Full text data of CLTA
CLTA
[Confidence: medium (present in either hRBCD or BSc_CH or PM22954596)]
Clathrin light chain A; Lca
Clathrin light chain A; Lca
hRBCD
IPI00014587
IPI00014587 Splice Isoform 1 Of Clathrin light chain A Clathrin is the major protein of the polyhedral coat of coated pits and vesicles, intracellular protein transport, isoform 2 soluble n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a Cytoplasmic face of coated pits and vesicles. Isoform 1 or 2 found at its expected molecular weight found at molecular weight
IPI00014587 Splice Isoform 1 Of Clathrin light chain A Clathrin is the major protein of the polyhedral coat of coated pits and vesicles, intracellular protein transport, isoform 2 soluble n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a Cytoplasmic face of coated pits and vesicles. Isoform 1 or 2 found at its expected molecular weight found at molecular weight
UniProt
P09496
ID CLCA_HUMAN Reviewed; 248 AA.
AC P09496; A8K4W3; B4DIN1; F5H6N3; Q2XPN5; Q53XZ1;
DT 01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
read moreDT 01-JUL-1989, sequence version 1.
DT 22-JAN-2014, entry version 134.
DE RecName: Full=Clathrin light chain A;
DE Short=Lca;
GN Name=CLTA;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS BRAIN AND NON-BRAIN).
RX PubMed=3267234;
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
RT 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.,
RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA 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.,
RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA Nakai K., Yada T., Nakamura Y., Ohara O., 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.,
RA Liang M., 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.,
RA Howe K.L., Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C.,
RA Ainscough R., Almeida J.P., Ambrose K.D., Ashwell R.I.S.,
RA Babbage A.K., Babbage S., Bagguley C.L., Bailey J., Banerjee R.,
RA Barker D.J., Barlow K.F., Bates K., Beasley H., Beasley O., Bird C.P.,
RA Bray-Allen S., Brown A.J., Brown J.Y., Burford D., Burrill W.,
RA Burton J., Carder C., Carter N.P., Chapman J.C., Chen Y., Clarke G.,
RA Clark S.Y., Clee C.M., Clegg S., Collier R.E., Corby N., Crosier M.,
RA Cummings A.T., Davies J., Dhami P., Dunn M., Dutta I., Dyer L.W.,
RA Earthrowl M.E., Faulkner L., Fleming C.J., Frankish A.,
RA Frankland J.A., French L., Fricker D.G., Garner P., Garnett J.,
RA 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.,
RA Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M.,
RA Lovell J., Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S.,
RA McLay K.E., McMurray A., Milne S., Nickerson T., Nisbett J.,
RA Nordsiek G., Pearce A.V., Peck A.I., Porter K.M., Pandian R.,
RA Pelan S., Phillimore B., Povey S., Ramsey Y., Rand V., Scharfe M.,
RA Sehra H.K., Shownkeen R., Sims S.K., Skuce C.D., Smith M.,
RA Steward C.A., Swarbreck D., Sycamore N., Tester J., Thorpe A.,
RA Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M., West A.P.,
RA Whitehead S.L., Willey D.L., Williams S.A., Wilming L., Wray P.W.,
RA 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.,
RA Rogers J., 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.,
RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA 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
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [8]
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
RT clathrin-mediated endocytosis.";
RL J. Biol. Chem. 281:15182-15193(2006).
RN [9]
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
RT the kinome across the cell cycle.";
RL Mol. Cell 31:438-448(2008).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-206 AND SER-236, AND
RP MASS SPECTROMETRY.
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 [11]
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 [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-105 AND SER-206, AND
RP MASS SPECTROMETRY.
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.,
RA Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full
RT phosphorylation site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [13]
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.,
RA Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(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
CC heavy chains and 3 light chains. Interacts with CALY; the
CC interaction stimulates clathrin self-assembly and clathrin-
CC mediated endocytosis.
