ID A0A0C9XKC4_9AGAR Unreviewed; 1055 AA.
AC A0A0C9XKC4;
DT 29-APR-2015, integrated into UniProtKB/TrEMBL.
DT 29-APR-2015, sequence version 1.
DT 27-MAR-2024, entry version 38.
DE RecName: Full=Class E vacuolar protein-sorting machinery protein HSE1 {ECO:0000256|ARBA:ARBA00017923};
DE AltName: Full=Class E vacuolar protein-sorting machinery protein hse1 {ECO:0000256|ARBA:ARBA00018978};
GN ORFNames=K443DRAFT_677967 {ECO:0000313|EMBL:KIK01954.1};
OS Laccaria amethystina LaAM-08-1.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Agaricomycetidae; Agaricales; Agaricineae; Hydnangiaceae; Laccaria.
OX NCBI_TaxID=1095629 {ECO:0000313|EMBL:KIK01954.1, ECO:0000313|Proteomes:UP000054477};
RN [1] {ECO:0000313|EMBL:KIK01954.1, ECO:0000313|Proteomes:UP000054477}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LaAM-08-1 {ECO:0000313|EMBL:KIK01954.1,
RC ECO:0000313|Proteomes:UP000054477};
RG DOE Joint Genome Institute;
RA Kuo A., Kohler A., Nagy L.G., Floudas D., Copeland A., Barry K.W.,
RA Cichocki N., Veneault-Fourrey C., LaButti K., Lindquist E.A., Lipzen A.,
RA Lundell T., Morin E., Murat C., Sun H., Tunlid A., Henrissat B.,
RA Grigoriev I.V., Hibbett D.S., Martin F., Nordberg H.P., Cantor M.N.,
RA Hua S.X.;
RL Submitted (APR-2014) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Proteomes:UP000054477}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LaAM-08-1 {ECO:0000313|Proteomes:UP000054477};
RG DOE Joint Genome Institute;
RG Mycorrhizal Genomics Consortium;
RA Kohler A., Kuo A., Nagy L.G., Floudas D., Copeland A., Barry K.W.,
RA Cichocki N., Veneault-Fourrey C., LaButti K., Lindquist E.A., Lipzen A.,
RA Lundell T., Morin E., Murat C., Riley R., Ohm R., Sun H., Tunlid A.,
RA Henrissat B., Grigoriev I.V., Hibbett D.S., Martin F.;
RT "Evolutionary Origins and Diversification of the Mycorrhizal Mutualists.";
RL Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Component of the ESCRT-0 complex which is the sorting
CC receptor for ubiquitinated cargo proteins at the multivesicular body
CC (MVB). {ECO:0000256|ARBA:ARBA00002654}.
CC -!- SUBCELLULAR LOCATION: Endosome membrane
CC {ECO:0000256|ARBA:ARBA00004125}; Peripheral membrane protein
CC {ECO:0000256|ARBA:ARBA00004125}; Cytoplasmic side
CC {ECO:0000256|ARBA:ARBA00004125}. 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 STAM family.
CC {ECO:0000256|ARBA:ARBA00009666}.
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DR EMBL; KN838599; KIK01954.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0C9XKC4; -.
DR STRING; 1095629.A0A0C9XKC4; -.
DR HOGENOM; CLU_010104_1_0_1; -.
DR OrthoDB; 620063at2759; -.
DR Proteomes; UP000054477; Unassembled WGS sequence.
DR GO; GO:0010008; C:endosome membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0035091; F:phosphatidylinositol binding; IEA:InterPro.
DR GO; GO:0043130; F:ubiquitin binding; IEA:InterPro.
DR GO; GO:0016197; P:endosomal transport; IEA:UniProt.
DR GO; GO:0006886; P:intracellular protein transport; IEA:UniProt.
DR GO; GO:0007034; P:vacuolar transport; IEA:UniProt.
DR CDD; cd21386; GAT_Hse1; 1.
DR CDD; cd11805; SH3_GRB2_like_C; 1.
DR CDD; cd16978; VHS_HSE1; 1.
DR Gene3D; 1.20.5.1940; -; 1.
DR Gene3D; 1.25.40.90; -; 1.
DR Gene3D; 2.30.30.40; SH3 Domains; 1.
DR InterPro; IPR008942; ENTH_VHS.
DR InterPro; IPR004152; GAT_dom.
DR InterPro; IPR036028; SH3-like_dom_sf.
DR InterPro; IPR001452; SH3_domain.
DR InterPro; IPR003903; UIM_dom.
DR InterPro; IPR002014; VHS_dom.
DR PANTHER; PTHR45929; JAK PATHWAY SIGNAL TRANSDUCTION ADAPTOR MOLECULE; 1.
