CLH_DROME
ID CLH_DROME Reviewed; 1678 AA.
AC P29742; Q540W2; Q9VXN6;
DT 01-APR-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-APR-1993, sequence version 1.
DT 03-AUG-2022, entry version 181.
DE RecName: Full=Clathrin heavy chain;
GN Name=Chc; ORFNames=CG9012;
OS Drosophila melanogaster (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7227;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=Canton-S; TISSUE=Head;
RX PubMed=8375651; DOI=10.1093/genetics/134.4.1119;
RA Bazinet C., Katzen A.L., Morgan M., Mahowald A.P., Lemmon S.K.;
RT "The Drosophila clathrin heavy chain gene: clathrin function is essential
RT in a multicellular organism.";
RL Genetics 134:1119-1134(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley;
RX PubMed=10731132; DOI=10.1126/science.287.5461.2185;
RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., Brandon R.C.,
RA Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C.,
RA Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A.,
RA An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A.,
RA Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V.,
RA Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J.,
RA Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E.,
RA Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B.,
RA Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I.,
RA Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C.,
RA Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S.,
RA Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M.,
RA Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D.,
RA Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F.,
RA Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D.,
RA Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A.,
RA Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C.,
RA McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C.,
RA Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L.,
RA Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R.,
RA Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V.,
RA Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F.,
RA Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J.,
RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R.,
RA Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y.,
RA Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T.,
RA Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S.,
RA Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W.,
RA Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M.,
RA Venter J.C.;
RT "The genome sequence of Drosophila melanogaster.";
RL Science 287:2185-2195(2000).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=Berkeley;
RX PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M.,
RA Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.;
RT "Annotation of the Drosophila melanogaster euchromatic genome: a systematic
RT review.";
RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Berkeley; TISSUE=Embryo;
RX PubMed=12537569; DOI=10.1186/gb-2002-3-12-research0080;
RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., George R.A.,
RA Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., Rubin G.M.,
RA Celniker S.E.;
RT "A Drosophila full-length cDNA resource.";
RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002).
RN [5]
RP INTERACTION WITH SAU.
RX PubMed=24786584; DOI=10.1371/journal.pgen.1004305;
RA Sechi S., Colotti G., Belloni G., Mattei V., Frappaolo A., Raffa G.D.,
RA Fuller M.T., Giansanti M.G.;
RT "GOLPH3 is essential for contractile ring formation and Rab11 localization
RT to the cleavage site during cytokinesis in Drosophila melanogaster.";
RL PLoS Genet. 10:E1004305-E1004305(2014).
CC -!- FUNCTION: Clathrin is the major protein of the polyhedral coat of
CC coated pits and vesicles.
CC -!- SUBUNIT: Clathrin triskelions, composed of 3 heavy chains and 3 light
CC chains, are the basic subunits of the clathrin coat (By similarity).
CC Interacts with sau (PubMed:24786584). {ECO:0000250|UniProtKB:Q00610,
CC ECO:0000269|PubMed:24786584}.
CC -!- INTERACTION:
CC P29742; P16568: BicD; NbExp=5; IntAct=EBI-160368, EBI-112159;
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 -!- DOMAIN: The C-terminal third of the heavy chains forms the hub of the
CC triskelion. This region contains the trimerization domain and the
CC light-chain binding domain involved in the assembly of the clathrin
CC lattice.
CC -!- DOMAIN: The N-terminal seven-bladed beta-propeller is formed by WD40-
CC like repeats, and projects inward from the polyhedral outer clathrin
CC coat. It constitutes a major protein-protein interaction node (By
CC similarity). {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the clathrin heavy chain family. {ECO:0000305}.
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DR EMBL; Z14133; CAA78507.1; -; mRNA.
DR EMBL; AE014298; AAF48522.1; -; Genomic_DNA.
DR EMBL; AE014298; AAN09367.1; -; Genomic_DNA.
DR EMBL; AE014298; AAS65352.1; -; Genomic_DNA.
DR EMBL; AE014298; AAS65353.1; -; Genomic_DNA.
DR EMBL; AE014298; ABW09424.1; -; Genomic_DNA.
DR EMBL; AE014298; ABW09425.1; -; Genomic_DNA.
DR EMBL; AY119615; AAM50269.1; -; mRNA.
DR PIR; S52588; S52588.
DR RefSeq; NP_001096993.1; NM_001103523.2.
DR RefSeq; NP_001096994.1; NM_001103524.2.