CC -!- INTERACTION:
CC Q9Y6A5:TACC3; NbExp=3; IntAct=EBI-1171169, EBI-2554984;
CC -!- SUBCELLULAR LOCATION: Cytoplasmic vesicle membrane; Peripheral
CC membrane protein; Cytoplasmic side. Membrane, coated pit;
CC Peripheral membrane protein; Cytoplasmic side. Note=Cytoplasmic
CC face of coated pits and vesicles.
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 Note=No experimental confirmation available;
CC Name=5;
CC IsoId=P09496-5; Sequence=VSP_047168, VSP_001095;
CC Note=No experimental confirmation available. Gene prediction
CC based on EST data;
CC -!- SIMILARITY: Belongs to the clathrin light chain family.
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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; CAD13387.1; -; Genomic_DNA.
DR EMBL; AL158830; CAD13388.1; -; 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 PIR; A31775; A31775.
DR RefSeq; NP_001070145.1; NM_001076677.2.
DR RefSeq; NP_001171689.1; NM_001184760.1.
DR RefSeq; NP_001171691.1; NM_001184762.1.
DR RefSeq; NP_001824.1; NM_001833.3.
DR RefSeq; NP_009027.1; NM_007096.3.
DR UniGene; Hs.522114; -.
DR ProteinModelPortal; P09496; -.
DR IntAct; P09496; 21.
DR MINT; MINT-1326541; -.
DR STRING; 9606.ENSP00000242285; -.
DR PhosphoSite; P09496; -.
DR DMDM; 116501; -.
DR OGP; P09496; -.
DR PaxDb; P09496; -.
DR PRIDE; P09496; -.
DR DNASU; 1211; -.
DR Ensembl; ENST00000242285; ENSP00000242285; ENSG00000122705.
DR Ensembl; ENST00000345519; ENSP00000242284; ENSG00000122705.
DR Ensembl; ENST00000396603; ENSP00000379848; ENSG00000122705.
DR Ensembl; ENST00000433436; ENSP00000401019; ENSG00000122705.
DR Ensembl; ENST00000470744; ENSP00000419746; ENSG00000122705.
DR Ensembl; ENST00000538225; ENSP00000442869; ENSG00000122705.
DR Ensembl; ENST00000540080; ENSP00000437508; ENSG00000122705.
DR GeneID; 1211; -.
DR KEGG; hsa:1211; -.
DR UCSC; uc003zzc.3; human.
DR CTD; 1211; -.
DR GeneCards; GC09P036180; -.
DR HGNC; HGNC:2090; CLTA.
DR HPA; CAB002665; -.
DR MIM; 118960; gene.
DR neXtProt; NX_P09496; -.
DR PharmGKB; PA26616; -.
DR eggNOG; NOG312397; -.
DR HOGENOM; HOG000008147; -.
DR HOVERGEN; HBG003386; -.
DR InParanoid; P09496; -.
DR KO; K04644; -.
DR OMA; MDDFDML; -.
DR OrthoDB; EOG79KPH4; -.
DR PhylomeDB; P09496; -.
DR Reactome; REACT_111045; Developmental Biology.
DR Reactome; REACT_111102; Signal Transduction.
DR Reactome; REACT_11123; Membrane Trafficking.
DR Reactome; REACT_116125; Disease.
DR Reactome; REACT_6900; Immune System.
DR ChiTaRS; CLTA; human.
DR GenomeRNAi; 1211; -.
DR NextBio; 4985; -.
DR PMAP-CutDB; P09496; -.
DR PRO; PR:P09496; -.
DR ArrayExpress; P09496; -.
DR Bgee; P09496; -.
DR CleanEx; HS_CLTA; -.
DR Genevestigator; P09496; -.
DR GO; GO:0030118; C:clathrin coat; NAS:UniProtKB.
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:0030669; C:clathrin-coated endocytic vesicle membrane; TAS:Reactome.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0005886; C:plasma membrane; TAS:Reactome.
DR GO; GO:0032588; C:trans-Golgi network membrane; TAS:Reactome.
DR GO; GO:0042277; F:peptide binding; IEA:Ensembl.
DR GO; GO:0005198; F:structural molecule activity; IEA:InterPro.
DR GO; GO:0019886; P:antigen processing and presentation of exogenous peptide antigen via MHC class II; TAS:Reactome.
