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Database: UniProt
Entry: A1CH82_ASPCL
LinkDB: A1CH82_ASPCL
Original site: A1CH82_ASPCL 
ID   A1CH82_ASPCL            Unreviewed;      1663 AA.
AC   A1CH82;
DT   23-JAN-2007, integrated into UniProtKB/TrEMBL.
DT   23-JAN-2007, sequence version 1.
DT   27-MAR-2024, entry version 92.
DE   RecName: Full=Clathrin heavy chain {ECO:0000256|PIRNR:PIRNR002290};
GN   ORFNames=ACLA_047060 {ECO:0000313|EMBL:EAW10237.1};
OS   Aspergillus clavatus (strain ATCC 1007 / CBS 513.65 / DSM 816 / NCTC 3887 /
OS   NRRL 1 / QM 1276 / 107).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Fumigati.
OX   NCBI_TaxID=344612 {ECO:0000313|EMBL:EAW10237.1, ECO:0000313|Proteomes:UP000006701};
RN   [1] {ECO:0000313|EMBL:EAW10237.1, ECO:0000313|Proteomes:UP000006701}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 1007 / CBS 513.65 / DSM 816 / NCTC 3887 / NRRL 1
RC   {ECO:0000313|Proteomes:UP000006701};
RX   PubMed=18404212; DOI=10.1371/journal.pgen.1000046;
RA   Fedorova N.D., Khaldi N., Joardar V.S., Maiti R., Amedeo P., Anderson M.J.,
RA   Crabtree J., Silva J.C., Badger J.H., Albarraq A., Angiuoli S., Bussey H.,
RA   Bowyer P., Cotty P.J., Dyer P.S., Egan A., Galens K., Fraser-Liggett C.M.,
RA   Haas B.J., Inman J.M., Kent R., Lemieux S., Malavazi I., Orvis J.,
RA   Roemer T., Ronning C.M., Sundaram J.P., Sutton G., Turner G., Venter J.C.,
RA   White O.R., Whitty B.R., Youngman P., Wolfe K.H., Goldman G.H.,
RA   Wortman J.R., Jiang B., Denning D.W., Nierman W.C.;
RT   "Genomic islands in the pathogenic filamentous fungus Aspergillus
RT   fumigatus.";
RL   PLoS Genet. 4:E1000046-E1000046(2008).
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|PIRNR:PIRNR002290}.
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DR   EMBL; DS027054; EAW10237.1; -; Genomic_DNA.
DR   RefSeq; XP_001271663.1; XM_001271662.1.
DR   STRING; 344612.A1CH82; -.
DR   EnsemblFungi; EAW10237; EAW10237; ACLA_047060.
DR   GeneID; 4704135; -.
DR   KEGG; act:ACLA_047060; -.
DR   VEuPathDB; FungiDB:ACLA_047060; -.
DR   eggNOG; KOG0985; Eukaryota.
DR   HOGENOM; CLU_002136_0_0_1; -.
DR   OMA; HCYDLLH; -.
DR   OrthoDB; 5474327at2759; -.
DR   Proteomes; UP000006701; 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; 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; PF13838; Clathrin_H_link; 1.
DR   Pfam; PF01394; Clathrin_propel; 3.
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|PIRNR:PIRNR002290};
KW   Cytoplasmic vesicle {ECO:0000256|ARBA:ARBA00023329,
KW   ECO:0000256|PIRNR:PIRNR002290}; Membrane {ECO:0000256|PIRNR:PIRNR002290};
KW   Reference proteome {ECO:0000313|Proteomes:UP000006701}.
