CLCB_RAT
ID CLCB_RAT Reviewed; 229 AA.
AC P08082;
DT 01-AUG-1988, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1988, sequence version 1.
DT 03-AUG-2022, entry version 156.
DE RecName: Full=Clathrin light chain B;
DE Short=Lcb;
GN Name=Cltb;
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 160-181, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC STRAIN=Sprague-Dawley; TISSUE=Hippocampus, and Spinal cord;
RA Lubec G., Afjehi-Sadat L., Chen W.-Q.;
RL Submitted (APR-2007) to UniProtKB.
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. Interacts (via N-terminus) with HIP1.
CC Interacts with HIP1R.
CC -!- SUBCELLULAR LOCATION: Cytoplasmic vesicle membrane; Peripheral membrane
CC protein; Cytoplasmic side. Membrane, coated pit; Peripheral membrane
CC protein; Cytoplasmic side. Note=Cytoplasmic face of coated pits and
CC vesicles.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=Brain;
CC IsoId=P08082-1; Sequence=Displayed;
CC Name=Non-brain;
CC IsoId=P08082-2; Sequence=VSP_001099;
CC -!- SIMILARITY: Belongs to the clathrin light chain family. {ECO:0000305}.
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DR EMBL; M15883; AAA40890.1; -; mRNA.
DR EMBL; M19262; AAA40891.1; -; mRNA.
DR PIR; B25994; LRRTB2.
DR RefSeq; NP_446287.1; NM_053835.1. [P08082-1]
DR RefSeq; XP_006253657.1; XM_006253595.3. [P08082-2]
DR AlphaFoldDB; P08082; -.
DR SMR; P08082; -.
DR BioGRID; 250496; 6.
DR IntAct; P08082; 3.
DR MINT; P08082; -.
DR STRING; 10116.ENSRNOP00000023651; -.
DR iPTMnet; P08082; -.
DR PhosphoSitePlus; P08082; -.
DR SwissPalm; P08082; -.
DR jPOST; P08082; -.
DR PaxDb; P08082; -.
DR PRIDE; P08082; -.
DR Ensembl; ENSRNOT00000023651; ENSRNOP00000023651; ENSRNOG00000017506. [P08082-1]
DR Ensembl; ENSRNOT00000115689; ENSRNOP00000085439; ENSRNOG00000017506. [P08082-2]
DR GeneID; 116561; -.
DR KEGG; rno:116561; -.
DR UCSC; RGD:621353; rat. [P08082-1]
DR CTD; 1212; -.
DR RGD; 621353; Cltb.
DR eggNOG; KOG4031; Eukaryota.
DR GeneTree; ENSGT00940000160186; -.
DR HOGENOM; CLU_091462_1_0_1; -.
DR InParanoid; P08082; -.
DR OMA; VRQNEQM; -.
DR OrthoDB; 1577821at2759; -.
DR PhylomeDB; P08082; -.
DR TreeFam; TF313162; -.
DR Reactome; R-RNO-190873; Gap junction degradation.
DR Reactome; R-RNO-196025; Formation of annular gap junctions.
DR Reactome; R-RNO-432720; Lysosome Vesicle Biogenesis.
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 PRO; PR:P08082; -.
DR Proteomes; UP000002494; Chromosome 17.
DR Bgee; ENSRNOG00000017506; Expressed in heart and 20 other tissues.
DR Genevisible; P08082; RN.
DR GO; GO:0060170; C:ciliary membrane; ISO:RGD.
DR GO; GO:0030118; C:clathrin coat; IDA:RGD.
DR GO; GO:0030132; C:clathrin coat of coated pit; NAS:UniProtKB.
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; IEA:Ensembl.
DR GO; GO:0005886; C:plasma membrane; ISO:RGD.
DR GO; GO:0099631; C:postsynaptic endocytic zone cytoplasmic component; IBA:GO_Central.
DR GO; GO:0098835; C:presynaptic endocytic zone membrane; IDA:SynGO.
DR GO; GO:0030672; C:synaptic vesicle membrane; IDA:SynGO.
DR GO; GO:0005802; C:trans-Golgi network; ISO:RGD.
DR GO; GO:0032050; F:clathrin heavy chain binding; IBA:GO_Central.
DR GO; GO:0005326; F:neurotransmitter transmembrane transporter activity; NAS:UniProtKB.
DR GO; GO:0042277; F:peptide binding; IDA:RGD.
DR GO; GO:0005198; F:structural molecule activity; IEA:InterPro.
DR GO; GO:0072583; P:clathrin-dependent endocytosis; IBA:GO_Central.
DR GO; GO:0006886; P:intracellular protein transport; IEA:InterPro.
DR GO; GO:0007269; P:neurotransmitter secretion; NAS:UniProtKB.
DR GO; GO:0006836; P:neurotransmitter transport; NAS:UniProtKB.
DR GO; GO:0016183; P:synaptic vesicle coating; NAS:UniProtKB.
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; Coated pit;
KW Cytoplasmic vesicle; Direct protein sequencing; Disulfide bond; Membrane;
KW Phosphoprotein; Reference proteome.
FT CHAIN 1..229
FT /note="Clathrin light chain B"
FT /id="PRO_0000205773"
FT REGION 1..80
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 93..155
FT /note="Involved in binding clathrin heavy chain"
FT MOD_RES 11
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P04975"
FT MOD_RES 13
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P04975"
FT MOD_RES 187
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P09497"
FT MOD_RES 204
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q6IRU5"
FT MOD_RES 217
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P09496"
FT DISULFID 199..209
FT /evidence="ECO:0000250"
FT VAR_SEQ 156..173
FT /note="Missing (in isoform Non-brain)"
FT /evidence="ECO:0000303|PubMed:3563513"
FT /id="VSP_001099"
SQ SEQUENCE 229 AA; 25117 MW; C4A05B07CEB92A85 CRC64;
MAEDFGFFSS SESGAPEAAE EDPAAAFLAQ QESEIAGIEN DSGFGAPAAS QVASAQPGLA
SGGGSEDMGT TVNGDVFQEA NGPADGYAAI AQADRLTQEP ESIRKWREEQ KKRLQELDAA
SKVTEQEWRE KAKKDLEEWN QRQSEQVEKN KINNRIADKA FYQQPDADTI GYVASEEAFV
KESKEETPGT EWEKVAQLCD FNPKSSKQCK DVSRLRSVLM SLKQTPLSR