DR GO; GO:0007411; P:axon guidance; TAS:Reactome.
DR GO; GO:0006897; P:endocytosis; IEA:Ensembl.
DR GO; GO:0007173; P:epidermal growth factor receptor signaling pathway; TAS:Reactome.
DR GO; GO:0006886; P:intracellular protein transport; NAS:UniProtKB.
DR GO; GO:0042059; P:negative regulation of epidermal growth factor receptor signaling pathway; TAS:Reactome.
DR GO; GO:0048011; P:neurotrophin TRK receptor signaling pathway; TAS:Reactome.
DR GO; GO:0006892; P:post-Golgi vesicle-mediated transport; TAS:Reactome.
DR InterPro; IPR000996; Clathrin_L-chain.
DR PANTHER; PTHR10639; PTHR10639; 1.
DR Pfam; PF01086; Clathrin_lg_ch; 1.
DR PROSITE; PS00224; CLATHRIN_LIGHT_CHN_1; 1.
DR PROSITE; PS00581; CLATHRIN_LIGHT_CHN_2; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Calcium; Coated pit; Complete proteome;
KW Cytoplasmic vesicle; Membrane; Phosphoprotein; Reference proteome.
FT CHAIN 1 248 Clathrin light chain A.
FT /FTId=PRO_0000205767.
FT REGION 100 162 Involved in binding clathrin heavy chain.
FT MOD_RES 105 105 Phosphoserine.
FT MOD_RES 206 206 Phosphoserine.
FT MOD_RES 236 236 Phosphoserine.
FT VAR_SEQ 73 124 Missing (in isoform 5).
FT /FTId=VSP_047168.
FT VAR_SEQ 162 180 RVADEAFYKQPFADVIGYV -> S (in isoform 4).
FT /FTId=VSP_043239.
FT VAR_SEQ 163 192 Missing (in isoform Non-brain and isoform
FT 5).
FT /FTId=VSP_001095.
FT VAR_SEQ 181 192 Missing (in isoform 3).
FT /FTId=VSP_024238.
FT CONFLICT 207 207 P -> Q (in Ref. 4; ABB76683).
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
//
ID CLCA_HUMAN Reviewed; 248 AA.
AC P09496; A8K4W3; B4DIN1; F5H6N3; Q2XPN5; Q53XZ1;
DT 01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
read moreDT 01-JUL-1989, sequence version 1.
DT 22-JAN-2014, entry version 134.
DE RecName: Full=Clathrin light chain A;
DE Short=Lca;
GN Name=CLTA;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS BRAIN AND NON-BRAIN).
RX PubMed=3267234;
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
RT 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.,
RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA 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.,
RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA Nakai K., Yada T., Nakamura Y., Ohara O., 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.,
RA Liang M., 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.,
RA Howe K.L., Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C.,
RA Ainscough R., Almeida J.P., Ambrose K.D., Ashwell R.I.S.,
RA Babbage A.K., Babbage S., Bagguley C.L., Bailey J., Banerjee R.,
RA Barker D.J., Barlow K.F., Bates K., Beasley H., Beasley O., Bird C.P.,
RA Bray-Allen S., Brown A.J., Brown J.Y., Burford D., Burrill W.,
RA Burton J., Carder C., Carter N.P., Chapman J.C., Chen Y., Clarke G.,
RA Clark S.Y., Clee C.M., Clegg S., Collier R.E., Corby N., Crosier M.,
RA Cummings A.T., Davies J., Dhami P., Dunn M., Dutta I., Dyer L.W.,
RA Earthrowl M.E., Faulkner L., Fleming C.J., Frankish A.,
RA Frankland J.A., French L., Fricker D.G., Garner P., Garnett J.,
RA 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.,
RA Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M.,
RA Lovell J., Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S.,
RA McLay K.E., McMurray A., Milne S., Nickerson T., Nisbett J.,
RA Nordsiek G., Pearce A.V., Peck A.I., Porter K.M., Pandian R.,
RA Pelan S., Phillimore B., Povey S., Ramsey Y., Rand V., Scharfe M.,
RA Sehra H.K., Shownkeen R., Sims S.K., Skuce C.D., Smith M.,
RA Steward C.A., Swarbreck D., Sycamore N., Tester J., Thorpe A.,
RA Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M., West A.P.,
RA Whitehead S.L., Willey D.L., Williams S.A., Wilming L., Wray P.W.,
RA 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.,
RA Rogers J., 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.,
RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA 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
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [8]
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
RT clathrin-mediated endocytosis.";
RL J. Biol. Chem. 281:15182-15193(2006).
