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Clathrin heavy chain

 CLH_DROME               Reviewed;        1678 AA.
P29742; Q540W2; Q9VXN6;
01-APR-1993, integrated into UniProtKB/Swiss-Prot.
01-APR-1993, sequence version 1.
22-NOV-2017, entry version 153.
RecName: Full=Clathrin heavy chain;
Name=Chc; ORFNames=CG9012;
Drosophila melanogaster (Fruit fly).
Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta;
Pterygota; Neoptera; Holometabola; Diptera; Brachycera; Muscomorpha;
Ephydroidea; Drosophilidae; Drosophila; Sophophora.
NCBI_TaxID=7227;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
STRAIN=Canton-S; TISSUE=Head;
PubMed=8375651;
Bazinet C., Katzen A.L., Morgan M., Mahowald A.P., Lemmon S.K.;
"The Drosophila clathrin heavy chain gene: clathrin function is
essential in a multicellular organism.";
Genetics 134:1119-1134(1993).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=Berkeley;
PubMed=10731132; DOI=10.1126/science.287.5461.2185;
Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X.,
Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D.,
Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G.,
Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D.,
Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M.,
Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S.,
Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P.,
Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I.,
Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P.,
de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M.,
Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P.,
Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W.,
Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K.,
Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J.,
Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C.,
Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A.,
Kimmel B.E., Kodira C.D., Kraft C.L., Kravitz S., Kulp D., Lai Z.,
Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X.,
Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D.,
Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A.,
Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L.,
Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M.,
Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G.,
Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H.,
Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J.,
Spier E., Spradling A.C., Stapleton M., Strong R., Sun E.,
Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X.,
Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J.,
Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A.,
Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L.,
Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S.C., Zhu X.,
Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.;
"The genome sequence of Drosophila melanogaster.";
Science 287:2185-2195(2000).
[3]
GENOME REANNOTATION.
STRAIN=Berkeley;
PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q.,
Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M.,
Lewis S.E.;
"Annotation of the Drosophila melanogaster euchromatic genome: a
systematic review.";
Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=Berkeley; TISSUE=Embryo;
PubMed=12537569; DOI=10.1186/gb-2002-3-12-research0080;
Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M.,
George R.A., Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H.,
Rubin G.M., Celniker S.E.;
"A Drosophila full-length cDNA resource.";
Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002).
[5]
INTERACTION WITH SAU.
PubMed=24786584; DOI=10.1371/journal.pgen.1004305;
Sechi S., Colotti G., Belloni G., Mattei V., Frappaolo A., Raffa G.D.,
Fuller M.T., Giansanti M.G.;
"GOLPH3 is essential for contractile ring formation and Rab11
localization to the cleavage site during cytokinesis in Drosophila
melanogaster.";
PLoS Genet. 10:E1004305-E1004305(2014).
-!- FUNCTION: Clathrin is the major protein of the polyhedral coat of
coated pits and vesicles.
-!- SUBUNIT: Clathrin triskelions, composed of 3 heavy chains and 3
light chains, are the basic subunits of the clathrin coat (By
similarity). Interacts with sau (PubMed:24786584).
{ECO:0000250|UniProtKB:Q00610, ECO:0000269|PubMed:24786584}.
-!- INTERACTION:
P16568:BicD; NbExp=5; IntAct=EBI-160368, EBI-112159;
-!- SUBCELLULAR LOCATION: Cytoplasmic vesicle membrane; Peripheral
membrane protein; Cytoplasmic side. Membrane, coated pit;
Peripheral membrane protein; Cytoplasmic side. Note=Cytoplasmic
face of coated pits and vesicles.
-!- DOMAIN: The C-terminal third of the heavy chains forms the hub of
the triskelion. This region contains the trimerization domain and
the light-chain binding domain involved in the assembly of the
clathrin lattice.
-!- 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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EMBL; Z14133; CAA78507.1; -; mRNA.
EMBL; AE014298; AAF48522.1; -; Genomic_DNA.
EMBL; AE014298; AAN09367.1; -; Genomic_DNA.
EMBL; AE014298; AAS65352.1; -; Genomic_DNA.
EMBL; AE014298; AAS65353.1; -; Genomic_DNA.
EMBL; AE014298; ABW09424.1; -; Genomic_DNA.
EMBL; AE014298; ABW09425.1; -; Genomic_DNA.
EMBL; AY119615; AAM50269.1; -; mRNA.
PIR; S52588; S52588.
RefSeq; NP_001096993.1; NM_001103523.2.
RefSeq; NP_001096994.1; NM_001103524.2.
RefSeq; NP_001285300.1; NM_001298371.1.
RefSeq; NP_477042.1; NM_057694.3.
RefSeq; NP_727901.1; NM_167466.2.
RefSeq; NP_996451.1; NM_206728.2.
