CLC_DROME
ID CLC_DROME Reviewed; 219 AA.
AC Q9VWA1; O61647;
DT 15-NOV-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 147.
DE RecName: Full=Clathrin light chain;
DE AltName: Full=dClc;
GN Name=Clc; ORFNames=CG6948;
OS Drosophila melanogaster (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7227;
RN [1] {ECO:0000305}
RP NUCLEOTIDE SEQUENCE [MRNA], AND DEVELOPMENTAL STAGE.
RX PubMed=10098605; DOI=10.1089/104454999315457;
RA Vasyukevich K., Bazinet C.;
RT "A Drosophila clathrin light-chain gene: sequence, mapping, and absence of
RT neuronal specialization.";
RL DNA Cell Biol. 18:235-241(1999).
RN [2] {ECO:0000305}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley;
RX PubMed=10731132; DOI=10.1126/science.287.5461.2185;
RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., Brandon R.C.,
RA Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C.,
RA Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A.,
RA An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A.,
RA Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V.,
RA Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J.,
RA Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E.,
RA Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B.,
RA Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I.,
RA Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C.,
RA Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S.,
RA Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M.,
RA Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D.,
RA Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F.,
RA Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D.,
RA Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A.,
RA Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C.,
RA McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C.,
RA Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L.,
RA Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R.,
RA Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V.,
RA Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F.,
RA Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J.,
RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R.,
RA Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y.,
RA Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T.,
RA Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S.,
RA Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W.,
RA Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M.,
RA Venter J.C.;
RT "The genome sequence of Drosophila melanogaster.";
RL Science 287:2185-2195(2000).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=Berkeley;
RX PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M.,
RA Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.;
RT "Annotation of the Drosophila melanogaster euchromatic genome: a systematic
RT review.";
RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Berkeley; TISSUE=Ovary;
RX PubMed=12537569; DOI=10.1186/gb-2002-3-12-research0080;
RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., George R.A.,
RA Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., Rubin G.M.,
RA Celniker S.E.;
RT "A Drosophila full-length cDNA resource.";
RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002).
CC -!- FUNCTION: Clathrin is the major protein of the polyhedral coat of
CC coated pits and vesicles. {ECO:0000250|UniProtKB:P04975}.
CC -!- SUBUNIT: Clathrin coats are formed from molecules containing 3 heavy
CC chains and 3 light chains. {ECO:0000250|UniProtKB:P04975}.
CC -!- INTERACTION:
CC Q9VWA1; Q9VAN8: Dmel\CG11882; NbExp=3; IntAct=EBI-193562, EBI-98352;
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 -!- DEVELOPMENTAL STAGE: Expressed throughout development.
CC {ECO:0000269|PubMed:10098605}.
CC -!- MISCELLANEOUS: There is no evidence of the neuronal splice variant
CC found in vertebrates. {ECO:0000269|PubMed:10098605}.
CC -!- SIMILARITY: Belongs to the clathrin light chain family. {ECO:0000305}.
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DR EMBL; AF055900; AAC14276.1; -; mRNA.
DR EMBL; AE014296; AAF49047.1; -; Genomic_DNA.
DR EMBL; AY121633; AAM51960.1; -; mRNA.
DR RefSeq; NP_001163480.1; NM_001170009.1.
DR RefSeq; NP_001163481.1; NM_001170010.2.
DR RefSeq; NP_001262101.1; NM_001275172.1.
DR RefSeq; NP_524178.2; NM_079454.3.
DR AlphaFoldDB; Q9VWA1; -.
DR SMR; Q9VWA1; -.
DR BioGRID; 65485; 6.
DR DIP; DIP-20236N; -.
DR IntAct; Q9VWA1; 1.
DR STRING; 7227.FBpp0290037; -.
DR PaxDb; Q9VWA1; -.
DR PRIDE; Q9VWA1; -.
DR DNASU; 40221; -.
DR EnsemblMetazoa; FBtr0074830; FBpp0074599; FBgn0024814.
DR EnsemblMetazoa; FBtr0300813; FBpp0290037; FBgn0024814.
DR EnsemblMetazoa; FBtr0301126; FBpp0290348; FBgn0024814.
DR EnsemblMetazoa; FBtr0332771; FBpp0305007; FBgn0024814.
DR GeneID; 40221; -.
DR KEGG; dme:Dmel_CG6948; -.
DR CTD; 1178; -.
DR FlyBase; FBgn0024814; Clc.
