ID   CLCB_BOVIN              Reviewed;         228 AA.
AC   P04975;
DT   13-AUG-1987, integrated into UniProtKB/Swiss-Prot.
DT   13-AUG-1987, sequence version 1.
DT   03-AUG-2022, entry version 158.
DE   RecName: Full=Clathrin light chain B;
DE            Short=Lcb;
GN   Name=CLTB; Synonyms=CLTLB;
OS   Bos taurus (Bovine).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC   Bovinae; Bos.
OX   NCBI_TaxID=9913;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=3821891; DOI=10.1038/326154a0;
RA   Jackson A.P., Seow H.-F., Holmes N., Drickamer K., Parham P.;
RT   "Clathrin light chains contain brain-specific insertion sequences and a
RT   region of homology with intermediate filaments.";
RL   Nature 326:154-159(1987).
RN   [2]
RP   PROTEIN SEQUENCE OF 9-27, AND PHOSPHORYLATION AT SER-11 AND SER-13.
RX   PubMed=3128543; DOI=10.1016/s0021-9258(18)60591-5;
RA   Hill B.L., Drickamer K., Brodsky F.M., Parham P.;
RT   "Identification of the phosphorylation sites of clathrin light chain LCb.";
RL   J. Biol. Chem. 263:5499-5501(1988).
RN   [3]
RP   DOMAIN CLATHRIN HEAVY CHAIN BINDING.
RX   PubMed=2434865; DOI=10.1038/326203a0;
RA   Brodsky F.M., Galloway C.J., Blank G.S., Jackson A.P., Seow H.-F.,
RA   Drickamer K., Parham P.;
RT   "Localization of clathrin light-chain sequences mediating heavy-chain
RT   binding and coated vesicle diversity.";
RL   Nature 326:203-205(1987).
RN   [4]
RP   DISULFIDE BONDS.
RX   PubMed=2930486; DOI=10.1042/bj2570775;
RA   Parham P., Brodsky F.M., Drickamer K.;
RT   "The occurrence of disulphide bonds in purified clathrin light chains.";
RL   Biochem. J. 257:775-781(1989).
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. Interacts (via N-terminus) with HIP1.
CC       Interacts with HIP1R.
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   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=Brain;
CC         IsoId=P04975-1; Sequence=Displayed;
CC       Name=Non-brain;
CC         IsoId=P04975-2; Sequence=VSP_001097;
CC   -!- SIMILARITY: Belongs to the clathrin light chain family. {ECO:0000305}.
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DR   EMBL; X04852; CAA28543.1; -; mRNA.
DR   EMBL; X04853; CAA28544.1; -; mRNA.
DR   PIR; C26599; C26599.
DR   RefSeq; NP_776702.1; NM_174277.2. [P04975-2]
DR   RefSeq; XP_005209178.1; XM_005209121.3. [P04975-1]
DR   PDB; 3LVG; X-ray; 7.94 A; D/E/F=89-169.
DR   PDB; 3LVH; X-ray; 9.00 A; D/E/F=1-169.
DR   PDB; 6WCJ; EM; 6.30 A; B/E/F/J/N/O=1-228.
DR   PDBsum; 3LVG; -.
DR   PDBsum; 3LVH; -.
DR   PDBsum; 6WCJ; -.
DR   AlphaFoldDB; P04975; -.
DR   SMR; P04975; -.
DR   BioGRID; 159016; 3.
DR   IntAct; P04975; 3.
DR   MINT; P04975; -.
DR   STRING; 9913.ENSBTAP00000055957; -.
DR   iPTMnet; P04975; -.
DR   PeptideAtlas; P04975; -.
DR   PRIDE; P04975; -.
DR   Ensembl; ENSBTAT00000014218; ENSBTAP00000014218; ENSBTAG00000010740. [P04975-2]
DR   Ensembl; ENSBTAT00000064630; ENSBTAP00000055957; ENSBTAG00000010740. [P04975-1]
DR   GeneID; 281698; -.
DR   KEGG; bta:281698; -.
DR   CTD; 1212; -.
DR   VEuPathDB; HostDB:ENSBTAG00000010740; -.
DR   eggNOG; KOG4031; Eukaryota.
DR   GeneTree; ENSGT00940000160186; -.
DR   HOGENOM; CLU_091462_1_0_1; -.
DR   InParanoid; P04975; -.
DR   OrthoDB; 1577821at2759; -.
DR   Proteomes; UP000009136; Chromosome 7.
DR   Bgee; ENSBTAG00000010740; Expressed in digestive system secreted substance and 105 other tissues.
DR   ExpressionAtlas; P04975; baseline and differential.
DR   GO; GO:0030118; C:clathrin coat; ISS:UniProtKB.
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: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; 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.
DR   PROSITE; PS00224; CLATHRIN_LIGHT_CHN_1; 1.
DR   PROSITE; PS00581; CLATHRIN_LIGHT_CHN_2; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Acetylation; Alternative splicing; Calcium; Coated pit;
KW   Cytoplasmic vesicle; Direct protein sequencing; Disulfide bond; Membrane;
KW   Phosphoprotein; Reference proteome.
FT   CHAIN           1..228
FT                   /note="Clathrin light chain B"
FT                   /id="PRO_0000205770"
FT   REGION          1..80
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          92..154
FT                   /note="Involved in binding clathrin heavy chain"
FT   MOD_RES         1
FT                   /note="Blocked amino end (Met)"
FT   MOD_RES         11
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000269|PubMed:3128543"
FT   MOD_RES         13
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000269|PubMed:3128543"
FT   MOD_RES         186
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:P09497"
FT   MOD_RES         203
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:Q6IRU5"
FT   MOD_RES         216
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P09496"
FT   DISULFID        198..208
FT                   /evidence="ECO:0000269|PubMed:2930486"
FT   VAR_SEQ         155..172
FT                   /note="Missing (in isoform Non-brain)"
FT                   /evidence="ECO:0000305"
FT                   /id="VSP_001097"
SQ   SEQUENCE   228 AA;  25082 MW;  3CE75F0884B47E1A CRC64;
     MADDFGFFSS SESGAPEAAE EDPAAAFLAQ QESEIAGIEN DEGFGAPAGS QGGLAQPGPA
     SGASEDMGAT VNGDVFQEAN GPADGYAAIA QADRLTQEPE SIRKWREEQR KRLQELDAAS
     KVMEQEWREK AKKDLEEWNQ RQSEQVEKNK INNRIADKAF YQQPDADIIG YVASEEAFVK
     ESKEETPGTE WEKVAQLCDF NPKSSKQCKD VSRLRSVLMS LKQTPLSR