RN [9]
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
RT the kinome across the cell cycle.";
RL Mol. Cell 31:438-448(2008).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-206 AND SER-236, AND
RP MASS SPECTROMETRY.
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 [11]
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 [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-105 AND SER-206, AND
RP MASS SPECTROMETRY.
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.,
RA Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full
RT phosphorylation site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [13]
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.,
RA Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(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
CC heavy chains and 3 light chains. Interacts with CALY; the
CC interaction stimulates clathrin self-assembly and clathrin-
CC mediated endocytosis.
CC -!- INTERACTION:
CC Q9Y6A5:TACC3; NbExp=3; IntAct=EBI-1171169, EBI-2554984;
CC -!- SUBCELLULAR LOCATION: Cytoplasmic vesicle membrane; Peripheral
CC membrane protein; Cytoplasmic side. Membrane, coated pit;
CC Peripheral membrane protein; Cytoplasmic side. Note=Cytoplasmic
CC face of coated pits and vesicles.
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 Note=No experimental confirmation available;
CC Name=5;
CC IsoId=P09496-5; Sequence=VSP_047168, VSP_001095;
CC Note=No experimental confirmation available. Gene prediction
CC based on EST data;
CC -!- SIMILARITY: Belongs to the clathrin light chain family.
CC -----------------------------------------------------------------------
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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; CAD13387.1; -; Genomic_DNA.
DR EMBL; AL158830; CAD13388.1; -; 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 PIR; A31775; A31775.
DR RefSeq; NP_001070145.1; NM_001076677.2.
DR RefSeq; NP_001171689.1; NM_001184760.1.
DR RefSeq; NP_001171691.1; NM_001184762.1.
DR RefSeq; NP_001824.1; NM_001833.3.
DR RefSeq; NP_009027.1; NM_007096.3.
DR UniGene; Hs.522114; -.
DR ProteinModelPortal; P09496; -.
DR IntAct; P09496; 21.
DR MINT; MINT-1326541; -.
DR STRING; 9606.ENSP00000242285; -.
DR PhosphoSite; P09496; -.
DR DMDM; 116501; -.
DR OGP; P09496; -.
DR PaxDb; P09496; -.
DR PRIDE; P09496; -.
DR DNASU; 1211; -.
DR Ensembl; ENST00000242285; ENSP00000242285; ENSG00000122705.
DR Ensembl; ENST00000345519; ENSP00000242284; ENSG00000122705.
DR Ensembl; ENST00000396603; ENSP00000379848; ENSG00000122705.
DR Ensembl; ENST00000433436; ENSP00000401019; ENSG00000122705.
DR Ensembl; ENST00000470744; ENSP00000419746; ENSG00000122705.
DR Ensembl; ENST00000538225; ENSP00000442869; ENSG00000122705.
DR Ensembl; ENST00000540080; ENSP00000437508; ENSG00000122705.
DR GeneID; 1211; -.
DR KEGG; hsa:1211; -.
DR UCSC; uc003zzc.3; human.
DR CTD; 1211; -.
DR GeneCards; GC09P036180; -.
DR HGNC; HGNC:2090; CLTA.
DR HPA; CAB002665; -.
DR MIM; 118960; gene.
DR neXtProt; NX_P09496; -.
DR PharmGKB; PA26616; -.
DR eggNOG; NOG312397; -.
DR HOGENOM; HOG000008147; -.
DR HOVERGEN; HBG003386; -.
DR InParanoid; P09496; -.
DR KO; K04644; -.
