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Database: UniProt
Entry: D2A6C5_TRICA
LinkDB: D2A6C5_TRICA
Original site: D2A6C5_TRICA 
ID   D2A6C5_TRICA            Unreviewed;      1684 AA.
AC   D2A6C5;
DT   09-FEB-2010, integrated into UniProtKB/TrEMBL.
DT   09-FEB-2010, sequence version 1.
DT   24-JAN-2024, entry version 76.
DE   RecName: Full=Clathrin heavy chain {ECO:0000256|PIRNR:PIRNR002290};
GN   Name=AUGUSTUS-3.0.2_15014 {ECO:0000313|EMBL:EFA04947.1};
GN   Synonyms=Chc {ECO:0000313|EMBL:AHY84716.1};
GN   ORFNames=TcasGA2_TC015014 {ECO:0000313|EMBL:EFA04947.1};
OS   Tribolium castaneum (Red flour beetle).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Coleoptera; Polyphaga; Cucujiformia;
OC   Tenebrionidae; Tenebrionidae incertae sedis; Tribolium.
OX   NCBI_TaxID=7070 {ECO:0000313|EMBL:EFA04947.1, ECO:0000313|Proteomes:UP000007266};
RN   [1] {ECO:0000313|EMBL:EFA04947.1, ECO:0000313|Proteomes:UP000007266}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Georgia GA2 {ECO:0000313|EMBL:EFA04947.1,
RC   ECO:0000313|Proteomes:UP000007266};
RX   PubMed=18362917; DOI=10.1038/nature06784;
RG   Tribolium Genome Sequencing Consortium;
RA   Richards S., Gibbs R.A., Weinstock G.M., Brown S.J., Denell R.,
RA   Beeman R.W., Gibbs R., Beeman R.W., Brown S.J., Bucher G., Friedrich M.,
RA   Grimmelikhuijzen C.J., Klingler M., Lorenzen M., Richards S., Roth S.,
RA   Schroder R., Tautz D., Zdobnov E.M., Muzny D., Gibbs R.A., Weinstock G.M.,
RA   Attaway T., Bell S., Buhay C.J., Chandrabose M.N., Chavez D.,
RA   Clerk-Blankenburg K.P., Cree A., Dao M., Davis C., Chacko J., Dinh H.,
RA   Dugan-Rocha S., Fowler G., Garner T.T., Garnes J., Gnirke A., Hawes A.,
RA   Hernandez J., Hines S., Holder M., Hume J., Jhangiani S.N., Joshi V.,
RA   Khan Z.M., Jackson L., Kovar C., Kowis A., Lee S., Lewis L.R., Margolis J.,
RA   Morgan M., Nazareth L.V., Nguyen N., Okwuonu G., Parker D., Richards S.,
RA   Ruiz S.J., Santibanez J., Savard J., Scherer S.E., Schneider B.,
RA   Sodergren E., Tautz D., Vattahil S., Villasana D., White C.S., Wright R.,
RA   Park Y., Beeman R.W., Lord J., Oppert B., Lorenzen M., Brown S., Wang L.,
RA   Savard J., Tautz D., Richards S., Weinstock G., Gibbs R.A., Liu Y.,
RA   Worley K., Weinstock G., Elsik C.G., Reese J.T., Elhaik E., Landan G.,
RA   Graur D., Arensburger P., Atkinson P., Beeman R.W., Beidler J., Brown S.J.,
RA   Demuth J.P., Drury D.W., Du Y.Z., Fujiwara H., Lorenzen M., Maselli V.,
RA   Osanai M., Park Y., Robertson H.M., Tu Z., Wang J.J., Wang S., Richards S.,
RA   Song H., Zhang L., Sodergren E., Werner D., Stanke M., Morgenstern B.,
RA   Solovyev V., Kosarev P., Brown G., Chen H.C., Ermolaeva O., Hlavina W.,
RA   Kapustin Y., Kiryutin B., Kitts P., Maglott D., Pruitt K., Sapojnikov V.,
RA   Souvorov A., Mackey A.J., Waterhouse R.M., Wyder S., Zdobnov E.M.,
RA   Zdobnov E.M., Wyder S., Kriventseva E.V., Kadowaki T., Bork P., Aranda M.,
RA   Bao R., Beermann A., Berns N., Bolognesi R., Bonneton F., Bopp D.,
RA   Brown S.J., Bucher G., Butts T., Chaumot A., Denell R.E., Ferrier D.E.,
RA   Friedrich M., Gordon C.M., Jindra M., Klingler M., Lan Q., Lattorff H.M.,
RA   Laudet V., von Levetsow C., Liu Z., Lutz R., Lynch J.A., da Fonseca R.N.,