DR RefSeq; NP_001285300.1; NM_001298371.1.
DR RefSeq; NP_477042.1; NM_057694.3.
DR RefSeq; NP_727901.1; NM_167466.2.
DR RefSeq; NP_996451.1; NM_206728.2.
DR RefSeq; NP_996452.1; NM_206729.2.
DR AlphaFoldDB; P29742; -.
DR SMR; P29742; -.
DR BioGRID; 58885; 112.
DR DIP; DIP-17970N; -.
DR IntAct; P29742; 10.
DR MINT; P29742; -.
DR STRING; 7227.FBpp0073966; -.
DR PaxDb; P29742; -.
DR PRIDE; P29742; -.
DR EnsemblMetazoa; FBtr0074179; FBpp0073966; FBgn0000319.
DR EnsemblMetazoa; FBtr0074180; FBpp0073967; FBgn0000319.
DR EnsemblMetazoa; FBtr0074181; FBpp0089397; FBgn0000319.
DR EnsemblMetazoa; FBtr0074182; FBpp0089398; FBgn0000319.
DR EnsemblMetazoa; FBtr0112797; FBpp0111709; FBgn0000319.
DR EnsemblMetazoa; FBtr0112798; FBpp0111710; FBgn0000319.
DR EnsemblMetazoa; FBtr0339445; FBpp0308531; FBgn0000319.
DR GeneID; 32537; -.
DR KEGG; dme:Dmel_CG9012; -.
DR CTD; 32537; -.
DR FlyBase; FBgn0000319; Chc.
DR VEuPathDB; VectorBase:FBgn0000319; -.
DR eggNOG; KOG0985; Eukaryota.
DR HOGENOM; CLU_002136_0_0_1; -.
DR InParanoid; P29742; -.
DR OMA; QVNEACV; -.
DR OrthoDB; 17940at2759; -.
DR PhylomeDB; P29742; -.
DR Reactome; R-DME-177504; Retrograde neurotrophin signalling.
DR Reactome; R-DME-190873; Gap junction degradation.
DR Reactome; R-DME-196025; Formation of annular gap junctions.
DR Reactome; R-DME-432720; Lysosome Vesicle Biogenesis.
DR Reactome; R-DME-432722; Golgi Associated Vesicle Biogenesis.
DR Reactome; R-DME-437239; Recycling pathway of L1.
DR Reactome; R-DME-5099900; WNT5A-dependent internalization of FZD4.
DR Reactome; R-DME-5140745; WNT5A-dependent internalization of FZD2, FZD5 and ROR2.
DR Reactome; R-DME-8856825; Cargo recognition for clathrin-mediated endocytosis.
DR Reactome; R-DME-8856828; Clathrin-mediated endocytosis.
DR Reactome; R-DME-8866427; VLDLR internalisation and degradation.
DR Reactome; R-DME-8964038; LDL clearance.
DR Reactome; R-DME-9013420; RHOU GTPase cycle.
DR Reactome; R-DME-9013424; RHOV GTPase cycle.
DR SignaLink; P29742; -.
DR BioGRID-ORCS; 32537; 1 hit in 3 CRISPR screens.
DR ChiTaRS; Chc; fly.
DR GenomeRNAi; 32537; -.
DR PRO; PR:P29742; -.
DR Proteomes; UP000000803; Chromosome X.
DR Bgee; FBgn0000319; Expressed in embryonic/larval hemocyte (Drosophila) and 36 other tissues.
DR ExpressionAtlas; P29742; baseline and differential.
DR Genevisible; P29742; DM.
DR GO; GO:0005938; C:cell cortex; IDA:FlyBase.
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; ISS:FlyBase.
DR GO; GO:0045334; C:clathrin-coated endocytic vesicle; IBA:GO_Central.
DR GO; GO:0005905; C:clathrin-coated pit; IDA:FlyBase.
DR GO; GO:0030136; C:clathrin-coated vesicle; IDA:FlyBase.
DR GO; GO:0031410; C:cytoplasmic vesicle; IDA:FlyBase.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IDA:FlyBase.
DR GO; GO:0005886; C:plasma membrane; IDA:FlyBase.
DR GO; GO:0098793; C:presynapse; IEA:GOC.
DR GO; GO:0030141; C:secretory granule; IDA:FlyBase.
DR GO; GO:0005802; C:trans-Golgi network; IDA:FlyBase.
