CLCA_RAT
ID CLCA_RAT Reviewed; 248 AA.
AC P08081;
DT 01-AUG-1988, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1988, sequence version 1.
DT 03-AUG-2022, entry version 159.
DE RecName: Full=Clathrin light chain A;
DE Short=Lca;
GN Name=Clta;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS BRAIN AND NON-BRAIN).
RX PubMed=3563513; DOI=10.1126/science.3563513;
RA Kirchhausen T., Scarmato P., Harrison S.C., Monroe J.J., Chow E.P.,
RA Mattaliano R.J., Ramachandran K.L., Smart J.E., Ahn A.H., Brosius J.;
RT "Clathrin light chains LCA and LCB are similar, polymorphic, and share
RT repeated heptad motifs.";
RL Science 236:320-324(1987).
RN [2]
RP PROTEIN SEQUENCE OF 103-111; 121-129; 142-149; 163-170; 217-223 AND
RP 236-242, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC STRAIN=Sprague-Dawley; TISSUE=Hippocampus;
RA Lubec G., Chen W.-Q.;
RL Submitted (APR-2007) to UniProtKB.
RN [3]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
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 -!- INTERACTION:
CC P08081; P53563-1: Bcl2l1; NbExp=2; IntAct=EBI-916140, EBI-287204;
CC P08081; P49418: AMPH; Xeno; NbExp=3; IntAct=EBI-916140, EBI-7121510;
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 -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=Brain;
CC IsoId=P08081-1; Sequence=Displayed;
CC Name=Non-brain;
CC IsoId=P08081-2; Sequence=VSP_001096;
CC -!- SIMILARITY: Belongs to the clathrin light chain family. {ECO:0000305}.
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DR EMBL; M15882; AAA40868.1; -; mRNA.
DR EMBL; M19261; AAA40870.1; -; mRNA.
DR EMBL; M19260; AAA40869.1; -; mRNA.
DR PIR; A25994; LRRTA1.
DR RefSeq; NP_114180.1; NM_031974.1. [P08081-1]
DR RefSeq; XP_006238166.1; XM_006238104.2.
DR RefSeq; XP_006238168.1; XM_006238106.2. [P08081-2]
DR AlphaFoldDB; P08081; -.
DR SMR; P08081; -.
DR BioGRID; 249837; 16.
DR CORUM; P08081; -.
DR DIP; DIP-36947N; -.
DR IntAct; P08081; 7.
DR MINT; P08081; -.
DR STRING; 10116.ENSRNOP00000019737; -.
DR iPTMnet; P08081; -.
DR PhosphoSitePlus; P08081; -.
DR SwissPalm; P08081; -.
DR jPOST; P08081; -.
DR PaxDb; P08081; -.
DR PRIDE; P08081; -.
DR Ensembl; ENSRNOT00000019737; ENSRNOP00000019737; ENSRNOG00000014635. [P08081-1]
DR Ensembl; ENSRNOT00000036366; ENSRNOP00000035138; ENSRNOG00000014635. [P08081-2]
DR GeneID; 83800; -.
DR KEGG; rno:83800; -.
DR UCSC; RGD:70919; rat. [P08081-1]
DR CTD; 1211; -.
DR RGD; 70919; Clta.
DR eggNOG; KOG4031; Eukaryota.
DR GeneTree; ENSGT00940000157347; -.
DR InParanoid; P08081; -.
DR OMA; PXESNGP; -.
DR OrthoDB; 1577821at2759; -.
DR PhylomeDB; P08081; -.
DR TreeFam; TF313162; -.
DR Reactome; R-RNO-177504; Retrograde neurotrophin signalling.
DR Reactome; R-RNO-190873; Gap junction degradation.
DR Reactome; R-RNO-196025; Formation of annular gap junctions.
DR Reactome; R-RNO-2132295; MHC class II antigen presentation.
DR Reactome; R-RNO-432720; Lysosome Vesicle Biogenesis.
DR Reactome; R-RNO-432722; Golgi Associated Vesicle Biogenesis.
DR Reactome; R-RNO-437239; Recycling pathway of L1.
DR Reactome; R-RNO-5099900; WNT5A-dependent internalization of FZD4.
