ID   CLC3_ORYSJ              Reviewed;         363 AA.
AC   Q6Z3A8; A0A0P0X5N0;
DT   16-NOV-2011, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   03-AUG-2022, entry version 86.
DE   RecName: Full=Clathrin light chain 3;
GN   OrderedLocusNames=Os07g0461500, LOC_Os07g27750; ORFNames=P0038F09.33;
OS   Oryza sativa subsp. japonica (Rice).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC   Oryzoideae; Oryzeae; Oryzinae; Oryza; Oryza sativa.
OX   NCBI_TaxID=39947;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Nipponbare;
RX   PubMed=16100779; DOI=10.1038/nature03895;
RG   International rice genome sequencing project (IRGSP);
RT   "The map-based sequence of the rice genome.";
RL   Nature 436:793-800(2005).
RN   [2]
RP   GENOME REANNOTATION.
RC   STRAIN=cv. Nipponbare;
RX   PubMed=18089549; DOI=10.1093/nar/gkm978;
RG   The rice annotation project (RAP);
RT   "The rice annotation project database (RAP-DB): 2008 update.";
RL   Nucleic Acids Res. 36:D1028-D1033(2008).
RN   [3]
RP   GENOME REANNOTATION.
RC   STRAIN=cv. Nipponbare;
RX   PubMed=24280374; DOI=10.1186/1939-8433-6-4;
RA   Kawahara Y., de la Bastide M., Hamilton J.P., Kanamori H., McCombie W.R.,
RA   Ouyang S., Schwartz D.C., Tanaka T., Wu J., Zhou S., Childs K.L.,
RA   Davidson R.M., Lin H., Quesada-Ocampo L., Vaillancourt B., Sakai H.,
RA   Lee S.S., Kim J., Numa H., Itoh T., Buell C.R., Matsumoto T.;
RT   "Improvement of the Oryza sativa Nipponbare reference genome using next
RT   generation sequence and optical map data.";
RL   Rice 6:4-4(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. {ECO:0000250}.
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; AP005256; BAC84161.1; -; Genomic_DNA.
DR   EMBL; AP008213; BAH93917.1; -; Genomic_DNA.
DR   EMBL; AP014963; BAT01366.1; -; Genomic_DNA.
DR   RefSeq; XP_015645976.1; XM_015790490.1.
DR   AlphaFoldDB; Q6Z3A8; -.
DR   SMR; Q6Z3A8; -.
DR   STRING; 4530.OS07T0461500-00; -.
DR   PaxDb; Q6Z3A8; -.
DR   PRIDE; Q6Z3A8; -.
DR   EnsemblPlants; Os07t0461500-00; Os07t0461500-00; Os07g0461500.
DR   GeneID; 9267670; -.
DR   Gramene; Os07t0461500-00; Os07t0461500-00; Os07g0461500.
DR   KEGG; osa:9267670; -.
DR   eggNOG; ENOG502QVX7; Eukaryota.
DR   HOGENOM; CLU_053778_2_0_1; -.
DR   InParanoid; Q6Z3A8; -.
DR   OMA; NGVEHVM; -.
DR   OrthoDB; 1299612at2759; -.
DR   Proteomes; UP000000763; Chromosome 7.
DR   Proteomes; UP000059680; Chromosome 7.
DR   Genevisible; Q6Z3A8; OS.
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: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; 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.
PE   3: Inferred from homology;
KW   Coated pit; Coiled coil; Cytoplasmic vesicle; Membrane; Reference proteome.
FT   CHAIN           1..363
FT                   /note="Clathrin light chain 3"
FT                   /id="PRO_0000414014"
FT   REGION          1..38
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          143..204
FT                   /note="Involved in binding clathrin heavy chain"
FT                   /evidence="ECO:0000250"
FT   REGION          236..363
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          151..183
FT                   /evidence="ECO:0000255"
FT   COMPBIAS        236..254
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        308..333
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   363 AA;  37773 MW;  7352D26B9843725E CRC64;
     MSSFDSVAAV AGDGDADDDD VLPPAPFDPA ADGAQGGLGA LRRGHRFATS YSSFGTAASE
     DDLAGAGAGT DGGVGAGIPL GSSSNGGAAY GYGGSGDVMN GHVDQIGDVM GGGVVVGDGG
     GIDDDLFAGA GDGDDGPVLP PPEAMKEEGI LRREWRRQNA LMLEEKERKE RERRGEIIAE
     ADEFKRSFAE KRKLNGDTNR AQNRDREKLF LAKQEKFHGE AEKQYWKAIA EMVPHEIPGL
     EKRGKRREKQ SAEANAKAKQ PGVVVVQGTK PGKPTDLSRM RQVLMKLKQT PPPHMAPPPP
     QPAKDTGGDT DANKDGEAEK AAGEIEKKAA GGEKEAAAGP PVTAAAAADA QANKAAAEET
     AKK