DR GO; GO:0032051; F:clathrin light chain binding; ISS:FlyBase.
DR GO; GO:0005198; F:structural molecule activity; IEA:InterPro.
DR GO; GO:0007268; P:chemical synaptic transmission; IMP:FlyBase.
DR GO; GO:0048749; P:compound eye development; IMP:FlyBase.
DR GO; GO:0046667; P:compound eye retinal cell programmed cell death; IMP:FlyBase.
DR GO; GO:0033227; P:dsRNA transport; IMP:FlyBase.
DR GO; GO:0006897; P:endocytosis; IMP:FlyBase.
DR GO; GO:0030198; P:extracellular matrix organization; IMP:FlyBase.
DR GO; GO:0006886; P:intracellular protein transport; IEA:InterPro.
DR GO; GO:0035002; P:liquid clearance, open tracheal system; IMP:FlyBase.
DR GO; GO:0008103; P:oocyte microtubule cytoskeleton polarization; IMP:FlyBase.
DR GO; GO:0045451; P:pole plasm oskar mRNA localization; IMP:FlyBase.
DR GO; GO:0010508; P:positive regulation of autophagy; IMP:FlyBase.
DR GO; GO:0045807; P:positive regulation of endocytosis; IMP:FlyBase.
DR GO; GO:0031623; P:receptor internalization; IGI:FlyBase.
DR GO; GO:0006898; P:receptor-mediated endocytosis; IBA:GO_Central.
DR GO; GO:0040008; P:regulation of growth; IMP:FlyBase.
DR GO; GO:0035159; P:regulation of tube length, open tracheal system; IMP:FlyBase.
DR GO; GO:0033363; P:secretory granule organization; IMP:FlyBase.
DR GO; GO:0007291; P:sperm individualization; IMP:FlyBase.
DR GO; GO:0016079; P:synaptic vesicle exocytosis; IMP:FlyBase.
DR Gene3D; 1.25.40.10; -; 4.
DR Gene3D; 2.130.10.110; -; 1.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR000547; Clathrin_H-chain/VPS_repeat.
DR InterPro; IPR015348; Clathrin_H-chain_linker_core.
DR InterPro; IPR016025; Clathrin_H-chain_N.
DR InterPro; IPR022365; Clathrin_H-chain_propeller_rpt.
DR InterPro; IPR016341; Clathrin_heavy_chain.
DR InterPro; IPR011990; TPR-like_helical_dom_sf.
DR Pfam; PF00637; Clathrin; 7.
DR Pfam; PF09268; Clathrin-link; 1.
DR Pfam; PF01394; Clathrin_propel; 5.
DR PIRSF; PIRSF002290; Clathrin_H_chain; 1.
DR SMART; SM00299; CLH; 7.
DR SUPFAM; SSF48371; SSF48371; 6.
DR SUPFAM; SSF50989; SSF50989; 1.
DR PROSITE; PS50236; CHCR; 7.
PE 1: Evidence at protein level;
KW Coated pit; Cytoplasmic vesicle; Membrane; Reference proteome; Repeat.
FT CHAIN 1..1678
FT /note="Clathrin heavy chain"
FT /id="PRO_0000205783"
FT REPEAT 538..684
FT /note="CHCR 1"
FT REPEAT 687..829
FT /note="CHCR 2"
FT REPEAT 834..973
FT /note="CHCR 3"
FT REPEAT 980..1125
FT /note="CHCR 4"
FT REPEAT 1129..1270
FT /note="CHCR 5"
FT REPEAT 1275..1421
FT /note="CHCR 6"
FT REPEAT 1424..1567
FT /note="CHCR 7"
FT REGION 24..67
FT /note="WD40-like repeat 1"
FT REGION 68..107
FT /note="WD40-like repeat 2"
FT REGION 108..149
FT /note="WD40-like repeat 3"
FT REGION 150..195
FT /note="WD40-like repeat 4"
FT REGION 196..257
FT /note="WD40-like repeat 5"
FT REGION 258..301
FT /note="WD40-like repeat 6"
FT REGION 302..330
FT /note="WD40-like repeat 7"
FT REGION 1334..1643
FT /note="Involved in binding clathrin light chain"
FT /evidence="ECO:0000250"
FT REGION 1552..1677
FT /note="Trimerization"
FT /evidence="ECO:0000250"
SQ 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