RA   Posnien N., Reuter R., Roth S., Savard J., Schinko J.B., Schmitt C.,
RA   Schoppmeier M., Schroder R., Shippy T.D., Simonnet F., Marques-Souza H.,
RA   Tautz D., Tomoyasu Y., Trauner J., Van der Zee M., Vervoort M.,
RA   Wittkopp N., Wimmer E.A., Yang X., Jones A.K., Sattelle D.B., Ebert P.R.,
RA   Nelson D., Scott J.G., Beeman R.W., Muthukrishnan S., Kramer K.J.,
RA   Arakane Y., Beeman R.W., Zhu Q., Hogenkamp D., Dixit R., Oppert B.,
RA   Jiang H., Zou Z., Marshall J., Elpidina E., Vinokurov K., Oppert C.,
RA   Zou Z., Evans J., Lu Z., Zhao P., Sumathipala N., Altincicek B.,
RA   Vilcinskas A., Williams M., Hultmark D., Hetru C., Jiang H.,
RA   Grimmelikhuijzen C.J., Hauser F., Cazzamali G., Williamson M., Park Y.,
RA   Li B., Tanaka Y., Predel R., Neupert S., Schachtner J., Verleyen P.,
RA   Raible F., Bork P., Friedrich M., Walden K.K., Robertson H.M., Angeli S.,
RA   Foret S., Bucher G., Schuetz S., Maleszka R., Wimmer E.A., Beeman R.W.,
RA   Lorenzen M., Tomoyasu Y., Miller S.C., Grossmann D., Bucher G.;
RT   "The genome of the model beetle and pest Tribolium castaneum.";
RL   Nature 452:949-955(2008).
RN   [2] {ECO:0000313|EMBL:EFA04947.1, ECO:0000313|Proteomes:UP000007266}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Georgia GA2 {ECO:0000313|EMBL:EFA04947.1,
RC   ECO:0000313|Proteomes:UP000007266};
RX   PubMed=19820115; DOI=10.1093/nar/gkp807;
RA   Kim H.S., Murphy T., Xia J., Caragea D., Park Y., Beeman R.W.,
RA   Lorenzen M.D., Butcher S., Manak J.R., Brown S.J.;
RT   "BeetleBase in 2010: revisions to provide comprehensive genomic information
RT   for Tribolium castaneum.";
RL   Nucleic Acids Res. 38:D437-D442(2010).
RN   [3] {ECO:0000313|EMBL:EFA04947.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=Georgia GA2 {ECO:0000313|EMBL:EFA04947.1};
RA   Shelton J.M., Herndon N., Coleman C., Lu N., Brown S.J.;
RT   "Tools and pipelines for BioNano data: molecule assembly pipeline and FASTA
RT   super scaffolding tool.";
RL   Submitted (NOV-2014) to the EMBL/GenBank/DDBJ databases.
RN   [4] {ECO:0000313|EMBL:AHY84716.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=Georgia-1 {ECO:0000313|EMBL:AHY84716.1};
RX   PubMed=25863352; DOI=10.1016/j.ibmb.2015.03.009;
RA   Xiao D., Gao X., Xu J., Liang X., Li Q., Yao J., Zhu K.Y.;
RT   "Clathrin-dependent endocytosis plays a predominant role in cellular uptake
RT   of double-stranded RNA in the red flour beetle.";
RL   Insect Biochem. Mol. Biol. 60:68-77(2015).
CC   -!- FUNCTION: Clathrin is the major protein of the polyhedral coat of
CC       coated pits and vesicles. {ECO:0000256|PIRNR:PIRNR002290}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasmic vesicle membrane
CC       {ECO:0000256|PIRNR:PIRNR002290}; Peripheral membrane protein
CC       {ECO:0000256|PIRNR:PIRNR002290}; Cytoplasmic side
CC       {ECO:0000256|PIRNR:PIRNR002290}. Membrane, coated pit
CC       {ECO:0000256|PIRNR:PIRNR002290}; Peripheral membrane protein
CC       {ECO:0000256|PIRNR:PIRNR002290}; Cytoplasmic side
CC       {ECO:0000256|PIRNR:PIRNR002290}. Membrane
CC       {ECO:0000256|ARBA:ARBA00004287}; Peripheral membrane protein
CC       {ECO:0000256|ARBA:ARBA00004287}; Cytoplasmic side
CC       {ECO:0000256|ARBA:ARBA00004287}.
