(data stored in SCRATCH zone)

SWISSPROT: Q757W9_ASHGO

ID   Q757W9_ASHGO            Unreviewed;       889 AA.
AC   Q757W9;
DT   05-JUL-2004, integrated into UniProtKB/TrEMBL.
DT   05-JUL-2004, sequence version 1.
DT   11-DEC-2019, entry version 89.
DE   RecName: Full=Vacuolar protein sorting-associated protein 35 {ECO:0000256|PIRNR:PIRNR009375};
GN   ORFNames=AGOS_AEL107W {ECO:0000313|EMBL:AAS52578.1};
OS   Ashbya gossypii (strain ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056)
OS   (Yeast) (Eremothecium gossypii).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Eremothecium.
OX   NCBI_TaxID=284811 {ECO:0000313|EMBL:AAS52578.1, ECO:0000313|Proteomes:UP000000591};
RN   [1] {ECO:0000313|EMBL:AAS52578.1, ECO:0000313|Proteomes:UP000000591}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056
RC   {ECO:0000313|Proteomes:UP000000591};
RX   PubMed=15001715; DOI=10.1126/science.1095781;
RA   Dietrich F.S., Voegeli S., Brachat S., Lerch A., Gates K., Steiner S.,
RA   Mohr C., Pohlmann R., Luedi P., Choi S., Wing R.A., Flavier A.,
RA   Gaffney T.D., Philippsen P.;
RT   "The Ashbya gossypii genome as a tool for mapping the ancient Saccharomyces
RT   cerevisiae genome.";
RL   Science 304:304-307(2004).
RN   [2] {ECO:0000313|Proteomes:UP000000591}
RP   GENOME REANNOTATION.
RC   STRAIN=ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056
RC   {ECO:0000313|Proteomes:UP000000591};
RX   PubMed=23749448; DOI=10.1534/g3.112.002881;
RA   Dietrich F.S., Voegeli S., Kuo S., Philippsen P.;
RT   "Genomes of Ashbya fungi isolated from insects reveal four mating-type
RT   loci, numerous translocations, lack of transposons, and distinct gene
RT   duplications.";
RL   G3 (Bethesda) 3:1225-1239(2013).
CC   -!- FUNCTION: Plays a role in vesicular protein sorting.
CC       {ECO:0000256|PIRNR:PIRNR009375}.
CC   -!- SIMILARITY: Belongs to the VPS35 family.
CC       {ECO:0000256|PIRNR:PIRNR009375}.
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DR   EMBL; AE016818; AAS52578.1; -; Genomic_DNA.
DR   RefSeq; NP_984754.1; NM_210108.1.
DR   STRING; 33169.AAS52578; -.
DR   EnsemblFungi; AAS52578; AAS52578; AGOS_AEL107W.
DR   GeneID; 4620943; -.
DR   KEGG; ago:AGOS_AEL107W; -.
DR   HOGENOM; HOG000196946; -.
DR   InParanoid; Q757W9; -.
DR   KO; K18468; -.
DR   OMA; HLWWATP; -.
DR   Proteomes; UP000000591; Chromosome V.
DR   GO; GO:0005623; C:cell; IEA:GOC.
DR   GO; GO:0005829; C:cytosol; IEA:GOC.
DR   GO; GO:0000329; C:fungal-type vacuole membrane; IEA:EnsemblFungi.
DR   GO; GO:0005770; C:late endosome; IBA:GO_Central.
DR   GO; GO:0030904; C:retromer complex; IBA:GO_Central.
DR   GO; GO:0030906; C:retromer, cargo-selective complex; IEA:EnsemblFungi.
DR   GO; GO:0140312; F:cargo adaptor activity; IEA:EnsemblFungi.
DR   GO; GO:0006886; P:intracellular protein transport; IBA:GO_Central.
DR   GO; GO:0060548; P:negative regulation of cell death; IEA:EnsemblFungi.
DR   GO; GO:1900102; P:negative regulation of endoplasmic reticulum unfolded protein response; IEA:EnsemblFungi.
DR   GO; GO:1904377; P:positive regulation of protein localization to cell periphery; IEA:EnsemblFungi.
DR   GO; GO:0045053; P:protein retention in Golgi apparatus; IEA:EnsemblFungi.
DR   GO; GO:0042147; P:retrograde transport, endosome to Golgi; IBA:GO_Central.
DR   Gene3D; 1.25.40.660; -; 1.
DR   InterPro; IPR005378; Vps35.
DR   InterPro; IPR042491; Vps35_C.
DR   PANTHER; PTHR11099; PTHR11099; 1.
DR   Pfam; PF03635; Vps35; 1.
DR   PIRSF; PIRSF009375; Retromer_Vps35; 1.
PE   3: Inferred from homology;
DR   PRODOM; Q757W9.
DR   SWISS-2DPAGE; Q757W9.
KW   Protein transport {ECO:0000256|PIRNR:PIRNR009375};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000591};
KW   Transport {ECO:0000256|PIRNR:PIRNR009375}.
SQ   SEQUENCE   889 AA;  101990 MW;  8AA5795E9A866D80 CRC64;
     MSYAESVEQA TGVIKQQTVL IQRHLAQRKL LDALKHISIM LTELRNPSLT PKQYYELYIL
     VYDALSVLSQ YLVENHPKRH HLADLYELVQ YAGNILPRLY LMITVGTAFL QIKDSPREEI
     LKDMIEMCKG VQNPVRGLFL RYYLSQRTKE WLLPQNGPAG NASEGRSQEN VENNVKKFNV
     EFIINNFIEM NKLWVRLQHY GPLRERELRT KERRELQILI GSNLVRLSQI VEDDSKLYAE
     VILPQLLDQI VQCRDVVSQE YLLDVICQVF PDEFHLATLP TLLETTLKFN PDVSINKVVS
     NLVERFNGYV ERQSGDIDSV QNTFRKLCIQ GQPTSASGDT ISSSGGLFFV FWRYLEKLSE
     QRPDLPLNDL FPLVQGILKL SLTWYPDVLS NVDCLFKFTV RKCQENGGPD ANPDYEYLFQ
     DLLLSMTSSS MFYRVLTECE SYQKLLSMQP VGLQKLVVNC ILDTIFKAGI TITNRIHLEK
     ILLLCESLIK VNNPKIHNSG EDAEQHSAQD DDPTSCLLNI EQEKLAQVVH ICRSQSIEKQ
     VELLLTCKSW FYKGGIQMRY TYPAVVTAFW KLIRKTDIKK SKYPSREKKY RQLIKQLFKY
     VSRCLSELGN TVGAPCADLV FKMNLQSAAI ADHLGLSEIS YDFFTQVFTI FEESLSDSRS
     QFQAIITMAQ TLQKTRSLYV ENYYDSLITR CTLYGSRLLK KQDQCRAVYL CSHLWWATEI
     PLIGEEEGIT DTFYREGKRV LECLQRSLRV ADSIMDNVQS CQLMVEILNR CCYYFVHGDE
     SATHVGPKYI NGLIELIETN LKSLKIEESV EFAESKLPKP SYANFVVGVD GSYIQVPTSP
     TATVAAVMSK PPNITISSLV PIVTGYLQRT LNYIEDQKVV DDRFRAIIV
//

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