ID A0A0V0TI53_9BILA Unreviewed; 1694 AA.
AC A0A0V0TI53;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 27-MAR-2024, entry version 28.
DE RecName: Full=Clathrin heavy chain {ECO:0000256|PIRNR:PIRNR002290};
GN Name=Cltc {ECO:0000313|EMBL:KRX38700.1};
GN ORFNames=T05_8227 {ECO:0000313|EMBL:KRX38700.1};
OS Trichinella murrelli.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC Trichinellida; Trichinellidae; Trichinella.
OX NCBI_TaxID=144512 {ECO:0000313|EMBL:KRX38700.1, ECO:0000313|Proteomes:UP000055048};
RN [1] {ECO:0000313|EMBL:KRX38700.1, ECO:0000313|Proteomes:UP000055048}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ISS417 {ECO:0000313|EMBL:KRX38700.1};
RA Korhonen P.K., Edoardo P., Giuseppe L.R., Gasser R.B.;
RT "Evolution of Trichinella species and genotypes.";
RL Submitted (JAN-2015) 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|ARBA:ARBA00009535, ECO:0000256|PIRNR:PIRNR002290}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KRX38700.1}.
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DR EMBL; JYDJ01000258; KRX38700.1; -; Genomic_DNA.
DR STRING; 144512.A0A0V0TI53; -.
DR Proteomes; UP000055048; Unassembled WGS sequence.
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; 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 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|ARBA:ARBA00023176, ECO:0000256|PIRNR:PIRNR002290};
KW Cytoplasmic vesicle {ECO:0000256|PIRNR:PIRNR002290};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|PIRNR:PIRNR002290};
KW Reference proteome {ECO:0000313|Proteomes:UP000055048};
KW Repeat {ECO:0000256|ARBA:ARBA00022737}.
FT DOMAIN 328..351
FT /note="Clathrin heavy chain linker core motif"
FT /evidence="ECO:0000259|Pfam:PF09268"
SQ SEQUENCE 1694 AA; 194679 MW; 6652BB9791AC4019 CRC64;
MTTSLPIRFQ EHAQLQNLGI SASNIGFSTV TMESDKYICV KEKVGDSAQV VVIDLNDISN
PMRRPISADS VIMNPVSKVL ALKAGKMLQV FDIDVKSKVK SCQFSEEVVF WRWLDVNNIA
LVSPTSVYHW TMESESVPVK MFDRMQSLND RRIINYKTDS KYMWLLLMGI DSRAVGNMQL
YSMERRVSQV IEGHAACFIN FKFGKNEEPS TLFSFATRQQ AFAKLHIVEV GTAPGKNASY
TKKVVDLFFP AEGQHDFPIA MQGSEKHGVI FIITKCGYIH VYDVEFAVCI YMNRISNETI
FVTTEYQLTS GILGITTKGQ VLSVSIDEQN VIPYITNTLQ NPDLAMRFAA RCDLPGAEDL
FVRKFTTLFN EQRYSEAAEI AAVAPKFILR TPQTIQKFQQ VSKETAGANA ILQYFAILLE
KSRLNKFETI ELCRPVLLQN RVQLIEKWLK ENKLECSEEL GDLIQAQGKD TTLALSVYLR
SHCHPKVILC FAETGSFDKI LLYAKRVGYQ PDYVFLLRQV IQKSGPEKAV EFARMLIKDE
EKPLADLNQI ADCFLEVNLV PQCTAFLLDA LKNDRPSEGP LQTRVLEINL LTNPAVADTI
LQQNIFHHYD RAHIAQLCEK VSLMQRALEH YTDLYDIKRA VVNTQSLNLD WLVNYFGTLS
VEDSMECLKA MLQANIRQNL QAVVKISSKY FEQLTTQALI DLFESFKSYE GLFYFLGSIV
NFSQDPEVHF KYIQAACRTG QIKEVERICR ESTFYEPERV KNFLKEAKLT DQLPLIIVCD
RFDFVHDLVL YLYQNNLHKY IEVFVQKVNS ARLPQVVGAL LDVDCSEDTI KQLILHTRNA
FSIDQLVEEV EKRNRLKLLQ PWLETKVHEG ATDAATHNAI AKIYIDSNNN AERFLRENPY
YDSRVIGKYC EKRDPHLACI AYERGHCDTE LINVCNENSL FKNLSRYMVC RRDSELWNQV
LQESNPYRRQ LIDQVVQTAL SETQDPDDVS VTVKAFMAAN LPNELIELLE KIVLDNGLFS
EHRNLQNLLI LTAIRADRPR VMEYVQRLEN YDAPDIANLA ITSELYEEAF AIYKKFDVNT
SAIKVLIDNI GNLDRAYEFA ERCNESGVWA QLAAAQLRHN MVKEAVDSFI KADDASYYVE
VVQTCSKTDH WEDLVRYLKM ARKKARESFI DTELVFAFAK TKRLAEMEDF VTGPNHAQIL
QVGERCFEEG MYDASKILFN NVSNFAKLAI TMVRLGEYNG SVDAARKANS TKTWKEVCYA
CVDAEQFQLA QTCGLHIVVH AEELEELNTY YQQRGYFEEL INLLEAALGL ERSHMGIFTE
LAILYSKYKP EKMREHLELF WSRVNIPKVL RAAEQAHLWA ELVFLYDKYE EYDNAVVTVM
KHPVEAWREQ HFKEIITKVA NIELYYKAMQ FYLDYKPLLL NDLLTVLAPR MDHTRAVAFF
TKNKHLPLIK PYLRAVQNQN NKAINEALNQ LLIEEEDYAG LRASIDAFDN YDNIALAQQL
EHHELIEFRR ISAYLYKGNN RWKQSVELCK KDKLYKDAIE FAAESRQSEL AEDLISYFLE
NNLKECFAAT LYQCYDLLHP DVILELAWRH DLMDFAMPYM IQVVRELTTT VQTLNEAEAK
RKEEANNVQA QSTDMMMPPQ LMLTYGMNAP AVALPHQQQQ QQQQSAQPGS AAAYSTNAYL
GSALYSSYPG YRMP
//
