ID D7SJV3_VITVI Unreviewed; 1705 AA.
AC D7SJV3;
DT 10-AUG-2010, integrated into UniProtKB/TrEMBL.
DT 10-AUG-2010, sequence version 1.
DT 27-MAR-2024, entry version 78.
DE RecName: Full=Clathrin heavy chain {ECO:0000256|PIRNR:PIRNR002290};
GN OrderedLocusNames=VIT_06s0004g06860 {ECO:0000313|EMBL:CBI15929.3};
OS Vitis vinifera (Grape).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; Vitales; Vitaceae; Viteae; Vitis.
OX NCBI_TaxID=29760 {ECO:0000313|EMBL:CBI15929.3, ECO:0000313|Proteomes:UP000009183};
RN [1] {ECO:0000313|Proteomes:UP000009183}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Pinot noir / PN40024 {ECO:0000313|Proteomes:UP000009183};
RX PubMed=17721507; DOI=10.1038/nature06148;
RG The French-Italian Public Consortium for Grapevine Genome Characterization.;
RA Jaillon O., Aury J.-M., Noel B., Policriti A., Clepet C., Casagrande A.,
RA Choisne N., Aubourg S., Vitulo N., Jubin C., Vezzi A., Legeai F.,
RA Hugueney P., Dasilva C., Horner D., Mica E., Jublot D., Poulain J.,
RA Bruyere C., Billault A., Segurens B., Gouyvenoux M., Ugarte E.,
RA Cattonaro F., Anthouard V., Vico V., Del Fabbro C., Alaux M.,
RA Di Gaspero G., Dumas V., Felice N., Paillard S., Juman I., Moroldo M.,
RA Scalabrin S., Canaguier A., Le Clainche I., Malacrida G., Durand E.,
RA Pesole G., Laucou V., Chatelet P., Merdinoglu D., Delledonne M.,
RA Pezzotti M., Lecharny A., Scarpelli C., Artiguenave F., Pe M.E., Valle G.,
RA Morgante M., Caboche M., Adam-Blondon A.-F., Weissenbach J., Quetier F.,
RA Wincker P.;
RT "The grapevine genome sequence suggests ancestral hexaploidization in major
RT angiosperm phyla.";
RL Nature 449:463-467(2007).
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; FN594951; CBI15929.3; -; Genomic_DNA.
DR RefSeq; XP_002276855.1; XM_002276819.3.
DR SMR; D7SJV3; -.
DR STRING; 29760.D7SJV3; -.
DR PaxDb; 29760-VIT_06s0004g06860-t01; -.
DR EnsemblPlants; Vitvi06g00669_t001; Vitvi06g00669_P001; Vitvi06g00669.
DR GeneID; 100251869; -.
DR Gramene; Vitvi06g00669_t001; Vitvi06g00669_P001; Vitvi06g00669.
DR KEGG; vvi:100251869; -.
DR eggNOG; KOG0985; Eukaryota.
DR HOGENOM; CLU_002136_0_0_1; -.
DR InParanoid; D7SJV3; -.
DR OMA; HCYDLLH; -.
DR OrthoDB; 5474327at2759; -.
DR Proteomes; UP000009183; Chromosome 6.
DR ExpressionAtlas; D7SJV3; baseline and differential.
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: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; 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; 2.
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:UP000009183};
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 1625..1652
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 1705 AA; 192951 MW; 65251410052F037C CRC64;
MAAANAPISM KEALTLSSIG ISPQFMTFTH VTMESDKYIC VRETAPQNSV VIIDMSMPMQ
PLRRPITADS ALMNPNSRIL ALKAQLPGTT QDHLQIFNIE MKAKMKSHQM PEQVVFWKWI
TPKMLGLVTQ TSVFHWSIEG DSEPVKMFER TANLVNNQII NYRCDPSEKW LVLIGIAPGS
PERPQLVKGN MQLFSVDQQR SQALEAHAAS FASFKVLGNE NPSTLICFAS KTTNAGQITS
KLHVIELGAQ PGKPGFTKKQ ADLFFPPDFA DDFPVSMQVS QKYGLIYVIT KLGLLFVYDL
ETASAVYRNR ISPDPIFLTA EASSIGGFYA INRRGQVLLA TVNEATIVPF VSGQLNNLEL
AVNLAKRGNL PGAENLVVQR FQELFAQTKY KEAAELAAES PQGLLRTPDT VAKFQSVPVQ
SGQTPPLLQY FGTLLTRGKL NAFESLELSR LVVNQNKKNL LENWLAEDKL ECSEELGDLV
KTVDNDLALK IYIKARATPK VVAAFAERRE FDKILIYSKQ VGYTPDYLFL LQTILRSDPQ
GAVNFALMMS QMEGGCPVDY NTITDLFLQR NLIREATAFL LDVLKPNLPE HGFLQSKVLE
INLVTFPNVA DAILANGMFS HYDRPRIAQL CEKAGLYVRA LQHYTELPDI KRVIVNTHAI
EPQALVEFFG TLSREWALEC MKDLLLVNLR ANLQIIVQTA KEYSEQLGVE ACIKLFEQFK
SYEGLYFFLG SYLSSSEDPD IHFKYIEAAA KTGQIKEVER VTRESNFYDA EKTKNFLMET
KLPDARPLIN VCDRFGFVPD LTHYLYTNNM LRYIEGYVQK VNPGNAPLVV GQLLDDECPE
DFIKGLILSV RSLLPVEPLV EECEKRNRLR LLTQFLEHLV SEGSQDVHVH NALGKIIIDS
NNNPEHFLTT NPYYDSRVVG KYCEKRDPTL AVVAYRRGQC DDELINVTNK NSLFKLQARY
VVERMDADLW EKVLSPDNEY RRQLIDQVVS TALPESKSPE QVSAAVKAFM TADLPHELIE
LLEKIVLQNS AFSGNFNLQN LLILTAIKAD PSRVMDYINR LDNFDGPAVG DVAVEAQLYE
EAFAIFKKFN LNVQAVNVLL DNIQSIERAV EFAFRVEEDA VWSQVAKAQL KEGLVSDAIE
SFIRADDATQ FLDVIRAAEN ANVYHDLVRY LLMVRQKTKE PKVDSELIYA YAKIDRLGDI
EEFILMPNVA NLQNVGDRLY DEALYEAAKI IFAFISNWAK LACTLVKLRQ FQGAVDAARK
ANSSKTWKEV CFACVDAEEF RLAQICGLNI IIQVDDLEEV SDYYQNRGCF NELISLMESG
LGLERAHMGI FTELGVLYAR YRPEKLMEHI KLFSTRLNIP KLIRACDEQQ HWKELTYLYI
QYDEFDNAAT TIMNHSPEAW DHMQFKDVAV KVANVELYYK AVHFYLQEHP DLINDLLNVL
ALRVDHTRVV DIMRKAGHLH LVKPYMVAVQ STNVAAVNEA LNGIHVEEED YDRLRESIDM
HDNFDQIGLA QKVEKHELLE MRRIAAYIYK KAGRWKQSIA LSKKDNLYKD AMETCSQSGD
RELAEELLVY FIEQKKKECF ASCLFVCYDL IRPDVVLELA WMNNMIDFAF PYLLQFIREY
TGKVDDLVKD RIEALKETKA KEEEEKDVVK QQNMYAQLLP LALPAPPMPG MGGAGMGGGF
AAPPPMGGMG MPPMPPFGMP PMGSY
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