DR OMA; MDDFDML; -.
DR OrthoDB; EOG79KPH4; -.
DR PhylomeDB; P09496; -.
DR Reactome; REACT_111045; Developmental Biology.
DR Reactome; REACT_111102; Signal Transduction.
DR Reactome; REACT_11123; Membrane Trafficking.
DR Reactome; REACT_116125; Disease.
DR Reactome; REACT_6900; Immune System.
DR ChiTaRS; CLTA; human.
DR GenomeRNAi; 1211; -.
DR NextBio; 4985; -.
DR PMAP-CutDB; P09496; -.
DR PRO; PR:P09496; -.
DR ArrayExpress; P09496; -.
DR Bgee; P09496; -.
DR CleanEx; HS_CLTA; -.
DR Genevestigator; P09496; -.
DR GO; GO:0030118; C:clathrin coat; NAS:UniProtKB.
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:0030669; C:clathrin-coated endocytic vesicle membrane; TAS:Reactome.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0005886; C:plasma membrane; TAS:Reactome.
DR GO; GO:0032588; C:trans-Golgi network membrane; TAS:Reactome.
DR GO; GO:0042277; F:peptide binding; IEA:Ensembl.
DR GO; GO:0005198; F:structural molecule activity; IEA:InterPro.
DR GO; GO:0019886; P:antigen processing and presentation of exogenous peptide antigen via MHC class II; TAS:Reactome.
DR GO; GO:0007411; P:axon guidance; TAS:Reactome.
DR GO; GO:0006897; P:endocytosis; IEA:Ensembl.
DR GO; GO:0007173; P:epidermal growth factor receptor signaling pathway; TAS:Reactome.
DR GO; GO:0006886; P:intracellular protein transport; NAS:UniProtKB.
DR GO; GO:0042059; P:negative regulation of epidermal growth factor receptor signaling pathway; TAS:Reactome.
DR GO; GO:0048011; P:neurotrophin TRK receptor signaling pathway; TAS:Reactome.
DR GO; GO:0006892; P:post-Golgi vesicle-mediated transport; TAS:Reactome.
DR InterPro; IPR000996; Clathrin_L-chain.
DR PANTHER; PTHR10639; PTHR10639; 1.
DR Pfam; PF01086; Clathrin_lg_ch; 1.
DR PROSITE; PS00224; CLATHRIN_LIGHT_CHN_1; 1.
DR PROSITE; PS00581; CLATHRIN_LIGHT_CHN_2; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Calcium; Coated pit; Complete proteome;
KW Cytoplasmic vesicle; Membrane; Phosphoprotein; Reference proteome.
FT CHAIN 1 248 Clathrin light chain A.
FT /FTId=PRO_0000205767.
FT REGION 100 162 Involved in binding clathrin heavy chain.
FT MOD_RES 105 105 Phosphoserine.
FT MOD_RES 206 206 Phosphoserine.
FT MOD_RES 236 236 Phosphoserine.
FT VAR_SEQ 73 124 Missing (in isoform 5).
FT /FTId=VSP_047168.
FT VAR_SEQ 162 180 RVADEAFYKQPFADVIGYV -> S (in isoform 4).
FT /FTId=VSP_043239.
FT VAR_SEQ 163 192 Missing (in isoform Non-brain and isoform
FT 5).
FT /FTId=VSP_001095.
FT VAR_SEQ 181 192 Missing (in isoform 3).
FT /FTId=VSP_024238.
FT CONFLICT 207 207 P -> Q (in Ref. 4; ABB76683).
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
//
MIM
118960
*RECORD*
*FIELD* NO
118960
*FIELD* TI
*118960 CLATHRIN, LIGHT POLYPEPTIDE A; CLTA
;;LCA
*FIELD* TX
DESCRIPTION
Clathrin is the main structural component of the lattice covering the
read morecytoplasmic face of the coated pits and coated vesicles in which
specific macromolecules are entrapped in the process of
receptor-mediated endocytosis. Clathrin is a large, soluble protein
composed of heavy chains, which have molecular masses of about 192 kD,
and light chains, which have molecular masses of about 32 to 38 kD. Two
major classes of clathrin light chains, referred to as LCA (CLTA) and
LCB (CTLB; 118970), have been identified (summary by Kirchhausen et al.,
1987).