RefSeq; NP_996452.1; NM_206729.2.
UniGene; Dm.3174; -.
ProteinModelPortal; P29742; -.
SMR; P29742; -.
BioGrid; 58885; 110.
DIP; DIP-17970N; -.
IntAct; P29742; 10.
MINT; MINT-1330735; -.
STRING; 7227.FBpp0073966; -.
PaxDb; P29742; -.
PRIDE; P29742; -.
EnsemblMetazoa; FBtr0074179; FBpp0073966; FBgn0000319.
EnsemblMetazoa; FBtr0074180; FBpp0073967; FBgn0000319.
EnsemblMetazoa; FBtr0074181; FBpp0089397; FBgn0000319.
EnsemblMetazoa; FBtr0074182; FBpp0089398; FBgn0000319.
EnsemblMetazoa; FBtr0112797; FBpp0111709; FBgn0000319.
EnsemblMetazoa; FBtr0112798; FBpp0111710; FBgn0000319.
EnsemblMetazoa; FBtr0339445; FBpp0308531; FBgn0000319.
GeneID; 32537; -.
KEGG; dme:Dmel_CG9012; -.
CTD; 32537; -.
FlyBase; FBgn0000319; Chc.
eggNOG; KOG0985; Eukaryota.
eggNOG; ENOG410XPH1; LUCA.
InParanoid; P29742; -.
KO; K04646; -.
OMA; VQQCTAF; -.
OrthoDB; EOG091G009O; -.
PhylomeDB; P29742; -.
Reactome; R-DME-8856825; Cargo recognition for clathrin-mediated endocytosis.
Reactome; R-DME-8856828; Clathrin-mediated endocytosis.
ChiTaRS; Chc; fly.
GenomeRNAi; 32537; -.
PRO; PR:P29742; -.
Proteomes; UP000000803; Chromosome X.
Bgee; FBgn0000319; -.
ExpressionAtlas; P29742; differential.
Genevisible; P29742; DM.
GO; GO:0005938; C:cell cortex; IDA:FlyBase.
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; ISS:FlyBase.
GO; GO:0005905; C:clathrin-coated pit; IDA:FlyBase.
GO; GO:0030136; C:clathrin-coated vesicle; IDA:FlyBase.
GO; GO:0031410; C:cytoplasmic vesicle; IDA:FlyBase.
GO; GO:0048471; C:perinuclear region of cytoplasm; IDA:FlyBase.
GO; GO:0005886; C:plasma membrane; IDA:FlyBase.
GO; GO:0098793; C:presynapse; IEA:GOC.
GO; GO:0030141; C:secretory granule; IDA:FlyBase.
GO; GO:0005802; C:trans-Golgi network; IDA:FlyBase.
GO; GO:0032051; F:clathrin light chain binding; ISS:FlyBase.
GO; GO:0005198; F:structural molecule activity; IEA:InterPro.
GO; GO:0007268; P:chemical synaptic transmission; IMP:FlyBase.
GO; GO:0048268; P:clathrin coat assembly; IEA:InterPro.
GO; GO:0048749; P:compound eye development; IMP:FlyBase.
GO; GO:0046667; P:compound eye retinal cell programmed cell death; IMP:FlyBase.
GO; GO:0033227; P:dsRNA transport; IMP:FlyBase.
GO; GO:0006897; P:endocytosis; IMP:FlyBase.
GO; GO:0030198; P:extracellular matrix organization; IMP:FlyBase.
GO; GO:0006886; P:intracellular protein transport; IEA:InterPro.
GO; GO:0035002; P:liquid clearance, open tracheal system; IMP:FlyBase.
GO; GO:0008103; P:oocyte microtubule cytoskeleton polarization; IMP:FlyBase.
GO; GO:0045451; P:pole plasm oskar mRNA localization; IMP:FlyBase.
GO; GO:0045807; P:positive regulation of endocytosis; IMP:FlyBase.
GO; GO:0045747; P:positive regulation of Notch signaling pathway; IMP:FlyBase.
GO; GO:2000366; P:positive regulation of STAT protein import into nucleus; IMP:FlyBase.
GO; GO:0007594; P:puparial adhesion; IMP:FlyBase.
GO; GO:0040008; P:regulation of growth; IMP:FlyBase.
GO; GO:0035159; P:regulation of tube length, open tracheal system; IMP:FlyBase.
GO; GO:0033363; P:secretory granule organization; IMP:FlyBase.
GO; GO:0007291; P:sperm individualization; IMP:FlyBase.
GO; GO:0016079; P:synaptic vesicle exocytosis; IMP:FlyBase.
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;
Coated pit; Complete proteome; Cytoplasmic vesicle; Membrane;
Reference proteome; Repeat.
