ID A0A0D2VCP0_GOSRA Unreviewed; 1705 AA.
AC A0A0D2VCP0;
DT 29-APR-2015, integrated into UniProtKB/TrEMBL.
DT 29-APR-2015, sequence version 1.
DT 27-MAR-2024, entry version 29.
DE RecName: Full=Clathrin heavy chain {ECO:0000256|PIRNR:PIRNR002290};
GN ORFNames=B456_010G196100 {ECO:0000313|EMBL:KJB67535.1};
OS Gossypium raimondii (New World cotton).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Malvales; Malvaceae; Malvoideae; Gossypium.
OX NCBI_TaxID=29730 {ECO:0000313|EMBL:KJB67535.1, ECO:0000313|Proteomes:UP000032304};
RN [1] {ECO:0000313|EMBL:KJB67535.1, ECO:0000313|Proteomes:UP000032304}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=23257886; DOI=10.1038/nature11798;
RA Paterson A.H., Wendel J.F., Gundlach H., Guo H., Jenkins J., Jin D.,
RA Llewellyn D., Showmaker K.C., Shu S., Udall J., Yoo M.J., Byers R.,
RA Chen W., Doron-Faigenboim A., Duke M.V., Gong L., Grimwood J., Grover C.,
RA Grupp K., Hu G., Lee T.H., Li J., Lin L., Liu T., Marler B.S., Page J.T.,
RA Roberts A.W., Romanel E., Sanders W.S., Szadkowski E., Tan X., Tang H.,
RA Xu C., Wang J., Wang Z., Zhang D., Zhang L., Ashrafi H., Bedon F.,
RA Bowers J.E., Brubaker C.L., Chee P.W., Das S., Gingle A.R., Haigler C.H.,
RA Harker D., Hoffmann L.V., Hovav R., Jones D.C., Lemke C., Mansoor S.,
RA ur Rahman M., Rainville L.N., Rambani A., Reddy U.K., Rong J.K.,
RA Saranga Y., Scheffler B.E., Scheffler J.A., Stelly D.M., Triplett B.A.,
RA Van Deynze A., Vaslin M.F., Waghmare V.N., Walford S.A., Wright R.J.,
RA Zaki E.A., Zhang T., Dennis E.S., Mayer K.F., Peterson D.G., Rokhsar D.S.,
RA Wang X., Schmutz J.;
RT "Repeated polyploidization of Gossypium genomes and the evolution of
RT spinnable cotton fibres.";
RL Nature 492:423-427(2012).
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; CM001749; KJB67535.1; -; Genomic_DNA.
DR EnsemblPlants; KJB67535; KJB67535; B456_010G196100.
DR Gramene; KJB67535; KJB67535; B456_010G196100.
DR Proteomes; UP000032304; Chromosome 10.
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:InterPro.
DR GO; GO:0032051; F:clathrin light chain binding; IEA:InterPro.
DR GO; GO:0005198; F:structural molecule activity; IEA:InterPro.
DR GO; GO:0006886; P:intracellular protein transport; IEA:UniProtKB-UniRule.
DR GO; GO:0016192; P:vesicle-mediated transport; IEA:InterPro.
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; 3.
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:SF34; CLATHRIN HEAVY CHAIN 1-RELATED; 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; 1.
DR PIRSF; PIRSF002290; Clathrin_H_chain; 1.
DR SMART; SM00299; CLH; 7.
DR SUPFAM; SSF48371; ARM repeat; 5.
DR SUPFAM; SSF50989; Clathrin heavy-chain terminal domain; 1.
DR PROSITE; PS50236; CHCR; 7.
PE 3: Inferred from homology;
KW Coated pit {ECO:0000256|ARBA:ARBA00023176, ECO:0000256|PIRNR:PIRNR002290};
KW Coiled coil {ECO:0000256|SAM:Coils};
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:UP000032304};
KW Repeat {ECO:0000256|ARBA:ARBA00022737}.