DR VEuPathDB; VectorBase:FBgn0024814; -.
DR eggNOG; KOG4031; Eukaryota.
DR GeneTree; ENSGT00940000176029; -.
DR HOGENOM; CLU_091462_0_0_1; -.
DR InParanoid; Q9VWA1; -.
DR OMA; FYENYNT; -.
DR OrthoDB; 1577821at2759; -.
DR PhylomeDB; Q9VWA1; -.
DR Reactome; R-DME-177504; Retrograde neurotrophin signalling.
DR Reactome; R-DME-190873; Gap junction degradation.
DR Reactome; R-DME-196025; Formation of annular gap junctions.
DR Reactome; R-DME-432720; Lysosome Vesicle Biogenesis.
DR Reactome; R-DME-432722; Golgi Associated Vesicle Biogenesis.
DR Reactome; R-DME-437239; Recycling pathway of L1.
DR Reactome; R-DME-5099900; WNT5A-dependent internalization of FZD4.
DR Reactome; R-DME-5140745; WNT5A-dependent internalization of FZD2, FZD5 and ROR2.
DR Reactome; R-DME-8856825; Cargo recognition for clathrin-mediated endocytosis.
DR Reactome; R-DME-8856828; Clathrin-mediated endocytosis.
DR Reactome; R-DME-8866427; VLDLR internalisation and degradation.
DR Reactome; R-DME-8964038; LDL clearance.
DR SignaLink; Q9VWA1; -.
DR BioGRID-ORCS; 40221; 0 hits in 3 CRISPR screens.
DR GenomeRNAi; 40221; -.
DR PRO; PR:Q9VWA1; -.
DR Proteomes; UP000000803; Chromosome 3L.
DR Bgee; FBgn0024814; Expressed in embryonic/larval hemocyte (Drosophila) and 23 other tissues.
DR ExpressionAtlas; Q9VWA1; baseline and differential.
DR Genevisible; Q9VWA1; DM.
DR GO; GO:0005938; C:cell cortex; IDA:FlyBase.
DR GO; GO:0030132; C:clathrin coat of coated pit; IDA:FlyBase.
DR GO; GO:0030130; C:clathrin coat of trans-Golgi network vesicle; IEA:InterPro.
DR GO; GO:0071439; C:clathrin complex; ISS:FlyBase.
DR GO; GO:0030125; C:clathrin vesicle coat; IDA:FlyBase.
DR GO; GO:0030136; C:clathrin-coated vesicle; IDA:FlyBase.
DR GO; GO:0005737; C:cytoplasm; IDA:FlyBase.
DR GO; GO:0072686; C:mitotic spindle; IDA:FlyBase.
DR GO; GO:0005886; C:plasma membrane; IDA:FlyBase.
DR GO; GO:0099631; C:postsynaptic endocytic zone cytoplasmic component; IBA:GO_Central.
DR GO; GO:0030672; C:synaptic vesicle membrane; IBA:GO_Central.
DR GO; GO:0032050; F:clathrin heavy chain binding; ISS:FlyBase.
DR GO; GO:0005198; F:structural molecule activity; IEA:InterPro.
DR GO; GO:0072583; P:clathrin-dependent endocytosis; IDA:FlyBase.
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; PS00581; CLATHRIN_LIGHT_CHN_2; 1.
PE 1: Evidence at protein level;
KW Calcium; Coated pit; Cytoplasmic vesicle; Membrane; Reference proteome.
FT CHAIN 1..219
FT /note="Clathrin light chain"
FT /id="PRO_0000205774"
FT REGION 32..136
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 96..158
FT /note="Involved in binding clathrin heavy chain"
FT /evidence="ECO:0000250"
FT COMPBIAS 100..136
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CONFLICT 218..219
FT /note="ST -> RHLGSFNYALA (in Ref. 1; AAC14276)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 219 AA; 23840 MW; 8B764209C2D0CCA4 CRC64;
MDFGDDFAAK EDVDPAAEFL AREQSALGDL EAEITGGSAS APPAASTDEG LGELLGGTAS
EGDLLSAGGT GGLESSTGSF EVIGGESNEP VGISGPPPSR EEPEKIRKWR EEQKQRLEEK
DIEEERKKEE LRQQSKKELD DWLRQIGESI SKTKLASRNA EKQAATLENG TIEPGTEWER
IAKLCDFNPK VNKAGKDVSR MRSIYLHLKQ NPIQVQKST
