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Clathrin heavy chain 1

 CLH1_MOUSE              Reviewed;        1675 AA.
Q68FD5;
24-MAY-2005, integrated into UniProtKB/Swiss-Prot.
23-JAN-2007, sequence version 3.
22-NOV-2017, entry version 120.
RecName: Full=Clathrin heavy chain 1;
Name=Cltc;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=C57BL/6J;
PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
Lindblad-Toh K., Eichler E.E., Ponting C.P.;
"Lineage-specific biology revealed by a finished genome assembly of
the mouse.";
PLoS Biol. 7:E1000112-E1000112(2009).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=C57BL/6J; TISSUE=Brain;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[3]
PROTEIN SEQUENCE OF 44-63; 87-96; 101-112; 145-157; 164-188; 190-205;
228-245; 270-278; 298-320; 355-366; 377-382; 430-444; 446-453;
457-481; 626-637; 768-780; 799-806; 838-852 AND 857-881.
STRAIN=C57BL/6J; TISSUE=Brain;
Lubec G., Kang S.U.;
Submitted (APR-2007) to UniProtKB.
[4]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-184; TYR-634; TYR-899;
TYR-1206; TYR-1477 AND TYR-1487, AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Brain;
PubMed=18034455; DOI=10.1021/pr0701254;
Ballif B.A., Carey G.R., Sunyaev S.R., Gygi S.P.;
"Large-scale identification and evolution indexing of tyrosine
phosphorylation sites from murine brain.";
J. Proteome Res. 7:311-318(2008).
[5]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-67; THR-105; SER-1167
AND SER-1494, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung,
Pancreas, Spleen, and Testis;
PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
"A tissue-specific atlas of mouse protein phosphorylation and
expression.";
Cell 143:1174-1189(2010).
[6]
INTERACTION WITH OCRL.
PubMed=20133602; DOI=10.1073/pnas.0914658107;
Swan L.E., Tomasini L., Pirruccello M., Lunardi J., De Camilli P.;
"Two closely related endocytic proteins that share a common OCRL-
binding motif with APPL1.";
Proc. Natl. Acad. Sci. U.S.A. 107:3511-3516(2010).
[7]
SUCCINYLATION [LARGE SCALE ANALYSIS] AT LYS-737 AND LYS-1441, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Embryonic fibroblast;
PubMed=23806337; DOI=10.1016/j.molcel.2013.06.001;
Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z.,
Zhang Y., Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.;
"SIRT5-mediated lysine desuccinylation impacts diverse metabolic
pathways.";
Mol. Cell 50:919-930(2013).
[8]
INTERACTION WITH USP2.
PubMed=26756164; DOI=10.1371/journal.pone.0145155;
Pouly D., Chenaux S., Martin V., Babis M., Koch R., Nagoshi E.,
Katanaev V.L., Gachon F., Staub O.;
"USP2-45 is a circadian clock output effector regulating calcium
absorption at the post-translational level.";
PLoS ONE 11:E0145155-E0145155(2016).
-!- FUNCTION: Clathrin is the major protein of the polyhedral coat of
coated pits and vesicles. Two different adapter protein complexes
link the clathrin lattice either to the plasma membrane or to the
trans-Golgi network. Acts as component of the TACC3/ch-
TOG/clathrin complex proposed to contribute to stabilization of
kinetochore fibers of the mitotic spindle by acting as inter-
microtubule bridge. The TACC3/ch-TOG/clathrin complex is required
for the maintenance of kinetochore fiber tension. Plays a role in
early autophagosome formation. {ECO:0000250|UniProtKB:P11442,
ECO:0000250|UniProtKB:Q00610}.
