A.I., Porter K.M., Pandian R., Pelan S., Phillimore B., Povey S., RA Ramsey Y., Rand V., Scharfe M., Sehra H.K., Shownkeen R., Sims S.K., RA Skuce C.D., Smith M., Steward C.A., Swarbreck D., Sycamore N., Tester J., RA Thorpe A., Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M., RA West A.P., Whitehead S.L., Willey D.L., Williams S.A., Wilming L., RA Wray P.W., Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M., RA Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S., Rogers J., RA Dunham I.; RT "DNA sequence and analysis of human chromosome 9."; RL Nature 429:369-374(2004). RN [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., RA Hunkapiller M.W., Myers E.W., Venter J.C.; RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases. RN [7] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM NON-BRAIN). RC TISSUE=Lung; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA project: RT the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [8] RP FUNCTION, AND SUBCELLULAR LOCATION. RX PubMed=15858577; DOI=10.1038/nature03502; RA Royle S.J., Bright N.A., Lagnado L.; RT "Clathrin is required for the function of the mitotic spindle."; RL Nature 434:1152-1157(2005). RN [9] RP INTERACTION WITH CALY. RX PubMed=16595675; DOI=10.1074/jbc.m600265200; RA Xiao J., Dai R., Negyessy L., Bergson C.; RT "Calcyon, a novel partner of clathrin light chain, stimulates clathrin- RT mediated endocytosis."; RL J. Biol. Chem. 281:15182-15193(2006). RN [10] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007; RA Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., RA Greff Z., Keri G., Stemmann O., Mann M.; RT "Kinase-selective enrichment enables quantitative phosphoproteomics of the RT kinome across the cell cycle."; RL Mol. Cell 31:438-448(2008). RN [11] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-206 AND SER-236, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=18669648; DOI=10.1073/pnas.0805139105; RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., RA Elledge S.J., Gygi S.P.; RT "A quantitative atlas of mitotic phosphorylation."; RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008). RN [12] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=19369195; DOI=10.1074/mcp.m800588-mcp200; RA Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G., RA Mann M., Daub H.; RT "Large-scale proteomics analysis of the human kinome."; RL Mol. Cell. Proteomics 8:1751-1764(2009). RN [13] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-105 AND SER-206, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=20068231; DOI=10.1126/scisignal.2000475; RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.; RT "Quantitative phosphoproteomics reveals widespread full phosphorylation RT site occupancy during mitosis."; RL Sci. Signal. 