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CLC_DICDI
ID   CLC_DICDI               Reviewed;         194 AA.
AC   Q8MN58; Q54ZJ2;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2002, sequence version 1.
DT   25-MAY-2022, entry version 90.
DE   RecName: Full=Clathrin light chain;
GN   Name=clc {ECO:0000312|dictyBase:DDB_G0277403};
GN   Synonyms=clcA {ECO:0000312|EMBL:AAQ95635.1}; ORFNames=DDB_G0277403;
OS   Dictyostelium discoideum (Slime mold).
OC   Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales;
OC   Dictyosteliaceae; Dictyostelium.
OX   NCBI_TaxID=44689;
RN   [1] {ECO:0000305, ECO:0000312|EMBL:AAQ95635.1}
RP   NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 118-127; 145-153 AND
RP   189-192, FUNCTION, SUBUNIT, AND DISRUPTION PHENOTYPE.
RX   PubMed=14617352; DOI=10.1046/j.1600-0854.2003.00144.x;
RA   Wang J., Virta V.C., Riddelle-Spencer K., O'Halloran T.J.;
RT   "Compromise of clathrin function and membrane association by clathrin light
RT   chain deletion.";
RL   Traffic 4:891-901(2003).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AX4;
RX   PubMed=12097910; DOI=10.1038/nature00847;
RA   Gloeckner G., Eichinger L., Szafranski K., Pachebat J.A., Bankier A.T.,
RA   Dear P.H., Lehmann R., Baumgart C., Parra G., Abril J.F., Guigo R.,
RA   Kumpf K., Tunggal B., Cox E.C., Quail M.A., Platzer M., Rosenthal A.,
RA   Noegel A.A.;
RT   "Sequence and analysis of chromosome 2 of Dictyostelium discoideum.";
RL   Nature 418:79-85(2002).
RN   [3] {ECO:0000312|EMBL:EAL68664.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AX4;
RX   PubMed=15875012; DOI=10.1038/nature03481;
RA   Eichinger L., Pachebat J.A., Gloeckner G., Rajandream M.A., Sucgang R.,
RA   Berriman M., Song J., Olsen R., Szafranski K., Xu Q., Tunggal B.,
RA   Kummerfeld S., Madera M., Konfortov B.A., Rivero F., Bankier A.T.,
RA   Lehmann R., Hamlin N., Davies R., Gaudet P., Fey P., Pilcher K., Chen G.,
RA   Saunders D., Sodergren E.J., Davis P., Kerhornou A., Nie X., Hall N.,
RA   Anjard C., Hemphill L., Bason N., Farbrother P., Desany B., Just E.,
RA   Morio T., Rost R., Churcher C.M., Cooper J., Haydock S., van Driessche N.,
RA   Cronin A., Goodhead I., Muzny D.M., Mourier T., Pain A., Lu M., Harper D.,
RA   Lindsay R., Hauser H., James K.D., Quiles M., Madan Babu M., Saito T.,
RA   Buchrieser C., Wardroper A., Felder M., Thangavelu M., Johnson D.,
RA   Knights A., Loulseged H., Mungall K.L., Oliver K., Price C., Quail M.A.,
RA   Urushihara H., Hernandez J., Rabbinowitsch E., Steffen D., Sanders M.,
RA   Ma J., Kohara Y., Sharp S., Simmonds M.N., Spiegler S., Tivey A.,
RA   Sugano S., White B., Walker D., Woodward J.R., Winckler T., Tanaka Y.,
RA   Shaulsky G., Schleicher M., Weinstock G.M., Rosenthal A., Cox E.C.,
RA   Chisholm R.L., Gibbs R.A., Loomis W.F., Platzer M., Kay R.R.,
RA   Williams J.G., Dear P.H., Noegel A.A., Barrell B.G., Kuspa A.;
RT   "The genome of the social amoeba Dictyostelium discoideum.";
RL   Nature 435:43-57(2005).
RN   [4] {ECO:0000305}
RP   IDENTIFICATION, AND INTERACTION WITH CHCA.
RX   PubMed=9425628; DOI=10.1006/prep.1997.0793;
RA   Riddelle-Spencer K.S., O'Halloran T.J.;
RT   "Purification of clathrin heavy and light chain from Dictyostelium
RT   discoideum.";
RL   Protein Expr. Purif. 11:250-256(1997).
RN   [5] {ECO:0000305}
RP   SUBCELLULAR LOCATION, AND INTERACTION WITH CHCA.
RX   PubMed=16734666; DOI=10.1111/j.1600-0854.2006.00438.x;
RA   Wang J., Wang Y., O'Halloran T.J.;
RT   "Clathrin light chain: importance of the conserved carboxy terminal domain
RT   to function in living cells.";
RL   Traffic 7:824-832(2006).
CC   -!- FUNCTION: Clathrin is the major protein of the polyhedral coat of
CC       coated pits and vesicles. {ECO:0000269|PubMed:14617352, ECO:0000305}.