-!- SUBUNIT: Clathrin triskelions, composed of 3 heavy chains and 3
light chains, are the basic subunits of the clathrin coat (By
similarity). In the presence of light chains, hub assembly is
influenced by both the pH and the concentration of calcium (By
similarity). Interacts with HIP1 (By similarity). Interacts with
DENND1A, DENND1B and DENND1C (By similarity). Interacts with ERBB2
(By similarity). Interacts with FKBP6 (By similarity). Interacts
with OCRL (PubMed:20133602). Interacts with CKAP5 and TACC3
forming the TACC3/ch-TOG/clathrin complex located at spindle
inter-microtubules bridges; the complex implicates clathrin
triskelions; TACC3 and CLTC are proposed to form a composite
microtubule interaction surface (By similarity). Plays a role in
early autopahgosome formation (By similarity). Interacts with
ATG16L1 (via N-terminus) (By similarity). Interacts with USP2
isoform 2 (PubMed:26756164). {ECO:0000250|UniProtKB:P49951,
ECO:0000250|UniProtKB:Q00610, ECO:0000269|PubMed:20133602,
ECO:0000269|PubMed:26756164}.
-!- INTERACTION:
Q15637:SF1 (xeno); NbExp=3; IntAct=EBI-769168, EBI-744603;
-!- SUBCELLULAR LOCATION: Cytoplasmic vesicle membrane {ECO:0000250};
Peripheral membrane protein {ECO:0000250}; Cytoplasmic side
{ECO:0000250}. Membrane, coated pit {ECO:0000250}; Peripheral
membrane protein {ECO:0000250}; Cytoplasmic side {ECO:0000250}.
Melanosome {ECO:0000250}. Cytoplasm, cytoskeleton, spindle
{ECO:0000250|UniProtKB:Q00610}. Note=Cytoplasmic face of coated
pits and vesicles. In complex with TACC3 and CKAP5 (forming the
TACC3/ch-TOG/clathrin complex) localized to inter-microtubule
bridges in mitotic spindles. {ECO:0000250,
ECO:0000250|UniProtKB:Q00610}.
-!- DOMAIN: The N-terminal seven-bladed beta-propeller is formed by
WD40-like repeats, and projects inward from the polyhedral outer
clathrin coat. It constitutes a major protein-protein interaction
node (By similarity). {ECO:0000250}.
-!- SIMILARITY: Belongs to the clathrin heavy chain family.
{ECO:0000305}.
-----------------------------------------------------------------------
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Distributed under the Creative Commons Attribution-NoDerivs License
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EMBL; AL592222; CAI25362.1; -; Genomic_DNA.
EMBL; BC079897; AAH79897.1; -; mRNA.
CCDS; CCDS25204.1; -.
RefSeq; NP_001003908.1; NM_001003908.1.
UniGene; Mm.254588; -.
ProteinModelPortal; Q68FD5; -.
SMR; Q68FD5; -.
BioGrid; 212086; 16.
CORUM; Q68FD5; -.
DIP; DIP-31947N; -.
IntAct; Q68FD5; 31.
MINT; MINT-4153227; -.
STRING; 10090.ENSMUSP00000099475; -.
iPTMnet; Q68FD5; -.
PhosphoSitePlus; Q68FD5; -.
SwissPalm; Q68FD5; -.
EPD; Q68FD5; -.
MaxQB; Q68FD5; -.
PaxDb; Q68FD5; -.
PRIDE; Q68FD5; -.
Ensembl; ENSMUST00000103186; ENSMUSP00000099475; ENSMUSG00000047126.
GeneID; 67300; -.
KEGG; mmu:67300; -.
UCSC; uc007kta.1; mouse.
CTD; 1213; -.
MGI; MGI:2388633; Cltc.
eggNOG; KOG0985; Eukaryota.
eggNOG; ENOG410XPH1; LUCA.
GeneTree; ENSGT00400000022107; -.
HOVERGEN; HBG005344; -.
InParanoid; Q68FD5; -.
KO; K04646; -.
TreeFam; TF300059; -.
Reactome; R-MMU-177504; Retrograde neurotrophin signalling.
Reactome; R-MMU-2132295; MHC class II antigen presentation.
Reactome; R-MMU-432720; Lysosome Vesicle Biogenesis.
Reactome; R-MMU-432722; Golgi Associated Vesicle Biogenesis.
Reactome; R-MMU-437239; Recycling pathway of L1.
Reactome; R-MMU-5099900; WNT5A-dependent internalization of FZD4.
Reactome; R-MMU-5140745; WNT5A-dependent internalization of FZD2, FZD5 and ROR2.
Reactome; R-MMU-8856825; Cargo recognition for clathrin-mediated endocytosis.
