ASI2_YEAST
ID ASI2_YEAST Reviewed; 289 AA.
AC P53895; D6W124;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 135.
DE RecName: Full=Protein ASI2;
DE AltName: Full=Amino acid sensor-independent protein 2;
GN Name=ASI2; OrderedLocusNames=YNL159C; ORFNames=N1735;
OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=559292;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 96604 / S288c / FY1679;
RX PubMed=8686380;
RX DOI=10.1002/(sici)1097-0061(199602)12:2<169::aid-yea894>3.0.co;2-b;
RA Nasr F., Becam A.-M., Herbert C.J.;
RT "The sequence of 36.8 kb from the left arm of chromosome XIV reveals 24
RT complete open reading frames: 18 correspond to new genes, one of which
RT encodes a protein similar to the human myotonic dystrophy kinase.";
RL Yeast 12:169-175(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169873;
RA Philippsen P., Kleine K., Poehlmann R., Duesterhoeft A., Hamberg K.,
RA Hegemann J.H., Obermaier B., Urrestarazu L.A., Aert R., Albermann K.,
RA Altmann R., Andre B., Baladron V., Ballesta J.P.G., Becam A.-M.,
RA Beinhauer J.D., Boskovic J., Buitrago M.J., Bussereau F., Coster F.,
RA Crouzet M., D'Angelo M., Dal Pero F., De Antoni A., del Rey F., Doignon F.,
RA Domdey H., Dubois E., Fiedler T.A., Fleig U., Floeth M., Fritz C.,
RA Gaillardin C., Garcia-Cantalejo J.M., Glansdorff N., Goffeau A.,
RA Gueldener U., Herbert C.J., Heumann K., Heuss-Neitzel D., Hilbert H.,
RA Hinni K., Iraqui Houssaini I., Jacquet M., Jimenez A., Jonniaux J.-L.,
RA Karpfinger-Hartl L., Lanfranchi G., Lepingle A., Levesque H., Lyck R.,
RA Maftahi M., Mallet L., Maurer C.T.C., Messenguy F., Mewes H.-W., Moestl D.,
RA Nasr F., Nicaud J.-M., Niedenthal R.K., Pandolfo D., Pierard A.,
RA Piravandi E., Planta R.J., Pohl T.M., Purnelle B., Rebischung C.,
RA Remacha M.A., Revuelta J.L., Rinke M., Saiz J.E., Sartorello F.,
RA Scherens B., Sen-Gupta M., Soler-Mira A., Urbanus J.H.M., Valle G.,
RA Van Dyck L., Verhasselt P., Vierendeels F., Vissers S., Voet M.,
RA Volckaert G., Wach A., Wambutt R., Wedler H., Zollner A., Hani J.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XIV and its
RT evolutionary implications.";
RL Nature 387:93-98(1997).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=24374639; DOI=10.1534/g3.113.008995;
RA Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL G3 (Bethesda) 4:389-398(2014).
RN [4]
RP FUNCTION.
RX PubMed=11454748; DOI=10.1093/genetics/158.3.973;
RA Forsberg H., Hammar M., Andreasson C., Moliner A., Ljungdahl P.O.;
RT "Suppressors of ssy1 and ptr3 null mutations define novel amino acid
RT sensor-independent genes in Saccharomyces cerevisiae.";
RL Genetics 158:973-988(2001).
RN [5]
RP TOPOLOGY [LARGE SCALE ANALYSIS].
RC STRAIN=ATCC 208353 / W303-1A;
RX PubMed=16847258; DOI=10.1073/pnas.0604075103;
RA Kim H., Melen K., Oesterberg M., von Heijne G.;
RT "A global topology map of the Saccharomyces cerevisiae membrane proteome.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:11142-11147(2006).
RN [6]
RP FUNCTION, SUBCELLULAR LOCATION, TOPOLOGY, AND LACK OF GLYCOSYLATION.
RX PubMed=17085444; DOI=10.1074/jbc.m609201200;
RA Zargari A., Boban M., Heessen S., Andreasson C., Thyberg J.,
RA Ljungdahl P.O.;
RT "Inner nuclear membrane proteins Asi1, Asi2, and Asi3 function in concert
RT to maintain the latent properties of transcription factors Stp1 and Stp2.";
RL J. Biol. Chem. 282:594-605(2007).
RN [7]
RP FUNCTION, AND SUBUNIT.
RX PubMed=25236469; DOI=10.1126/science.1255638;
RA Foresti O., Rodriguez-Vaello V., Funaya C., Carvalho P.;
RT "Quality control of inner nuclear membrane proteins by the Asi complex.";
RL Science 346:751-755(2014).
