UniProt: A0A1D6EJ91

Database: UniProt
Entry: A0A1D6EJ91_MAIZE

LinkDB:  A0A1D6EJ91_MAIZE 
Original site:  A0A1D6EJ91_MAIZE

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Ontology (7)   
   GO (7)   
DNA sequence (1)   
   EMBL (1)   
Protein domain (13)   
   InterPro (7)   
   Pfam (4)   
   PROSITE (1)   
   SMART (1)   
All databases (21)   

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ID   A0A1D6EJ91_MAIZE        Unreviewed;      1520 AA.
AC   A0A1D6EJ91;
DT   30-NOV-2016, integrated into UniProtKB/TrEMBL.
DT   30-NOV-2016, sequence version 1.
DT   27-MAR-2024, entry version 36.
DE   RecName: Full=Clathrin heavy chain {ECO:0000256|PIRNR:PIRNR002290};
GN   ORFNames=ZEAMMB73_Zm00001d005090 {ECO:0000313|EMBL:ONM20222.1};
OS   Zea mays (Maize).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; PACMAD clade;
OC   Panicoideae; Andropogonodae; Andropogoneae; Tripsacinae; Zea.
OX   NCBI_TaxID=4577 {ECO:0000313|EMBL:ONM20222.1};
RN   [1] {ECO:0000313|EMBL:ONM20222.1, ECO:0000313|Proteomes:UP000007305}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. B73 {ECO:0000313|EnsemblPlants:Zm00001eb094250_P001,
RC   ECO:0000313|Proteomes:UP000007305};
RC   TISSUE=Seedling {ECO:0000313|EMBL:ONM20222.1};
RG   Maize Genome Sequencing Project;
RA   Ware D.;
RT   "Update maize B73 reference genome by single molecule sequencing
RT   technologies.";
RL   Submitted (DEC-2015) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EnsemblPlants:Zm00001eb094250_P001}
RP   IDENTIFICATION.
RC   STRAIN=cv. B73 {ECO:0000313|EnsemblPlants:Zm00001eb094250_P001};
RG   EnsemblPlants;
RL   Submitted (MAY-2021) to UniProtKB.
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; CM007648; ONM20147.1; -; Genomic_DNA.
DR   EMBL; CM007648; ONM20195.1; -; Genomic_DNA.
DR   EMBL; CM007648; ONM20198.1; -; Genomic_DNA.
DR   EMBL; CM007648; ONM20214.1; -; Genomic_DNA.
DR   EMBL; CM007648; ONM20222.1; -; Genomic_DNA.
DR   EMBL; CM007648; ONM20233.1; -; Genomic_DNA.
DR   EnsemblPlants; Zm00001eb094250_T001; Zm00001eb094250_P001; Zm00001eb094250.
DR   Gramene; Zm00001eb094250_T001; Zm00001eb094250_P001; Zm00001eb094250.
DR   Proteomes; UP000007305; Chromosome 2.
DR   ExpressionAtlas; A0A1D6EJ91; 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; 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: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   1: Evidence at protein 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   Proteomics identification {ECO:0007829|PeptideAtlas:A0A1D6EJ91};
KW   Reference proteome {ECO:0000313|Proteomes:UP000007305};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737}.
FT   DOMAIN          154..177
FT                   /note="Clathrin heavy chain linker core motif"
FT                   /evidence="ECO:0000259|Pfam:PF09268"
SQ   SEQUENCE   1520 AA;  172409 MW;  B860EBA767BB2F48 CRC64;
     MQLFSVDQQR SQALEAHAAS FATFKVVGNE NPSTLICFAS KTTNAGQITS KLHVIELGAQ
     PGKPGFSKKQ ADLFFPPDFQ DDFPVAMQVS QKYGLIYVIT KLGLLFVYDL ETAAAVYRNR
     ISPDPIFLTA ESSSTGGFYA INRRGQVLHA TVNDATVVPF VSGQLNNLEL AVNLAKRANL
     PGAENLVVQR FQELFAQTKY KEAAELAAES PQGLLRTPET VAKFQSVPVQ AGQTPPLLQY
     FGTLLTRGKL NAFESLELSR LVVNQNKKNL LENWLAEDKL ECSEELGDLV KTVDNDLALK
     IYIKARATPK VVAAFAERRE FDKILIYSKQ VGYTPDYLFL LQTILRTDPQ GAVNFALMMS
     QMEGGCPVDY NTITDLFLQR NMIREATAFL LDVLKPNLPE HAFLQTKVLE INLVTYPNVA
     DAILANGMFS HYDRPRIAQL CEKAGLYLRA LQHYAELPDI KRAIVNTHAI EPQALVEFFG
     TLSREWALEC MKDLLLVNLR GNLQIVVQAA KEYSEQLGVD ACIKLFEQFK SYEGLYFFLG
     SYLSSSEDPE IHFKYIEAAA RTGQIKEVER VTRESNFYDA EKTKNFLMEA KLPDARPLIN
     VCDRFGFVPD LTHYLYTNNM LRYIEGYVQK VNPGNAPLVV GQLLDDECPE DFIKGLILSV
     RSLLPVEPLV DECEKRNRLR LLTQFLEHLV SEGSQDVHVH NALGKIIIDS NNNPEHFLTT
     NPFYDSRVVG KYCEKRDPTL AVVAYRRGQC DDELIIVTNK NSLFKLQARY VVERMDGDLW
     DKVLQPENEY RRQLIDQVVS TALPESKSPE QVSAAVKAFM TADLPHELIE LLEKIVLQNS
     AFSGNFNLQN LLILTAIKAD PSRVMDYVNR LDNFDGPAVG EVAVEAQLYE EAFAIFKKFN
     LNVQAVDVLL DNIRSIERAE EFAFRVEEDA VWSQVAKAQL REGLVSEAIE SFIRADDAAH
     FLDVIRAAEE ANVYNDLVKY LLMVRQKARE PKVDGELIFA YAKIDRLSDI EEFILMPNVA
     NLQNVGDRLY DEELYEAAKI IYAFISNWAK LAVTLVKLKQ FQGAVDAARK ANSAKTWKEV
     CFACVDAEEF RLAQICGLNI IIQVDDLEEV SEYYQNRGCF SELIALMESG LGLERAHMGI
     FTELGVLYAR YRSEKLMEHI KLFSTRLNIP KLIRACDEQQ HWKELTYLYI QYDEFDNAVT
     TIMNHSPDAW DHMQFKDVCV KVANVELYYK AVHFYLQEHP DLINDMLNVL ALRLDHTRVV
     DIMRKAGQLH LVKPYMVAVQ SNNVSAVNEA LNELYVEEED YERLRESVDM HDNFDQIGLA
     QKLEKHELLE MRRIAAYIYK KAGRWKQSIA LSKKDNMYKD CMETCSQSGD RELSEDLLVY
     FIEQGKKECF ASCLFICYDL IRPDVALELA WMNNMLDFAF PYLLQFIREY TSKVDDLVKD
     RIESQNEERV KEKEEKDLVA QQNMYAQLLP LALPAPPMPG MGGPPPPMGG MGMPPMGGMG
     MPPMGPGPMP AFGMPAMGSY
//

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