CLONING
Jackson et al. (1987) identified 4 distinct forms of bovine clathrin
light chains. This molecular variability derived from tissue-specific
splicing of Lca and Lcb genes.
Brodsky et al. (1987) identified that part of the light chain sequence
that mediates heavy chain binding and is the region of strongest
homology with intermediate filament proteins. Sequence analysis shows an
overall homology of 60% between LCA and LCB and the presence of
brain-specific insertion sequences.
Jackson and Parham (1988) compared cDNAs encoding the brain and nonbrain
forms of human LCA and LCB with their homologs in cow and rat. The
significant differences that distinguish LCA from LCB and the brain from
the nonbrain forms show remarkable preservation in all 3 species. Each
clathrin triskelion consists of 3 heavy chains and 3 light chains. In
the brain, tissue-specific mRNA splicing yields larger forms of LCA and
LCB, containing additional insertion sequences of 30 and 18 amino acids,
respectively.
MAPPING
By Southern blot analysis on genomic DNA extracted from a panel of
mouse-human somatic cell hybrids and by isotopic in situ hybridization,
Ponnambalam et al. (1994) assigned the CLTA gene to human 12q23-q24.
However, Gross (2011) mapped the CLTA gene to chromosome 9p13.3 based on
an alignment of the CLTA sequence (GenBank GENBANK AK225153) with the
genomic sequence (GRCh37).
BIOCHEMICAL FEATURES
Kirchhausen et al. (1987) studied the structure of the clathrin light
chains. The clathrin unit that assembles into coats has 3 extended legs,
500 angstroms in length, splayed out in a pinwheel-like structure
(triskelion). Each of the legs is built from a single heavy chain, with
a light chain bound to each proximal segment.
GENE FUNCTION
Royle et al. (2005) showed that clathrin stabilizes fibers of the
mitotic spindle to aid congression of chromosomes. Clathrin bound to the
spindle directly by the N-terminal domain of clathrin heavy chain.
Depletion of clathrin heavy chain using RNA interference prolonged
mitosis; kinetochore fibers were destabilized, leading to defective
congression of chromosomes to the metaphase plate and persistent
activation of the spindle checkpoint. Normal mitosis was rescued by
clathrin triskelia but not the N-terminal domain of clathrin heavy
chain, indicating that stabilization of kinetochore fibers was dependent
on the unique structure of clathrin.
Deborde et al. (2008) showed that clathrin is required for polarity of
the basolateral plasma membrane proteins in the epithelial cell line
MDCK. Clathrin knockdown depolarized most basolateral proteins, by
interfering with their biosynthetic delivery and recycling, but did not
affect the polarity of apical proteins. Quantitative live imaging showed
that chronic and acute clathrin knockdown selectively slowed down the
exit of basolateral proteins from the Golgi complex, and promoted their
missorting into apical carrier vesicles. Deborde et al. (2008) concluded
that their results demonstrated a broad requirement for clathrin in
basolateral protein trafficking in epithelial cells.
*FIELD* RF
1. Brodsky, F. M.; Galloway, C. J.; Blank, G. S.; Jackson, A. P.;
Seow, H.-F.; Drickamer, K.; Parham, P.: Localization of clathrin
light-chain sequences mediating heavy-chain binding and coated vesicle
diversity. Nature 326: 203-205, 1987.
2. Deborde, S.; Perret, E.; Gravotta, D.; Deora, A.; Salvarezza, S.;
Schreiner, R.; Rodriguez-Boulan, E.: Clathrin is a key regulator
of basolateral polarity. Nature 452: 719-723, 2008.
3. Gross, M. B.: Personal Communication. Baltimore, Md. 2/2/2011.
4. Jackson, A. P.; Parham, P.: Structure of human clathrin light
chains: conservation of light chain polymorphism in three mammalian
species. J. Biol. Chem. 263: 16688-16695, 1988.
