CLCA_MOUSE
ID CLCA_MOUSE Reviewed; 235 AA.
AC O08585;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 03-OCT-2012, sequence version 2.
DT 25-MAY-2022, entry version 122.
DE RecName: Full=Clathrin light chain A;
DE Short=Lca;
GN Name=Clta;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=MDF1;
RA Scott L.M., Mueller L., Collins S.J.;
RT "E3, a hematopoietic-specific transcript directly regulated by the retinoic
RT acid receptor alpha.";
RL Submitted (APR-1997) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [3]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-193 AND SER-223, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [4]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-229, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic fibroblast;
RX PubMed=23806337; DOI=10.1016/j.molcel.2013.06.001;
RA Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y.,
RA Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.;
RT "SIRT5-mediated lysine desuccinylation impacts diverse metabolic
RT pathways.";
RL Mol. Cell 50:919-930(2013).
CC -!- FUNCTION: Clathrin is the major protein of the polyhedral coat of
CC coated pits and vesicles. Acts as 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 (By similarity). {ECO:0000250|UniProtKB:P09496}.
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 (By
CC similarity). Interacts with CKAP5 and TACC3 forming the TACC3/ch-
CC TOG/clathrin complex located at spindle inter-microtubules bridges; the
CC complex implicates clathrin triskelions (By similarity). {ECO:0000250,
CC ECO:0000250|UniProtKB:P09496}.
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:0000250|UniProtKB:P09496}. Note=Cytoplasmic face of coated pits
CC and vesicles.In complex with TACC3 and CKAP5 (forming the TACC3/ch-
CC TOG/clathrin complex) localized to inter-microtubule bridges in mitotic
CC spindles. {ECO:0000250|UniProtKB:P09496}.
CC -!- SIMILARITY: Belongs to the clathrin light chain family. {ECO:0000305}.
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DR EMBL; U91848; AAB51286.1; -; mRNA.
DR EMBL; AL732563; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; O08585; -.
DR SMR; O08585; -.
DR STRING; 10090.ENSMUSP00000103481; -.
DR iPTMnet; O08585; -.
DR PhosphoSitePlus; O08585; -.
DR SwissPalm; O08585; -.
DR EPD; O08585; -.
DR jPOST; O08585; -.
DR MaxQB; O08585; -.
DR PRIDE; O08585; -.
DR ProteomicsDB; 283281; -.
DR MGI; MGI:894297; Clta.
DR eggNOG; KOG4031; Eukaryota.
DR InParanoid; O08585; -.
DR Reactome; R-MMU-177504; Retrograde neurotrophin signalling.
DR Reactome; R-MMU-190873; Gap junction degradation.
DR Reactome; R-MMU-196025; Formation of annular gap junctions.
DR Reactome; R-MMU-2132295; MHC class II antigen presentation.
DR Reactome; R-MMU-432720; Lysosome Vesicle Biogenesis.
DR Reactome; R-MMU-432722; Golgi Associated Vesicle Biogenesis.
DR Reactome; R-MMU-437239; Recycling pathway of L1.
DR Reactome; R-MMU-5099900; WNT5A-dependent internalization of FZD4.
DR Reactome; R-MMU-5140745; WNT5A-dependent internalization of FZD2, FZD5 and ROR2.
DR Reactome; R-MMU-8856825; Cargo recognition for clathrin-mediated endocytosis.
DR Reactome; R-MMU-8856828; Clathrin-mediated endocytosis.
DR Reactome; R-MMU-8866427; VLDLR internalisation and degradation.
DR Reactome; R-MMU-8964038; LDL clearance.
DR ChiTaRS; Clta; mouse.
DR PRO; PR:O08585; -.
DR Proteomes; UP000000589; Unplaced.
DR RNAct; O08585; protein.
DR GO; GO:0030118; C:clathrin coat; ISO:MGI.
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; ISO:MGI.
DR GO; GO:0030125; C:clathrin vesicle coat; IBA:GO_Central.
DR GO; GO:0005905; C:clathrin-coated pit; ISO:MGI.
DR GO; GO:0030136; C:clathrin-coated vesicle; ISO:MGI.
DR GO; GO:0031410; C:cytoplasmic vesicle; IDA:BHF-UCL.
DR GO; GO:0098978; C:glutamatergic synapse; IDA:SynGO.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0098843; C:postsynaptic endocytic zone; IDA:SynGO.
DR GO; GO:0099631; C:postsynaptic endocytic zone cytoplasmic component; IDA:SynGO.
DR GO; GO:0098835; C:presynaptic endocytic zone membrane; ISO:MGI.
DR GO; GO:0005819; C:spindle; IEA:UniProtKB-SubCell.
DR GO; GO:0030672; C:synaptic vesicle membrane; ISO:MGI.
DR GO; GO:0032050; F:clathrin heavy chain binding; ISO:MGI.
DR GO; GO:0051020; F:GTPase binding; ISO:MGI.
DR GO; GO:0042277; F:peptide binding; ISO:MGI.
DR GO; GO:0044877; F:protein-containing complex binding; ISO:MGI.
DR GO; GO:0005198; F:structural molecule activity; IEA:InterPro.
DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0048268; P:clathrin coat assembly; ISO:MGI.
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.
DR PROSITE; PS00224; CLATHRIN_LIGHT_CHN_1; 1.
DR PROSITE; PS00581; CLATHRIN_LIGHT_CHN_2; 1.
PE 1: Evidence at protein level;
KW Acetylation; Calcium; Cell cycle; Cell division; Coated pit; Cytoplasm;
KW Cytoplasmic vesicle; Cytoskeleton; Membrane; Mitosis; Phosphoprotein;
KW Reference proteome.
FT CHAIN 1..235
FT /note="Clathrin light chain A"
FT /id="PRO_0000205768"
FT REGION 1..32
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 99..161
FT /note="Involved in binding clathrin heavy chain"
FT MOD_RES 104
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P09496"
FT MOD_RES 193
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 210
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q6IRU5"
FT MOD_RES 223
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 229
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:23806337"
FT CONFLICT 9
FT /note="A -> D (in Ref. 1; AAB51286)"
FT /evidence="ECO:0000305"
FT CONFLICT 38..39
FT /note="QQ -> HE (in Ref. 1; AAB51286)"
FT /evidence="ECO:0000305"
FT CONFLICT 68
FT /note="A -> G (in Ref. 1; AAB51286)"
FT /evidence="ECO:0000305"
FT CONFLICT 162..164
FT /note="VAD -> AAE (in Ref. 1; AAB51286)"
FT /evidence="ECO:0000305"
FT CONFLICT 175
FT /note="L -> V (in Ref. 1; AAB51286)"
FT /evidence="ECO:0000305"
FT CONFLICT 203
FT /note="R -> P (in Ref. 1; AAB51286)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 235 AA; 25604 MW; 1594B3F3F204C221 CRC64;
MAELDPFGAP AGAPGGPALG NGVAGAGEED PAAAFLAQQE SEIAGIENDE AFAILDGGAP
GRATRRAAGG PDAVDGVMNG EYYQESNGPT DSYAAISEVD RLQSEPESIR KWREEQTERL
EALDANSRKQ EAEWKEKAIK ELEEWYARQD EQLQKTKANN RVADEAFYKQ PFADLIGYVA
AEEAFVNDID ESSPGTEWER VARLCDFNPK SSKQAKDVSR MRSVLISLKQ APLVH
