ID U6H1D6_9EIME Unreviewed; 1701 AA.
AC U6H1D6;
DT 22-JAN-2014, integrated into UniProtKB/TrEMBL.
DT 22-JAN-2014, sequence version 1.
DT 27-MAR-2024, entry version 36.
DE RecName: Full=Clathrin heavy chain {ECO:0000256|PIRNR:PIRNR002290};
GN ORFNames=EPH_0001910 {ECO:0000313|EMBL:CDI86270.1};
OS Eimeria praecox.
OC Eukaryota; Sar; Alveolata; Apicomplexa; Conoidasida; Coccidia;
OC Eucoccidiorida; Eimeriorina; Eimeriidae; Eimeria.
OX NCBI_TaxID=51316 {ECO:0000313|EMBL:CDI86270.1};
RN [1] {ECO:0000313|EMBL:CDI86270.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Houghton {ECO:0000313|EMBL:CDI86270.1};
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:CDI86270.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Houghton {ECO:0000313|EMBL:CDI86270.1};
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; HG695046; CDI86270.1; -; Genomic_DNA.
DR EnsemblProtists; CDI86270; CDI86270; EPH_0001910.
DR VEuPathDB; ToxoDB:EPH_0001910; -.
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 1701 AA; 190509 MW; C4C803EC606C7509 CRC64;
MAQQLPVQLT PIVNLADTGV KSASFRFGNV AVDGDKHLVV RDVESNELYF VSLNPKEALE
APGSPGAYSV SKKPTQAEAA LHHPTDPIVA LRAKADGGQQ VVQVLNLETK ARMGTAPMSE
SVVYWRWVAP RVLALVTDKA VWHWTLGEGA EAGEPQKICE REGRLAEGVQ IIGYSTDKEM
KWCVLTGIST QDGGKTIDGS LQLYSMELKK HQQLEGHAAC FGGLVVDEAQ GPQPVICFAE
KKRGSPEFKL HVRDLAPKRE DGKPPLRVCT DISLSPDAPS DFPLAVHLSK KLGLVFLVTK
GGFLLLFDAF TGTQLLRHRI SQDPVFLTAD SPQTGGVITV HKKGVVALTT VSVGLLGPYM
QHALPHLPNR AQIYLSLAKR YGLPGADDAL VQAFNQHFAS GDYRGAARIC ATLKSGRLRT
PQVLQQFKSV PAQPGQTSAI LLYFSTLLEY GSLNAVESLE LVRPVVAQGR KDFVTTWLRE
DKLECTEELG DVLRPLDSAL ATQVYKKAKA GQKVMLMLVE QGKTDELLEY AAQTRMQADY
SALLRTMLAT NPEGAMAFAQ KLLATEPPLV DPNQVVDVLL QQQRFQELSS LLLEYLKGNK
PEQGPLQTRL FEINLKHSPQ VAEAIFQMEM LTHYDRQKVG ALCEAAGLYQ RALENYTELA
DVKRVLLQTG GKISQEWMVQ FFGRMAPEVC VEILTDMLRS SSQNLQAVVG VAIKFHEKLG
TERLIAMFER FSSYEGIFYF LGSILAFSTD PEVHFKYIEA AAKLNHTQEV ERVCRESKHY
EPQRVKEFLK QANLSDPRPL IYVCDLHGFV VELTEYLYKH SLLRYIEVYV SRVNSANAPM
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 LVKANDGEVF REVVEKATEQ GAFEALADYL LMARKSITIK
DQTLDSELLY SYAMTERLED LEMFLNGPNT ANVQAVGDRL FEQGRYEAAK ILYQSLPNYS
KLASCFVRMK DFGAAVDAAR KAKNPKTWKE VAFGALNNGD IKCAHTAGLQ LIAHPDLLDA
LVEEYERWGL HKQLMELLET GAQGERTHVG LFTELGVLYA TYDSTKLMDH CKQHKARMNI
PRLIRTCEKC CLWKEAVYLH TIYDEYEQAA NCMILHPTAW QHDQFIQVVQ KVSNVELLYR
AISFYLEEHP LQLCALLKGI DRKVDHSRVV QQLRKAGHLP LIEKYLQEQL PLNVAAVNEA
MLELLVEAQD EERIRELISE CDNFDQLGLA KQLEGHNELG LRRIAALLYQ KNKKYSLAME
LSKKDAQLQD CIETAKESGS AQLVEDLLKY FLTELKDPEA FAACLHSCCD LVKPDVALEL
AWRHKVVDFI MPYLIHVVRD VNTRLDQLDK QQQQQQQLQQ SAPNDYVPDY SMQPMTMLPG
MGGLALMPPA SNCTPSHQTF G
//