FT DOMAIN 344..367
FT /note="Clathrin heavy chain linker core motif"
FT /evidence="ECO:0000259|Pfam:PF09268"
FT COILED 1615..1650
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 1705 AA; 193316 MW; 525E53EBA3735639 CRC64;
MAAANAPIAM KEVLTLPSVG INPQFITFTN VTMESDKYIC VRETAPQNSV VIIDMSMPMQ
PLRRPITADS ALMNPNSRIL ALKAQLPGTT QDHLQIFNIE MKAKIKSHQM PEPVVFWKWI
TPKTLGLVTQ TSVYHWSIEG DSEPVKMFER TANLVNNQII NYKCDPSEKW LVLIGIAPGA
PERPQLVKGN MQLFSVDQQR SQALESHAAS FAQFKVPGNE NPSILISFAT KSFNAGQIVS
KLHVIELGAQ PGKPSFSKKQ ADLFFPPDFQ DDFPVAMQIS HKYSLIYVIT KLGLLFVYDL
ETATAVYRNR ISPDPIFLTS EASSAGGFYA INRRGQVLLA TVNEATIVPF VSSQLNNLEL
AVNLAKRGNL PGAENLVVQR FQELFAQTKY KEAAELAAES PQGILRTPDT VAKFQSVPVQ
AGQTPPLLQY FGTLLTKGKL NAFESLELSR LVVNQNKKNL LENWLAEDKL ECSEELGDLV
KTVDNDLALK IYIKARATPK VVAAFAERRE FDKILIYSKQ VGYSPDYLFL LQTILRTDPQ
GAVNFALMMS QMEGGCPVDY NTITDLFLQR NLIREATAFL LDVLKPNLPE HAFLQTKVLE
INLVTFPNVA DAILANGMFS HYDRPRIAQL CEKAGLYVRA LQHYSELPDI KRVIVNTHAI
EPQSLVEFFG TLSREWALEC MKDLLLVNLR GNLQIIVQVA KEYCEQLGVE ACIKLFEQFK
SYEGLYFFLG SYLSSSEDPD IHFKYIEAAA KTGQIKEVER VTRESNFYDA EKTKNFLMEA
KLPDARPLIN VCDRFGFVPD LTHYLYTNNM LRYIEGYVQK VNPGNAPLVV GQLLDDECPE
DFIKGLILSV RSLLPVEPLV DECEKRNRLR LLTQFLEHLV SEGSQDVHVH NALGKIIIES
NNNPEHFLTT NPYYDSRVVG KYCEKRDPTL AVVAYRRGQC DDELINVTNK NSLFKLQARY
VVERMDGDLW EKVLNPENEY RRHLIDQVVS TALPESKSPE QVSAAVKAFM TADLPHELIE
LLEKIVLQNS AFSGNFNLQN LLILTAIKAD PSRVMDYINR LDNFDGPAVG EVAVEAQLYE
EAFSIFKKFN LNVQAVNVLL DNIRNIDRAV EFAFRVEEDA VWSQVAKAQL REGLVSDAIE
SFIRADDATH FLDVIRASED ANVYPDLVRY LLMVRQKVKE PKVDSELIYA YAKIDRLGEI
EEFILMPNVA NLQNVGDRLF DEELYEAAKI IFAFISNWAK LAVTLVRLKQ FQGAVDAARK
ANSAKTWKEV CFACVDAEEF RLAQICGLNV IVQVDDLEEV SEYYQNRGCF NELISLMESG
LGLERAHMGI FTELGVLYAR YRPEKLMEHI KLFSTRLNIP KLIRACDEQQ HWKELTYLYI
QYDEFDNAAT TVMNHSPEAW DHMQFKDIIV KVASVELYYK AVHFYLQEHP DLINDMLNVL
ALRVDHTRVV DIMRKAGHLR LVKPYMVAVQ SNNVLAVNEA LNEIYVEEED YDRLRESIDL
HDNFDQIGLA QKIEKHELLE MRRVAAYIYK KAGRWKQSIA LSKKDNHYRD AMETASQSGE
RELAEELLVY FIEQKECFAS CLFVCYDLIR ADVALELAWI NNMIDFAFPY LLQFIREYTG
KVDELIKDKI EAQKEVKAKE QEEKEVIAQQ NMYAQLLPLA LPAPPMPGMG GPTMGGGFAP
PPPPMGGMGM PPMPPYGMPP MGSSY
//
