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AT222_ASPNC
ID   AT222_ASPNC             Reviewed;         600 AA.
AC   A2QTX8;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   06-MAR-2007, sequence version 1.
DT   25-MAY-2022, entry version 62.
DE   RecName: Full=Autophagy-related protein 22-2;
GN   Name=atg22-2; ORFNames=An09g03630;
OS   Aspergillus niger (strain CBS 513.88 / FGSC A1513).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Circumdati.
OX   NCBI_TaxID=425011;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 513.88 / FGSC A1513 / ATCC MYA-4892;
RX   PubMed=17259976; DOI=10.1038/nbt1282;
RA   Pel H.J., de Winde J.H., Archer D.B., Dyer P.S., Hofmann G., Schaap P.J.,
RA   Turner G., de Vries R.P., Albang R., Albermann K., Andersen M.R.,
RA   Bendtsen J.D., Benen J.A.E., van den Berg M., Breestraat S., Caddick M.X.,
RA   Contreras R., Cornell M., Coutinho P.M., Danchin E.G.J., Debets A.J.M.,
RA   Dekker P., van Dijck P.W.M., van Dijk A., Dijkhuizen L., Driessen A.J.M.,
RA   d'Enfert C., Geysens S., Goosen C., Groot G.S.P., de Groot P.W.J.,
RA   Guillemette T., Henrissat B., Herweijer M., van den Hombergh J.P.T.W.,
RA   van den Hondel C.A.M.J.J., van der Heijden R.T.J.M., van der Kaaij R.M.,
RA   Klis F.M., Kools H.J., Kubicek C.P., van Kuyk P.A., Lauber J., Lu X.,
RA   van der Maarel M.J.E.C., Meulenberg R., Menke H., Mortimer M.A.,
RA   Nielsen J., Oliver S.G., Olsthoorn M., Pal K., van Peij N.N.M.E.,
RA   Ram A.F.J., Rinas U., Roubos J.A., Sagt C.M.J., Schmoll M., Sun J.,
RA   Ussery D., Varga J., Vervecken W., van de Vondervoort P.J.J., Wedler H.,
RA   Woesten H.A.B., Zeng A.-P., van Ooyen A.J.J., Visser J., Stam H.;
RT   "Genome sequencing and analysis of the versatile cell factory Aspergillus
RT   niger CBS 513.88.";
RL   Nat. Biotechnol. 25:221-231(2007).
CC   -!- FUNCTION: Vacuolar effluxer which mediate the efflux of amino acids
CC       resulting from autophagic degradation. The release of autophagic amino
CC       acids allows the maintenance of protein synthesis and viability during
CC       nitrogen starvation (By similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Vacuole membrane {ECO:0000250}; Multi-pass
CC       membrane protein {ECO:0000250}. Note=Vacuole and punctate structures.
CC       {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the ATG22 family. {ECO:0000305}.
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DR   EMBL; AM270199; CAK96806.1; -; Genomic_DNA.
DR   AlphaFoldDB; A2QTX8; -.
DR   PaxDb; A2QTX8; -.
DR   EnsemblFungi; CAK96806; CAK96806; An09g03630.
DR   VEuPathDB; FungiDB:An09g03630; -.
DR   HOGENOM; CLU_017518_1_0_1; -.
DR   Proteomes; UP000006706; Chromosome 1L.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005774; C:vacuolar membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0032974; P:amino acid transmembrane export from vacuole; IEA:InterPro.
DR   GO; GO:0006914; P:autophagy; IEA:UniProtKB-KW.
DR   CDD; cd17483; MFS_Atg22_like; 1.
DR   Gene3D; 1.20.1250.20; -; 1.
DR   InterPro; IPR044738; Atg22.
DR   InterPro; IPR024671; Atg22-like.
DR   InterPro; IPR036259; MFS_trans_sf.
DR   Pfam; PF11700; ATG22; 1.
DR   SUPFAM; SSF103473; SSF103473; 1.
PE   3: Inferred from homology;
KW   Amino-acid transport; Autophagy; Glycoprotein; Membrane;
KW   Reference proteome; Transmembrane; Transmembrane helix; Transport; Vacuole.
FT   CHAIN           1..600
FT                   /note="Autophagy-related protein 22-2"
FT                   /id="PRO_0000318017"
FT   TRANSMEM        41..61
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        117..137
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        149..168
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        186..206
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        271..291
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        304..324
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        378..398
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        414..434
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        449..469
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        484..506
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        526..546
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        549..569
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   REGION          1..30
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          234..257
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CARBOHYD        444
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   600 AA;  64957 MW;  BCA3221BF5B2D92D CRC64;
     MAFASPPASP PDEDGQARAP RYPGEDTTPT SRQEIWGWYA YGIAAEVFAV CGVGSFLPLT
     LEQLARERGF LQSSHLPCVG PDSPSAPKES SPAMFRRDDT NEQCVVGLMG LEINTASFAM
     YTFSLAVLVQ ALTLISFSAL ADYENNRKTL LVTFGFIGSA TSMLFVFIAP PVFVLGALLV
     VVGVVCLGSS FVVLNSFLPV LVASDPSIQN SNKESAAELH RLDPEAEYVH ARTSFDGDEP
     THRPPTGLGL GGATGTSSPE LQLSTKISSK GVGLGYCAAV FVQILSILLL FTLSKTSISK
     ASGTLPLRFV LLLVGIWWFS FTMVSRRWLR NRPGPPLEST STGASSHQPR WRIWLHLVAF
     AWKSLWKTVK IALKLREVIV FLVAWFLLSD AMATVSGTAI LFARTELKMS TTMVALLSIT
     ATLSGMAGAF LWPIVSRYFG LKSNHTIMVC IALFELIPLY GMLAYIPLFK KWGVIGLQQP
     WEIYPLAIVH GVVSGGLSSY CRSFFGLLIP PGMEAAFYAL YAATDKGSSF IGPAIVGVLI
     DATGQVRSGF FFIAVLIVLP IPLVWMVDAE KGRKEGLKIS EDVVRGGEGE DEEVEGLLAR
 
 
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