Reactome; R-MMU-8856828; Clathrin-mediated endocytosis.
Reactome; R-MMU-8866427; VLDLR internalisation and degradation.
Reactome; R-MMU-8964038; LDL clearance.
ChiTaRS; Cltc; mouse.
PRO; PR:Q68FD5; -.
Proteomes; UP000000589; Chromosome 11.
Bgee; ENSMUSG00000047126; -.
CleanEx; MM_CLTC; -.
ExpressionAtlas; Q68FD5; baseline and differential.
Genevisible; Q68FD5; MM.
GO; GO:0030118; C:clathrin coat; ISO:MGI.
GO; GO:0030132; C:clathrin coat of coated pit; IEA:InterPro.
GO; GO:0030130; C:clathrin coat of trans-Golgi network vesicle; IEA:InterPro.
GO; GO:0071439; C:clathrin complex; ISO:MGI.
GO; GO:0030136; C:clathrin-coated vesicle; ISO:MGI.
GO; GO:0005829; C:cytosol; IEA:GOC.
GO; GO:0005768; C:endosome; ISO:MGI.
GO; GO:0070062; C:extracellular exosome; ISO:MGI.
GO; GO:0031012; C:extracellular matrix; ISO:MGI.
GO; GO:1903561; C:extracellular vesicle; ISO:MGI.
GO; GO:0005925; C:focal adhesion; ISO:MGI.
GO; GO:0005764; C:lysosome; ISO:MGI.
GO; GO:0042470; C:melanosome; IEA:UniProtKB-SubCell.
GO; GO:0016020; C:membrane; IMP:ParkinsonsUK-UCL.
GO; GO:0030117; C:membrane coat; IDA:MGI.
GO; GO:0005739; C:mitochondrion; IDA:MGI.
GO; GO:1990498; C:mitotic spindle microtubule; ISO:MGI.
GO; GO:0031523; C:Myb complex; ISO:MGI.
GO; GO:0043209; C:myelin sheath; IDA:UniProtKB.
GO; GO:0043234; C:protein complex; ISO:MGI.
GO; GO:0005819; C:spindle; ISO:MGI.
GO; GO:0032051; F:clathrin light chain binding; ISO:MGI.
GO; GO:0097718; F:disordered domain specific binding; ISO:MGI.
GO; GO:0003725; F:double-stranded RNA binding; ISO:MGI.
GO; GO:0050750; F:low-density lipoprotein particle receptor binding; ISO:MGI.
GO; GO:0019901; F:protein kinase binding; IPI:ParkinsonsUK-UCL.
GO; GO:0003723; F:RNA binding; ISO:MGI.
GO; GO:0005198; F:structural molecule activity; IEA:InterPro.
GO; GO:1990381; F:ubiquitin-specific protease binding; ISO:MGI.
GO; GO:0006914; P:autophagy; IEA:UniProtKB-KW.
GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
GO; GO:0048268; P:clathrin coat assembly; ISO:MGI.
GO; GO:0072583; P:clathrin-dependent endocytosis; ISO:MGI.
GO; GO:0006886; P:intracellular protein transport; IEA:InterPro.
GO; GO:0000278; P:mitotic cell cycle; ISO:MGI.
GO; GO:0090307; P:mitotic spindle assembly; ISO:MGI.
GO; GO:1900126; P:negative regulation of hyaluronan biosynthetic process; ISS:UniProtKB.
GO; GO:1903077; P:negative regulation of protein localization to plasma membrane; ISO:MGI.
GO; GO:0001649; P:osteoblast differentiation; ISO:MGI.
GO; GO:0031623; P:receptor internalization; ISO:MGI.
GO; GO:0006898; P:receptor-mediated endocytosis; ISO:MGI.
GO; GO:0060236; P:regulation of mitotic spindle organization; ISO:MGI.
GO; GO:0042147; P:retrograde transport, endosome to Golgi; ISO:MGI.
GO; GO:0045056; P:transcytosis; ISO:MGI.
GO; GO:0033572; P:transferrin transport; ISO:MGI.
Gene3D; 1.25.40.10; -; 4.
Gene3D; 1.25.40.30; -; 1.
InterPro; IPR016024; ARM-type_fold.