CC   -!- SUBUNIT: Clathrin coats are formed from molecules containing 3 heavy
CC       chains and 3 light chains. {ECO:0000269|PubMed:14617352,
CC       ECO:0000269|PubMed:9425628, ECO:0000305}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasmic vesicle membrane
CC       {ECO:0000269|PubMed:16734666, ECO:0000305}; Peripheral membrane protein
CC       {ECO:0000269|PubMed:16734666}; Cytoplasmic side
CC       {ECO:0000269|PubMed:16734666}. Membrane, coated pit
CC       {ECO:0000269|PubMed:16734666, ECO:0000305}; Peripheral membrane protein
CC       {ECO:0000269|PubMed:16734666}; Cytoplasmic side
CC       {ECO:0000269|PubMed:16734666}. Note=Cytoplasmic face of coated pits and
CC       vesicles. Localized to punctae scattered within the cytoplasm, along
CC       the plasma membrane and concentrated in the perinuclear region.
CC       {ECO:0000269|PubMed:16734666, ECO:0000305}.
CC   -!- DISRUPTION PHENOTYPE: Cells fail to undergo cytokinesis in suspension
CC       culture and show osmoregulation defects. Late development is impaired
CC       in mutants lacking clc which produce misshapen projections rather than
CC       a fruiting body. Mutants lacking clc showed a reduction in the ability
CC       of clathrin to assemble onto membrane, though assembly of clathrin
CC       heavy chain triskelions was unaffected. {ECO:0000269|PubMed:14617352}.
CC   -!- SIMILARITY: Belongs to the clathrin light chain family. {ECO:0000305}.
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DR   EMBL; AY394008; AAQ95635.1; -; mRNA.
DR   EMBL; AAFI02000020; EAL68664.1; -; Genomic_DNA.
DR   RefSeq; XP_642650.1; XM_637558.1.
DR   AlphaFoldDB; Q8MN58; -.
DR   SMR; Q8MN58; -.
DR   STRING; 44689.DDB0191305; -.
DR   PaxDb; Q8MN58; -.
DR   PRIDE; Q8MN58; -.
DR   EnsemblProtists; EAL68664; EAL68664; DDB_G0277403.
DR   GeneID; 8621066; -.
DR   KEGG; ddi:DDB_G0277403; -.
DR   dictyBase; DDB_G0277403; clc.
DR   eggNOG; KOG4031; Eukaryota.
DR   HOGENOM; CLU_1404819_0_0_1; -.
DR   InParanoid; Q8MN58; -.
DR   OMA; NNRDHNK; -.
DR   Reactome; R-DDI-196025; Formation of annular gap junctions.
DR   Reactome; R-DDI-432720; Lysosome Vesicle Biogenesis.
DR   Reactome; R-DDI-437239; Recycling pathway of L1.
DR   Reactome; R-DDI-8856828; Clathrin-mediated endocytosis.
DR   Reactome; R-DDI-8866427; VLDLR internalisation and degradation.
DR   Reactome; R-DDI-8964038; LDL clearance.
DR   PRO; PR:Q8MN58; -.
DR   Proteomes; UP000002195; Chromosome 2.
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; IDA:dictyBase.
DR   GO; GO:0005737; C:cytoplasm; IDA:dictyBase.
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:0009992; P:cellular water homeostasis; IMP:dictyBase.
DR   GO; GO:0048268; P:clathrin coat assembly; IMP:dictyBase.
DR   GO; GO:0072583; P:clathrin-dependent endocytosis; IBA:GO_Central.
DR   GO; GO:0031154; P:culmination involved in sorocarp development; IMP:dictyBase.
DR   GO; GO:0006897; P:endocytosis; ISS:dictyBase.
DR   GO; GO:0006886; P:intracellular protein transport; ISS:dictyBase.
DR   GO; GO:0006869; P:lipid transport; ISS:dictyBase.
DR   GO; GO:0000281; P:mitotic cytokinesis; IMP:dictyBase.
DR   GO; GO:0006898; P:receptor-mediated endocytosis; ISS:dictyBase.
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; Direct protein sequencing; Membrane;
KW   Reference proteome.
FT   CHAIN           1..194
FT                   /note="Clathrin light chain"
FT                   /id="PRO_0000315878"
FT   REGION          44..156
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          124..194
FT                   /note="Required for binding clathrin heavy chain,
FT                   localization to punctae, and for cytokinesis and fruiting
FT                   body development"
FT                   /evidence="ECO:0000269|PubMed:16734666"
FT   COMPBIAS        44..69
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        74..146
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   194 AA;  22137 MW;  70CE8D860765FB8F CRC64;
     MSDPFGEENV EITEEFVEGD INENDLIDGN VEYVDGNGIS FETTTFDNSN NNNNNNNHNN
     NSYNSGFDGD LSSVDGDMKP KETAPAMREY LEKHEKEMQE KKKKSEEKRQ KKIAEAKQSL
     DNFYSEREAK KKTALKNNRD HNKSLETDST SGNTTHTWES VVSMIDLQAK PNPANKDTSR
     MREILIRLKN QPIV
 
 
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