ID S3DS24_GLAL2 Unreviewed; 1685 AA.
AC S3DS24;
DT 18-SEP-2013, integrated into UniProtKB/TrEMBL.
DT 18-SEP-2013, sequence version 1.
DT 27-MAR-2024, entry version 41.
DE RecName: Full=Clathrin heavy chain {ECO:0000256|PIRNR:PIRNR002290};
GN ORFNames=GLAREA_00403 {ECO:0000313|EMBL:EPE29243.1};
OS Glarea lozoyensis (strain ATCC 20868 / MF5171).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC Helotiales; Helotiaceae; Glarea.
OX NCBI_TaxID=1116229 {ECO:0000313|EMBL:EPE29243.1, ECO:0000313|Proteomes:UP000016922};
RN [1] {ECO:0000313|EMBL:EPE29243.1, ECO:0000313|Proteomes:UP000016922}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 20868 / MF5171 {ECO:0000313|Proteomes:UP000016922};
RX PubMed=23688303; DOI=10.1186/1471-2164-14-339;
RA Chen L., Yue Q., Zhang X., Xiang M., Wang C., Li S., Che Y.,
RA Ortiz-Lopez F.J., Bills G.F., Liu X., An Z.;
RT "Genomics-driven discovery of the pneumocandin biosynthetic gene cluster in
RT the fungus Glarea lozoyensis.";
RL BMC Genomics 14:339-339(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}. 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; KE145367; EPE29243.1; -; Genomic_DNA.
DR RefSeq; XP_008083352.1; XM_008085161.1.
DR STRING; 1116229.S3DS24; -.
DR GeneID; 19459461; -.
DR KEGG; glz:GLAREA_00403; -.
DR eggNOG; KOG0985; Eukaryota.
DR HOGENOM; CLU_002136_0_0_1; -.
DR OMA; HCYDLLH; -.
DR OrthoDB; 5474327at2759; -.
DR Proteomes; UP000016922; 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; 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; 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; 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:UP000016922}.
FT REGION 1625..1651
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1625..1641
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1685 AA; 189873 MW; C1301B867CFA132A CRC64;
MAPSLPIKFT ELLQLTSSQV NVDQASIGFN SCTLESDSFI CVREKKNEAA SPEVIIVDLK
QNNNVIRRPI KADSAIMHWT KQVIALKAQS RTLQIFDLAQ KAKLKSATMS EDVVFWKWFS
ETSLGLVTDS AVYHWDVFDA NQASPVEVFK RNQNLAGCQI INYRVSDDGK WMVVIGITQQ
QGRVVGAMQL HSRDRGISQA IEGHAAAFGT LRLEGAPADT KVFTFAVRTA TGAKLHIVEV
DHQTTNPTFS KKAVDVYFPA EAVNDFPVAM QVSQKYSIIY LVTKYGFIHL YDLETGTCIF
MNRISSETIF ITTADSQSEG LVGINRKGQV LAVAVDETTI INYLLQNPAN SGLAVKLASR
AGLPGADNLY AQQFDQLISA GNYAEAAKIA ANSPRGFLRT PQTIDRFKSL PAVPGQLSII
LQYFGMLLDK GTLNKHETLE LVRPVLAQQR KHLLEKWMKE NKLDCSEELG DIVRPHDLNL
ALSIYLRANV APKVVAAFAE TGQFEKILPY ATQVGYQPDY IVLLQNIVRL SPDKGAEFAT
QLANNESGPL VDIERVVDVF QSQNMVQAAT AFLLDALKDN KPEQGNLQTR LLEMNLMNAP
QVADAILGND MFSHYDRPRI AQLCEGAGLV QRALEHYDDP DAIKRVLVNI AAQPNFSQDW
LTNFFGRLSL EQSLDCLDAM LKSNIRQNLA SVVQIATKYS DLLGATRLID LFEKYKTYEG
LFYYLGSIVN LSEDPDVNFK YIEAATKMGQ FNEVERICRD SNHFNPEKVK NFLKEAKLTE
QLPLIIVCDR FNFIHDLVLY LYQNQQFKSI EVYVQRVNPA RTPAVVGGLL DVDCDESIIK
NLLQTVNPAS VPIDDLVAEV ETRNRLKILL PFLEATLAAG NQQQAVYNAL AKIYIDSNNA
PEKFLKENDL YNTLTVGKYC EKRDPNLAFI AYQKGQNDLE LVNITNENSM FKAQSRYLLN
RADTELWSFV LSPNNIHRRS VVDQVISTAV PESTEPDKVS VAVAAFLQAD LPGELIELLE
KIVLEPSPFS DNENLQNLLI LTATKADKAR VMDYIHRLDA YNAPDIANIC IEVGLFEEAF
EVYKKINDHK SAANVLVEHI VSIDRAHEYA ERVELPEVWS RVAKAQLDGL RVSDGIASYI
RAEDPSNYLE VIEIATHAGK DEDLIKFLRM SRKTLREPAI DTALAFAYAR TEQLSELEDF
LRGTNVADIE ESGDKAYAEG FHQAAKIFFT SISNWAKLAT TLVHLEDYQA AVECARKANN
IKVWKQVNAA CVEKKEFRLA QICGLNLIVD AEELQGLVKQ YERNGYFDEL ISLLEQGLGL
ERCHMGIFTE LGIALSKYHP DRVMEHLKLF WGRINIPKMI RACEEAHLWP ELVFLYCHYD
EWDNAALAMM ERAADAWEHH SFKDIIVKVA NLEIYYRALN FYLQQQPSLL TDLLQALTPR
IDVNRVVKMF EKSDNIPLIK PFLLNVQTQN KKIVNNAIND LLIEEEDYKT LRDSVENYDN
YDPVELAQRL EKHDLVFFRQ IAANIYRKNK RWEKSIALSK QDKLFKDAIE TAAMSAKSDV
VEELLRYFVD IGSRECYVGM LYACYELIPI HVVMEVSWRH GLTDFTMPFM INYLAQQSST
IETLKKDNEE RKSREKSQET DDSNTPILGG GRLMITAGPG GRQSPAPFAQ TNGFAPQATG
FGGGF
//
