CLC1_SCHPO
ID CLC1_SCHPO Reviewed; 229 AA.
AC Q9USP6; O42710;
DT 06-DEC-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 115.
DE RecName: Full=Clathrin light chain;
DE Short=CLC;
GN Name=clc1; ORFNames=SPBC9B6.08;
OS Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC Schizosaccharomyces.
OX NCBI_TaxID=284812;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=972 / ATCC 24843;
RX PubMed=11859360; DOI=10.1038/nature724;
RA Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.,
RA Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S.,
RA Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S.,
RA Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D.,
RA Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P.,
RA Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K.,
RA O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M.,
RA Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N.,
RA Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A.,
RA Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R.,
RA Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M.,
RA Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A.,
RA Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A.,
RA Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H.,
RA Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S.,
RA Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C.,
RA Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A.,
RA Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M.,
RA del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S.,
RA Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R.,
RA Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G.,
RA Nurse P.;
RT "The genome sequence of Schizosaccharomyces pombe.";
RL Nature 415:871-880(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 6-229.
RA Kawamukai M.;
RT "S.pombe clathrin light chain.";
RL Submitted (MAR-1998) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-229, AND IDENTIFICATION BY
RP MASS SPECTROMETRY.
RX PubMed=18257517; DOI=10.1021/pr7006335;
RA Wilson-Grady J.T., Villen J., Gygi S.P.;
RT "Phosphoproteome analysis of fission yeast.";
RL J. Proteome Res. 7:1088-1097(2008).
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.
CC -!- SUBCELLULAR LOCATION: Cytoplasmic vesicle membrane {ECO:0000250};
CC Peripheral membrane protein {ECO:0000250}; Cytoplasmic side
CC {ECO:0000250}. Membrane, coated pit {ECO:0000250}; Peripheral membrane
CC protein {ECO:0000250}; Cytoplasmic side {ECO:0000250}. Note=Cytoplasmic
CC face of coated pits and vesicles. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the clathrin light chain family. {ECO:0000305}.
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DR EMBL; CU329671; CAB42369.1; -; Genomic_DNA.
DR EMBL; AB011822; BAA25104.1; -; mRNA.
DR PIR; T40789; T40789.
DR PIR; T43331; T43331.
DR RefSeq; NP_595750.1; NM_001021650.2.
DR AlphaFoldDB; Q9USP6; -.
DR SMR; Q9USP6; -.
DR BioGRID; 277817; 9.
DR IntAct; Q9USP6; 2.
DR STRING; 4896.SPBC9B6.08.1; -.
DR iPTMnet; Q9USP6; -.
DR MaxQB; Q9USP6; -.
DR PaxDb; Q9USP6; -.
DR PRIDE; Q9USP6; -.
DR EnsemblFungi; SPBC9B6.08.1; SPBC9B6.08.1:pep; SPBC9B6.08.
DR GeneID; 2541305; -.
DR KEGG; spo:SPBC9B6.08; -.
DR PomBase; SPBC9B6.08; clc1.
DR VEuPathDB; FungiDB:SPBC9B6.08; -.
DR eggNOG; KOG4031; Eukaryota.
DR HOGENOM; CLU_069856_0_0_1; -.
DR InParanoid; Q9USP6; -.
DR OMA; FYENYNT; -.
DR PhylomeDB; Q9USP6; -.
DR Reactome; R-SPO-196025; Formation of annular gap junctions.
DR Reactome; R-SPO-432720; Lysosome Vesicle Biogenesis.
DR Reactome; R-SPO-437239; Recycling pathway of L1.
DR Reactome; R-SPO-8856828; Clathrin-mediated endocytosis.
DR Reactome; R-SPO-8866427; VLDLR internalisation and degradation.
DR Reactome; R-SPO-8964038; LDL clearance.
DR PRO; PR:Q9USP6; -.
DR Proteomes; UP000002485; Chromosome II.
DR GO; GO:0030479; C:actin cortical patch; IDA:PomBase.
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:0005737; C:cytoplasm; HDA:PomBase.
DR GO; GO:0031410; C:cytoplasmic vesicle; IDA:PomBase.
DR GO; GO:0005768; C:endosome; IDA:PomBase.
DR GO; GO:0005794; C:Golgi apparatus; IDA:PomBase.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0032050; F:clathrin heavy chain binding; IBA:GO_Central.
DR GO; GO:0005198; F:structural molecule activity; IEA:InterPro.
DR GO; GO:0072583; P:clathrin-dependent endocytosis; IGI:PomBase.
DR GO; GO:0006887; P:exocytosis; IMP:PomBase.
DR GO; GO:0006886; P:intracellular protein transport; NAS:PomBase.
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 Coated pit; Cytoplasmic vesicle; Membrane; Phosphoprotein;
KW Reference proteome.
FT CHAIN 1..229
FT /note="Clathrin light chain"
FT /id="PRO_0000205775"
FT REGION 1..24
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 76..132
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 98..132
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 229
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
SQ SEQUENCE 229 AA; 25863 MW; B4139F2A55283318 CRC64;
MSQFPALEDF DDGLVTAPVD DSKNNTDFLE REKLALGEDA GQFETPEDKD ALLNFENDSE
AEQTRFEQNF PPIDAEMQAS GTFSAPKAPY MGQAEVHPPE DESGDPEPVR KWKEDQMKRI
QERDESSKKL RESNIEKARK AIDDFYENFN DKRDKVIAKS RKEQEKLLEE NESKSTGTTS
WERILKLIDL SDKPEAHGRS TERFRELLIS LAKDSNAPGA AGTTVSSSS
