ID A0A066XKA4_COLSU Unreviewed; 1682 AA.
AC A0A066XKA4;
DT 03-SEP-2014, integrated into UniProtKB/TrEMBL.
DT 03-SEP-2014, sequence version 1.
DT 27-MAR-2024, entry version 45.
DE RecName: Full=Clathrin heavy chain {ECO:0000256|PIRNR:PIRNR002290};
GN ORFNames=CSUB01_09803 {ECO:0000313|EMBL:KDN68089.1};
OS Colletotrichum sublineola (Sorghum anthracnose fungus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Glomerellales; Glomerellaceae; Colletotrichum;
OC Colletotrichum graminicola species complex.
OX NCBI_TaxID=1173701 {ECO:0000313|EMBL:KDN68089.1, ECO:0000313|Proteomes:UP000027238};
RN [1] {ECO:0000313|Proteomes:UP000027238}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TX430BB {ECO:0000313|Proteomes:UP000027238};
RX PubMed=24926053; DOI=10.1128/genomeA.00540-14;
RA Baroncelli R., Sanz-Martin J.M., Rech G.E., Sukno S.A., Thon M.R.;
RT "Draft genome sequence of Colletotrichum sublineola, a destructive pathogen
RT of cultivated sorghum.";
RL Genome Announc. 2:E0054014-E0054014(2014).
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}.
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:KDN68089.1}.
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DR EMBL; JMSE01000732; KDN68089.1; -; Genomic_DNA.
DR STRING; 1173701.A0A066XKA4; -.
DR eggNOG; KOG0985; Eukaryota.
DR HOGENOM; CLU_002136_0_0_1; -.
DR OMA; HCYDLLH; -.
DR OrthoDB; 5474327at2759; -.
DR Proteomes; UP000027238; 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:UP000027238}.
FT REGION 1624..1647
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1624..1640
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1682 AA; 190010 MW; 6ED234FEB0A68E4B CRC64;
MAPLPIKFQE LIQLQTAGVE DSSIGFNSCT LESDSYVCIR EKKNEAAQPE VVIVDLKNGN
NVTRRPIKAD SAIMHWTRQV IALKAQSRTL QIFDLEKKAK LKSTTMNEDV QYWKWINETS
LGLVTDTAVY HWDVYDPSQA QPVEVFKRNA NLNGCQIINY RTNAEGKWMV VVGISQQQGR
VVGSMQLYSK DRGISQAIEG HAAAFGTLRL EGAPADTKLF TFAVRTATGA KLHIVEVDHA
ESNPVFPKKA VDIFFPPEAV SDFPVAMQVS QKYGVIFMVT KYGFIHVYDL ETAACIFMNR
ISSDTIFTTC PDSESRGIVG INRKGQVLFV SMDDNNVIPY LLQNPANTEM AIKMASRAGL
PGADNLYARQ FEQLFNSGQF MEAAKIAANS PRQFLRTPET IEKFKALPQQ PGQMSFVLQY
FGLLLDKGAL NEHESIELAQ PVLAQNRLNL LEKWQKENKL TPSERLGDLV RPHDLNMALA
MYIKANVPHK VVAGLAETGQ FDKILPYASK TGYQPDYVQL LQHIVRVNPE KGAEFATALA
NNEGGSLVDI ERVVDIFQSQ GMIQQATAFL LDALKDNRPD QGHLQTRLLE MNLMNAPQVA
DAILGNDMFS HFDKTRIATL CEQAGLAQKA LELYEDPAAI KRVVVNIAAT PNFNLDWLTG
FFGKLSVEQS LDCLDAMIKH NIRQNLQAVV QVATKYSDLL GPVRLIDLFE KYKTAEGLFY
YLGSIVNLSE DPDVHFKYIE AATKMGQFNE VERICRDSNY FNAEKVKNFL KEARLQEQLP
LIIVCDRFNF VHDLVLYLYQ QQQFQSIETY VQRVNPSRTP AVIGGLLDVD CDESIIKNLL
STVNPASIPI DELVSEVETR NRLKLLLPFL EATLAAGNQQ QAVFNALAKI YIDSNNNPEK
FLKENDQYDT LAVGKYCEKR DPNLAFIAYS KGQNDLELVN ITNENGMYRN QARYLLERAD
RELWTFVLSE NNIHRRSVID QVTATAVPES TDPAKVSEAV AAFLACDLPL ELIELLEKIV
LEPSPFSDNA NLQNLLLFTA AKADKGKVMD YIHRLDNFSA PDIASACIDV GLHEEAFEIF
KKTGDKTSAV NVLIENVVSI DRAQAYAEEV DLPEVWSKVA KAQLDGLRVS DSIESYIKAE
DPKNYEEVIE TSVRAGKDED LVKYLRMARK TLREPAIDTA LAFCYARLDE LGELEDFLRG
TNVANIEESG DKAYEEGLYQ ASKIFFTSIS NWAKLATTLV HLEEYQAAVE CARKANNIKV
WKQVHEACVD KKEFRLAQIC GLNLIVDAEQ LQTLVKQYER NGYFDELIGL LEQGLGLERA
HMGMFTELGI ALSKYHPERL MEHLKLFWSR MNLPKIIRAC EEANLWPELV FCYYHYDEFD
NAALAVIERP ENSWEHQQFK EIVVKVANLE IYYRAINFYL EQHPSLLTDL LQALTPRIDV
NRVVKMFEKS DNLPLIKPFL LNVQSQNKRT VNNAINDLLI EEEDYKTLRD SVENYDNYDP
VDLAGRLEKH DLIFFRQIAA NIYRKNKRWE KSIALSKQDK LFKDAIETAA ISGKTDVVED
LLRYFVDIGS RECYVGMLYA CYDLIRPDLV LEISWRNGLT DFAMPYMINM LCQQTKELAT
LKADNEARKS KEKEQEKDET NTPILGGNRL MITAGPGGMG GAPPTPYGQT NGFAPQPTGF
GF
//
