ID M2RJN5_CERS8 Unreviewed; 844 AA.
AC M2RJN5;
DT 01-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 01-MAY-2013, sequence version 1.
DT 27-MAR-2024, entry version 44.
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=CERSUDRAFT_81790 {ECO:0000313|EMBL:EMD39001.1};
OS Ceriporiopsis subvermispora (strain B) (White-rot fungus) (Gelatoporia
OS subvermispora).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Polyporales; Gelatoporiaceae; Gelatoporia.
OX NCBI_TaxID=914234 {ECO:0000313|EMBL:EMD39001.1, ECO:0000313|Proteomes:UP000016930};
RN [1] {ECO:0000313|EMBL:EMD39001.1, ECO:0000313|Proteomes:UP000016930}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=B {ECO:0000313|EMBL:EMD39001.1,
RC ECO:0000313|Proteomes:UP000016930};
RX PubMed=22434909; DOI=10.1073/pnas.1119912109;
RA Fernandez-Fueyo E., Ruiz-Duenas F.J., Ferreira P., Floudas D.,
RA Hibbett D.S., Canessa P., Larrondo L.F., James T.Y., Seelenfreund D.,
RA Lobos S., Polanco R., Tello M., Honda Y., Watanabe T., Watanabe T.,
RA Ryu J.S., Kubicek C.P., Schmoll M., Gaskell J., Hammel K.E., St John F.J.,
RA Vanden Wymelenberg A., Sabat G., Splinter BonDurant S., Syed K.,
RA Yadav J.S., Doddapaneni H., Subramanian V., Lavin J.L., Oguiza J.A.,
RA Perez G., Pisabarro A.G., Ramirez L., Santoyo F., Master E., Coutinho P.M.,
RA Henrissat B., Lombard V., Magnuson J.K., Kuees U., Hori C., Igarashi K.,
RA Samejima M., Held B.W., Barry K.W., LaButti K.M., Lapidus A.,
RA Lindquist E.A., Lucas S.M., Riley R., Salamov A.A., Hoffmeister D.,
RA Schwenk D., Hadar Y., Yarden O., de Vries R.P., Wiebenga A., Stenlid J.,
RA Eastwood D., Grigoriev I.V., Berka R.M., Blanchette R.A., Kersten P.,
RA Martinez A.T., Vicuna R., Cullen D.;
RT "Comparative genomics of Ceriporiopsis subvermispora and Phanerochaete
RT chrysosporium provide insight into selective ligninolysis.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:5458-5463(2012).
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; KB445794; EMD39001.1; -; Genomic_DNA.
DR AlphaFoldDB; M2RJN5; -.
DR STRING; 914234.M2RJN5; -.
DR HOGENOM; CLU_010104_1_0_1; -.
DR OrthoDB; 620063at2759; -.
DR Proteomes; UP000016930; 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; PF00018; SH3_1; 1.
DR Pfam; PF00790; VHS; 1.
DR PRINTS; PR00452; SH3DOMAIN.
DR SMART; SM00326; SH3; 1.
DR SMART; SM00288; VHS; 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:UP000016930};
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 284..343
FT /note="SH3"
FT /evidence="ECO:0000259|PROSITE:PS50002"
FT REGION 193..226
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 243..282
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 444..483
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 529..629
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 663..844
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 195..226
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 246..282
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 529..569
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 570..584
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 585..613
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 669..712
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 729..783
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 790..821
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 844 AA; 91351 MW; 7F15CEDBC87B955C CRC64;
MFRGGQPNPY DEIVGKTTDE NLTGENWELI LNLCDKVQDE GEQGARNVTA SVLKRLAHRN
PNVQLYTLTL AEALSKNCGI EVHREVASRA FTQGLEKLVT DRTTHDKVRR RTLALVAQWT
SDFEKDPTLG IMEECYESLK SKGYKFEAPD EAPPLEVDDE VRRREEEELQ RVLEMSMHDK
GGRAQWEQYS LAASGGAGGS GSHSGTAPSV KPPSASPAPS TVTHRQGSYA QQPVYGGYVP
SASPAISASA EPSQSSSSAV TSVTTTSVST GSPVSTHSTQ DGIPVVTRVR ALHAFEPTEP
GELPFEKGDI IKVVDRGYKD WWRGQLKGRT GIFPVNYVEP LPEPTPAELA KEAEQEASVF
SQAANVDRLL TMLRAMDPVK DNLADNEEIQ ELYRSCMTLR PRIVKLIDKY SQKRAELVAM
NESFVKARTI FDRMMEDSLA RHTGIYDGRG PYPQVQPYIP RPDSRARQDG PAPGGPQAYG
WNPALYDQPG YNAYPAPVAA YNPGPESGYP GPAPQQPFVD PNAYAQRRQS MYPQQSSYPG
QPGAPNPYLQ QEQQAYPSAQ PAVQPQTTPH PQGIMPPQHE PTPQAQPVMQ PQVQAQSPQA
QQQPSQQQAA PHPSQGGPPY IFDPNTTYTD PNVQAWAQYY AQGGKDPTGA VYFLTVPGIK
EGPAPVQPAR NASQETVQPQ QQPHSPVVEA TQPASTAPLH SFPQQQQGQA GPESALAGAL
GSAPPLVQRI PEQGSQPQVS PISPTAQAAQ PQFYQAPGSS PNSSFHSTTM PQQQQQPSQE
AYGASPYAPT GYPQQASSPP AGDAPPSQQG WQQQYYSLPN QFAGMEVSGE GHQSAGPQGV
GAPA
//