3:RA3-RA3(2010). RN [14] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=21269460; DOI=10.1186/1752-0509-5-17; RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., RA Bennett K.L., Superti-Furga G., Colinge J.; RT "Initial characterization of the human central proteome."; RL BMC Syst. Biol. 5:17-17(2011). RN [15] RP INTERACTION WITH TACC3 AND CKAP5, FUNCTION, AND SUBCELLULAR LOCATION. RX PubMed=21297582; DOI=10.1038/emboj.2011.15; RA Booth D.G., Hood F.E., Prior I.A., Royle S.J.; RT "A TACC3/ch-TOG/clathrin complex stabilises kinetochore fibres by inter- RT microtubule bridging."; RL EMBO J. 30:906-919(2011). RN [16] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=22905912; DOI=10.1021/pr300539b; RA Rosenow A., Noben J.P., Jocken J., Kallendrusch S., Fischer-Posovszky P., RA Mariman E.C., Renes J.; RT "Resveratrol-induced changes of the human adipocyte secretion profile."; RL J. Proteome Res. 11:4733-4743(2012). RN [17] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-105, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma, and Erythroleukemia; RX PubMed=23186163; DOI=10.1021/pr300630k; RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J., RA Mohammed S.; RT "Toward a comprehensive characterization of a human cancer cell RT phosphoproteome."; RL J. Proteome Res. 12:260-271(2013). RN [18] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Liver; RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014; RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., RA Ye M., Zou H.; RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver RT phosphoproteome."; RL J. Proteomics 96:253-262(2014). RN [19] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=25944712; DOI=10.1002/pmic.201400617; RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D., RA Lane L., Bairoch A., Van Dorsselaer A., Carapito C.; RT "N-terminome analysis of the human mitochondrial proteome."; RL Proteomics 15:2519-2524(2015). CC -!- FUNCTION: Clathrin is the major protein of the polyhedral coat of CC coated pits and vesicles. Acts as a component of the TACC3/ch- CC TOG/clathrin complex proposed to contribute to stabilization of CC kinetochore fibers of the mitotic spindle by acting as inter- CC microtubule bridge (PubMed:15858577, PubMed:21297582). CC {ECO:0000305|PubMed:15858577, ECO:0000305|PubMed:21297582}. CC -!- SUBUNIT: Clathrin coats are formed from molecules containing 3 heavy CC chains and 3 light chains. Interacts with CALY; the interaction CC stimulates clathrin self-assembly and clathrin-mediated endocytosis. CC Interacts with CKAP5 and TACC3 forming the TACC3/ch-TOG/clathrin CC complex located at spindle inter-microtubules bridges; the complex CC implicates clathrin triskelions. {ECO:0000269|PubMed:16595675, CC ECO:0000269|PubMed:21297582}. CC -!- INTERACTION: CC P09496; Q9NYX4: CALY; NbExp=4; IntAct=EBI-1171169, EBI-10904725; CC P09496; Q00610: CLTC; NbExp=4; IntAct=EBI-1171169, EBI-354967; CC P09496; Q9Y6A5: TACC3; NbExp=3; IntAct=EBI-1171169, EBI-2554984; CC P09496-2; P55212: CASP6; NbExp=3; IntAct=EBI-4401010, EBI-718729; CC P09496-2; O94985-2: CLSTN1; NbExp=3; IntAct=EBI-4401010, EBI-16041593; CC P09496-2; Q8NI60: COQ8A; NbExp=3; IntAct=EBI-4401010, EBI-745535; CC P09496-2; O00291: HIP1; NbExp=3; IntAct=EBI-4401010, EBI-473886; CC P09496-2; P13473-2: LAMP2; NbExp=3; IntAct=EBI-4401010, EBI-21591415; CC P09496-2; O75400-2: PRPF40A; NbExp=3; IntAct=EBI-4401010, EBI-5280197; CC P09496-2; Q9Y371: SH3GLB1; NbExp=3; IntAct=EBI-4401010, EBI-2623095; CC -!