FT   REGION          1606..1663
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1620..1636
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1663 AA;  189647 MW;  3832135AE5311D06 CRC64;
     MAPLPIKFTE LINTLESDHY VCVRQKLNED DKPQVIILNL KNNNEVIKRP INADSAIMHW
     SKNIIALRAQ GRTIQIFDLT AKQKLKSAVM NEDVVYWKWF SEKCLGLVTE ASVYHWDVFD
     PTQNQPIKIF DRLPNLSGCQ IINYRVNDDE KWMVVVGISQ QQGRVVGSMQ LYSKDRGISQ
     FIEGHAAAFA SIRVEGSPLE HKLFTFAVRT QTGAKLQIAE IDHQEPNPRF QKKAVEVYFP
     QEAVNDFPVA MQVSRKYDIV YLVTKYGFIH LYDLETGTCI FMNRISSETI FTTAPDSDSA
     GLVGVNRKGQ VLSVSVDEGT IIQYLMENPA MSGLAVKLAS KAGLPGADHL YQQQFDNLLA
     QGNYSEAAKI AANSPRGFLR TPETINRFKN APQTGQQMSV ILQYFGMLLD KGSLNKYESV
     ELVRPVLQQN RKHLLEKWTR ENKLEASEEL GDIVRPYDMN MALSIYLQAN VPNKVIAGFA
     ETGQFDKILS YSKQVGYQPD YTQLLQHIVR VNPEKGAEFA AQLANEESGA LIDLDRVVDV
     FLSQNMIQQA TSFLLDALKD NKPEHGHLQT RLLEMNLVNA PQVADAILGN EIFTHYDRPR
     ISQLCENAGL IQRALENTDD PAVIKRNIVR TDKLNPEWLM NYFGRLSVEQ TIECMDTMLE
     VNIRQNLQAV VQLATKFSDL LGPGRLISLF EKYRTAEGLY YYLGSIVNLS EDPEVHFKYI
     EAATAMGQLT EVERICRESN YYNPEKVKNF LKEARLTEQL PLIIVCDRFN FIHDLVLYLY
     QNQQYKSIEV YVQRVNPSRT PAVVGGLLDV DCDEAIIKNL LSTVEPSVIP IDELVSEVES
     RNRLKLLLPF LEATLASGNQ QQAVYNALAK IYIDSNNNPE KFLKENDLYD TLTVGKYCEK
     RDPNLAYVAY RKGQNDLELI NITNENSMYR AQARYLVERA DSEIWSFVLS ENNLHRRSLV
     DQVIATAVPE STEPDKVSVA VKAFLEADLP GELIELLEKI ILEPSPFSDN GSLQNLLMLT
     AAKADKGRLM DYIHQLSEFS ADEIAEMCIS VGLYEEAFEI YKKVNNYIAA VNVLVENIVS
     IDRAQEFAER VELPDVWSKV AKAQLDGLRV SDSIESYIRA NDPSNYNEVI ETAIHAGKDE
     DLVKYLKMAR KTLREPAIDT ALAFCYARLD QLLELEDFLR STNVADIETS GDKAYAEGYH
     QAAKIFYTSI SNWAKLATTL VHLEDYQAAV ECARKANSVK VWKEVNLACV DKKEFRLAQI
     CGLNLIVHAE ELQDLVRQYE RHGYFDELIS VLEAGLGLER AHMGMFTELG IALSKYHPDR
     VMEHLKLFWS RINIPKMIRA CEEANLWPEL VFLYCHYDEW DNAALAMMER AADAWEHHSF
     KDIIVKVANL EIYYRALNFY LQEQPLLLTD LLQVLTSRID VNRVVRIFQT SDNIPLIKPF
     LLNVQNQNKR TVNDAINDLL IEEEDYKTLR DSVDNYDNFD AVELAQRLEK HDLIFFRQIA
     ANIYRNNKRW EKSIALSKQD KLYKDAIETA AISGKSDVVE ELLRYFVDIG SRECYVGMLY
     ACYDLIRPDV ILEMSWRHGL NDFTMPFMIN FLCEQTRTIE MLKKDNEERK SREVTQQKEE
     DNTPILGGSR LMLTQGPSTP APAPMAYGQP NGIAPQATGF RPF
//
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