CC   -!- SIMILARITY: Belongs to the clathrin heavy chain family.
CC       {ECO:0000256|ARBA:ARBA00009535, ECO:0000256|PIRNR:PIRNR002290}.
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DR   EMBL; KJ476828; AHY84716.1; -; mRNA.
DR   EMBL; KQ971347; EFA04947.1; -; Genomic_DNA.
DR   RefSeq; NP_001280512.1; NM_001293583.1.
DR   STRING; 7070.D2A6C5; -.
DR   EnsemblMetazoa; TC015014_001; TC015014_001; TC015014.
DR   GeneID; 656193; -.
DR   KEGG; tca:656193; -.
DR   eggNOG; KOG0985; Eukaryota.
DR   HOGENOM; CLU_002136_0_0_1; -.
DR   InParanoid; D2A6C5; -.
DR   OMA; VMEISWR; -.
DR   OrthoDB; 5474327at2759; -.
DR   Proteomes; UP000007266; Linkage group 6.
DR   GO; GO:0005938; C:cell cortex; IBA:GO_Central.
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; IBA:GO_Central.
DR   GO; GO:0045334; C:clathrin-coated endocytic vesicle; IBA:GO_Central.
DR   GO; GO:0032051; F:clathrin light chain binding; IBA:GO_Central.
DR   GO; GO:0005198; F:structural molecule activity; IEA:InterPro.
DR   GO; GO:0006886; P:intracellular protein transport; IEA:UniProtKB-UniRule.
DR   GO; GO:0006898; P:receptor-mediated endocytosis; IBA:GO_Central.
DR   Gene3D; 1.25.40.730; -; 1.
DR   Gene3D; 2.130.10.110; Clathrin heavy-chain terminal domain; 1.
DR   Gene3D; 1.25.40.10; Tetratricopeptide repeat domain; 4.
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   PANTHER; PTHR10292:SF1; CLATHRIN HEAVY CHAIN; 1.
DR   PANTHER; PTHR10292; CLATHRIN HEAVY CHAIN RELATED; 1.
DR   Pfam; PF00637; Clathrin; 7.
DR   Pfam; PF09268; Clathrin-link; 1.
DR   Pfam; PF13838; Clathrin_H_link; 1.
DR   Pfam; PF01394; Clathrin_propel; 5.
DR   PIRSF; PIRSF002290; Clathrin_H_chain; 1.
DR   SMART; SM00299; CLH; 7.
DR   SUPFAM; SSF48371; ARM repeat; 6.
DR   SUPFAM; SSF50989; Clathrin heavy-chain terminal domain; 1.
DR   PROSITE; PS50236; CHCR; 7.
PE   2: Evidence at transcript level;
KW   Coated pit {ECO:0000256|ARBA:ARBA00023176, ECO:0000256|PIRNR:PIRNR002290};
KW   Cytoplasmic vesicle {ECO:0000256|ARBA:ARBA00023329,
KW   ECO:0000256|PIRNR:PIRNR002290};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|PIRNR:PIRNR002290};
KW   Reference proteome {ECO:0000313|Proteomes:UP000007266};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737}.
