CLCB_MOUSE
ID CLCB_MOUSE Reviewed; 229 AA.
AC Q6IRU5; Q8BR04; Q8CDX9; Q9CV35;
DT 12-APR-2005, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 136.
DE RecName: Full=Clathrin light chain B;
DE Short=Lcb;
GN Name=Cltb;
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 [LARGE SCALE MRNA] (ISOFORMS 2 AND 3).
RC STRAIN=C57BL/6J; TISSUE=Corpora quadrigemina, Head, and Tongue;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=C57BL/6J; TISSUE=Brain;
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 [3]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Heart, Lung, and Pancreas;
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-204, 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.
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=3;
CC Name=1;
CC IsoId=Q6IRU5-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q6IRU5-2; Sequence=VSP_013382;
CC Name=3;
CC IsoId=Q6IRU5-3; Sequence=VSP_013383;
CC -!- SIMILARITY: Belongs to the clathrin light chain family. {ECO:0000305}.
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DR EMBL; AK009844; BAB26539.1; -; mRNA.
DR EMBL; AK029382; BAC26430.1; -; mRNA.
DR EMBL; AK045989; BAC32563.1; -; mRNA.
DR EMBL; BC070404; AAH70404.1; -; mRNA.
DR CCDS; CCDS26533.1; -. [Q6IRU5-2]
DR CCDS; CCDS84024.1; -. [Q6IRU5-1]
DR RefSeq; NP_001334441.1; NM_001347512.1. [Q6IRU5-1]
DR RefSeq; NP_083146.1; NM_028870.4. [Q6IRU5-2]
DR AlphaFoldDB; Q6IRU5; -.
DR SMR; Q6IRU5; -.
DR BioGRID; 216666; 11.
DR IntAct; Q6IRU5; 1.
DR STRING; 10090.ENSMUSP00000089198; -.
DR iPTMnet; Q6IRU5; -.
DR PhosphoSitePlus; Q6IRU5; -.
DR SwissPalm; Q6IRU5; -.
DR REPRODUCTION-2DPAGE; Q6IRU5; -.
DR EPD; Q6IRU5; -.
DR jPOST; Q6IRU5; -.
DR MaxQB; Q6IRU5; -.
DR PeptideAtlas; Q6IRU5; -.
DR PRIDE; Q6IRU5; -.
DR ProteomicsDB; 285473; -. [Q6IRU5-1]
DR ProteomicsDB; 285474; -. [Q6IRU5-2]
DR ProteomicsDB; 285475; -. [Q6IRU5-3]
DR Antibodypedia; 29088; 235 antibodies from 27 providers.
DR DNASU; 74325; -.
DR Ensembl; ENSMUST00000049575; ENSMUSP00000053371; ENSMUSG00000047547. [Q6IRU5-1]
DR Ensembl; ENSMUST00000091609; ENSMUSP00000089198; ENSMUSG00000047547. [Q6IRU5-2]
DR GeneID; 74325; -.
DR KEGG; mmu:74325; -.
DR UCSC; uc007qon.1; mouse. [Q6IRU5-1]
DR CTD; 1212; -.
DR MGI; MGI:1921575; Cltb.
DR VEuPathDB; HostDB:ENSMUSG00000047547; -.
DR eggNOG; KOG4031; Eukaryota.
DR GeneTree; ENSGT00940000160186; -.
DR HOGENOM; CLU_091462_1_0_1; -.
DR InParanoid; Q6IRU5; -.
DR OMA; VRQNEQM; -.
DR OrthoDB; 1577821at2759; -.
DR PhylomeDB; Q6IRU5; -.
DR TreeFam; TF313162; -.
DR Reactome; R-MMU-190873; Gap junction degradation.
DR Reactome; R-MMU-196025; Formation of annular gap junctions.
DR Reactome; R-MMU-432720; Lysosome Vesicle Biogenesis.
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 BioGRID-ORCS; 74325; 0 hits in 75 CRISPR screens.
DR ChiTaRS; Cltb; mouse.
DR PRO; PR:Q6IRU5; -.
DR Proteomes; UP000000589; Chromosome 13.
DR RNAct; Q6IRU5; protein.
DR Bgee; ENSMUSG00000047547; Expressed in embryonic brain and 245 other tissues.
DR ExpressionAtlas; Q6IRU5; baseline and differential.
DR Genevisible; Q6IRU5; MM.
DR GO; GO:0060170; C:ciliary membrane; IDA:MGI.
DR GO; GO:0030118; C:clathrin coat; ISS: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:0030125; C:clathrin vesicle coat; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; ISO:MGI.
DR GO; GO:0005886; C:plasma membrane; IDA:MGI.
DR GO; GO:0099631; C:postsynaptic endocytic zone cytoplasmic component; IBA:GO_Central.
DR GO; GO:0098835; C:presynaptic endocytic zone membrane; ISO:MGI.
DR GO; GO:0030672; C:synaptic vesicle membrane; ISO:MGI.
DR GO; GO:0005802; C:trans-Golgi network; IDA:MGI.
DR GO; GO:0032050; F:clathrin heavy chain binding; IBA:GO_Central.
DR GO; GO:0042277; F:peptide binding; ISO:MGI.
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 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; Disulfide bond; Membrane; Phosphoprotein;
KW Reference proteome.
FT CHAIN 1..229
FT /note="Clathrin light chain B"
FT /id="PRO_0000205772"
FT REGION 1..70
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 93..155
FT /note="Involved in binding clathrin heavy chain"
FT COMPBIAS 54..70
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
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:0007744|PubMed:23806337"
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..229
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_013383"
FT VAR_SEQ 156..173
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_013382"
SQ SEQUENCE 229 AA; 25172 MW; 62C87F71DB9F782A CRC64;
MAEDFGFFSS SESGAPEAAE EDPAAAFLAQ QESEIAGIEN DPGFGAPAAS QVASAQPGLA
SGAGSEDMST TVNGDVFQEA NGPADGYAAI AQADRLTQEP ESIRKWREEQ KKRLQELDAA
SKVTEQEWRE KAKKDLEEWN QRQSEQVEKN KINNRIADKA FYQQPDADTI GYVASEEAFV
KESKEETPGT EWEKVAQLCD FNPKSSKQCK DVSRLRSVLM SLKQTPLSR