CLH2_ORYSJ
ID CLH2_ORYSJ Reviewed; 1708 AA.
AC Q2QYW2;
DT 16-NOV-2011, integrated into UniProtKB/Swiss-Prot.
DT 24-JAN-2006, sequence version 1.
DT 25-MAY-2022, entry version 94.
DE RecName: Full=Clathrin heavy chain 2;
GN OrderedLocusNames=Os12g0104800, LOC_Os12g01390;
OS Oryza sativa subsp. japonica (Rice).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC Oryzoideae; Oryzeae; Oryzinae; Oryza; Oryza sativa.
OX NCBI_TaxID=39947;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Nipponbare;
RX PubMed=16188032; DOI=10.1186/1741-7007-3-20;
RG The rice chromosomes 11 and 12 sequencing consortia;
RT "The sequence of rice chromosomes 11 and 12, rich in disease resistance
RT genes and recent gene duplications.";
RL BMC Biol. 3:20-20(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Nipponbare;
RX PubMed=16100779; DOI=10.1038/nature03895;
RG International rice genome sequencing project (IRGSP);
RT "The map-based sequence of the rice genome.";
RL Nature 436:793-800(2005).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=cv. Nipponbare;
RX PubMed=18089549; DOI=10.1093/nar/gkm978;
RG The rice annotation project (RAP);
RT "The rice annotation project database (RAP-DB): 2008 update.";
RL Nucleic Acids Res. 36:D1028-D1033(2008).
RN [4]
RP GENOME REANNOTATION.
RC STRAIN=cv. Nipponbare;
RX PubMed=24280374; DOI=10.1186/1939-8433-6-4;
RA Kawahara Y., de la Bastide M., Hamilton J.P., Kanamori H., McCombie W.R.,
RA Ouyang S., Schwartz D.C., Tanaka T., Wu J., Zhou S., Childs K.L.,
RA Davidson R.M., Lin H., Quesada-Ocampo L., Vaillancourt B., Sakai H.,
RA Lee S.S., Kim J., Numa H., Itoh T., Buell C.R., Matsumoto T.;
RT "Improvement of the Oryza sativa Nipponbare reference genome using next
RT generation sequence and optical map data.";
RL Rice 6:4-4(2013).
CC -!- FUNCTION: Clathrin is the major protein of the polyhedral coat of
CC coated pits and vesicles.
CC -!- SUBUNIT: Clathrin triskelions, composed of 3 heavy chains and 3 light
CC chains, are the basic subunits of the clathrin coat. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasmic vesicle membrane {ECO:0000250};
CC Peripheral membrane protein {ECO:0000250}; Cytoplasmic side
CC {ECO:0000250}. Membrane, coated pit {ECO:0000250}; Peripheral membrane
CC protein {ECO:0000250}; Cytoplasmic side {ECO:0000250}. Note=Cytoplasmic
CC face of coated pits and vesicles. {ECO:0000250}.
CC -!- DOMAIN: The C-terminal third of the heavy chains forms the hub of the
CC triskelion. This region contains the trimerization domain and the
CC light-chain binding domain involved in the assembly of the clathrin
CC lattice.
CC -!- DOMAIN: The N-terminal seven-bladed beta-propeller is formed by WD40-
CC like repeats, and projects inward from the polyhedral outer clathrin
CC coat. It constitutes a major protein-protein interaction node (By
CC similarity). {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the clathrin heavy chain family. {ECO:0000305}.
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DR EMBL; DP000011; ABA95598.1; -; Genomic_DNA.
DR EMBL; AP008218; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AP014968; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; XP_015619821.1; XM_015764335.1.
DR AlphaFoldDB; Q2QYW2; -.
DR SMR; Q2QYW2; -.
DR STRING; 39947.Q2QYW2; -.
DR PaxDb; Q2QYW2; -.
DR PRIDE; Q2QYW2; -.
DR GeneID; 4351255; -.
DR KEGG; osa:4351255; -.
DR HOGENOM; CLU_002136_1_0_1; -.
DR InParanoid; Q2QYW2; -.
DR OrthoDB; 17940at2759; -.
DR Proteomes; UP000000763; Chromosome 12.
DR Proteomes; UP000059680; Chromosome 12.
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:InterPro.
DR GO; GO:0006898; P:receptor-mediated endocytosis; IBA:GO_Central.
DR Gene3D; 1.25.40.10; -; 3.
DR Gene3D; 2.130.10.110; -; 1.
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 Pfam; PF00637; Clathrin; 7.
DR Pfam; PF09268; Clathrin-link; 1.
DR Pfam; PF01394; Clathrin_propel; 2.
DR PIRSF; PIRSF002290; Clathrin_H_chain; 1.
DR SMART; SM00299; CLH; 7.
DR SUPFAM; SSF48371; SSF48371; 5.
DR SUPFAM; SSF50989; SSF50989; 1.
DR PROSITE; PS50236; CHCR; 7.
PE 3: Inferred from homology;
KW Coated pit; Cytoplasmic vesicle; Membrane; Reference proteome; Repeat.
