ID   CLC2_ORYSJ              Reviewed;         291 AA.
AC   Q5Z402; A0A0P0X1I4;
DT   16-NOV-2011, integrated into UniProtKB/Swiss-Prot.
DT   23-NOV-2004, sequence version 1.
DT   03-AUG-2022, entry version 93.
DE   RecName: Full=Clathrin light chain 2;
GN   OrderedLocusNames=Os06g0731800, LOC_Os06g51510;
GN   ORFNames=B1206D04.26, OsJ_22754;
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).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Nipponbare;
RX   PubMed=15685292; DOI=10.1371/journal.pbio.0030038;
RA   Yu J., Wang J., Lin W., Li S., Li H., Zhou J., Ni P., Dong W., Hu S.,
RA   Zeng C., Zhang J., Zhang Y., Li R., Xu Z., Li S., Li X., Zheng H., Cong L.,
RA   Lin L., Yin J., Geng J., Li G., Shi J., Liu J., Lv H., Li J., Wang J.,
RA   Deng Y., Ran L., Shi X., Wang X., Wu Q., Li C., Ren X., Wang J., Wang X.,
RA   Li D., Liu D., Zhang X., Ji Z., Zhao W., Sun Y., Zhang Z., Bao J., Han Y.,
RA   Dong L., Ji J., Chen P., Wu S., Liu J., Xiao Y., Bu D., Tan J., Yang L.,
RA   Ye C., Zhang J., Xu J., Zhou Y., Yu Y., Zhang B., Zhuang S., Wei H.,
RA   Liu B., Lei M., Yu H., Li Y., Xu H., Wei S., He X., Fang L., Zhang Z.,
RA   Zhang Y., Huang X., Su Z., Tong W., Li J., Tong Z., Li S., Ye J., Wang L.,
RA   Fang L., Lei T., Chen C.-S., Chen H.-C., Xu Z., Li H., Huang H., Zhang F.,
RA   Xu H., Li N., Zhao C., Li S., Dong L., Huang Y., Li L., Xi Y., Qi Q.,
RA   Li W., Zhang B., Hu W., Zhang Y., Tian X., Jiao Y., Liang X., Jin J.,
RA   Gao L., Zheng W., Hao B., Liu S.-M., Wang W., Yuan L., Cao M.,
RA   McDermott J., Samudrala R., Wang J., Wong G.K.-S., Yang H.;
RT   "The genomes of Oryza sativa: a history of duplications.";
RL   PLoS Biol. 3:266-281(2005).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=cv. Nipponbare;
RX   PubMed=12869764; DOI=10.1126/science.1081288;
RG   The rice full-length cDNA consortium;
RT   "Collection, mapping, and annotation of over 28,000 cDNA clones from
RT   japonica rice.";
RL   Science 301:376-379(2003).
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; AP006616; BAD62498.1; -; Genomic_DNA.
DR   EMBL; AP008212; BAF20580.1; -; Genomic_DNA.
DR   EMBL; AP014962; BAS99661.1; -; Genomic_DNA.
DR   EMBL; CM000143; EEE66409.1; -; Genomic_DNA.
DR   EMBL; AK069288; BAG91360.1; -; mRNA.
DR   RefSeq; XP_015644113.1; XM_015788627.1.
DR   AlphaFoldDB; Q5Z402; -.
DR   SMR; Q5Z402; -.
DR   STRING; 4530.OS06T0731800-01; -.
DR   PaxDb; Q5Z402; -.
DR   PRIDE; Q5Z402; -.
DR   EnsemblPlants; Os06t0731800-01; Os06t0731800-01; Os06g0731800.
DR   GeneID; 4342159; -.
DR   Gramene; Os06t0731800-01; Os06t0731800-01; Os06g0731800.
DR   KEGG; osa:4342159; -.
DR   eggNOG; ENOG502QVX7; Eukaryota.
DR   HOGENOM; CLU_053778_2_0_1; -.
DR   InParanoid; Q5Z402; -.
DR   OMA; STHQHDD; -.
DR   OrthoDB; 1299612at2759; -.
DR   Proteomes; UP000000763; Chromosome 6.
DR   Proteomes; UP000007752; Chromosome 6.
DR   Proteomes; UP000059680; Chromosome 6.
DR   Genevisible; Q5Z402; 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   2: Evidence at transcript level;
KW   Coated pit; Coiled coil; Cytoplasmic vesicle; Membrane; Reference proteome.
FT   CHAIN           1..291
FT                   /note="Clathrin light chain 2"
FT                   /id="PRO_0000414013"
FT   REGION          1..91
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          84..146
FT                   /note="Involved in binding clathrin heavy chain"
FT                   /evidence="ECO:0000250"
FT   REGION          183..291
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          93..120
FT                   /evidence="ECO:0000255"
FT   COMPBIAS        33..51
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        183..199
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   291 AA;  31290 MW;  319747BB3FA39CC3 CRC64;
     MATAFDSPTA SPAASPFDDD SFLRFDAAAP APAPADAFPP SPEPYAFRPD APSPFGMPEA
     NGSLHDDPFA APDNDNGPVL PPPNQMGADE GFLLREWRRQ NAILLEEKEK KEKEMRNQII
     LDAKEFKKAF VEKRKLNVET SKDQNREREK LYLANQEKFH AGADKQYWKA ISELIPHEIA
     NIEKRGAKKD KDKEKKPGIV VIQGPKPGKP TDMSRMRQIL LKLKHTPPPH MKPPPPPAAA
     TGKDGAAGKD GAKVAAAASK DASANGSVPE MEKAAAAAAP AAAATEPIAA A