ID G0VCJ9_NAUCC Unreviewed; 237 AA.
AC G0VCJ9;
DT 19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT 19-OCT-2011, sequence version 1.
DT 27-MAR-2024, entry version 53.
DE RecName: Full=Vacuolar protein sorting-associated protein 28 {ECO:0000256|PIRNR:PIRNR017535};
DE AltName: Full=ESCRT-I complex subunit VPS28 {ECO:0000256|PIRNR:PIRNR017535};
GN Name=NCAS0C02190 {ECO:0000313|EMBL:CCC69209.1};
GN OrderedLocusNames=NCAS_0C02190 {ECO:0000313|EMBL:CCC69209.1};
OS Naumovozyma castellii (strain ATCC 76901 / BCRC 22586 / CBS 4309 / NBRC
OS 1992 / NRRL Y-12630) (Yeast) (Saccharomyces castellii).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Naumovozyma.
OX NCBI_TaxID=1064592 {ECO:0000313|EMBL:CCC69209.1, ECO:0000313|Proteomes:UP000001640};
RN [1] {ECO:0000313|EMBL:CCC69209.1, ECO:0000313|Proteomes:UP000001640}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 76901 / BCRC 22586 / CBS 4309 / NBRC 1992 / NRRL Y-12630
RC {ECO:0000313|Proteomes:UP000001640};
RX PubMed=22123960; DOI=10.1073/pnas.1112808108;
RA Gordon J.L., Armisen D., Proux-Wera E., OhEigeartaigh S.S., Byrne K.P.,
RA Wolfe K.H.;
RT "Evolutionary erosion of yeast sex chromosomes by mating-type switching
RT accidents.";
RL Proc. Natl. Acad. Sci. U.S.A. 108:20024-20029(2011).
RN [2]
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Type strain:CBS 4309;
RA Gordon J.L., Armisen D., Proux-Wera E., OhEigeartaigh S.S., Byrne K.P.,
RA Wolfe K.H.;
RT "Genome sequence of Naumovozyma castellii.";
RL Submitted (AUG-2011) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Component of the ESCRT-I complex (endosomal sorting complex
CC required for transport I), a regulator of vesicular trafficking
CC process. {ECO:0000256|PIRNR:PIRNR017535}.
CC -!- SIMILARITY: Belongs to the VPS28 family.
CC {ECO:0000256|PIRNR:PIRNR017535, ECO:0000256|PROSITE-ProRule:PRU00642}.
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DR EMBL; HE576754; CCC69209.1; -; Genomic_DNA.
DR RefSeq; XP_003675575.1; XM_003675527.1.
DR AlphaFoldDB; G0VCJ9; -.
DR STRING; 1064592.G0VCJ9; -.
DR GeneID; 11527903; -.
DR KEGG; ncs:NCAS_0C02190; -.
DR eggNOG; KOG3284; Eukaryota.
DR HOGENOM; CLU_076417_0_0_1; -.
DR InParanoid; G0VCJ9; -.
DR OMA; CDEFPTV; -.
DR OrthoDB; 5486880at2759; -.
DR Proteomes; UP000001640; Chromosome 3.
DR GO; GO:0000813; C:ESCRT I complex; IEA:UniProtKB-UniRule.
DR GO; GO:0032509; P:endosome transport via multivesicular body sorting pathway; IEA:InterPro.
DR GO; GO:0072666; P:establishment of protein localization to vacuole; IEA:UniProt.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-UniRule.
DR GO; GO:0043162; P:ubiquitin-dependent protein catabolic process via the multivesicular body sorting pathway; IEA:UniProt.
DR GO; GO:0007034; P:vacuolar transport; IEA:UniProt.
DR Gene3D; 1.20.120.1130; -; 1.
DR Gene3D; 1.20.1440.200; -; 1.
DR InterPro; IPR037202; ESCRT_assembly_dom.
DR InterPro; IPR007143; Vps28.
DR InterPro; IPR017899; VPS28_C.
DR InterPro; IPR037206; VPS28_C_sf.
DR InterPro; IPR017898; VPS28_N.
DR InterPro; IPR038358; VPS28_N_sf.
DR PANTHER; PTHR12937; VACUOLAR PROTEIN SORTING 28, ISOFORM 2 VPS28; 1.
DR PANTHER; PTHR12937:SF0; VACUOLAR PROTEIN SORTING-ASSOCIATED PROTEIN 28 HOMOLOG; 1.
DR Pfam; PF03997; VPS28; 1.
DR PIRSF; PIRSF017535; VPS28; 1.
DR SUPFAM; SSF140111; Endosomal sorting complex assembly domain; 1.
DR SUPFAM; SSF140427; VPS28 C-terminal domain-like; 1.
DR PROSITE; PS51310; VPS28_C; 1.
DR PROSITE; PS51313; VPS28_N; 1.
PE 3: Inferred from homology;
KW Endosome {ECO:0000256|ARBA:ARBA00022753, ECO:0000256|PIRNR:PIRNR017535};
KW Protein transport {ECO:0000256|ARBA:ARBA00022927,
KW ECO:0000256|PIRNR:PIRNR017535};
KW Reference proteome {ECO:0000313|Proteomes:UP000001640};
KW Transport {ECO:0000256|ARBA:ARBA00022448, ECO:0000256|PIRNR:PIRNR017535}.
FT DOMAIN 16..128
FT /note="VPS28 N-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51313"
FT DOMAIN 143..237
FT /note="VPS28 C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51310"
SQ SEQUENCE 237 AA; 27124 MW; D2771807F17C66C3 CRC64;
MSARAPINHF GTTNSTRPFP PQLYQELPLF PPETTTSKDK ETIDSLSEIY SIIIALDHVE
KAYLRDSITD SQYTATVNKL LAQYNTYLNN ENVRAQFHDL KHFRERFNIV ASNAITRLER
GIPVTVEHAI DNEQGQNQGE NKFNGKNVAE ATGNFITVMD ALKLNYKAKD QLHPLLAELL
LSVNRVTNVN FEHRAKLVEW IVKINKMQVD QLLTDNEVRE LLFDLDLAYK SFYALLG
//