- SUBCELLULAR LOCATION: Cytoplasmic vesicle membrane; Peripheral membrane CC protein; Cytoplasmic side. Membrane, coated pit; Peripheral membrane CC protein; Cytoplasmic side. Cytoplasm, cytoskeleton, spindle CC {ECO:0000269|PubMed:21297582, ECO:0000305|PubMed:15858577}. CC Note=Cytoplasmic face of coated pits and vesicles. In complex with CC TACC3 and CKAP5 (forming the TACC3/ch-TOG/clathrin complex) localized CC to inter-microtubule bridges in mitotic spindles. {ECO:0000305}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=5; CC Name=Brain; CC IsoId=P09496-1; Sequence=Displayed; CC Name=Non-brain; CC IsoId=P09496-2; Sequence=VSP_001095; CC Name=3; CC IsoId=P09496-3; Sequence=VSP_024238; CC Name=4; CC IsoId=P09496-4; Sequence=VSP_043239; CC Name=5; CC IsoId=P09496-5; Sequence=VSP_047168, VSP_001095; CC -!- SIMILARITY: Belongs to the clathrin light chain family. {ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; M20471; AAA51817.1; -; mRNA. DR EMBL; M20472; AAA59505.1; -; mRNA. DR EMBL; DQ270158; ABB76683.1; -; mRNA. DR EMBL; BT007170; AAP35834.1; -; mRNA. DR EMBL; AK291078; BAF83767.1; -; mRNA. DR EMBL; AK295692; BAG58543.1; -; mRNA. DR EMBL; AL158830; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AL161792; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CH471071; EAW58312.1; -; Genomic_DNA. DR EMBL; BC009201; AAH09201.1; -; mRNA. DR EMBL; BC019287; AAH19287.1; -; mRNA. DR CCDS; CCDS43802.1; -. [P09496-3] DR CCDS; CCDS55306.1; -. [P09496-4] DR CCDS; CCDS55307.1; -. [P09496-5] DR CCDS; CCDS6600.1; -. [P09496-2] DR CCDS; CCDS6601.1; -. [P09496-1] DR PIR; A31775; A31775. DR RefSeq; NP_001070145.1; NM_001076677.3. [P09496-3] DR RefSeq; NP_001171689.1; NM_001184760.2. [P09496-4] DR RefSeq; NP_001171691.1; NM_001184762.2. [P09496-5] DR RefSeq; NP_001824.1; NM_001833.4. [P09496-2] DR RefSeq; NP_009027.1; NM_007096.4. [P09496-1] DR PDB; 6E5N; NMR; -; A=46-61. DR AlphaFoldDB; P09496; -. DR SMR; P09496; -. DR BioGRID; 107621; 383. DR ComplexPortal; CPX-26707; Clathrin, endocytosis-mediating complex, CLTA variant. DR ComplexPortal; CPX-26726; Clathrin, endocytosis-mediating complex, CLTA-CLTB mixed lattice variant. DR FunCoup; P09496; 3210. DR IntAct; P09496; 245. DR MINT; P09496; -. DR NDEx; IQUERY-CP-CLTA; 10 NDEx IQuery Curated Pathways. DR STRING; 9606.ENSP00000242285; -. DR BindingDB; P09496; -. DR ChEMBL; CHEMBL4295706; -. DR TCDB; 8.A.137.1.1; the clathrin (clathrin) family. DR GlyGen; P09496; 2 sites, 1 O-linked glycan (1 site). DR iPTMnet; P09496; -. DR MetOSite; P09496; -. DR PhosphoSitePlus; P09496; -. DR SwissPalm; P09496; -. DR BioMuta; CLTA; -. DR DMDM; 116501; -. DR OGP; P09496; -. DR jPOST; P09496; -. DR MassIVE; P09496; -. DR PaxDb; 9606-ENSP00000242285; -. DR PeptideAtlas; P09496; -. DR ProteomicsDB; 27239; -. DR ProteomicsDB; 52236; -. [P09496-1] DR ProteomicsDB; 52237; -. [P09496-2] DR ProteomicsDB; 52238; -. [P09496-3] DR ProteomicsDB; 52239; -. [P09496-4] DR Pumba; P09496; -. DR TopDownProteomics; P09496-1; -. [P09496-1] DR TopDownProteomics; P09496-2; -. [P09496-2] DR Antibodypedia; 3626; 462 antibodies from 35 providers. DR DNASU; 1211; -. DR Ensembl; ENST00000242285.11; ENSP00000242285.6; ENSG00000122705.19. [P09496-1] DR Ensembl; ENST00000345519.10; ENSP00000242284.6; ENSG00000122705.19. [P09496-2] DR Ensembl; ENST00000396603.6; ENSP00000379848.2; ENSG00000122705.19. [P09496-3] DR Ensembl; ENST00000470744.5; ENSP00000419746.1; ENSG00000122705.19. [P09496-4] DR Ensembl; ENST00000540080.5; ENSP00000437508.1; ENSG00000122705.19. [P09496-5] DR