ID A0A0N4UKK1_DRAME Unreviewed; 1689 AA.
AC A0A0N4UKK1;
DT 09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT 08-JUN-2016, sequence version 2.
DT 27-MAR-2024, entry version 31.
DE RecName: Full=Clathrin heavy chain {ECO:0000256|PIRNR:PIRNR002290};
GN ORFNames=DME_LOCUS2301 {ECO:0000313|EMBL:VDN52328.1};
OS Dracunculus medinensis (Guinea worm).
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Spirurina; Dracunculoidea; Dracunculidae; Dracunculus.
OX NCBI_TaxID=318479 {ECO:0000313|Proteomes:UP000038040, ECO:0000313|WBParaSite:DME_0000827101-mRNA-1};
RN [1] {ECO:0000313|WBParaSite:DME_0000827101-mRNA-1}
RP IDENTIFICATION.
RG WormBaseParasite;
RL Submitted (APR-2016) to UniProtKB.
RN [2] {ECO:0000313|EMBL:VDN52328.1, ECO:0000313|Proteomes:UP000274756}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
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; UYYG01000054; VDN52328.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0N4UKK1; -.
DR STRING; 318479.A0A0N4UKK1; -.
DR WBParaSite; DME_0000827101-mRNA-1; DME_0000827101-mRNA-1; DME_0000827101.
DR Proteomes; UP000038040; Unplaced.
DR Proteomes; UP000274756; 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; 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; 4.
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:UP000274756};
KW Repeat {ECO:0000256|ARBA:ARBA00022737}.
FT DOMAIN 331..354
FT /note="Clathrin heavy chain linker core motif"
FT /evidence="ECO:0000259|Pfam:PF09268"
FT COILED 1606..1636
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 1689 AA; 193181 MW; A65CC48C3404F18C CRC64;
MATPLPIKFQ EHISLQNLGI NAANIGFATL TMESDKFIVV REKIGDSSQV VIIDLNDISN
PLRRPITADS VIMNPATKVL ALKSNKTLQI FNIELKSKMK AYNMPEEVTF WKWVNMNTIA
IVSETSVYHW SLQGDSIPVK TFERHATLNG FQIINYRADF DCKWLLLIGI AARDNRVVGA
MQLYSTERKV SQPIEGHAAC FVPFKMEGNP NPSNLFCFSV RTTQGGKLHI IEVGTTTTQN
KPFQKKQVDV YYPAEAASDF PVAMQASSKQ GIVYLVTKYG YVHLYDIETA VCIYMNRISS
ETIFVTAEYT ITEGIIGVNR KGQVLSVSID ENNMIPYVTQ TLQNPELALK LAIRCDLPGA
EELFVRKFNL LFANGNYSEA AKVAATAPRG ILRTPQTIQK FQQCPATASG GPSPLLQYFG
ILLDQGQLNK YETLELCKPV VAQGRKQLLE KWLTEGKLDC SEELGDLIKP HDVNIALSVY
LRGNVPHKVV QCFAETGQFE KIILYAKKVN FEPDYLFQLR QILRSNPDVG AKFAQMLVTE
GGDEPLADIN QIVSCFEEVQ AIPQCTSFLL EVLKRDNESE GYLQTKLLEM NLLYAPQVAD
AILGNQMFHH YDRAAIGQLC EKAGLLQRAL EHFTDLYDIK RTVVHTQHLK PDWLVNYFGQ
LSVDDSLECL KAMLQTNMRQ NLQIVVQIAT KYHEQLTTNA LIDLFESFKS YEGLFYFLGA
IVNFSQDPEV HFKYIQAATR TGQIKEVERL CRESNCYEAE RVKNYLKEAK LTDQLPLIIV
CDRHGMVHDL VLYLYRNNLQ KYIEVFVQKV NPSRLPIVVG GLLDVDCSED AIKQLIINTR
GKFDIDELVE EVEKRNRLKL LAPWLEMRVQ EGMTDAATHN ALAKIYIDAN NNPERFLREN
PYYDSRVVGK YCEKRDPHFA CLAYERGQCD LELINVCNEN SLFKNLSRYL VKRRDFVLWA
QVLAEDNQHR RQLIDQVVQT ALSETQDPED ISATVKAFMA ADLPNELIEL LEKIVLDNSA
FSEHRNLQNL LILTAIKADR SRVMEYIQKL DNYDAPDIAN IAVSNELYEE AFAIFKKFDV
NTAAINVLID NVVNLDRAYE FAERCNEPGV WASLAKAQLK EGLVKEAVDS FIKADDPTAY
MEVVCKCAET DSWEDLVRYL QMARKKSRES YIETELVYAY AKTNRLTDLE EFISGPNHAQ
IQQIGDRCFD NEMYEAAKIL FNSISNFAKL SVTLVRLGEF QGAVDAARKA NSTKTWKQVC
FACVDNEEFR LAQICGLHIV VHADELEELN NYYQERGHFE ELIGLLEAAL GLERAHMGMF
TELAILYSKY KPEKMREHLE LFWSRVNIPK VLRAAEHAHL WSELVFLYDK YEEYDNAAQT
MMQHPTEAWR EQHFKEVITK VANIELYYKA MQFYLDYKPL LLNDLLIVLT PRLDHSRTVS
FFHKLDQLPL IKPYLRQVQT QNNKSVNEAL NQVLIEEEDY ASLRASIDAY DNFDNIALAQ
QLEKHELIEF RRISAYLYKG NNRWKQSVEL CKKDKLYKDA MEYAAESRQP EIAEELLAFF
LDNKLYDCFA ASLYQMYDLL HPDVIMELAW KHKIMDFAMP YMIQVMRDYH NRIDKLERAE
AERKEEVREK QQQNGGMIEP QLMLTFGGAP MNALPQIPGT YVAPGGSYGG SPAPGMYGAA
IYPGGSYAM
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