ID HSE1_ASPTN Reviewed; 597 AA.
AC Q0CJU8;
DT 26-JUN-2007, integrated into UniProtKB/Swiss-Prot.
DT 17-OCT-2006, sequence version 1.
DT 27-MAR-2024, entry version 87.
DE RecName: Full=Class E vacuolar protein-sorting machinery protein hse1;
GN Name=hse1; ORFNames=ATEG_06036;
OS Aspergillus terreus (strain NIH 2624 / FGSC A1156).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Circumdati.
OX NCBI_TaxID=341663;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NIH 2624 / FGSC A1156;
RA Birren B.W., Lander E.S., Galagan J.E., Nusbaum C., Devon K., Henn M.,
RA Ma L.-J., Jaffe D.B., Butler J., Alvarez P., Gnerre S., Grabherr M.,
RA Kleber M., Mauceli E.W., Brockman W., Rounsley S., Young S.K., LaButti K.,
RA Pushparaj V., DeCaprio D., Crawford M., Koehrsen M., Engels R.,
RA Montgomery P., Pearson M., Howarth C., Larson L., Luoma S., White J.,
RA Alvarado L., Kodira C.D., Zeng Q., Oleary S., Yandava C., Denning D.W.,
RA Nierman W.C., Milne T., Madden K.;
RT "Annotation of the Aspergillus terreus NIH2624 genome.";
RL Submitted (SEP-2005) 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:0000250}.
CC -!- SUBUNIT: Component of the ESCRT-0 complex composed of HSE1 and VPS27.
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Endosome membrane {ECO:0000250}; Peripheral
CC membrane protein {ECO:0000250}; Cytoplasmic side {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the STAM family. {ECO:0000305}.
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DR EMBL; CH476601; EAU33797.1; -; Genomic_DNA.
DR RefSeq; XP_001215214.1; XM_001215214.1.
DR AlphaFoldDB; Q0CJU8; -.
DR SMR; Q0CJU8; -.
DR STRING; 341663.Q0CJU8; -.
DR EnsemblFungi; EAU33797; EAU33797; ATEG_06036.
DR GeneID; 4321440; -.
DR VEuPathDB; FungiDB:ATEG_06036; -.
DR eggNOG; KOG2199; Eukaryota.
DR HOGENOM; CLU_010104_1_1_1; -.
DR OMA; QVYRDWW; -.
DR OrthoDB; 620063at2759; -.
DR Proteomes; UP000007963; 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; PR00452; SH3DOMAIN.
DR PRINTS; PR01887; SPECTRNALPHA.
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; Membrane; Protein transport; Reference proteome; SH3 domain;
KW Transport.
FT CHAIN 1..597
FT /note="Class E vacuolar protein-sorting machinery protein
FT hse1"
FT /id="PRO_0000292489"
FT DOMAIN 16..145
FT /note="VHS"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00218"
FT DOMAIN 162..181
FT /note="UIM"
FT /evidence="ECO:0000305"
FT DOMAIN 224..283
FT /note="SH3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00192"
FT REGION 140..164
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 178..218
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 380..597
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 183..218
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 388..414
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 433..461
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 507..534
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 538..567
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 597 AA; 65592 MW; 6889980721DD6CEE CRC64;
MFRAQQNAFD DAVAKATDEN LTSENWEYIL DVCDKVAAEE SGAKDAVAAL IKRLAHRNAN
VQLYTLELGN ALAQNCGPKI HRELASRSFT DALLRLANDR NTHQQVKAKI LERMQEWTEM
FASNPDFGIM EQAYMKLKTQ NPNLQPPSKP GKREITEADR QKEEEELQMA LALSIREKPS
TAPHPQAESS ASAAAAATTP TGAASAGQAQ PAASQAVPSG TSAATVSRVR ALFDFQPSEP
GELQFRKGDV IAVLESVYKD WWKGSLRGQT GIFPLNYVEK LPDPTVEELQ REAQMEAEVF
GQIKNVEKLL TLLSTRSSEP NVQDNEEITA LYHSTLAIRP KLIELIGKYS QKKDEFTQLN
EKFIKARRDY EALLEASMSH PAQPQYGRPG QPQYPYPGPG APMGYPPGGP QPDQRYFSPR
PQGHMYPPTS QSPGPRNHTP PAAAPYQQAP SHPPAQPQQH TAPDAYPPQH HRPESTYDHP
QELSTSVYDS PVEQRPPYPG AQIPAAIHQH FQQQQQQQQD YSPSVYSPDE SKPPGTQQVP
YPATPAANQP PPMHQPPPVP GAAAAPTPYP VNAPGASYQA YKPPQGGPAS NPASFYQ
//