Ensembl; ENST00000869064.1; ENSP00000539123.1; ENSG00000122705.19. [P09496-2] DR GeneID; 1211; -. DR KEGG; hsa:1211; -. DR MANE-Select; ENST00000345519.10; ENSP00000242284.6; NM_001833.4; NP_001824.1. [P09496-2] DR UCSC; uc003zzc.4; human. [P09496-1] DR AGR; HGNC:2090; -. DR ClinPGx; PA26616; -. DR CTD; 1211; -. DR DisGeNET; 1211; -. DR GeneCards; CLTA; -. DR HGNC; HGNC:2090; CLTA. DR HPA; ENSG00000122705; Low tissue specificity. DR MalaCards; CLTA; -. DR MIM; 118960; gene. DR OpenTargets; ENSG00000122705; -. DR VEuPathDB; HostDB:ENSG00000122705; -. DR eggNOG; KOG4031; Eukaryota. DR GeneTree; ENSGT00940000157347; -. DR InParanoid; P09496; -. DR OMA; XAAEEAF; -. DR OrthoDB; 5512at2759; -. DR PAN-GO; P09496; 5 GO annotations based on evolutionary models. DR PhylomeDB; P09496; -. DR PathwayCommons; P09496; -. DR Reactome; R-HSA-168275; Entry of Influenza Virion into Host Cell via Endocytosis. DR Reactome; R-HSA-177504; Retrograde neurotrophin signalling. DR Reactome; R-HSA-190873; Gap junction degradation. DR Reactome; R-HSA-196025; Formation of annular gap junctions. DR Reactome; R-HSA-2132295; MHC class II antigen presentation. DR Reactome; R-HSA-3928665; EPH-ephrin mediated repulsion of cells. DR Reactome; R-HSA-432720; Lysosome Vesicle Biogenesis. DR Reactome; R-HSA-432722; Golgi Associated Vesicle Biogenesis. [P09496-1] DR Reactome; R-HSA-437239; Recycling pathway of L1. DR Reactome; R-HSA-5099900; WNT5A-dependent internalization of FZD4. DR Reactome; R-HSA-5140745; WNT5A-dependent internalization of FZD2, FZD5 and ROR2. DR Reactome; R-HSA-8856825; Cargo recognition for clathrin-mediated endocytosis. DR Reactome; R-HSA-8856828; Clathrin-mediated endocytosis. DR Reactome; R-HSA-8866427; VLDLR internalisation and degradation. DR Reactome; R-HSA-8964038; LDL clearance. DR SignaLink; P09496; -. DR SIGNOR; P09496; -. DR Agora; ENSG00000122705; -. DR BioGRID-ORCS; 1211; 31 hits in 1164 CRISPR screens. DR ChiTaRS; CLTA; human. DR GenomeRNAi; 1211; -. DR Pharos; P09496; Tbio. DR PRO; PR:P09496; -. DR Proteomes; UP000005640; Chromosome 9. DR RNAct; P09496; protein. DR Bgee; ENSG00000122705; Expressed in nasal cavity epithelium and 213 other cell types or tissues. DR ExpressionAtlas; P09496; baseline and differential. DR GO; GO:0030118; C:clathrin coat; IMP:CAFA. 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; IDA:FlyBase. DR GO; GO:0030125; C:clathrin vesicle coat; IBA:GO_Central. DR GO; GO:0045334; C:clathrin-coated endocytic vesicle; NAS:ARUK-UCL. DR GO; GO:0031410; C:cytoplasmic vesicle; ISS:BHF-UCL. DR GO; GO:0005829; C:cytosol; TAS:Reactome. DR GO; GO:0036020; C:endolysosome membrane; TAS:Reactome. DR GO; GO:0005768; C:endosome; IDA:HPA. DR GO; GO:0005828; C:kinetochore microtubule; NAS:ComplexPortal. DR GO; GO:0005764; C:lysosome; IDA:HPA. DR GO; GO:0016020; C:membrane; HDA:UniProtKB. DR GO; GO:1990498; C:mitotic spindle microtubule; NAS:ComplexPortal. DR GO; GO:0005886; C:plasma membrane; IDA:HPA. DR GO; GO:0098843; C:postsynaptic endocytic zone; IEA:Ensembl. DR GO; GO:0098835; C:presynaptic endocytic zone membrane; IEA:Ensembl. DR GO; GO:0030672; C:synaptic vesicle membrane; IBA:GO_Central. DR GO; GO:0032588; C:trans-Golgi network membrane; TAS:Reactome. DR GO; GO:0032050; F:clathrin