ID A0A1V6Q2P5_9EURO Unreviewed; 635 AA.
AC A0A1V6Q2P5;
DT 07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT 07-JUN-2017, sequence version 1.
DT 27-MAR-2024, entry version 25.
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=PENANT_c016G08108 {ECO:0000313|EMBL:OQD83548.1};
OS Penicillium antarcticum.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium.
OX NCBI_TaxID=416450 {ECO:0000313|EMBL:OQD83548.1, ECO:0000313|Proteomes:UP000191672};
RN [1] {ECO:0000313|Proteomes:UP000191672}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IBT 31811 {ECO:0000313|Proteomes:UP000191672};
RX PubMed=28368369; DOI=10.1038/nmicrobiol.2017.44;
RA Nielsen J.C., Grijseels S., Prigent S., Ji B., Dainat J., Nielsen K.F.,
RA Frisvad J.C., Workman M., Nielsen J.;
RT "Global analysis of biosynthetic gene clusters reveals vast potential of
RT secondary metabolite production in Penicillium species.";
RL Nat. Microbiol. 2:17044-17044(2017).
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 -!- SUBUNIT: Component of the ESCRT-0 complex composed of HSE1 and VPS27.
CC {ECO:0000256|ARBA:ARBA00011446}.
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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:OQD83548.1}.
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DR EMBL; MDYN01000016; OQD83548.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1V6Q2P5; -.
DR STRING; 416450.A0A1V6Q2P5; -.
DR OrthoDB; 620063at2759; -.
DR Proteomes; UP000191672; 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; 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; PR00499; P67PHOX.
DR PRINTS; PR00452; SH3DOMAIN.
DR SMART; SM00326; SH3; 1.
DR SMART; SM00288; VHS; 1.
DR SUPFAM; SSF48464; ENTH/VHS domain; 1.
DR SUPFAM; SSF50044; SH3-domain; 1.
DR PROSITE; PS50002; SH3; 1.
DR PROSITE; PS50179; VHS; 1.
PE 3: Inferred from homology;
KW Endosome {ECO:0000256|ARBA:ARBA00022753};
KW Membrane {ECO:0000256|ARBA:ARBA00023136};
KW Protein transport {ECO:0000256|ARBA:ARBA00022927};
KW Reference proteome {ECO:0000313|Proteomes:UP000191672};
KW SH3 domain {ECO:0000256|ARBA:ARBA00022443, ECO:0000256|PROSITE-
KW ProRule:PRU00192}; Transport {ECO:0000256|ARBA:ARBA00022448}.
FT DOMAIN 16..145
FT /note="VHS"
FT /evidence="ECO:0000259|PROSITE:PS50179"
FT DOMAIN 227..286
FT /note="SH3"
FT /evidence="ECO:0000259|PROSITE:PS50002"
FT REGION 384..635
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 418..433
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 459..490
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 520..563
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 564..593
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 635 AA; 69740 MW; 54856321A581AD55 CRC64;
MFRAQQNAFD DAVAKATDEN LTSENWEYIL DVCDKVGSEE SGAKEAVAAM IKRLAHRNAN
VQLYTLELGN SLAQNCGLKI HRELASRSFT DALLRLANDR NTHQQVKSKI LERMEEWTQM
FASNPDFGIM EQAYMKLKTT NPNLQPPSKP GKREITDVDR RMEEEELQMA LALSIKDKPS
GPAGAPAARA ESSAAPASAA VSAATLAQAN PAEPAEAQPV LSGTSVATVS RVRALFDFQP
SEPGELQFRK GDIIAVLESV YKDWWKGSLR GQTGIFPLNY VEKLPDPTVD ELQREAQMEA
DVFGQIKSVE KLLTLLSTRN TDLNVSENEE ISNLYEATLK IRPKLIELIG KYSQKKDEFT
QLNEKFIKAR RDYESLLEAS MAHPTQPQYG RPPQPQYAYP GAAAAGYAGP PQAESRYFSP
RPQDTTPIQA TAPYYGGEQT MPYRPASHSP DPRNQVPAIA PPVQQQAPQS DPYAPVQHRP
QSTYDHPQEL GTSAYDSPVD HPAPAQRLPY PPGAQAQGLP AGHQQFQQQQ QQQQQQDYSP
SVYSTDDTPQ IPPVSTMPQQ IPHQFQQPPY PNSPAASHQP PPSHQPPPVP GATSQPAQYT
SYSPAPPAPA GTGEYQAYQP PQGGAAGSNP ASFYR
//
