ID I1M7S3_SOYBN Unreviewed; 1700 AA.
AC I1M7S3;
DT 13-JUN-2012, integrated into UniProtKB/TrEMBL.
DT 13-JUN-2012, sequence version 1.
DT 27-MAR-2024, entry version 71.
DE RecName: Full=Clathrin heavy chain {ECO:0000256|PIRNR:PIRNR002290};
GN Name=100786715 {ECO:0000313|EnsemblPlants:KRH14933};
GN ORFNames=GLYMA_14G058300 {ECO:0000313|EMBL:KRH14933.1};
OS Glycine max (Soybean) (Glycine hispida).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Fabales; Fabaceae; Papilionoideae; 50 kb inversion clade;
OC NPAAA clade; indigoferoid/millettioid clade; Phaseoleae; Glycine;
OC Glycine subgen. Soja.
OX NCBI_TaxID=3847 {ECO:0000313|EnsemblPlants:KRH14933};
RN [1] {ECO:0000313|EMBL:KRH14933.1, ECO:0000313|EnsemblPlants:KRH14933}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Williams 82 {ECO:0000313|EnsemblPlants:KRH14933};
RC TISSUE=Callus {ECO:0000313|EMBL:KRH14933.1};
RX PubMed=20075913; DOI=10.1038/nature08670;
RA Schmutz J., Cannon S.B., Schlueter J., Ma J., Mitros T., Nelson W.,
RA Hyten D.L., Song Q., Thelen J.J., Cheng J., Xu D., Hellsten U., May G.D.,
RA Yu Y., Sakurai T., Umezawa T., Bhattacharyya M.K., Sandhu D.,
RA Valliyodan B., Lindquist E., Peto M., Grant D., Shu S., Goodstein D.,
RA Barry K., Futrell-Griggs M., Abernathy B., Du J., Tian Z., Zhu L., Gill N.,
RA Joshi T., Libault M., Sethuraman A., Zhang X.-C., Shinozaki K.,
RA Nguyen H.T., Wing R.A., Cregan P., Specht J., Grimwood J., Rokhsar D.,
RA Stacey G., Shoemaker R.C., Jackson S.A.;
RT "Genome sequence of the palaeopolyploid soybean.";
RL Nature 463:178-183(2010).
RN [2] {ECO:0000313|EnsemblPlants:KRH14933}
RP IDENTIFICATION.
RC STRAIN=Williams 82 {ECO:0000313|EnsemblPlants:KRH14933};
RG EnsemblPlants;
RL Submitted (FEB-2018) to UniProtKB.
RN [3] {ECO:0000313|EMBL:KRH14933.1}
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Callus {ECO:0000313|EMBL:KRH14933.1};
RA Schmutz J., Cannon S., Schlueter J., Ma J., Mitros T., Nelson W., Hyten D.,
RA Song Q., Thelen J., Cheng J., Xu D., Hellsten U., May G., Yu Y.,
RA Sakurai T., Umezawa T., Bhattacharyya M., Sandhu D., Valliyodan B.,
RA Lindquist E., Peto M., Grant D., Shu S., Goodstein D., Barry K.,
RA Futrell-Griggs M., Abernathy B., Du J., Tian Z., Zhu L., Gill N., Joshi T.,
RA Libault M., Sethuraman A., Zhang X., Shinozaki K., Nguyen H., Wing R.,
RA Cregan P., Specht J., Grimwood J., Rokhsar D., Stacey G., Shoemaker R.,
RA Jackson S.;
RT "WGS assembly of Glycine max.";
RL Submitted (JUL-2018) to the EMBL/GenBank/DDBJ databases.
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; CM000847; KRH14933.1; -; Genomic_DNA.
DR RefSeq; XP_003544075.1; XM_003544027.3.
DR AlphaFoldDB; I1M7S3; -.
DR SMR; I1M7S3; -.
DR STRING; 3847.I1M7S3; -.
DR PaxDb; 3847-GLYMA14G06340-1; -.
DR EnsemblPlants; KRH14933; KRH14933; GLYMA_14G058300.
DR GeneID; 100786715; -.
DR Gramene; KRH14933; KRH14933; GLYMA_14G058300.
DR KEGG; gmx:100786715; -.
DR eggNOG; KOG0985; Eukaryota.
DR HOGENOM; CLU_002136_0_0_1; -.
DR InParanoid; I1M7S3; -.
DR OMA; XLECSEE; -.