DR PANTHER; PTHR45929:SF3; JAK PATHWAY SIGNAL TRANSDUCTION ADAPTOR MOLECULE; 1.
DR Pfam; PF03127; GAT; 1.
DR Pfam; PF14604; SH3_9; 1.
DR Pfam; PF00790; VHS; 1.
DR PRINTS; PR00452; SH3DOMAIN.
DR SMART; SM00326; SH3; 1.
DR SMART; SM00288; VHS; 1.
DR SUPFAM; SSF81995; beta-sandwich domain of Sec23/24; 1.
DR SUPFAM; SSF48464; ENTH/VHS domain; 1.
DR SUPFAM; SSF89009; GAT-like domain; 1.
DR SUPFAM; SSF50044; SH3-domain; 1.
DR PROSITE; PS50002; SH3; 1.
DR PROSITE; PS50330; UIM; 1.
DR PROSITE; PS50179; VHS; 1.
PE 3: Inferred from homology;
KW Endosome {ECO:0000256|ARBA:ARBA00022753};
KW Protein transport {ECO:0000256|ARBA:ARBA00022927};
KW Reference proteome {ECO:0000313|Proteomes:UP000054477};
KW SH3 domain {ECO:0000256|ARBA:ARBA00022443, ECO:0000256|PROSITE-
KW ProRule:PRU00192}; Transport {ECO:0000256|ARBA:ARBA00022448}.
FT DOMAIN 17..147
FT /note="VHS"
FT /evidence="ECO:0000259|PROSITE:PS50179"
FT DOMAIN 317..376
FT /note="SH3"
FT /evidence="ECO:0000259|PROSITE:PS50002"
FT REGION 176..225
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 244..312
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 477..624
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 654..678
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 694..726
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 799..872
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 909..1055
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 180..225
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 255..312
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 533..563
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 590..624
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 799..856
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 919..951
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 965..991
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1003..1017
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1055 AA; 114970 MW; 3082E3403269234B CRC64;
MFGGGATNPY DEIVIKATDE NLTSENWEII LNLCDKVQDE GGEGARNVIA ALLKRLAHRN
PNVQLYALSL AESLTKNLGI ELHREIASKA FTQGLEKIVT DRTTHEKVRK RALGLIAMWT
DEFESDTTLG IMEDCYNNLK AKNYKFEQPS EPPPPTVDDE IRRKEEEELQ RVLEMSMQDK
GGRNQWSNYS AASSSGAGGS GSSSSVNRNN NAPAATSSAS TSKSTPAAAP AASAAAFTQP
KYNAGYVPAR TPTPEAVPQQ KQQQQQPHQP HVHQPQQQPS QPSPQQRPAA SSSTVSVIST
TSAATSPTAV TMPTSGNIVT RVRALHTFEP TEPGELAFDK GDVIKVVDRG YKDWWRGQLK
GRTGIFPVNY VEAMPEPTAT ELAKEAEQEA AVFSQAVNVE KLLNMLRALD PVKDNLADNE
EIQELYRSSM ALRPKIVKLI DKYSQKRADL VSMNETFVRA RSIFDRMMEE SLARHTGVYD
QPTYRPPQYA QPQGPIRRDS RSGSAAGRGA GPQAYGWNPS LYEQPGYNAY PASASAYPQQ
QQQQQQQQQQ AQQPHQQQQP EFGGGSPPPA AYAYGVVPQG GYAGQQPGLP YGQQGPTPYP
QQQVPQGQGQ PQLQTQQQQP QQVLQGQPAQ QLNLQAIQQQ QLLQSLQQQP IQPQQQQPVQ
QQPVQQQPVQ QQPIQPIQQA QSLQQQAQPV QQQAQPIQQQ QQQPGREQPV QQQQQPGREQ
PIQQQPIQQQ PVQQQLVQQQ PIQQQPVQQQ LVQQQPIQQQ PIQEQEQPVQ QAQPIQQQVQ
PVQQAQFIQQ QTQPIQQAQP VQQAQPIEQA QPIQPQAQPV QQAQPIQQQA QPTQQPKQGY
QLHDQPIQQQ QTAAAAAAPA ESGPPFVFDP NTTYSDPNVQ AWAQYYAQGG MDLAGAVYFI
SVPGVTEPAP AAPGSPQRAT GFAAQQQQTA VGGSNESLQQ QQQQQPANDA GYAGQQRLHD
QGHPQPERQS SPQLQAGAGG GAASSSPRTS LGDGARGGPS GGHSSPVQAS STPSWVLPKK
TAEPRLGSSP TNSAMAYGGA GPSGAYYAGN GNGQV
//