5. Jackson, A. P.; Seow, H.-F.; Holmes, N.; Drickamer, K.; Parham,
P.: Clathrin light chains contain brain-specific insertion sequences
and a region of homology with intermediate filaments. Nature 326:
154-159, 1987.
6. Kirchhausen, T.; Scarmato, P.; Harrison, S. C.; Monroe, J. J.;
Chow, E. P.; Mattaliano, R. J.; Ramachandran, K. L.; Smart, J. E.;
Ahn, A. H.; Brosius, J.: Clathrin light chains LCA and LCB are similar,
polymorphic, and share repeated heptad motifs. Science 236: 320-324,
1987.
7. Ponnambalam, S.; Jackson, A. P.; LeBeau, M. M.; Pravtcheva, D.;
Ruddle, F. H.; Alibert, C.; Parham, P.: Chromosomal location and
some structural features of human clathrin light-chain genes (CLTA
and CLTB). Genomics 24: 440-444, 1994.
8. Royle, S. J.; Bright, N. A.; Lagnado, L.: Clathrin is required
for the function of the mitotic spindle. Nature 434: 1152-1157,
2005.
*FIELD* CN
Matthew B. Gross - updated: 2/2/2011
Ada Hamosh - updated: 5/21/2008
Ada Hamosh - updated: 5/25/2005
*FIELD* CD
Victor A. McKusick: 4/27/1987
*FIELD* ED
mgross: 04/20/2011
mgross: 2/2/2011
alopez: 5/28/2008
terry: 5/21/2008
tkritzer: 5/25/2005
terry: 5/25/2005
terry: 4/23/1999
mark: 2/23/1997
terry: 6/18/1996
carol: 1/18/1995
supermim: 3/16/1992
supermim: 3/20/1990
ddp: 10/26/1989
carol: 3/1/1989
carol: 12/22/1988
*RECORD*
*FIELD* NO
118960
*FIELD* TI
*118960 CLATHRIN, LIGHT POLYPEPTIDE A; CLTA
;;LCA
*FIELD* TX
DESCRIPTION
Clathrin is the main structural component of the lattice covering the
read morecytoplasmic face of the coated pits and coated vesicles in which
specific macromolecules are entrapped in the process of
receptor-mediated endocytosis. Clathrin is a large, soluble protein
composed of heavy chains, which have molecular masses of about 192 kD,
and light chains, which have molecular masses of about 32 to 38 kD. Two
major classes of clathrin light chains, referred to as LCA (CLTA) and
LCB (CTLB; 118970), have been identified (summary by Kirchhausen et al.,
1987).
CLONING
Jackson et al. (1987) identified 4 distinct forms of bovine clathrin
light chains. This molecular variability derived from tissue-specific
splicing of Lca and Lcb genes.
Brodsky et al. (1987) identified that part of the light chain sequence
that mediates heavy chain binding and is the region of strongest
homology with intermediate filament proteins. Sequence analysis shows an
overall homology of 60% between LCA and LCB and the presence of
brain-specific insertion sequences.
Jackson and Parham (1988) compared cDNAs encoding the brain and nonbrain
forms of human LCA and LCB with their homologs in cow and rat. The
significant differences that distinguish LCA from LCB and the brain from
the nonbrain forms show remarkable preservation in all 3 species. Each
clathrin triskelion consists of 3 heavy chains and 3 light chains. In
the brain, tissue-specific mRNA splicing yields larger forms of LCA and
LCB, containing additional insertion sequences of 30 and 18 amino acids,
respectively.
MAPPING
By Southern blot analysis on genomic DNA extracted from a panel of
mouse-human somatic cell hybrids and by isotopic in situ hybridization,
Ponnambalam et al. (1994) assigned the CLTA gene to human 12q23-q24.
However, Gross (2011) mapped the CLTA gene to chromosome 9p13.3 based on
an alignment of the CLTA sequence (GenBank GENBANK AK225153) with the
genomic sequence (GRCh37).