heavy chain binding; IPI:FlyBase. DR GO; GO:0051020; F:GTPase binding; IEA:Ensembl. DR GO; GO:0042277; F:peptide binding; IEA:Ensembl. DR GO; GO:0044877; F:protein-containing complex binding; IEA:Ensembl. DR GO; GO:0005198; F:structural molecule activity; IEA:InterPro. DR GO; GO:0007059; P:chromosome segregation; NAS:ComplexPortal. DR GO; GO:0048268; P:clathrin coat assembly; IMP:CAFA. DR GO; GO:0072318; P:clathrin coat disassembly; NAS:ComplexPortal. DR GO; GO:0072583; P:clathrin-dependent endocytosis; NAS:ComplexPortal. DR GO; GO:0006886; P:intracellular protein transport; IEA:InterPro. DR GO; GO:0000278; P:mitotic cell cycle; NAS:ComplexPortal. DR GO; GO:0007052; P:mitotic spindle organization; NAS:ComplexPortal. DR GO; GO:0048488; P:synaptic vesicle endocytosis; IEA:Ensembl. DR InterPro; IPR000996; Clathrin_L-chain. DR PANTHER; PTHR10639; CLATHRIN LIGHT CHAIN; 1. DR PANTHER; PTHR10639:SF1; CLATHRIN LIGHT CHAIN A; 1. DR Pfam; PF01086; Clathrin_lg_ch; 1. DR PROSITE; PS00224; CLATHRIN_LIGHT_CHN_1; 1. DR PROSITE; PS00581; CLATHRIN_LIGHT_CHN_2; 1. DR PDBsum; 6E5N; -. PE 1: Evidence at protein level; KW 3D-structure; Acetylation; Alternative splicing; Calcium; Cell cycle; KW Cell division; Coated pit; Cytoplasm; Cytoplasmic vesicle; Cytoskeleton; KW Membrane; Mitosis; Phosphoprotein; Proteomics identification; KW Reference proteome. FT CHAIN 1..248 FT /note="Clathrin light chain A" FT /id="PRO_0000205767" FT REGION 1..92 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 100..162 FT /note="Involved in binding clathrin heavy chain" FT COMPBIAS 13..25 FT /note="Gly residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 61..71 FT /note="Pro residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOD_RES 105 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:20068231, FT ECO:0007744|PubMed:23186163" FT MOD_RES 206 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18669648, FT ECO:0007744|PubMed:20068231" FT MOD_RES 223 FT /note="N6-acetyllysine" FT /evidence="ECO:0000250|UniProtKB:Q6IRU5" FT MOD_RES 236 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18669648" FT MOD_RES 242 FT /note="N6-acetyllysine" FT /evidence="ECO:0000250|UniProtKB:O08585" FT VAR_SEQ 73..124 FT /note="Missing (in isoform 5)" FT /evidence="ECO:0000305" FT /id="VSP_047168" FT VAR_SEQ 162..180 FT /note="RVADEAFYKQPFADVIGYV -> S (in isoform 4)" FT /evidence="ECO:0000303|PubMed:14702039" FT /id="VSP_043239" FT VAR_SEQ 163..192 FT /note="Missing (in isoform Non-brain and isoform 5)" FT /evidence="ECO:0000303|PubMed:14702039, FT ECO:0000303|PubMed:15489334, ECO:0000303|PubMed:3267234, FT ECO:0000303|Ref.2" FT /id="VSP_001095" FT VAR_SEQ 181..192 FT /note="Missing (in isoform 3)" FT /evidence="ECO:0000303|Ref.4" FT /id="VSP_024238" FT CONFLICT 207 FT /note="P -> Q (in Ref. 4; ABB76683)" FT /evidence="ECO:0000305" FT HELIX 47..54 FT /evidence="ECO:0007829|PDB:6E5N" FT TURN 55..57 FT /evidence="ECO:0007829|PDB:6E5N" SQ SEQUENCE 248 AA; 27077 MW; 8D8A3B49E6353D93 CRC64; MAELDPFGAP AGAPGGPALG NGVAGAGEED PAAAFLAQQE SEIAGIENDE AFAILDGGAP GPQPHGEPPG GPDAVDGVMN GEYYQESNGP TDSYAAISQV DRLQSEPESI RKWREEQMER LEALDANSRK QEAEWKEKAI KELEEWYARQ DEQLQKTKAN NRVADEAFYK QPFADVIGYV TNINHPCYSL EQAAEEAFVN DIDESSPGTE WERVARLCDF NPKSSKQAKD VSRMRSVLIS LKQAPLVH //