InterPro; IPR000547; Clathrin_H-chain/VPS_repeat.
InterPro; IPR012331; Clathrin_H-chain_linker.
InterPro; IPR015348; Clathrin_H-chain_linker_core.
InterPro; IPR022365; Clathrin_H-chain_propeller_rpt.
InterPro; IPR016341; Clathrin_heavy_chain.
InterPro; IPR011990; TPR-like_helical_dom_sf.
Pfam; PF00637; Clathrin; 7.
Pfam; PF09268; Clathrin-link; 1.
Pfam; PF01394; Clathrin_propel; 5.
PIRSF; PIRSF002290; Clathrin_H_chain; 1.
SMART; SM00299; CLH; 7.
SUPFAM; SSF48371; SSF48371; 6.
PROSITE; PS50236; CHCR; 7.
1: Evidence at protein level;
Acetylation; Autophagy; Cell cycle; Cell division; Coated pit;
Complete proteome; Cytoplasm; Cytoplasmic vesicle; Cytoskeleton;
Direct protein sequencing; Membrane; Mitosis; Phosphoprotein;
Reference proteome; Repeat.
INIT_MET 1 1 Removed. {ECO:0000250|UniProtKB:Q00610}.
CHAIN 2 1675 Clathrin heavy chain 1.
/FTId=PRO_0000205779.
REPEAT 537 683 CHCR 1.
REPEAT 686 828 CHCR 2.
REPEAT 833 972 CHCR 3.
REPEAT 979 1124 CHCR 4.
REPEAT 1128 1269 CHCR 5.
REPEAT 1274 1420 CHCR 6.
REPEAT 1423 1566 CHCR 7.
REGION 2 479 Globular terminal domain.
REGION 24 67 WD40-like repeat 1.
REGION 68 107 WD40-like repeat 2.
REGION 108 149 WD40-like repeat 3.
REGION 150 195 WD40-like repeat 4.
REGION 196 257 WD40-like repeat 5.
REGION 258 301 WD40-like repeat 6.
REGION 302 330 WD40-like repeat 7.
REGION 449 465 Binding site for the uncoating ATPase,
involved in lattice disassembly.
{ECO:0000255}.
REGION 480 523 Flexible linker.
REGION 524 1675 Heavy chain arm.
REGION 524 634 Distal segment.
REGION 639 1675 Proximal segment.
REGION 1213 1522 Involved in binding clathrin light chain.
{ECO:0000250}.
REGION 1550 1675 Trimerization. {ECO:0000250}.
MOD_RES 2 2 N-acetylalanine.
{ECO:0000250|UniProtKB:Q00610}.
MOD_RES 67 67 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 105 105 Phosphothreonine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 184 184 Phosphotyrosine.
{ECO:0000244|PubMed:18034455}.
MOD_RES 394 394 Phosphothreonine.
{ECO:0000250|UniProtKB:Q00610}.
MOD_RES 634 634 Phosphotyrosine.
{ECO:0000244|PubMed:18034455}.
MOD_RES 737 737 N6-succinyllysine.
{ECO:0000244|PubMed:23806337}.
MOD_RES 856 856 N6-acetyllysine.
{ECO:0000250|UniProtKB:Q00610}.
MOD_RES 899 899 Phosphotyrosine.
{ECO:0000244|PubMed:18034455}.
MOD_RES 1167 1167 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 1206 1206 Phosphotyrosine.
{ECO:0000244|PubMed:18034455}.
MOD_RES 1229 1229 Phosphoserine.
{ECO:0000250|UniProtKB:Q00610}.
MOD_RES 1441 1441 N6-acetyllysine; alternate.
{ECO:0000250|UniProtKB:Q00610}.
MOD_RES 1441 1441 N6-succinyllysine; alternate.
{ECO:0000244|PubMed:23806337}.
MOD_RES 1477 1477 Phosphotyrosine.
{ECO:0000244|PubMed:18034455}.
MOD_RES 1487 1487 Phosphotyrosine.
{ECO:0000244|PubMed:18034455}.
MOD_RES 1494 1494 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 1501 1501 N6-acetyllysine.
{ECO:0000250|UniProtKB:Q00610}.
