UniProt: K1X2Q9

Database: UniProt
Entry: K1X2Q9_MARBU

LinkDB:  K1X2Q9_MARBU 
Original site:  K1X2Q9_MARBU

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Ontology (7)   
   GO (7)   
Gene (2)   
   KEGG GENES (1)   
   NCBI-Gene (1)   
Protein sequence (1)   
   RefSeq(pep) (1)   
DNA sequence (1)   
   EMBL (1)   
Protein domain (11)   
   InterPro (6)   
   Pfam (3)   
   PROSITE (1)   
   SMART (1)   
Literature (1)   
   PubMed (1)   
All databases (23)   

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ID   K1X2Q9_MARBU            Unreviewed;      1684 AA.
AC   K1X2Q9;
DT   28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT   28-NOV-2012, sequence version 1.
DT   27-MAR-2024, entry version 49.
DE   RecName: Full=Clathrin heavy chain {ECO:0000256|PIRNR:PIRNR002290};
GN   ORFNames=MBM_02539 {ECO:0000313|EMBL:EKD19302.1};
OS   Marssonina brunnea f. sp. multigermtubi (strain MB_m1) (Marssonina leaf
OS   spot fungus).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC   Helotiales; Drepanopezizaceae; Drepanopeziza.
OX   NCBI_TaxID=1072389 {ECO:0000313|EMBL:EKD19302.1, ECO:0000313|Proteomes:UP000006753};
RN   [1] {ECO:0000313|EMBL:EKD19302.1, ECO:0000313|Proteomes:UP000006753}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MB_m1 {ECO:0000313|EMBL:EKD19302.1,
RC   ECO:0000313|Proteomes:UP000006753};
RX   PubMed=22876864; DOI=10.1186/1471-2164-13-382;
RA   Zhu S., Cao Y.-Z., Jiang C., Tan B.-Y., Wang Z., Feng S., Zhang L.,
RA   Su X.-H., Brejova B., Vinar T., Xu M., Wang M.-X., Zhang S.-G.,
RA   Huang M.-R., Wu R., Zhou Y.;
RT   "Sequencing the genome of Marssonina brunnea reveals fungus-poplar co-
RT   evolution.";
RL   BMC Genomics 13:382-382(2012).
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; JH921431; EKD19302.1; -; Genomic_DNA.
DR   RefSeq; XP_007290428.1; XM_007290366.1.
DR   STRING; 1072389.K1X2Q9; -.
DR   GeneID; 18758474; -.
DR   KEGG; mbe:MBM_02539; -.
DR   eggNOG; KOG0985; Eukaryota.
DR   HOGENOM; CLU_002136_0_0_1; -.
DR   InParanoid; K1X2Q9; -.
DR   OMA; HCYDLLH; -.
DR   OrthoDB; 5474327at2759; -.
DR   Proteomes; UP000006753; 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:UP000006753}.
FT   REGION          1659..1684
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1684 AA;  189845 MW;  224D69FCFB35DCA7 CRC64;
     MAPALPIRFT ELLQLTNPTV GVDQASIGFN SCTLESDSFI CVREKKNEAA SPEVVIIEIK
     NNNNVIRRPI KADSAIMHWT KQIIALKAQS RTLQIFDLGQ KQKLKSATMN EDVVFWKWFS
     ETTLGLVTDT TVYHWDIFDP NQASPVEVFK RNQNLTGCQI INYRVSDDGK WMVLVGITQQ
     QGRVVGAMQL YSRDRGISQA IEGHAAAFGT LRLEGAPADT KVFTFSVRTA TGAKLHIVEV
     DHQASNPTFA KKAVDVYFPT EAVNDFPVAM QVSQKYSIIY LVTKYGFIHL YDLETGTCMF
     MNRISSETIF ITAPDNESAG IVGVNRKGQV LSVAVDETTI IPYLLQNPAN SSMAVKLASR
     AGLPGADNLY AQQFDQLLNS GNYPDAAKIA ANSPRGFLRT PQTIERFKAL PSAPGQLSVI
     LQYFGMLLDK GTLNKHETLE LVKPVLAQSR KHLLEKWMKE NKLDCSEELG DIVRPHDLNL
     ALSIYLRAGV PAKVVAAFAE SGQFDKILPY ASQVGYQPDY VVLLQNIIRL SPEKGSEFAT
     QLANNEGGSL VDIERVVDVF QSQGMVQPAT AFLLDALKDN KPEQANLQTR LLEMNLVNAP
     QVADAILGND MFSHYDKARI ATLCEQAGLS QRALEHYQDP ESIKRVIVNI VATPNFNQEW
     LNSFFGRLSL EQSLDCLDAM LKTNIRQNLG AVVQIATKYS DLLGPVRLID LLEKYKTSEG
     LFYYLGSIVN LSEDQDVNFK YIEAATKMGQ FPEVERICRD SNYYDPVKVR NFLKEAKLTE
     QLPLIIVCDR FNFIHDLVLY LYQNQQFKSI EVYVQRVNPA RTPAVIGGLL DVDCDESIIK
     NLLTTVNPAS VPIDELVSEV ESRNRLKILL PFLEATLAAG NQQQAVYNAL AKIYIDSNNN
     PERFLKENDQ YDTLVVGNYC SKRDPNLAMI AFSKGQNDLE LVSITNENSM FKAQARYLLE
     RADNELWSFV LSPNNIHRRS VVDQVISTAV PESTEPDKVS IAVSSFLAAD LPLELIELLE
     KIVLEPSPFS DNENLQNLLL LTATKADKGR VMDYIHRLEA YNAPDIAAIC IEVGLFEEAF
     EAYKKINDHK SAANVLVEHV VSIDRAQEYA ERVELPEVWS TVAKAQLDGL RVSDAIASYI
     RAEDPSNYNE VIEIATHAGK DEDLIKYLRM ARKTLREPPI DTGLAFAYAR TDQLSELEDF
     LRGTNVADIE VSGDKAYAEG YHQAAKIFFT SVSNWAKLAT TLVHLEEYQA AVECARKANN
     IKVWKQVNAA CVEKKEFRLA QICGLNLIVD AEELQDLVKQ YERNGYFDEL ISLLEQGLGL
     ERAHMGMFTE LGIALSRYHP DRVMEHLKLF WSRINIPKMI RATEDAHLWP ELVFLYCHYD
     EWDNAALAMM ERAADAWEHH SFKDIVVKVA NLEIYYRALN FYLQEQPSLL TDLLQALTPR
     IDVNRVVKMF EKSDNIPLIK PFLLNVQTQN KKIVNSAIND LLIEEEDYKT LRDSVENYDN
     YDPVELAQRL ERHDLVFFRQ IAANIYRKNK RWDKSIALSK QDKLFKDAIE TAAMSGKSDV
     VEELLRYFVD IGSRECYVGM LYACYDLIPI HVVMEISWRH GLTDFTMPFM INYLAQQGST
     IEMLKKDNEE RKLREKSNEK EESNAPILGG NRLMITAGPG GRQSPAPFAQ TNGFAPQPTG
     YGGF
//

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