ID U6LHM3_9EIME Unreviewed; 1746 AA.
AC U6LHM3;
DT 22-JAN-2014, integrated into UniProtKB/TrEMBL.
DT 22-JAN-2014, sequence version 1.
DT 27-MAR-2024, entry version 33.
DE RecName: Full=Clathrin heavy chain {ECO:0000256|PIRNR:PIRNR002290};
GN ORFNames=EBH_0021940 {ECO:0000313|EMBL:CDJ48748.1};
OS Eimeria brunetti.
OC Eukaryota; Sar; Alveolata; Apicomplexa; Conoidasida; Coccidia;
OC Eucoccidiorida; Eimeriorina; Eimeriidae; Eimeria.
OX NCBI_TaxID=51314 {ECO:0000313|EMBL:CDJ48748.1};
RN [1] {ECO:0000313|EMBL:CDJ48748.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Houghton {ECO:0000313|EMBL:CDJ48748.1};
RA Reid A.J., Blake D., Billington K., Browne H., Dunn M., Hung S.,
RA Kawahara F., Miranda-Saavedra D., Mourier T., Nagra H., Otto T.D.,
RA Rawlings N., Sanchez A., Sanders M., Subramaniam C., Tay Y., Dear P.,
RA Doerig C., Gruber A., Parkinson J., Shirley M., Wan K.L., Berriman M.,
RA Tomley F., Pain A.;
RT "Genomic analysis of the causative agents of coccidiosis in chickens.";
RL Submitted (OCT-2013) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:CDJ48748.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Houghton {ECO:0000313|EMBL:CDJ48748.1};
RA Aslett M.;
RL Submitted (OCT-2013) 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}.
CC -!- SIMILARITY: Belongs to the clathrin heavy chain family.
CC {ECO:0000256|PIRNR:PIRNR002290}.
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DR EMBL; HG711279; CDJ48748.1; -; Genomic_DNA.
DR EnsemblProtists; CDJ48748; CDJ48748; EBH_0021940.
DR VEuPathDB; ToxoDB:EBH_0021940; -.
DR OrthoDB; 5474327at2759; -.
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; 4.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR000547; Clathrin_H-chain/VPS_repeat.
DR InterPro; IPR016025; Clathrin_H-chain_N.
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; PF13838; Clathrin_H_link; 1.
DR PIRSF; PIRSF002290; Clathrin_H_chain; 1.
DR SMART; SM00299; CLH; 7.
DR SUPFAM; SSF48371; ARM repeat; 6.
DR SUPFAM; SSF50989; Clathrin heavy-chain terminal domain; 1.
DR PROSITE; PS50236; CHCR; 7.
PE 3: Inferred from homology;
KW Coated pit {ECO:0000256|PIRNR:PIRNR002290};
KW Cytoplasmic vesicle {ECO:0000256|PIRNR:PIRNR002290};
KW Membrane {ECO:0000256|PIRNR:PIRNR002290}.
SQ SEQUENCE 1746 AA; 194973 MW; 8EF528969D013B46 CRC64;
MAQQLPVQLT QIVNLGDTGV KSASFRFGNV AVDGDKHLVV RDVESNELYF VSLNPKEALE
SPGSPGAYSV TKKPTQAEAA LHHPTDPIVA LRAKADGGQQ VVQVLNLETK ARMGTAPMSE
SIVYWRWVAP RVLALVTDKA VWHWTLAEGT DAGEPQKICE REGRLAEGVQ IIGYSTDKEM
KWCVLTGIST QDGGKTIDGS LQLYSMELKK HQQLEGHAAC FGGLVVDEAL GPQPVICFAE
KKRGSPEFKL HVRDLAPKRE DGKPPLRVCT DIALSPDAPS DFPLAVHLSK KLGLVFLVTK
GGFLLLFDAF TGTQLLRHRI SQDPVFLTAD SPQTGGVITV HKKGVVALTT VNVGLLGPYM
QHGLPHLPNR AQIYLSLAKR YGLPGADDAL VQAFTQHFAS GDYRGAARIC ATLKSGRLRT
PQVLQQFKGV PAQPGQTSAI LLYFSTLLEY GSLNAVESLE LVRPVVAQGR KDFVTTWLRE
DKLECTEELG DVLRPLDPAL ATQVYKKAKA GQKVMLMLVE QGKTDELLEY AAQTRMQADY
SALLRSMLAT NPEGAVAFAQ KLLATEPPLV DPNQVVDVLL QQQRFQELSS LLLEYLKGNK
PEQGPLQTRL FEINLKHSPQ VAEAIFQMEM LTHYDRQKVG ALCEAAGLYQ RALENYTELT
DVKRVLLQTG GKISQEWMAQ FFGRMAPEVC VEILTDMLRA SSQNLQAVVG VAIKFHEQLG
TERLIAMFER FSSYEGIFYF LGSILAFSTD PEVHFKYIEA AAKLNHTQEV ERVCRESKHY
EPQRVKEFLK QAKLSDPRPL IYVCDLHGFV VELTEYLYKH SLLRYIEVYV SRVNAANAPL
VVGALVDLDA PEDFIKQLLQ AVRGNCSASQ LVEEVEKRNR LRLLLQWLEQ RVAEGNQDPA
VHNALAKIFI DTNRDAENFL KTNAFYDSME VGKYCEERDP HLAFIAYKRA WGPCDTQLVE
LTNKNGLFRL QARYLVERQC AELWAYVLRP ENNYRRSVID QVVSSALPES SSADEVSAAV
NAFISAQLPQ ELTELLEKIV LHNSDFSSNQ NLQNLLILTA IKAEPSRVMG YINRLQNFDG
AAIAQVALEN GLREEALTIY RKFGLLAEAA DTLLEAAAGG GEQELERAQE FAQRCGNAEV
WRKLGRAQLR QGRVVEAVDS LIKANDGEVF REVVEKATEQ GAFEALAEYL LMARKSVTIK
DQTLDSELLY SYAMTERLDD LEMFLNGPNT ANVQAVGDRL FDQGRYQAAK ILYQSLPNYS
KLASCFVRMK DFGAAVDAAR KAKNPKTWKE VAFGALNEGD IKCAHTAGLQ LIAHPDLLDA
LVEEYERWGL HKQLMELLET GAQGERTHVG LFTELGVLYA TYDSAKLMDH CKQHKARMNI
PRLIRTCENC CLWKEAVYLH TIYDEYEQAA NCMILHPTAW QHDQFIQVVQ KVSNVELLYR
AISFYLEEHP LQLCALLKGM DRKVDHSRVV QQLRKAGHLP LIEKYLQEQL PLNVAAVNEA
MLELLVEAQD EERIRELITE CDNFDQLGLA KQLEGHNELG MRRIAALLYQ KNKKYSLAIE
LSKKDAQLQD CIETAKESGS AQLVEDLLKY FLTDLKDPEA FAACLHSCCD LVKPDVALEL
AWRHKVVDFI MPYLIHVVRD VNTRLDQLGK QQQQQQQLQQ SAPNDYVPDY SMQPMTMLPG
MGGLALMPPA PNCTPSHQTF GQFSETMVLF GSCKHPSSVG TPASVAISAG LLSELMEGPA
EGRSLD
//