BIOCHEMICAL FEATURES
Kirchhausen et al. (1987) studied the structure of the clathrin light
chains. The clathrin unit that assembles into coats has 3 extended legs,
500 angstroms in length, splayed out in a pinwheel-like structure
(triskelion). Each of the legs is built from a single heavy chain, with
a light chain bound to each proximal segment.
GENE FUNCTION
Royle et al. (2005) showed that clathrin stabilizes fibers of the
mitotic spindle to aid congression of chromosomes. Clathrin bound to the
spindle directly by the N-terminal domain of clathrin heavy chain.
Depletion of clathrin heavy chain using RNA interference prolonged
mitosis; kinetochore fibers were destabilized, leading to defective
congression of chromosomes to the metaphase plate and persistent
activation of the spindle checkpoint. Normal mitosis was rescued by
clathrin triskelia but not the N-terminal domain of clathrin heavy
chain, indicating that stabilization of kinetochore fibers was dependent
on the unique structure of clathrin.
Deborde et al. (2008) showed that clathrin is required for polarity of
the basolateral plasma membrane proteins in the epithelial cell line
MDCK. Clathrin knockdown depolarized most basolateral proteins, by
interfering with their biosynthetic delivery and recycling, but did not
affect the polarity of apical proteins. Quantitative live imaging showed
that chronic and acute clathrin knockdown selectively slowed down the
exit of basolateral proteins from the Golgi complex, and promoted their
missorting into apical carrier vesicles. Deborde et al. (2008) concluded
that their results demonstrated a broad requirement for clathrin in
basolateral protein trafficking in epithelial cells.
*FIELD* RF
1. Brodsky, F. M.; Galloway, C. J.; Blank, G. S.; Jackson, A. P.;
Seow, H.-F.; Drickamer, K.; Parham, P.: Localization of clathrin
light-chain sequences mediating heavy-chain binding and coated vesicle
diversity. Nature 326: 203-205, 1987.
2. Deborde, S.; Perret, E.; Gravotta, D.; Deora, A.; Salvarezza, S.;
Schreiner, R.; Rodriguez-Boulan, E.: Clathrin is a key regulator
of basolateral polarity. Nature 452: 719-723, 2008.
3. Gross, M. B.: Personal Communication. Baltimore, Md. 2/2/2011.
4. Jackson, A. P.; Parham, P.: Structure of human clathrin light
chains: conservation of light chain polymorphism in three mammalian
species. J. Biol. Chem. 263: 16688-16695, 1988.
5. Jackson, A. P.; Seow, H.-F.; Holmes, N.; Drickamer, K.; Parham,
P.: Clathrin light chains contain brain-specific insertion sequences
and a region of homology with intermediate filaments. Nature 326:
154-159, 1987.
6. Kirchhausen, T.; Scarmato, P.; Harrison, S. C.; Monroe, J. J.;
Chow, E. P.; Mattaliano, R. J.; Ramachandran, K. L.; Smart, J. E.;
Ahn, A. H.; Brosius, J.: Clathrin light chains LCA and LCB are similar,
polymorphic, and share repeated heptad motifs. Science 236: 320-324,
1987.
7. Ponnambalam, S.; Jackson, A. P.; LeBeau, M. M.; Pravtcheva, D.;
Ruddle, F. H.; Alibert, C.; Parham, P.: Chromosomal location and
some structural features of human clathrin light-chain genes (CLTA
and CLTB). Genomics 24: 440-444, 1994.
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2005.
*FIELD* CN
Matthew B. Gross - updated: 2/2/2011
Ada Hamosh - updated: 5/21/2008
Ada Hamosh - updated: 5/25/2005
*FIELD* CD
Victor A. McKusick: 4/27/1987
*FIELD* ED
mgross: 04/20/2011
mgross: 2/2/2011
alopez: 5/28/2008
terry: 5/21/2008
tkritzer: 5/25/2005
terry: 5/25/2005
terry: 4/23/1999
mark: 2/23/1997
terry: 6/18/1996
carol: 1/18/1995
supermim: 3/16/1992
supermim: 3/20/1990
ddp: 10/26/1989
carol: 3/1/1989
carol: 12/22/1988