CLCA_BOVIN
ID CLCA_BOVIN Reviewed; 243 AA.
AC P04973; Q17QD2;
DT 13-AUG-1987, integrated into UniProtKB/Swiss-Prot.
DT 13-AUG-1987, sequence version 1.
DT 03-AUG-2022, entry version 146.
DE RecName: Full=Clathrin light chain A;
DE Short=Lca;
GN Name=CLTA;
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] (ISOFORMS BRAIN AND NON-BRAIN).
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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
RC STRAIN=Hereford; TISSUE=Fetal cerebellum;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (JUN-2006) to the EMBL/GenBank/DDBJ databases.
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).
CC -!- FUNCTION: Clathrin is the major protein of the polyhedral coat of
CC coated pits and vesicles. Acts as component of the TACC3/ch-
CC TOG/clathrin complex proposed to contribute to stabilization of
CC kinetochore fibers of the mitotic spindle by acting as inter-
CC microtubule bridge (By similarity). {ECO:0000250|UniProtKB:P09496}.
CC -!- SUBUNIT: Clathrin coats are formed from molecules containing 3 heavy
CC chains and 3 light chains. Interacts with CALY; the interaction
CC stimulates clathrin self-assembly and clathrin-mediated endocytosis (By
CC similarity). Interacts with CKAP5 and TACC3 forming the TACC3/ch-
CC TOG/clathrin complex located at spindle inter-microtubules bridges; the
CC complex implicates clathrin triskelions (By similarity). {ECO:0000250,
CC ECO:0000250|UniProtKB:P09496}.
CC -!- SUBCELLULAR LOCATION: Cytoplasmic vesicle membrane; Peripheral membrane
CC protein; Cytoplasmic side. Membrane, coated pit; Peripheral membrane
CC protein; Cytoplasmic side. Cytoplasm, cytoskeleton, spindle
CC {ECO:0000250|UniProtKB:P09496}. Note=Cytoplasmic face of coated pits
CC and vesicles. In complex with TACC3 and CKAP5 (forming the TACC3/ch-
CC TOG/clathrin complex) localized to inter-microtubule bridges in mitotic
CC spindles. {ECO:0000250|UniProtKB:P09496}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=Brain;
CC IsoId=P04973-1; Sequence=Displayed;
CC Name=Non-brain;
CC IsoId=P04973-2; Sequence=VSP_001094;
CC Name=3;
CC IsoId=P04973-3; Sequence=VSP_024237;
CC -!- SIMILARITY: Belongs to the clathrin light chain family. {ECO:0000305}.
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DR EMBL; X04849; CAA28540.1; -; mRNA.
DR EMBL; X04851; CAA28542.1; -; mRNA.
DR EMBL; BC118427; AAI18428.1; -; mRNA.
DR PIR; A26599; A26599.
DR RefSeq; NP_776447.1; NM_174022.2. [P04973-1]
DR RefSeq; XP_005210116.1; XM_005210059.2. [P04973-3]
DR RefSeq; XP_005210119.1; XM_005210062.2. [P04973-2]
DR PDB; 1XI4; EM; 7.90 A; J/K/L/M/N/O/P/Q/R=95-164.
DR PDB; 3IYV; EM; 7.90 A; J/K/L/M/N/O/P/Q/R=95-164.
DR PDBsum; 1XI4; -.
DR PDBsum; 3IYV; -.
DR AlphaFoldDB; P04973; -.
DR SMR; P04973; -.
DR BioGRID; 158447; 2.
DR IntAct; P04973; 2.
DR MINT; P04973; -.
DR STRING; 9913.ENSBTAP00000001518; -.
DR PaxDb; P04973; -.
DR PeptideAtlas; P04973; -.
DR PRIDE; P04973; -.
DR Ensembl; ENSBTAT00000001518; ENSBTAP00000001518; ENSBTAG00000001137. [P04973-1]
DR Ensembl; ENSBTAT00000066509; ENSBTAP00000058861; ENSBTAG00000001137. [P04973-3]
DR Ensembl; ENSBTAT00000084231; ENSBTAP00000061205; ENSBTAG00000001137. [P04973-2]
DR GeneID; 281078; -.
DR KEGG; bta:281078; -.
DR CTD; 1211; -.
DR VEuPathDB; HostDB:ENSBTAG00000001137; -.
DR eggNOG; KOG4031; Eukaryota.
DR GeneTree; ENSGT00940000157347; -.
DR HOGENOM; CLU_091462_1_0_1; -.
DR InParanoid; P04973; -.
DR OMA; PXESNGP; -.
DR OrthoDB; 1577821at2759; -.
DR TreeFam; TF313162; -.
DR EvolutionaryTrace; P04973; -.
DR Proteomes; UP000009136; Chromosome 8.
DR Bgee; ENSBTAG00000001137; Expressed in isthmus of fallopian tube and 105 other tissues.
DR ExpressionAtlas; P04973; baseline and differential.
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:0071439; C:clathrin complex; IEA:Ensembl.
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:0005819; C:spindle; IEA:UniProtKB-SubCell.
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:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0048268; P:clathrin coat assembly; IEA:Ensembl.
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; Cell cycle;
KW Cell division; Coated pit; Cytoplasm; Cytoplasmic vesicle; Cytoskeleton;
KW Membrane; Mitosis; Phosphoprotein; Reference proteome.
FT CHAIN 1..243
FT /note="Clathrin light chain A"
FT /id="PRO_0000205766"
FT REGION 1..22
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 49..87
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 95..157
FT /note="Involved in binding clathrin heavy chain"
FT MOD_RES 1
FT /note="Blocked amino end (Met)"
FT MOD_RES 100
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P09496"
FT MOD_RES 201
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P09496"
FT MOD_RES 218
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q6IRU5"
FT MOD_RES 231
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P09496"
FT MOD_RES 237
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:O08585"
FT VAR_SEQ 158..187
FT /note="Missing (in isoform Non-brain)"
FT /evidence="ECO:0000303|PubMed:3821891"
FT /id="VSP_001094"
FT VAR_SEQ 176..187
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|Ref.2"
FT /id="VSP_024237"
FT CONFLICT 14
FT /note="P -> H (in Ref. 1; CAA28542)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 243 AA; 26723 MW; B1967A24DC14A06F CRC64;
MAELDPFGVP AGGPALGNGV AGEEDPAAAF LAQQESEIAG IENDEAFAIL DGGAPGSQPH
GEPPGIPDAV DGVTNGDYYQ ESNGPTDSYA AISQVDRLQS EPESIRKWRE EQTERLEALD
ANSRKQEAEW KEKAIKELDE WYARQDEQLQ KTKANNRVAD EAFYKQPFAD VIGYVTNINH
PCYSLEQAAE EAFVNDIEES SPGTEWERVA RLCDFNPKSS KQAKDVSRMR SVLISLKQAP
LVH