SEQUENCE 1675 AA; 191557 MW; 6C41EBD89EB7D56B CRC64;
MAQILPIRFQ EHLQLQNLGI NPANIGFSTL TMESDKFICI REKVGEQAQV VIIDMNDPSN
PIRRPISADS AIMNPASKVI ALKAGKTLQI FNIEMKSKMK AHTMTDDVTF WKWISLNTVA
LVTDNAVYHW SMEGESQPVK MFDRHSSLAG CQIINYRTDA KQKWLLLTGI SAQQNRVVGA
MQLYSVDRKV SQPIEGHAAS FAQFKMEGNA EESTLFCFAV RGQAGGKLHI IEVGTPPTGN
QPFPKKAVDV FFPPEAQNDF PVAMQISEKH DVVFLITKYG YIHLYDLETG TCIYMNRISG
ETIFVTAPHE ATAGIIGVNR KGQVLSVCVE EENIIPYITN VLQNPDLALR MAVRNNLAGA
EELFARKFNA LFAQGNYSEA AKVAANAPKG ILRTPDTIRR FQSVPAQPGQ TSPLLQYFGI
LLDQGQLNKY ESLELCRPVL QQGRKQLLEK WLKEDKLECS EELGDLVKSV DPTLALSVYL
RANVPNKVIQ CFAETGQVQK IVLYAKKVGY TPDWIFLLRN VMRISPDQGQ QFAQMLVQDE
EPLADITQIV DVFMEYNLIQ QCTAFLLDAL KNNRPSEGPL QTRLLEMNLM HAPQVADAIL
GNQMFTHYDR AHIAQLCEKA GLLQRALEHF TDLYDIKRAV VHTHLLNPEW LVNYFGSLSV
EDSLECLRAM LSANIRQNLQ ICVQVASKYH EQLSTQSLIE LFESFKSFEG LFYFLGSIVN
FSQDPDVHFK YIQAACKTGQ IKEVERICRE SNCYDPERVK NFLKEAKLTD QLPLIIVCDR
FDFVHDLVLY LYRNNLQKYI EIYVQKVNPS RLPVVIGGLL DVDCSEDVIK NLILVVRGQF
STDELVAEVE KRNRLKLLLP WLEARIHEGC EEPATHNALA KIYIDSNNNP ERFLRENPYY
DSRVVGKYCE KRDPHLACVA YERGQCDLEL INVCNENSLF KSLSRYLVRR KDPELWGSVL
LESNPYRRPL IDQVVQTALS ETQDPEEVSV TVKAFMTADL PNELIELLEK IVLDNSVFSE
HRNLQNLLIL TAIKADRTRV MEYINRLDNY DAPDIANIAI SNELFEEAFA IFRKFDVNTS
AVQVLIEHIG NLDRAYEFAE RCNEPAVWSQ LAKAQLQKGM VKEAIDSYIK ADDPSSYMEV
VQAANASGNW EELVKYLQMA RKKARESYVE TELIFALAKT NRLAELEEFI NGPNNAHIQQ
VGDRCYDEKM YDAAKLLYNN VSNFGRLAST LVHLGEYQAA VDGARKANST RTWKEVCFAC
VDGKEFRLAQ MCGLHIVVHA DELEELINYY QDRGYFEELI TMLEAALGLE RAHMGMFTEL
AILYSKFKPQ KMREHLELFW SRVNIPKVLR AAEQAHLWAE LVFLYDKYEE YDNAIITMMN
HPTDAWKEGQ FKDIITKVAN VELYYKAIQF YLEFKPLLLN DLLMVLSPRL DHTRAVNYFS
KVKQLPLVKP YLRSVQNHNN KSVNESLNNL FITEEDYQAL RTSIDAYDNF DNISLAQRLE
KHELIEFRRI AAYLFKGNNR WKQSVELCKK DSLYKDAMQY ASESKDTELA EELLQWFLQE
EKRECFGACL FTCYDLLRPD VVLETAWRHN IMDFAMPYFI QVMKEYLTKV DKLDASESLR
KEEEQATETQ PIVYGQPQLM LTAGPSVAVP PQAPFGYGYT APPYGQPQPG FGYSM


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