FT   DOMAIN          338..361
FT                   /note="Clathrin heavy chain linker core motif"
FT                   /evidence="ECO:0000259|Pfam:PF09268"
FT   REPEAT          544..690
FT                   /note="CHCR"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01006"
FT   REPEAT          693..835
FT                   /note="CHCR"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01006"
FT   REPEAT          840..979
FT                   /note="CHCR"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01006"
FT   REPEAT          986..1131
FT                   /note="CHCR"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01006"
FT   REPEAT          1135..1276
FT                   /note="CHCR"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01006"
FT   REPEAT          1281..1427
FT                   /note="CHCR"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01006"
FT   REPEAT          1430..1573
FT                   /note="CHCR"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01006"
SQ   SEQUENCE   1684 AA;  192312 MW;  71F2F7ADECCCD72A CRC64;
     MTQQLLPIKF QEHLQLTNVG INVANISFAT LTMESDKFIC VREKVGDTSQ VVIIDMGDTA
     NPIRRPITAE SAIMNPASKV IALKGKAGVE AQKTLQIFNI EMKSKMKAHT MSEDVIFWKW
     ISLNTLALVT ETSVYHWSME GDSTPVKMFD RHSSLNGCQI INYRTDPKQN WLLLVGISAQ
     QSRVVGAMQL YSVERKCSQP IEGHAASFAT FKMEGNPEPS TLFCFAVRTV QGGKLHIIEV
     GQSPAGNQPF PKKTVDVFFP PEAQNDFPVA MQVSAKYDVI YLITKYGYIH MYDIESAICI
     YMNRISSETI FVTAPHESTG GIIGVNRRGQ VLSVSVDEDS IIRYVNQVLH NPDLALRIAT
     RNNLAGAEEL FVNKFQMLFT NGQYAEAAKV AANAPKGILR TPATIQMFQQ VPTQPGQNSP
     LLQYFGILLD QGQLNRYESL ELCKPVLLQG RKQLLEKWLK EDKLECSEEL GDLVKQADST
     LALSVYLRAN VPAKVIQSFA ETGQFQKIVL YAKKVNYTPD YIYLLRSVMR TNPDQGAAFA
     SMLVADEEPL ADINQIVDIF MEQNMVQQCT AFLLDALKHN RPTEGHLQTR LLEMNLMSAP
     QVADAILGNN MFTHYDRAHI AQLCEKAGLL QRALEHYTDL YDIKRAVVHT HLLPMDWLVN
     FFGTLSVEDS LECLKAMLTA NIRQNLQICV QIATKYHEQL TTKALIDLFE SFKSYEGLFY
     FLGSIVNFSQ DPDVHFKYIQ AACKTGQIKE VERICRESNC YNPESVKNFL KEAKLTDQLP
     LIIVCDRFDF VHDLVLYLYR NSLQKYIEIY VQKVNPSRLP VVVGGLLDVD CAEDIIKNLI
     LVVRGQFSTD ELVEEVEKRN RLKLLLPWLE SRVHEGCVEP ATHNALAKIY IDSNNNAERF
     LKENQWYDSR VVGRYCEKRD PHLACVAYER GQCDRELIAV CNENSLFKSE ARYLVRRRDP
     ELWAEVLQES NPYRRQLIDQ VVQTALSETQ DPEDISVTVK AFMTADLPNE LIELLEKIVL
     DSSVFSDHRN LQNLLILTAI KADATRVMDY INRLDNYDAP DIANIAINNH LYEEAFAIFK
     KFDVNTSAIQ VLIEQVNNLD RAYEFAERCN EPAVWSQLAK AQLNQGLVKE AIDSYIKADD
     PSAYMAVVET ASKNNSWEDL VRYLQMARKK SRESYIESEL IYSYAKTGRL ADLEEFISGP
     NHADIQKIGD RCFDDKMYDA AKLLYNNVSN FARLAITLVH LKEFQGAVDS ARKANSTRTW
     KEVCFACVDA EEFRLAQMCG MHIVVHADEL QDLINYYQDR GYFEELIGLL EAALGLERAH
     MGMFTELAIL YSKYKPAKMR EHLELFWSRV NIPKVLRAAE QAHLWAELVF LYDKYEEYDN
     AVLAMMAHPT EAWREGHFKD IITKVANIEL YYKAIQFYLD YKPLLLNDLL LVLAPRMDHT
     RAVAFFTKTG HLQLVKSYLR SVQNLNNKAI NEALNSLLIE EEDFQGLRTS IDAFDNFDNI
     GLAQKLEKHE LTEFRRIAAY LYKGNNRWKQ SVELCKKDRL FRDAMEYTAE SKNQELAEEL
     LAWFLERKAY DCFAACLYQC YDLLRPDVIL ELAWRHKIMD LAMPYLIQVT RELTTKVEKL
     EQSDAQRQSE AAEETHKPMM INEPQLMLTA GPGMGIPPQA YVPPQAYAQP GYAPQMPYGA
     YPGM
//
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