ID A0A1I8AX39_9BILA Unreviewed; 1672 AA.
AC A0A1I8AX39;
DT 18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT 18-JAN-2017, sequence version 1.
DT 27-MAR-2024, entry version 28.
DE RecName: Full=Clathrin heavy chain {ECO:0000256|PIRNR:PIRNR002290};
OS Steinernema glaseri.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Tylenchina; Panagrolaimomorpha; Strongyloidoidea; Steinernematidae;
OC Steinernema.
OX NCBI_TaxID=37863 {ECO:0000313|Proteomes:UP000095287, ECO:0000313|WBParaSite:L893_g9975.t1};
RN [1] {ECO:0000313|WBParaSite:L893_g9975.t1}
RP IDENTIFICATION.
RG WormBaseParasite;
RL Submitted (NOV-2016) to UniProtKB.
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 WBParaSite; L893_g9975.t1; L893_g9975.t1; L893_g9975.
DR Proteomes; UP000095287; Unplaced.
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; 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 Cytoplasmic vesicle {ECO:0000256|ARBA:ARBA00023329,
KW ECO:0000256|PIRNR:PIRNR002290};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|PIRNR:PIRNR002290};
KW Repeat {ECO:0000256|ARBA:ARBA00022737}.
FT DOMAIN 328..351
FT /note="Clathrin heavy chain linker core motif"
FT /evidence="ECO:0000259|Pfam:PF09268"
FT REGION 1617..1672
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1653..1672
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1672 AA; 190632 MW; C8C4377571A617D0 CRC64;
MIPIKFEEHL SLQNVGVSLN NIGFATLTME SDKYIVVREK VGDSSQVVII DLADPTNPNR
RPITADSVIM NPDRKILALK SARTLQIFDL ESKQKLKSHN STEDIGFWKW MNNKLIGMST
DSGVYHWSLE GDSPPVKVFE RHQTMISSQI INYRMDADGK FLLLIGIGPK DNRVVGQMQL
YSTERKVSQP IEGHAACFVK VKVENNPHPS NLFCFAVRNQ TGGKLHIIEV GTPMTGNNAF
QKKQVDVYFP TEAQSDFPVA MQASAKHGLV YLVTKYGYVH LYDIETGTCI FMNRISSDTV
FITTEYTLTG GIMGVNRKGQ VLSVSINEQT MIPYVTQNLQ NPDLALRLAV RCDLPGAEEL
FVRKFNLLFG NGNYQEAAKV AATAPKGILR TPQTIQQFQQ CPSPPGGGAT PLLQYFGMLL
DQGQLNKFET LELCRPVLQQ GRKQLLEKWL QENKLECSEE LGDLVRPHDP NIALSVYLRG
NVPHKVVQCF AETGQFDKII LYAKKVGFEP DYLFQLRQVL RTNPDKAADF AKMLSTEGGD
EPLADLNQIV DCFAEVQAIK QCTSFLLEAL RGDRESEGHL QTRLLEMNLV HAPQVADAIL
GNKMFNHYDR AVVGQLCEKA GLLQRALEHF TDLYDIKKAV IHTSLLNTEW LVNYFGSLSV
DDSLECLKAM LHANMRQNLQ VVIQIASKYH EQLTAPALID LFESFKNFEG LYYFLGSIVN
FSQDPEVHFK FIQAACRTGQ VKEVERICRD SNCYDAERVK NYLKEAKLSD QLPLIIVCDR
HEMVHDLVLY LYQNSLQKYI EVFVHKVNPA RLPIVVGALL DVDCSEDAIK QLIVNTRGKF
DIDELVKEVE NRNRLKILAP WLETRVQEGN TDPATHNAIA KIYIDSNNNP DRFLRENAYY
DPLVVGRYCE KRDPHFAYLA YERGGCDQEL ISVCNENSLF KNLARYLVRR RDMALWGQVL
SESNPYRRQL IDQVVQTALS ETQDPEDISA TVKAFMAADL PNELIELLEK IVLDNSAFSE
HRNLQNLLIL TAIKADTSRV MEYIQKLDNY DAPDIANIAI GSNLYEEAFA IFKKFDVNTS
AISVLIDNVN NLDRAYEFAE KCNEPAVWAF LAKAQLKENL VKEAVDSFIR ADDPGSYLDV
VAKCTETESW EDLVRYLQMA RKKSRDSFIE TELAFAYAKT NRLTDLDEFI AGPNHAQVIQ
VGDRCFDMGM YEAAKSLYNS VSNFAKLSVT LVRLGEYQSA VDAARKANST KTWKQVCFAC
VDKEEFRLAQ LCGLYIVVHA DELEELINYY QDRGFFKELI ALLEGALGLE RAHMGMFTEL
AILYSKFKPE KMREHLELFW SRVNIPKVLR AAEKAHLYSE LVFLYDKYEE YDNAANTMMS
HPTEAWREQH FKDVIAKVAN VELYYKAMQF YLDFKPMLLN DLLVVLSPRL DHSRTVSFLT
KANQLPLVKP YLRQVQNLNN KSVNESLNQL FIDEEDYEAL RTSINAYDNF DNIGLASKLE
NHELVEFRRI SAYLFKGNNR WKQSVELCKK DKLYKDAMEF AAESHDSAIA EELLAYFLEN
KLYDCFSAAL YTCYDLLNPD TIMELAWKHK IMDYAMPYMF QVLREYRTRI ENLEKAEAER
KQETSESQQN GGMGETPLML TYGAHQMTPS NPMAPNPMAP PVPPQNPYGG FF
//
