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Database: UniProt
Entry: S9V6R4_9TRYP
LinkDB: S9V6R4_9TRYP
Original site: S9V6R4_9TRYP 
ID   S9V6R4_9TRYP            Unreviewed;      1700 AA.
AC   S9V6R4;
DT   16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT   16-OCT-2013, sequence version 1.
DT   27-MAR-2024, entry version 39.
DE   RecName: Full=Clathrin heavy chain {ECO:0000256|PIRNR:PIRNR002290};
GN   ORFNames=STCU_08194 {ECO:0000313|EMBL:EPY22636.1};
OS   Strigomonas culicis.
OC   Eukaryota; Discoba; Euglenozoa; Kinetoplastea; Metakinetoplastina;
OC   Trypanosomatida; Trypanosomatidae; Strigomonadinae; Strigomonas.
OX   NCBI_TaxID=28005 {ECO:0000313|EMBL:EPY22636.1, ECO:0000313|Proteomes:UP000015354};
RN   [1] {ECO:0000313|EMBL:EPY22636.1, ECO:0000313|Proteomes:UP000015354}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=23560078;
RA   Motta M.C., Martins A.C., de Souza S.S., Catta-Preta C.M., Silva R.,
RA   Klein C.C., de Almeida L.G., de Lima Cunha O., Ciapina L.P., Brocchi M.,
RA   Colabardini A.C., de Araujo Lima B., Machado C.R., de Almeida Soares C.M.,
RA   Probst C.M., de Menezes C.B., Thompson C.E., Bartholomeu D.C., Gradia D.F.,
RA   Pavoni D.P., Grisard E.C., Fantinatti-Garboggini F., Marchini F.K.,
RA   Rodrigues-Luiz G.F., Wagner G., Goldman G.H., Fietto J.L., Elias M.C.,
RA   Goldman M.H., Sagot M.F., Pereira M., Stoco P.H., de Mendonca-Neto R.P.,
RA   Teixeira S.M., Maciel T.E., de Oliveira Mendes T.A., Urmenyi T.P.,
RA   de Souza W., Schenkman S., de Vasconcelos A.T.;
RT   "Predicting the Proteins of Angomonas deanei, Strigomonas culicis and Their
RT   Respective Endosymbionts Reveals New Aspects of the Trypanosomatidae
RT   Family.";
RL   PLoS ONE 8:E60209-E60209(2013).
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:EPY22636.1}.
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DR   EMBL; ATMH01008194; EPY22636.1; -; Genomic_DNA.
DR   EnsemblProtists; EPY22636; EPY22636; STCU_08194.
DR   OrthoDB; 5474327at2759; -.
DR   Proteomes; UP000015354; 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; 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; 6.
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:UP000015354};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737}.
FT   DOMAIN          338..356
FT                   /note="Clathrin heavy chain linker core motif"
FT                   /evidence="ECO:0000259|Pfam:PF09268"
FT   REGION          1635..1700
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1667..1688
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1700 AA;  190739 MW;  27420CDA55400A73 CRC64;
     MANSPLGINE VFQLNSVNGG LRPGSVSFKN VTITSDKYVC VRDVQQEGQV SLVIVDLEKR
     ESMRNNVRDA ESAVMNPAKK ILALRSGRNL QIFDVEASKR LKAVVFTDDV LYWSWVDEKT
     VGIVTGTAVY HWDLEGAADG SPTRFFDRPA DYDAAVQVLS YKVDADKRWA VVCGVTRDAS
     GAMVGKALLY SVDNAVARVM EGHAVTFIST ATPSDSRKSN IMCLAWNSPQ QGGQVMIMEL
     PTASKSDITV PRRVYPVQIA QGDFPVALHV SERHKLLTGI TSRGKCFLMD VFTGTLLYEQ
     QFTQAVIFSG AGDKRTGGVV MVNNQGAVVR VGPDDGSIIN YVKNRMQNAG LALRIAGTAN
     LGGVDDLFRV QLDNCLRSGN VEEAIRVCLK APNNSLRTRE VLTRFLQLPQ QPGQAPAIST
     YFKMALAEGS LNESESVELA RAVVPKGGVA YVKQQFDEGK LTASEELGDL VAQADPDMAM
     KLFHSGSAHA KVVNVLLQRN ETQKAVEYCK RANYTPDWRV IMQNFVRVNP QDAVNLGVML
     YRDLADKPVI DAGEMVDMFV SSQHTQQATE LLLEILRDHN GEDTMDLQTK LLEINLKYSH
     PSVSEKIFAR NICQFYDGMK LAPLCERTGL HQRAIECYIT AQKQDPDLDN LANIRRCLQQ
     AQTFNPEWLV EFFGKLNKED SLKCLSDLTE NARKNFKVMV QVATKYNDAL GAKELIDLFL
     DKNLYDVLYY YLGAIVPYTR DPEVHFRYIE AAAEMGQMQE LERMTRESPC YDAERTKNYL
     KNKKLTDLWP FINVCDQHDM IGEMVHYLVE TGNEACIEQF VTRRSPAKAP QVAKALIECN
     VSEEFIKSVL NAVGSMCPVE ELVAATEEVG RLHLIKEWLE ERKNEKKTDR ALFTALAKIY
     VDIGQRPEEF LASNDYYDAE VVGTYCESRN PNLAFVAYMK GHASVPLIDL CRRNGLYKQE
     ARYLVREQNL ELWAEVLASD DADRRQLIDA VQQTALPESE VSEEVSTTVR AFMNANLTEE
     LTSLLDQIVV HGRFRKNRFL ENLLIMSAVR ARKDRVMEYV TGLEDYDAKD IANIATGAGM
     HDVAFVVYDK HGLHKEAAHV LLHDLNDVAR GRAYTQKVDQ PAVWSELGAH LVSVDEVHEG
     IECLIKAKNA ELVQEVTSAA ERTNQYGDLI KYLTMARKYS KTKDNKIDTA LVITYAKTGR
     LGELEEFLKE THNVKIAAIA DKCFADELYE SAKVLYSVGN NFAKLALTEV KLHNLAAAVE
     AANKAKSTTT FKEVNLACIE AKEMKLASIC AVPVVLRAEE VSGMCNRYES RGLWEDLYNV
     LKTAAGNQGA HMGVFTEMGV ILAKYRPEKL LEHINMYLKK LNTHKMLSVC EQYHHWVPLR
     VLHVNNEDYL AAANCMMEHY ADAWDHEIFK DVINHLGSSD VVYVAIGFYL KTHPELLNDF
     LTAVFKKVDP ERVMVEVRRR APIYIIRQYL QAAQERNAKN VNEALNTLYM EEEDFNALRH
     SVETYNNFDA QELTAVLEKK EMFEFRRIAL LLHRRNKRFA HAIAVAKENK LYEEAIATAA
     ESSDAEIVDD LLDFFAKDFP ECFAACLYTC YDLLEPASVL QKAWLYGRTE IAMPYLVQAI
     QEFTGKVNRM ERSMTDAQSA AKDAARRAGP AAGGPGPLMI EQGTGVPPPN MMPPPQAMHM
     PPPQQAHYGA PPQFGSGRPF
//
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