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Database: UniProt
Entry: A0A180H6D7_PUCT1
LinkDB: A0A180H6D7_PUCT1
Original site: A0A180H6D7_PUCT1 
ID   A0A180H6D7_PUCT1        Unreviewed;      1705 AA.
AC   A0A180H6D7;
DT   07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT   07-SEP-2016, sequence version 1.
DT   27-MAR-2024, entry version 24.
DE   RecName: Full=Clathrin heavy chain {ECO:0000256|PIRNR:PIRNR002290};
GN   ORFNames=PTTG_01415 {ECO:0000313|EMBL:OAV99983.1};
OS   Puccinia triticina (isolate 1-1 / race 1 (BBBD)) (Brown leaf rust fungus).
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Pucciniomycotina;
OC   Pucciniomycetes; Pucciniales; Pucciniaceae; Puccinia.
OX   NCBI_TaxID=630390 {ECO:0000313|EMBL:OAV99983.1};
RN   [1] {ECO:0000313|EMBL:OAV99983.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=1-1 BBBD Race 1 {ECO:0000313|EMBL:OAV99983.1};
RG   The Broad Institute Genome Sequencing Platform;
RA   Ward D., Feldgarden M., Earl A., Young S.K., Zeng Q., Koehrsen M.,
RA   Alvarado L., Berlin A., Bochicchio J., Borenstein D., Chapman S.B.,
RA   Chen Z., Engels R., Freedman E., Gellesch M., Goldberg J., Griggs A.,
RA   Gujja S., Heilman E., Heiman D., Hepburn T., Howarth C., Jen D., Larson L.,
RA   Lewis B., Mehta T., Park D., Pearson M., Roberts A., Saif S., Shea T.,
RA   Shenoy N., Sisk P., Stolte C., Sykes S., Thomson T., Walk T., White J.,
RA   Yandava C., Izard J., Baranova O.V., Blanton J.M., Tanner A.C.,
RA   Dewhirst F.E., Haas B., Nusbaum C., Birren B.;
RL   Submitted (NOV-2009) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:OAV99983.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=1-1 BBBD Race 1 {ECO:0000313|EMBL:OAV99983.1};
RA   Cuomo C.A., Bakkeren G., Szabo L., Khalil H., Joly D., Goldberg J.,
RA   Young S., Zeng Q., Fellers J.;
RT   "Comparative analysis highlights variable genome content of wheat rusts and
RT   divergence of the mating loci.";
RL   Submitted (MAY-2016) 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}.
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:OAV99983.1}.
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DR   EMBL; ADAS02000001; OAV99983.1; -; Genomic_DNA.
DR   STRING; 630390.A0A180H6D7; -.
DR   VEuPathDB; FungiDB:PTTG_01415; -.
DR   OrthoDB; 5474327at2759; -.
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; 5.
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          336..359
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   1705 AA;  192383 MW;  66015766E93F68F0 CRC64;
     MAEQRPISFC EHVQLTALGV QPASIGFNTL TMESERYVCV REEVNSAKQV IIIDLADANN
     VMRRPISAES AIMHPVQKVI ALRAQRQLQV FNIELKQKVK SHAMNEDVSF WKWINDSTLG
     IVTETAVYHW AALDPTSPPV KVFDRNANLA GHQIINYRAS PDEKWMVLVG ITGNPSNPSA
     FKVKGSMQLY NKDRAVSQSI EGHAASFADY RLEGATTDSK LFAFAVRTAA GAKLHIVEID
     HQAGQPVFAK KAVDVFFPPE ATNDFPVAMQ VSKKHKIIYM VTKYGFIHLY DVETAACIYM
     NRISGETIFV TAEHETSSGI IGVNRKGQVL SVTVDEETIV PFILNTLKNP ELAIKLASRA
     DLPGADDIYV QQFQQLFSSG QFSEAAKVAA NSPRGILRTP QTIEQFKAVP MQPGQLSPIL
     QYFGILLERG KLNQHESLEL ARPVLVQGRK QLLEKWLKED KLDCSEELGD IVRAHDMTLA
     LSVYLRANIP NKVCACFAET GQSSKIVVYA KRVGFTPDYA SLLQHITRLS PDSGAEFASS
     LINDESGPLV DVERVIDIFM AQNMIQQATS FLLDALKENK PEQGYLQTKL LEMNLLNAPQ
     VADAILGNEM FSHYDRPSVA NLCEKAGLLQ RALEHYEDIS DIKRVLVHTN LLNTDWLVNY
     FGKLTVDQTV DCFCEMLKVN IRQNLQIVVQ AATKYSDLVG SVRLIEMFES FKTFEGLYYY
     LGSIVNLSTD PEVHFKYIQA ATRTGQIREV ERICRESNYY PPEKVKNFLK EAKLSDQLPL
     IIVCDRFDFV HDLVLFLYQN GLTSFIEVYV QKVNSQRAPQ VIGGLLDVDA DEMMIKNLLA
     SVTGPIPVDE LVEEVEKRNR LKLILPWLEA RIAMGITDVG LYNAMAKILI DSNQNPEAFL
     KENTIYDPLT IGKYCEKRDP TLAYIAYARG FCDEDLIRIT NENSMFKLQA RYLVKRRQLE
     LWAQVLQPDN MHRRQLVDQV VSTAVPESQN PEDVSVTVKA FLAADLPIEL IELLEKIVLE
     PSPFSDNANL KKLLLLTAIR SEKGKVMGYI DKLEDIDVSE IAGIAIEHGL FEEAFTLFRK
     HKMHLEAMNV LVEHVVSIDR AAQYATKVNE PAVWSRLGKA QLDGLRIKDA IDSYIKADDP
     TNYLELIETA DRAGKHDDMV RYLQMARKTL REPKIDTELC VAYAKTDRLH DMEEFLSMSN
     VADQLSAGEQ VFEAGLYEAA RLLFSAISNW ARLATTLIYL GDNQAAVDCA RKAGNTQVWK
     QVNSACIDKK EFRLAQVCGL NLVVHAEELQ SLVKLYENRG YFEELMQLLE AGLGLERAHM
     GMFTELSILY AKHKPAKLME HLKLFWSRIN IPKVIRATEQ AHLWPELVFL YIHYDEFDNA
     VLAMMERSAD AWDHGQFKDI VVKVANVELY YKALSFYLQE QPTLLTDLLT VLVPRIDHTR
     VVKIFQKTDN LPLIKPYLIA VQHLDLPAIN EAYHDLLIEE EDYATLRDSL SNHDNFDQVS
     LAKRLENHEL LEFRRLAALL YAKNGKFEES IGLSKDDKLF KDAMITAASS ASNEIVEELL
     EYFVKIGNKE CFAACLYICY DLIRPDVVED LQWRHALNDY TMPYRLQQMR EQTSRLEQIE
     RQLKELSLRS AKAVEETESQ PIIGPGFGGR LMLTQGPSNG MMVGQPTGAY GGGPPSAGGM
     MRGMQAQPTG MMGQQFTGMP GMMGF
//
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