DR Reactome; R-RNO-5140745; WNT5A-dependent internalization of FZD2, FZD5 and ROR2.
DR Reactome; R-RNO-8856825; Cargo recognition for clathrin-mediated endocytosis.
DR Reactome; R-RNO-8856828; Clathrin-mediated endocytosis.
DR Reactome; R-RNO-8866427; VLDLR internalisation and degradation.
DR Reactome; R-RNO-8964038; LDL clearance.
DR PRO; PR:P08081; -.
DR Proteomes; UP000002494; Chromosome 5.
DR Bgee; ENSRNOG00000014635; Expressed in cerebellum and 20 other tissues.
DR ExpressionAtlas; P08081; baseline and differential.
DR Genevisible; P08081; RN.
DR GO; GO:0030118; C:clathrin coat; IDA:RGD.
DR GO; GO:0030132; C:clathrin coat of coated pit; NAS:RGD.
DR GO; GO:0030130; C:clathrin coat of trans-Golgi network vesicle; IEA:InterPro.
DR GO; GO:0071439; C:clathrin complex; ISO:RGD.
DR GO; GO:0030125; C:clathrin vesicle coat; IBA:GO_Central.
DR GO; GO:0030669; C:clathrin-coated endocytic vesicle membrane; TAS:Reactome.
DR GO; GO:0005905; C:clathrin-coated pit; IDA:RGD.
DR GO; GO:0030136; C:clathrin-coated vesicle; IDA:RGD.
DR GO; GO:0031410; C:cytoplasmic vesicle; ISO:RGD.
DR GO; GO:0098978; C:glutamatergic synapse; ISO:RGD.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0098843; C:postsynaptic endocytic zone; ISO:RGD.
DR GO; GO:0099631; C:postsynaptic endocytic zone cytoplasmic component; ISO:RGD.
DR GO; GO:0098835; C:presynaptic endocytic zone membrane; IDA:SynGO.
DR GO; GO:0005819; C:spindle; IEA:UniProtKB-SubCell.
DR GO; GO:0030672; C:synaptic vesicle membrane; IDA:CAFA.
DR GO; GO:0032050; F:clathrin heavy chain binding; ISO:RGD.
DR GO; GO:0051020; F:GTPase binding; IPI:CAFA.
DR GO; GO:0042277; F:peptide binding; IDA:RGD.
DR GO; GO:0044877; F:protein-containing complex binding; IPI:RGD.
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:RGD.
DR GO; GO:0072583; P:clathrin-dependent endocytosis; IBA:GO_Central.
DR GO; GO:0006897; P:endocytosis; IEP:RGD.
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; Alternative splicing; Calcium; Cell cycle; Cell division;
KW Coated pit; Cytoplasm; Cytoplasmic vesicle; Cytoskeleton;
KW Direct protein sequencing; Membrane; Mitosis; Phosphoprotein;
KW Reference proteome.
FT CHAIN 1..248
FT /note="Clathrin light chain A"
FT /id="PRO_0000205769"
FT REGION 1..93
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 100..162
FT /note="Involved in binding clathrin heavy chain"
FT MOD_RES 105
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P09496"
FT MOD_RES 206
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P09496"
FT MOD_RES 223
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q6IRU5"
FT MOD_RES 236
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P09496"
FT MOD_RES 242
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:O08585"
FT VAR_SEQ 163..192
FT /note="Missing (in isoform Non-brain)"
FT /evidence="ECO:0000303|PubMed:3563513"
FT /id="VSP_001096"
SQ SEQUENCE 248 AA; 26981 MW; C939E85B0FD2E124 CRC64;
MAELDPFGAP AGAPGGPALG NGVAGAGEED PAAAFLAQQE SEIAGIENDE AFAILDGGAP
GPQAHGEPPG GPDAVDGVMN GEYYQESNGP TDSYAAISEV DRLQSEPESI RKWREEQTER
LEALDANSRK QEAEWKEKAV KELEEWYARQ DEQLQKTKAS NRVADEAFYK QPFADVIGYV
TNINHPCYSL EQAAEEAFVN DIDESSPGTE WERVARLCDF NPKSSKQAKD VSRMRSVLIS
LKQAPLVH
