ID G2XJH5_VERDV Unreviewed; 1679 AA.
AC G2XJH5;
DT 16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT 16-NOV-2011, sequence version 1.
DT 27-MAR-2024, entry version 60.
DE RecName: Full=Clathrin heavy chain {ECO:0000256|PIRNR:PIRNR002290};
GN ORFNames=VDAG_10376 {ECO:0000313|EMBL:EGY20678.1};
OS Verticillium dahliae (strain VdLs.17 / ATCC MYA-4575 / FGSC 10137)
OS (Verticillium wilt).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Glomerellales; Plectosphaerellaceae; Verticillium.
OX NCBI_TaxID=498257 {ECO:0000313|EMBL:EGY20678.1};
RN [1] {ECO:0000313|EMBL:EGY20678.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=VdLs.17 {ECO:0000313|EMBL:EGY20678.1};
RG The Broad Institute Genome Sequencing Platform;
RA Ma L.-J.J., Klosterman S.J., Subbarao K., Dobinson K., Veronese P.,
RA Kang S., Gold S.E., Young S., Jaffe D., Gnerre S., Berlin A., Heiman D.,
RA Hepburn T., Sykes S., Alvarado L., Kodira C.D., Lander E., Galagan J.,
RA Nusbaum C., Birren B.;
RT "The Genome Sequence of Verticillium dahliae VdLs.17.";
RL Submitted (MAR-2008) 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|PIRNR:PIRNR002290}.
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DR EMBL; DS572729; EGY20678.1; -; Genomic_DNA.
DR RefSeq; XP_009658140.1; XM_009659845.1.
DR STRING; 498257.G2XJH5; -.
DR EnsemblFungi; EGY20678; EGY20678; VDAG_10376.
DR GeneID; 20711839; -.
DR KEGG; vda:VDAG_10376; -.
DR eggNOG; KOG0985; Eukaryota.
DR HOGENOM; CLU_002136_0_0_1; -.
DR InParanoid; G2XJH5; -.
DR OMA; HCYDLLH; -.
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; 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}.
FT REGION 1624..1679
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1624..1639
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1659..1673
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1679 AA; 190049 MW; 8B7B06B78A255133 CRC64;
MAALPIRFEE LVQLKSVGVE DSSITFNSCT LESDAYVCIR EQKGDASPEV VIVDLKNGNN
VTRRPIKADS AIMHWSRQVI ALKAQSRTLQ IFDLEQKQKL KSATMNEDVQ YWKWVTETTL
GLVTESSVFH WDVYDPSQAA PVKIFERNAN LSGCQIINYR TNVDNKWMVV VGIAQREGRI
VGAMQLYSKD RGISQAIEGH AAAFGTIRLE GAPADTKLFT FSVRTATGAK LHVVEVDHAE
SNPVFQKKAV DVYFPPEATN DFPVAMQVSQ KYGVIFMVTK YGFIHVYDLE SGSCIFMNRI
SSDTIFTTCP DRDSSGIVGI NRKGQVLFVT IDDSNIISYL LQNPANTEMA IKMASRAGLP
GADDLYKRQF EQLFNNGSYM EAAKVAANSP RGFLRSAETI EKFKRLPQQP GSMSFILQYF
GMLLDKGALN EHETLELAQP VLAQNRMNLL EKWMKEGKLH SSERLGDLIR PHDINTALAV
YLKANVPQKV VAGFAETGQF DKILPYSQQA GYSPDYVQLL QHIVRINPEK GAEFATSLAN
HEGGSLVDIA RVVDIFQSQG MIQQATAFLL DALKENSPEQ GQLQTRLLEM NLMNAPQVAD
AILGNEMFSH FDKPRIASLC EQAGLSQKAL ELYEDPEAIK RVVVNIAGTP NFNQDWLNGF
FGKLSVEQSL DCLDAMMKHN IRQNLQSVVT IATKYSDLLG PVQLVDLFEK YKTAEGLFYY
LGSVVNLSEE PDVIFKYIES ATKMGQFNEV ERICRDNNFY NAEKVKNFLK EAKLQEQLPL
IIVCDRFNFV HDLVLYLYQN QQFQSIETYV QRVNPSRTPA VIGGLLDVDC DEGIIKNLLS
TVNPQSIPID DLVQEVESRN RLKLLLPFLE QMLSAGMEQQ AVYNALAKIY IDSNNNPEKF
LKENDKYDSL SVGKYCEKRD PNLAYIAYSK GQNDLELVNI TNENSMYRAQ ARYLLERSDR
ELWDFVLSEN NIHRRSVIDQ VTSTAVPEST DPSKVSVAVA ALLGNDLPLE LIELLEKIVL
EPSPFSDNQN LQNLLLFTAA KADKSKVMDY IHKLDGYSAP DIANACIEVG LHEEAFEIYK
KTGDKGSAVN VLVDHVVSID RAQAFAEEVD QPEVWSKVAK AQLDGVRVSD AIESYIKADD
PRNYEEVIET AVHAGKNEDL VKYLRMARKT LREPPIDTAL AFCYARLDQL SELEDFLRGT
NVANIEESGD KAYEEGFFEA AKIFFTSISN WAKLATTLVH LGDYQAAVEC ARKANNIKVW
KQVHEACVEK KEFRLAQICG LNLIVDAEQL TTLVKQYERN GYFDELISLL EQGLGLERAH
MGMFTELGIA LSRYHPERLM EHLKLFWSRV NMPKLIRACE EATLWPELVF CYYHYDEYDN
AALAVIERPE NSWEHHQFKE IIVKVANLEI YYRAIKFYIE QHPSLLTDLL QVLTPRIDVN
RVVKLFEKND DLPLIKPFLL NVQTQNKRTV NNAINDLLIE EEDYKTLRDS VENYDNYDPV
DLAARLEKHD LIFFRQIAAN IYRKNKRWEK SIALSKQDKL YKDAIETAAI SSKTDIVEDL
LRYFVDIGSR ECYVGMLYSC YDLIRPDLVL EISWRHGLND FTMPYMINML CQQTKELATL
KADNEARKAK DKEQEKDDTN TPILGGNRLM ITAGPGGSQS PAPYGQTNGF APQATGYGF
//