DR OrthoDB; 5474327at2759; -.
DR Proteomes; UP000008827; Chromosome 14.
DR ExpressionAtlas; I1M7S3; 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; 2.
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:UP000008827};
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 1617..1651
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 1700 AA; 192567 MW; 9FC2C3D97619916F CRC64;
MAAANAPITM KEALTLPSIG INSQFITFTH VTMESDKYIC VRETAPQNSV VIIDMNMPNQ
PLRRPITADS ALMNPNSRIL ALKAQLQGTT QDHLQIFNIE MKAKMKSYQM PEQVVFWKWI
SPKMLGLVTQ TSVYHWSIEG DSEPVKMFER TANLANNQII NYRCDPTEKW LVLIGIAPGA
PERAQLVKGN MQLFSVDQQR SQALEAHAAS FAQFKVPGNE NPSVLISFAS KTLNAGQVIS
KLHVIELGAQ PGRPSFTKKQ ADLFFPPDFA DDFPVAMQIS HKYNLIYVIT KLGLLFVYDL
ETATAVYRNR ISPDPIFLTS EATSVGGFYA INRRGQVLLA TVNEQTIVNF VSGQLNNLEL
AVSLAKRGNL PGAEKLVVER FHELFAQTKY KEAAELAAES PQGILRTPDT VAKFQSVPVQ
AGQTPPLLQY FGTLLTRGKL NAFESLELSR LVVNQNKKNL LENWLAEDKL ECSEELGDLV
KTVDNDLALK IYIKARATPK VVAAFAERRE FDKILIYSKQ VGYTPDYLFL LQTILRTDPQ
GAVNFALMMS QMEGGSPVDY NTITDLFLQR NLIREATAFL LDVLKPNLPE HGFLQTKVLE
INLVTFPNVA DAILANGMFS HYDRPRIAQL CEKAGLYVRA LQHYTELPDI KRVIVNTHAI
EPQSLVEFFG TLSKEWALEC MKDLLLANLR GNLQIIVQVA KEYCEQLGVD ACIKLFEQFR
SYEGLYFFLG SYLSSSEDPD IHFKYIEAAA KTGQIKEVER VTRESNFYDA EKTKNFLMEA
KLPDARPLIN VCDRFGFVPD LTHYLYTNNM VRYIEGYVQK VNPGNAPLVV GQLLDDECAE
DFIKGLILSV RSLLPVEPLV EECEKRNRLR MLTQFLEHLV SEGSQDVHVH NALGKIIIDS
NNNPEHFLTT NPYYDSRVVG KYCEKRDPTL AVVAYRRGQC DDELINVTNK NSLFKLQARY
VVERMDGDLW AKVLDPDNEY RRQLIDQVVS TALPESSSPE QVSAAVKAFM TADLPHELIE
LLEKIVLQNS AFSGNFNLQN LLILTAIKAD PSRVMDYVNR LDNFDGPAVG EMAVEAQLYE
EAFAIFKKFN LNVQAVNVLL DKIHSIDRAV EFAFRVEEDA VWSQVAKAQL RDGLVSDAIE
SFIRADDATQ FLDVIRAAED GNVYHDLVKY LLMVRGKAKE PKVDSELIYA YAKIDRLSDI
EEFILMPNVA NLQNVGDRLY DEALYEAAKI IFAFISNWAK LAITLVKLQQ FQGAVDAARK
ANSSKTWKEV CFACVDAEEF RLAQICGLNI IIQVDDLEEV SEYYQNRGCF NELISLMESG
LGLERAHMGI FTELGVLYAR YRPEKLMEHI KLFSTRLNIP KLIRACDEQQ HWKELTYLYI
QYGEFDNAAT TIMNHSPEAW DHMQFKDVVV KVANVELYYK AVHFYLEEHP DLINDVLNVL
ALRVDHARVV DIMRKAGHLR LVKPYMIAVQ SNNVSAVNEA LNEIYVEEED YDRLRESIDL
HDNFDQIGLA QKIEKHELLE MRRVAAYIYK KAGRWKQSIA LSKKDNLYKD AMETASQSGE
RELAEELLVY FIDQGKKECF ASCLFVCYDL IRADIVLELA WMHNMIDFAF PYLLQFIREY
TGKVDELVKD KIEAQNEVKA KEQEEKDVVA QQNMYAQLLP LALPAPPMPG MGGFAPPPPM
GGLGMPPMPP YGMPPMGSSF
//
