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Database: UniProt
Entry: A0A0N1I0L8_LEPSE
LinkDB: A0A0N1I0L8_LEPSE
Original site: A0A0N1I0L8_LEPSE 
ID   A0A0N1I0L8_LEPSE        Unreviewed;      1698 AA.
AC   A0A0N1I0L8;
DT   09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT   09-DEC-2015, sequence version 1.
DT   24-JAN-2024, entry version 33.
DE   RecName: Full=Clathrin heavy chain {ECO:0000256|PIRNR:PIRNR002290};
GN   ORFNames=ABL78_2636 {ECO:0000313|EMBL:KPI88274.1};
OS   Leptomonas seymouri.
OC   Eukaryota; Discoba; Euglenozoa; Kinetoplastea; Metakinetoplastina;
OC   Trypanosomatida; Trypanosomatidae; Leishmaniinae; Leptomonas.
OX   NCBI_TaxID=5684 {ECO:0000313|EMBL:KPI88274.1, ECO:0000313|Proteomes:UP000038009};
RN   [1] {ECO:0000313|EMBL:KPI88274.1, ECO:0000313|Proteomes:UP000038009}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 30220 {ECO:0000313|EMBL:KPI88274.1,
RC   ECO:0000313|Proteomes:UP000038009};
RX   PubMed=26317207;
RA   Kraeva N., Butenko A., Hlavacova J., Kostygov A., Myskova J., Grybchuk D.,
RA   Lestinova T., Votypka J., Volf P., Opperdoes F., Flegontov P., Lukes J.,
RA   Yurchenko V.;
RT   "Leptomonas seymouri: Adaptations to the Dixenous Life Cycle Analyzed by
RT   Genome Sequencing, Transcriptome Profiling and Co-infection with Leishmania
RT   donovani.";
RL   PLoS Pathog. 11:E1005127-E1005127(2015).
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:KPI88274.1}.
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DR   EMBL; LJSK01000056; KPI88274.1; -; Genomic_DNA.
DR   EnsemblProtists; KPI88274; KPI88274; ABL78_2636.
DR   VEuPathDB; TriTrypDB:Lsey_0056_0130; -.
DR   OMA; VMEISWR; -.
DR   OrthoDB; 5474327at2759; -.
DR   Proteomes; UP000038009; 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   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   Repeat {ECO:0000256|ARBA:ARBA00022737}.
FT   DOMAIN          334..356
FT                   /note="Clathrin heavy chain linker core motif"
FT                   /evidence="ECO:0000259|Pfam:PF09268"
FT   REPEAT          542..700
FT                   /note="CHCR"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01006"
FT   REPEAT          702..844
FT                   /note="CHCR"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01006"
FT   REPEAT          849..988
FT                   /note="CHCR"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01006"
FT   REPEAT          995..1139
FT                   /note="CHCR"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01006"
FT   REPEAT          1143..1286
FT                   /note="CHCR"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01006"
FT   REPEAT          1291..1437
FT                   /note="CHCR"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01006"
FT   REPEAT          1440..1583
FT                   /note="CHCR"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01006"
FT   COILED          1619..1646
FT                   /evidence="ECO:0000256|SAM:Coils"
SQ   SEQUENCE   1698 AA;  191789 MW;  05536827C949624E CRC64;
     MNSPSVSAEI FQLNSVTGGL HAGSISFKNV TIESEKYVCV RDVQDDGQTS LVIVDLEKRE
     SIRNNVRDAE SCVMNPKSKI LALRSGRNLQ VFDVDASKRL KATLFTDDVA YWHWIDDRTL
     GIVTATAVYH WSLDTAADDA PQHIFDRGAD YDGSVQVLSY RTDEAKKWLV VTGVARDMSG
     AMVGKALLYS VENRSSRVLD GHACCFISTA TPSESRKCNI MCMAWNSPQQ GGNVMIMELP
     TGSKTDLSLP RRLYNIRIQP GDFPVAMHVS DRHKLLTVAT SRGSYALMDI FTGTILTEQQ
     FTQAVVFRGA DDSKVGGVVC VNNQGSVIRI GPNDNGIINY VKSNMQNAEL ALRIASTANL
     GGVDDLFKVQ LENYMRSGNV EEAVRMCLRA PGNSLRTRET LLRFMQMPQQ PGQPPAISTY
     FKIVLAGTNL NEFESVELAR AVVPKGGIGY VKQQFDEGKL TPSEELGDLV QSADGDMALK
     IFHQCNAHAK VLNVLLQRNE TQKAVEYCKR ANFSPDWRVI MNNFIRVAPQ DAVNLGLMLY
     REMGDTPVLS AEEIVDMFVS SQRIQQATEF LLEILRNHND ESTMELQTKL LEMNLKYSHP
     SVAEKIFARN ICQFYDGMKL APLCERAGLY QHAIECYITA QKQDPDLDNL ASIRRCLQQS
     QNFNPEWLVE FFGKLNKQDS LKCLEDLCAN ARQNFKVIVQ VATKYSDALG ATDLIELFLE
     HNLYDVLYYY LGAIVPYTRD PEVHFRYIEA AAELGQMQEL ERMTRESPCY DAERTKNYLK
     NKKLTDLWPF INVCDQHNTV NEMVHYLVET SNESYIEQYV TRRSPGKTPE VVKALIECNT
     SEDFIRNLLS SVGTMCPIEE LVECAEDAGR LHLIKQWLED RRSEKKTDTA LFNALAKIYV
     DIGQSPEQFL NENEYYDAKV VGQYCETRDP NLAYIAYRHG HCSEELIELC HRNGMYKQLA
     RYLVKEQNLD LWANVLSKNS SQRQQLVESV QQTALPETEV SEEVSTTVRA FMNANLTEEL
     TSLLDQIVVH GRFRKNRFLE NLLIMSAVRA RKDKVMEYVT SLEDYDAKDI ANIASGAGMH
     EVAFVVYTRH DMQKESVKVL LQDMNDVSRG RAFAQKVDMP EVWSVLGEYL VKQDEVHEGI
     ECLIKAKNAD LVTEVTAAAE RTNNYGDLIK YLTMARQYSR AKDNKIDTAL VITYAKTGRL
     GELEEFLKVT HNVKIGQIAD RCFDDKLYES ARVLYTVANN YVRLASTEVK LHNLNAAVDA
     ANKAKSISTF KEVNLACIEA GELKLAGICA VPVVLKAEEV SSMCNRYETR GLWEELFTVL
     KNAASLQGAH MAIFTEMGVL LAKYRPEKLV EHVNMYPKKI NTHKMISVCE QHHHWVVLRL
     LHINNEDWLA AANAMMQHYA DAFDHEIFKD VIGHLGASDV VYTAIGFYLK TRPEQLSDFL
     SSLFKRVDPE RVMLEVKKVA PIYVVRTYLE AAQERNAKKV NEALNDLYIE EEDFKALRHS
     VETFNNYDSE ELSSRLEKME LFEFRKIALL LHRKNKRYAH AIAVAKENKL YVEAIDAAAE
     SGDSELVTGL LDYFVKDHPE CFAACLYTCY DLLKPSTVMQ KAWLNQRTEV AMPYMIQVIE
     EYSGKVDRME KSMMDAQTAA KDAARRAGPM QGPGAVPLMI ENAGMPPMGG MAPPVQMGMP
     PPRTNLGVPP QFGSGRPF
//
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