FT CHAIN 1..1708
FT /note="Clathrin heavy chain 2"
FT /id="PRO_0000414016"
FT REPEAT 551..697
FT /note="CHCR 1"
FT REPEAT 700..842
FT /note="CHCR 2"
FT REPEAT 847..986
FT /note="CHCR 3"
FT REPEAT 993..1138
FT /note="CHCR 4"
FT REPEAT 1142..1283
FT /note="CHCR 5"
FT REPEAT 1288..1434
FT /note="CHCR 6"
FT REPEAT 1437..1580
FT /note="CHCR 7"
FT REGION 1..492
FT /note="Globular terminal domain"
FT /evidence="ECO:0000250"
FT REGION 25..67
FT /note="WD40-like repeat 1"
FT REGION 68..113
FT /note="WD40-like repeat 2"
FT REGION 114..155
FT /note="WD40-like repeat 3"
FT REGION 156..205
FT /note="WD40-like repeat 4"
FT REGION 206..270
FT /note="WD40-like repeat 5"
FT REGION 271..314
FT /note="WD40-like repeat 6"
FT REGION 315..343
FT /note="WD40-like repeat 7"
FT REGION 462..478
FT /note="Binding site for the uncoating ATPase, involved in
FT lattice disassembly"
FT /evidence="ECO:0000250"
FT REGION 493..536
FT /note="Flexible linker"
FT /evidence="ECO:0000250"
FT REGION 537..1708
FT /note="Heavy chain arm"
FT /evidence="ECO:0000250"
FT REGION 537..648
FT /note="Distal segment"
FT /evidence="ECO:0000250"
FT REGION 653..1708
FT /note="Proximal segment"
FT /evidence="ECO:0000250"
FT REGION 1227..1536
FT /note="Involved in binding clathrin light chain"
FT /evidence="ECO:0000250"
FT REGION 1564..1708
FT /note="Trimerization"
FT /evidence="ECO:0000250"
SQ SEQUENCE 1708 AA; 193348 MW; D49EFE3B4064FE40 CRC64;
MAAANAPIAM REALTLTSLG IAPQFVTFTH VTMESEKYIC VRETSPQNSV VIVDMAMPAQ
PLRRPITADS ALMNPNTRIL ALKAQIPGTT QDHLQIFNIE AKTKIKSHQM PEQVVFWKWI
TPKLLGLVTQ TSVYHWSIEG DSEPAKMFDR TANLANNQII NYRCDPSEKW LVLIGIAPGA
PERPQLVKGN MQLFSVDQQR SQALEAHAAS FASFKVVGNE NPSTLICFAS KTTNAGQITS
KLHVIELGAQ PGKPGFSKKQ ADLFFPPDFQ DDFPVAMQIS QKYGLIYVIT KLGLLFVYDL
ETAAAVYRNR ISPDPIFLTA ESSASGGFYA INRRGQVLHA TVNDATIVPF VSSQLNNLEL
AVNLAKRANL PGAENLVVQR FQELFAQTKY KEAAELAAES PQGLLRTPDT VAKFQSVPVQ
AGQTPPLLQY FGTLLTRGKL NAYESLELSR LVVNQNKKNL LENWLAEDKL ECSEELGDLV
KTVDNDLALK IYIKARATPK VVAAFAERRE FDKILIYSKQ VGYTPDYLFL LQTILRTDPQ
GAVNFALMMS QMEGGCPVDY NTITDLFLQR NMIREATAFL LDVLKPNLPE HAFLQTKVLE
INLVTYPNVA DAILANGMFS HYDRPRVAQL CEKAGLYLRA LQHYTELPDI KRVMVNTHAI
EPQALVEFFG TLSREWALEC MKDLLLVNLR GNLQIVVQAA KEYSEQLGVD ACIKLFEQFK
SYEGLYFFLG AYLSSSEDPD IHFKYIEAAA RTGQIKEVER VTRESNFYDA EKTKNFLMEA
KLPDARPLIN VCDRFGFVPD LTHYLYTNNM LRYIEGYVQK VNPGNAPLVV GQLLDDECPE
DFIKGLILSV RSLLPVEPLV DECEKRNRLR LLTQFLEHLV SEGSQDVHVH NALGKIIIDS
NNNPEHFLTT NPFYDSRVVG KYCEKRDPTL AVVAYRRGQC DDELINVTNK NSLFKLQARY
VVERMDGDLW DKVLQPENEY RRQLIDQVVS TALPESKSPE QVSAAVKAFM TADLPHELIE
LLEKIVLQNS AFSGNFNLQN LLILTAIKAD PSRVMDYVNR LDNFDGPAVG EVAVEAQLFE
EAFAIFKKFN LNVQAVNVLL DNIRSIERAE EFAFRVEEDA VWSQVAKAQL REGLVSEAIE
SFIRADDATH FLDVIRAAEE ANVYDDLVKY LLMVRQKARE PKVDGELIFA YAKIDRLSDI
EEFILMPNVA NLQNVGDRLY DEELYEAAKI IYAFISNWAK LAVTLVKLKQ FQGAVDAARK
ANSAKTWKEV CFACVDAEEF RLAQICGLNI IVQVDDLEEV SEYYQNRGCF NELISLMESG
LGLERAHMGI FTELGVLYAR YRPEKLMEHI KLFSTRLNIP KLIRACDEQQ HWKELTYLYI
QYDEFDNAAT TIMNHSPDAW DHMQFKDVAV KVANVELYYK AVHFYLQEHP DLINDLLNVL
ALRLDHTRVV DIMRKAGQLH LVKPYMVAVQ SNNVSAVNES LNELYVEEED YERLRESVDM
HDNFDQIGLA QKLEKHELLE MRRIAAYIYK KAGRWKQSIA LSKKDNMYKD CMETCSQSGD
RELSEDLLVY FIEQGKKECF ASCLFICYDL IRADVALELA WMNNMVDFAF PYLLQFIREY
TSKVDELVKD RIESQNEVRA KEKEEKDLVA QQNMYAQLLP LALPAPPGMG GPPPPMGMPG
MPPMGGMGMP PMGPGPMPAY GMPPMGSY
