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Database: UniProt
Entry: A0A137QP11_9AGAR
LinkDB: A0A137QP11_9AGAR
Original site: A0A137QP11_9AGAR 
ID   A0A137QP11_9AGAR        Unreviewed;       935 AA.
AC   A0A137QP11;
DT   11-MAY-2016, integrated into UniProtKB/TrEMBL.
DT   11-MAY-2016, sequence version 1.
DT   24-JAN-2024, entry version 30.
DE   RecName: Full=Vacuolar protein sorting-associated protein 41 {ECO:0000256|PIRNR:PIRNR028921};
GN   ORFNames=AN958_06465 {ECO:0000313|EMBL:KXN89003.1};
OS   Leucoagaricus sp. SymC.cos.
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC   Agaricomycetidae; Agaricales; Agaricineae; Agaricaceae; Leucoagaricus.
OX   NCBI_TaxID=1714833 {ECO:0000313|EMBL:KXN89003.1, ECO:0000313|Proteomes:UP000070249};
RN   [1] {ECO:0000313|EMBL:KXN89003.1, ECO:0000313|Proteomes:UP000070249}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SymC.cos {ECO:0000313|EMBL:KXN89003.1,
RC   ECO:0000313|Proteomes:UP000070249};
RA   Hu H.;
RT   "Leucoagaricus sp. SymC.cos WGS genome.";
RL   Submitted (JAN-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Required for vacuolar assembly and vacuolar traffic.
CC       {ECO:0000256|PIRNR:PIRNR028921}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasmic vesicle, clathrin-coated vesicle
CC       {ECO:0000256|ARBA:ARBA00004132}. Vacuole
CC       {ECO:0000256|PIRNR:PIRNR028921}. Vesicle
CC       {ECO:0000256|ARBA:ARBA00004373}.
CC   -!- SIMILARITY: Belongs to the VPS41 family.
CC       {ECO:0000256|ARBA:ARBA00009582, ECO:0000256|PIRNR:PIRNR028921}.
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DR   EMBL; KQ962117; KXN89003.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A137QP11; -.
DR   STRING; 1714833.A0A137QP11; -.
DR   OrthoDB; 8838at2759; -.
DR   Proteomes; UP000070249; Unassembled WGS sequence.
DR   GO; GO:0030136; C:clathrin-coated vesicle; IEA:UniProtKB-SubCell.
DR   GO; GO:0000329; C:fungal-type vacuole membrane; IEA:UniProtKB-UniRule.
DR   GO; GO:0030897; C:HOPS complex; IEA:UniProtKB-UniRule.
DR   GO; GO:0005770; C:late endosome; IEA:UniProtKB-UniRule.
DR   GO; GO:0034058; P:endosomal vesicle fusion; IEA:UniProtKB-UniRule.
DR   GO; GO:0006623; P:protein targeting to vacuole; IEA:InterPro.
DR   Gene3D; 1.25.40.10; Tetratricopeptide repeat domain; 1.
DR   Gene3D; 2.130.10.10; YVTN repeat-like/Quinoprotein amine dehydrogenase; 1.
DR   InterPro; IPR000547; Clathrin_H-chain/VPS_repeat.
DR   InterPro; IPR011990; TPR-like_helical_dom_sf.
DR   InterPro; IPR016902; VPS41.
DR   InterPro; IPR045111; Vps41/Vps8.
DR   InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR   InterPro; IPR036322; WD40_repeat_dom_sf.
DR   InterPro; IPR001680; WD40_rpt.
DR   InterPro; IPR001841; Znf_RING.
DR   PANTHER; PTHR12616; VACUOLAR PROTEIN SORTING VPS41; 1.
DR   PANTHER; PTHR12616:SF1; VACUOLAR PROTEIN SORTING-ASSOCIATED PROTEIN 41 HOMOLOG; 1.
DR   Pfam; PF00637; Clathrin; 1.
DR   PIRSF; PIRSF028921; VPS41; 2.
DR   SMART; SM00299; CLH; 1.
DR   SMART; SM00184; RING; 1.
DR   SMART; SM00320; WD40; 2.
DR   SUPFAM; SSF50978; WD40 repeat-like; 1.
DR   PROSITE; PS50236; CHCR; 1.
PE   3: Inferred from homology;
KW   Golgi apparatus {ECO:0000256|ARBA:ARBA00023034};
KW   Protein transport {ECO:0000256|PIRNR:PIRNR028921};
KW   Reference proteome {ECO:0000313|Proteomes:UP000070249};
KW   Transport {ECO:0000256|PIRNR:PIRNR028921};
KW   Vacuole {ECO:0000256|PIRNR:PIRNR028921}.
FT   REPEAT          609..753
FT                   /note="CHCR"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01006"
FT   DOMAIN          832..926
FT                   /note="RING-type"
FT                   /evidence="ECO:0000259|SMART:SM00184"
FT   REGION          228..260
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        233..250
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   935 AA;  104891 MW;  07F9AE522FD78EC7 CRC64;
     MALGTHAGII HLLDLTGKRI KSYKPHYASI VDVSFDTNAD FVATASIDGQ VVVHSINTTE
     SYSFDLKRPM RTVALESNFG RRNSRALVYG GLAGNLILQE KGWLGHKETL LHSNEGPIWQ
     VRWRGRLIAW ANDLGVKIYD HTSQTRITFI DRPQDSPRAD LFKCNLHWQD DSTLLIAWAD
     MIKVARIRER PRMTTSSASA NLPPFVVEIT AVFQLDCMIA GIVPHPTPNT SGPPDGLLVN
     NGSASIKSTS SSEKRSEKHT PPLTSFLIIA YSPPETFADE MTEDRARQAR KQADRPEMRI
     ISRAGEELAA DAITVTDFQK WGCNDYVLVE GISGDGPAGM DPETRSYVVL SPRDLVRVRP
     RDRRDHVAWL LERQRYEEAL EEVEKIEADG LLKKTEAVRP LAGDTQAEGE DLLSAVEIGQ
     KYIRHLVNEG EFVKAAKLTP KVCGHDSKKW EDWIFVFADK QHLQAIIPYV PTDSPKLDHL
     VYEMMLAHFL THDRKTLLQM IKEWPRDIYD ISAVIVAVRS ELDKATSEPK SLSTPSSTVI
     LMEYTANRQP GKALPFYLRL RRPNVFELIK EHNLFTDVQD QVLLLVEFDH ELMEKRKAAG
     QEIGRSEAIS LLVNNMHSIP IIRAVQQLQN KPYYLFLYLD ALVERDPHLV SEFADLQVKL
     YAEFATTRLI DFLRASTYYN LEMAYEVCNE RNLVPEMVFL LGRMGNNKKA LNLIIERLGD
     VQRAIEFAKE QSDDDLWEDL LKYSETRPNF IRGLLENVGV EISPIRLIRR IKNGLEIPGL
     KEALIKILQD FHLQISLLEG CGAILDGDCA DLAGRLQRGQ GAGFFLTAKT ECPICNKTIQ
     DNSQGKGLVI LFLCRHVVHV SCVPGRDSGT SEGENGSLMR SLEPYLGEGG FGFGSSVGAG
     GRKGISGSVA LESMIRSRLE RGCPVCHKAG EGRRM
//
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