CHAIN 1 1678 Clathrin heavy chain.
/FTId=PRO_0000205783.
REPEAT 538 684 CHCR 1.
REPEAT 687 829 CHCR 2.
REPEAT 834 973 CHCR 3.
REPEAT 980 1125 CHCR 4.
REPEAT 1129 1270 CHCR 5.
REPEAT 1275 1421 CHCR 6.
REPEAT 1424 1567 CHCR 7.
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 1334 1643 Involved in binding clathrin light chain.
{ECO:0000250}.
REGION 1552 1677 Trimerization. {ECO:0000250}.
SEQUENCE 1678 AA; 191177 MW; 73CAF8631BEE9BA3 CRC64;
MTQPLPIRFQ EHLQLTNVGI NANSFSFSTL TMESDKFICV REKVNDTAQV VIIDMNDATN
PTRRPISADS AIMNPASKVI ALKAQKTLQI FNIEMKSKMK AHTMNEDVVF WKWISLNTLA
LVTETSVFHW SMEGDSMPQK MFDRHSSLNG CQIINYRCNA SQQWLLLVGI SALPSRVAGA
MQLYSVERKV SQAIEGHAAS FATFKIDANK EPTTLFCFAV RTATGGKLHI IEVGAPPNGN
QPFAKKAVDV FFPPEAQNDF PVAMQVSAKY DTIYLITKYG YIHLYDMETA TCIYMNRISA
DTIFVTAPHE ASGGIIGVNR KGQVLSVTVD EEQIIPYINT VLQNPDLALR MAVRNNLAGA
EDLFVRKFNK LFTAGQYAEA AKVAALAPKA ILRTPQTIQR FQQVQTPAGS TTPPLLQYFG
ILLDQGKLNK FESLELCRPV LLQGKKQLCE KWLKEEKLEC SEELGDLVKA SDLTLALSIY
LRANVPNKVI QCFAETGQFQ KIVLYAKKVN YTPDYVFLLR SVMRSNPEQG AGFASMLVAE
EEPLADINQI VDIFMEHSMV QQCTAFLLDA LKHNRPAEGA LQTRLLEMNL MSAPQVADAI
LGNAMFTHYD RAHIAQLCEK AGLLQRALEH YTDLYDIKRA VVHTHMLNAE WLVSFFGTLS
VEDSLECLKA MLTANLRQNL QICVQIATKY HEQLTNKALI DLFEGFKSYD GLFYFLSSIV
NFSQDPEVHF KYIQAACKTN QIKEVERICR ESNCYNPERV KNFLKEAKLT DQLPLIIVCD
RFDFVHDLVL YLYRNNLQKY IEIYVQKVNP SRLPVVVGGL LDVDCSEDII KNLILVVKGQ
FSTDELVEEV EKRNRLKLLL PWLESRVHEG CVEPATHNAL AKIYIDSNNN PERYLKENQY
YDSRVVGRYC EKRDPHLACV AYERGLCDRE LIAVCNENSL FKSEARYLVG RRDAELWAEV
LSESNPYKRQ LIDQVVQTAL SETQDPDDIS VTVKAFMTAD LPNELIELLE KIILDSSVFS
DHRNLQNLLI LTAIKADRTR VMDYINRLEN YDAPDIANIA ISNQLYEEAF AIFKKFDVNT
SAIQVLIDQV NNLERANEFA ERCNEPAVWS QLAKAQLQQG LVKEAIDSYI KADDPSAYVD
VVDVASKVES WDDLVRYLQM ARKKARESYI ESELIYAYAR TGRLADLEEF ISGPNHADIQ
KIGNRCFSDG MYDAAKLLYN NVSNFARLAI TLVYLKEFQG AVDSARKANS TRTWKEVCFA
CVDAEEFRLA QMCGLHIVVH ADELEDLINY YQNRGYFDEL IALLESALGL ERAHMGMFTE
LAILYSKFKP SKMREHLELF WSRVNIPKVL RAAESAHLWS ELVFLYDKYE EYDNAVLAMM
AHPTEAWREG HFKDIITKVA NIELYYKAIE FYLDFKPLLL NDMLLVLAPR MDHTRAVSYF
SKTGYLPLVK PYLRSVQSLN NKAINEALNG LLIDEEDYQG LRNSIDGFDN FDNIALAQKL
EKHELTEFRR IAAYLYKGNN RWKQSVELCK KDKLYKDAME YAAESCKQDI AEELLGWFLE
RDAYDCFAAC LYQCYDLLRP DVILELAWKH KIVDFAMPYL IQVLREYTTK VDKLELNEAQ
REKEDDSTEH KNIIQMEPQL MITAGPAMGI PPQYAQNYPP GAATVTAAGG RNMGYPYL


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