ID A0A158QJM0_HAEPC Unreviewed; 1609 AA.
AC A0A158QJM0;
DT 08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT 08-JUN-2016, sequence version 1.
DT 27-MAR-2024, entry version 31.
DE RecName: Full=Clathrin heavy chain {ECO:0000256|PIRNR:PIRNR002290};
GN ORFNames=HPLM_LOCUS3010 {ECO:0000313|EMBL:VDO19954.1};
OS Haemonchus placei (Barber's pole worm).
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Strongyloidea; Trichostrongylidae; Haemonchus.
OX NCBI_TaxID=6290 {ECO:0000313|Proteomes:UP000038042, ECO:0000313|WBParaSite:HPLM_0000301801-mRNA-1};
RN [1] {ECO:0000313|WBParaSite:HPLM_0000301801-mRNA-1}
RP IDENTIFICATION.
RG WormBaseParasite;
RL Submitted (APR-2016) to UniProtKB.
RN [2] {ECO:0000313|EMBL:VDO19954.1, ECO:0000313|Proteomes:UP000268014}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MHpl1 {ECO:0000313|EMBL:VDO19954.1,
RC ECO:0000313|Proteomes:UP000268014};
RG Pathogen Informatics;
RL Submitted (NOV-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; UZAF01016093; VDO19954.1; -; Genomic_DNA.
DR STRING; 6290.A0A158QJM0; -.
DR WBParaSite; HPLM_0000301801-mRNA-1; HPLM_0000301801-mRNA-1; HPLM_0000301801.
DR OMA; HCYDLLH; -.
DR Proteomes; UP000038042; Unplaced.
DR Proteomes; UP000268014; 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; 4.
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: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 Pfam; PF01394; Clathrin_propel; 2.
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 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:UP000268014};
KW Repeat {ECO:0000256|ARBA:ARBA00022737}.
FT DOMAIN 300..323
FT /note="Clathrin heavy chain linker core motif"
FT /evidence="ECO:0000259|Pfam:PF09268"
FT COILED 1580..1607
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 1609 AA; 184210 MW; 7182501F2A6050AD CRC64;
MESDKFIVVR EMIGDSQQVV IIDLADPMNP QRRPISADSV IMHPSAKIIA LKSGKTLQIF
NIELKAKVKA HQNAEDIIFW KWINEKTIAL VSETAVYHWS IEGESAPTKM FERHQSLAGS
QIINYRADLE CKWLVLVGIA AKENRVVGSM QLYSTERRVS QPIEGHAASF VRFKMDGNPH
PSNLFCFSVK NEAGGKLHVI EVGSPPAGNQ PFPKKAVDVP YTAETANDFP VSMQASSKHG
IAYLVTKHGL VHLYDMESGS RIYSNRISTD TVFVTCEYQA TGGIMGINRK GQVLSVSIDE
NNMIPFVTQQ LQNPDLALRL AVRCDLPGAE ELFVRKFNLL FGNGQFAEAA KVAATAPQGI
LRTPQTIQKF QQCPANPGGG ASPLLQYFGI LLDQGKLNKY ETLELCRPVL AQGRKELLNK
WLNDQKLECC EELGDLVRPH DPTVALSIYL RGNVPHKVVQ CFAETGQFDK IILYAKRVGF
EPDYLFQLRQ ILRSGNQEAG AKFAQMMVME SENGEPLADL NQIIDCFMEV QAVQPCTQFL
LEVLKGDKPE EGHLQTRLLE MNLLAAPQVA DAILGNKMFS HYDRPQIGQL CEKAGLLQRA
LEHFTDLYDI KRTVVHTTHF KPDWLVNYFG TLSVDDSLEC LKAMLTQNIR QNLQVVVQIA
SKYHEQLGTD KLIDMFETHK SYEGLFYFLG SIVNFSQDPE VHFKYIQAAT RTGQIKEVER
ICRESNCYDA ERVKNFLKEA KLADQLPLII VCDRHDMVHD LVLYLYRNQL QKYIEVFVQK
VNSARLPIVV GGLLDVDCSE DAIKQLILNT RGKFDIDELV AEVEKRNRLK LLSHWLESRV
QDGATDAATH NAMAKIYIDA NNNPDRFLRE NPYYDSRVVG KYCEKRDPHF AFLAYERGQC
DAELIAVCNE NSLFKNLARY LVRRRDYGLW EQVLNEENQY RRQLIDQVVQ TALSETQDPE
DISATVKAFM AADLPNELIE LLEKIVLDNS AFSEHRNLQN LLILTAMRAD RSRVMEYIQK
LDNYDAPDIA NIAISSELYE EAFAIFKKFD VNNSAINVLI DNVANLDRAY EFAEKCNQSD
VWASLAKAQL RQDMVKEAVD SFIRADDPGA YMEVVSKCTQ TEHWEDLVRF LQMARKKSRE
SYIETELVYA YAKTGRLTEL EEFISGPNHA QIGLIGDRCF DNGMYEAAKI LFNNISNFAK
LSVTLVRLGE YQGAVDAARK ANSTKTWKQV CFACVENGEF RLAQMCGLHI VVHADELEEL
NNFYQDRGHF EELIGLLEAA LGLERAHMGM FTELAILYSK YKPEKMREHL ELFWSRVNIP
KVLRAAEHAH LWAELVFLYD KYEEFDNAAL TMMQHPTESW REQHFKEVIA KVANVELYYK
AMQFYLDYKP LLINDLLAVL SPRLDHSRTV QFFSKLKHIP LIKPYLKQVQ NLNNKAINEA
LNQLLIDEED HAGLRASIDS HDNFDNIALA QQLENHPLVE FRRISAYLFK GNNRWKQSIE
LCKKDKLYKD AMEYAAESRS SELAEELIAF FLDERLYECF AAALYHCYDL LHPHVILELA
WKNKITDYAM PYMVQVFRDF QIRIERLERA EAERKDEQRE QQQQNGMTS
//