CC -!- FUNCTION: Part of the nuclear inner membrane (INM)-specific branch of
CC the ER-associated degradation (ERAD) pathway, required for the
CC elimination of misfolded proteins in the INM, a specialized ER
CC subdomain. Required for ERG11 degradation (PubMed:25236469). Negative
CC regulator of SPS-sensor signaling. Together with ASI2 and ASI3,
CC prevents the unprocessed precursor forms of STP1 and STP2 that escape
CC cytoplasmic anchoring from inducing SPS-sensor-regulated genes in the
CC absence of inducing signals (PubMed:17085444). Controls amino acid
CC permease (AAP) gene expression in response to amino acid availability,
CC a process mediated by the transcription factors STP1 and STP1
CC (PubMed:11454748). {ECO:0000269|PubMed:11454748,
CC ECO:0000269|PubMed:17085444, ECO:0000269|PubMed:25236469}.
CC -!- SUBUNIT: Component of the Asi complex, which contains ASI1, ASI2 and
CC ASI3. {ECO:0000269|PubMed:25236469}.
CC -!- SUBCELLULAR LOCATION: Nucleus inner membrane
CC {ECO:0000269|PubMed:17085444}; Multi-pass membrane protein
CC {ECO:0000269|PubMed:17085444}.
CC -!- PTM: Not glycosylated. {ECO:0000269|PubMed:17085444}.
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DR EMBL; X92517; CAA63280.1; -; Genomic_DNA.
DR EMBL; Z71435; CAA96046.1; -; Genomic_DNA.
DR EMBL; BK006947; DAA10390.1; -; Genomic_DNA.
DR PIR; S60968; S60968.
DR RefSeq; NP_014240.1; NM_001182997.1.
DR AlphaFoldDB; P53895; -.
DR SMR; P53895; -.
DR BioGRID; 35670; 210.
DR ComplexPortal; CPX-3248; Asi ubiquitin ligase complex.
DR DIP; DIP-4337N; -.
DR IntAct; P53895; 4.
DR STRING; 4932.YNL159C; -.
DR iPTMnet; P53895; -.
DR PaxDb; P53895; -.
DR PRIDE; P53895; -.
DR EnsemblFungi; YNL159C_mRNA; YNL159C; YNL159C.
DR GeneID; 855563; -.
DR KEGG; sce:YNL159C; -.
DR SGD; S000005103; ASI2.
DR VEuPathDB; FungiDB:YNL159C; -.
DR eggNOG; ENOG502RZCQ; Eukaryota.
DR HOGENOM; CLU_074623_0_0_1; -.
DR InParanoid; P53895; -.
DR OMA; RYKGVHR; -.
DR BioCyc; YEAST:G3O-33175-MON; -.
DR PRO; PR:P53895; -.
DR Proteomes; UP000002311; Chromosome XIV.
DR RNAct; P53895; protein.
DR GO; GO:0097658; C:Asi complex; IDA:SGD.
DR GO; GO:0005783; C:endoplasmic reticulum; HDA:SGD.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005637; C:nuclear inner membrane; IDA:SGD.
DR GO; GO:0071230; P:cellular response to amino acid stimulus; IMP:SGD.
DR GO; GO:0036369; P:transcription factor catabolic process; IMP:SGD.
DR GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IMP:SGD.
PE 1: Evidence at protein level;
KW Membrane; Nucleus; Reference proteome; Transmembrane; Transmembrane helix.
FT CHAIN 1..289
FT /note="Protein ASI2"
FT /id="PRO_0000203414"
FT TOPO_DOM 1..222
FT /note="Nuclear"
FT /evidence="ECO:0000269|PubMed:17085444"
FT TRANSMEM 223..243
FT /note="Helical"
FT /evidence="ECO:0000305|PubMed:17085444"
FT TOPO_DOM 244..247
FT /note="Perinuclear space"
FT /evidence="ECO:0000269|PubMed:17085444"
FT TRANSMEM 248..268
FT /note="Helical"
FT /evidence="ECO:0000305|PubMed:17085444"
FT TOPO_DOM 269..289
FT /note="Nuclear"
FT /evidence="ECO:0000269|PubMed:17085444"
FT REGION 28..50
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 289 AA; 32986 MW; 95C425488F1E3724 CRC64;
MARPQNHRRS NWTERDDNDD YLFQRFLEES ETRHSREPSP VTEQSQQELQ QDVQQAIDGI
FNSLRRNMSS TSNINRAANM DATTNGNGGI NADTIRATNA NTADSPFTAR QQSPLRTFLR
NLFILDYFIG LILFPFSVYN ILRSGFNSMT FSENDFIIEI VGYWKFAKIF GSGGTTLIAY
KDTGKLGLLG KFHNIIVFYS SPVIKHIMKS RDGNEPNLNW IRLMFAKAFE LFVKVSTILI
YLAYGVSGTV YMVTAGFFFV LCLLFTVIRR YKGVHRMLVS QRITGPGVF
