ID W1PE37_AMBTC Unreviewed; 1703 AA.
AC W1PE37;
DT 19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT 19-MAR-2014, sequence version 1.
DT 27-MAR-2024, entry version 49.
DE RecName: Full=Clathrin heavy chain {ECO:0000256|PIRNR:PIRNR002290};
GN ORFNames=AMTR_s00007p00168430 {ECO:0000313|EMBL:ERN05320.1};
OS Amborella trichopoda.
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Amborellales; Amborellaceae; Amborella.
OX NCBI_TaxID=13333 {ECO:0000313|EMBL:ERN05320.1, ECO:0000313|Proteomes:UP000017836};
RN [1] {ECO:0000313|Proteomes:UP000017836}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=24357323;
RG Amborella Genome Project;
RT "The Amborella genome and the evolution of flowering plants.";
RL Science 342:1241089-1241089(2013).
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; KI394011; ERN05320.1; -; Genomic_DNA.
DR RefSeq; XP_006843645.1; XM_006843582.2.
DR STRING; 13333.W1PE37; -.
DR EnsemblPlants; ERN05320; ERN05320; AMTR_s00007p00168430.
DR GeneID; 18433494; -.
DR Gramene; ERN05320; ERN05320; AMTR_s00007p00168430.
DR KEGG; atr:18433494; -.
DR eggNOG; KOG0985; Eukaryota.
DR HOGENOM; CLU_002136_0_0_1; -.
DR OMA; HCYDLLH; -.
DR OrthoDB; 5474327at2759; -.
DR Proteomes; UP000017836; Unassembled WGS sequence.
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: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; 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 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:UP000017836};
KW Repeat {ECO:0000256|ARBA:ARBA00022737}.
FT DOMAIN 344..367
FT /note="Clathrin heavy chain linker core motif"
FT /evidence="ECO:0000259|Pfam:PF09268"
SQ SEQUENCE 1703 AA; 193373 MW; 47BF74DD1E03C6F4 CRC64;
MAAATAPITM KEALTLTSLG INPQFITFTH VTMESEKYIC VRETAPQNSV VIIDMNMPMQ
PLRRPITADS ALMNPNSRIL ALKAQIPGTT QDHLQIFNIE MKAKMKSHQM PEQVVFWKWI
TPKMLGLVTQ TSVYHWSIEG DSEPVKMFER TANLLNNQII NYRCDPSEKW LVLIGIAPGA
AERPQLVKGN MQLFSVDQQR SQALEAHAAS FASIKVAGNE NPSTLICFAS KTTNAGQITS
KLHVIELGAQ PGKPGFTKRQ ADLFFPPDFA DDFPVAMQIS HKYSLIYVIT KLGLLFVYDL
ETATAVYRNR ISPDPIFLTT EASSLGGFYA VNRRGQVLLA TVNEATIVPF VSGQLNNLEL
AVNLAKRGNL PGAENLVVQR FQELFSQTKY KEAAELAADS PQGILRTPDT VAKFQSVPVQ
SGQTPPLLQY FGTLLTKGKL NAFESLELSR LVVNQNKKNL LENWLAEDKL ECSEELGDLV
KTVDNDLALK IYIKARATPK VVAAFAERRE FDKILIYSKQ VGYTPDYLFL LQTILRTDPQ
GAVNFALMMS QMEGGCPVDY NTITDLFLQR NMIREATAFL LDVLKPNLPE HAFLQTKVLE
INLVTFPNVA DAILANGMFS HYDRPRVAQL CEKAGLYMRA LQHYTELPDI KRVIVNTHAI
EPQSLVEFFG TLSREWALEC MKDLLVVNLR GNLQIIVQVA KEYSEQLGVD ACIRIFEQFK
SYEGLYFFLG SYLSSSEDPD IHFKYIEAAA KTGQIKEVER VTRESNFYDP EKTKNFLMEA
KLPDARPLIN VCDRFGFVPD LTHYLYSNNM LRYIEGYVQK VSPANAPLVV GQLLDDECPE
DFIKGLILSV RSLLPVEPLV EECEKRNRLR LLTQFLEHLV SEGSQDVHVH NALGKIIIDS
NNNPEHFLTT NPYYDSRVVG KYCEKRDPTL AVVAYRRGQC DDELINVTNK NSLFKLQARY
VVERMEPELW EKVLNPENTY RRQLIDQVVS TALPESKSPE QVSAAVKAFM TADLPHELIE
LLEKIVLQNS AFSGNFNLQN LLILTAIKAD KSRVMDYINR LENFDGPAVG EVAVEHELYE
EAFAIFKKFS LNVQAVNVLL DNIRSIDRAV EFAFRVEEDA VWSQVAKAQL KEGLVSDAIE
SFIRADDATQ FLDVIRAAEE TNVYHDLVKY LLMVRQKVKE PKVDSELIYA YAKIDRLGEI
EEFILSPNVA NLQNVGDRLY DEALYEAAKI IFAYISNWAK LASTLVKLKQ FQGAVDAARK
ANSSKTWKEI CFACVDAEEF RLAQICGLNI IVQVDDLEEV SDYYQNRGCF NELISLMESG
LGLERAHMGI FTELGILYAR YRPEKLMEHI KLFATRLNIP KLIRVCDEQQ HWKELTYLYI
QYDEFDNAAT TMMNHSPEAW DHMQFKDVAV KVANVELYYK AVHFYLQEHP EYINDLLHVL
ALRVDHTRVV DIMRKAGQLH LVKPYMVEVQ SNNVAAVNEA LNEIYIEEED YDRLRESIDL
HDNFDQIGLA QKLEKHELLE MRRIAAYIYK KAGRWRQSVQ LSKKDNLYQD AMETSSQSGD
RELAEELLVY FIEQGKKECF ASCLFTCYDL IRPDVALELA WMNNMIDFVF PYLLQFIREY
TTKVDELVKD KLEALTETKV KEKEEKDLVA QQNMYAQLLP LALPAPPMAG MGSGFAPPPP
MGGMGMPPMP PFGMPPPPPM GGY
//
