ASI1_YEAST
ID ASI1_YEAST Reviewed; 624 AA.
AC P54074; D6VZU2;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 146.
DE RecName: Full=ERAD-associated E3 ubiquitin-protein ligase ASI1;
DE EC=2.3.2.27;
DE AltName: Full=Amino acid sensor-independent protein 1;
GN Name=ASI1; OrderedLocusNames=YMR119W; ORFNames=YM8564.01, YM9718.18;
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 [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169872;
RA Bowman S., Churcher C.M., Badcock K., Brown D., Chillingworth T.,
RA Connor R., Dedman K., Devlin K., Gentles S., Hamlin N., Hunt S., Jagels K.,
RA Lye G., Moule S., Odell C., Pearson D., Rajandream M.A., Rice P.,
RA Skelton J., Walsh S.V., Whitehead S., Barrell B.G.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XIII.";
RL Nature 387:90-93(1997).
RN [2]
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 [3]
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 [4]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX PubMed=14562095; DOI=10.1038/nature02026;
RA Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W.,
RA Weissman J.S., O'Shea E.K.;
RT "Global analysis of protein localization in budding yeast.";
RL Nature 425:686-691(2003).
RN [5]
RP FUNCTION, SUBCELLULAR LOCATION, GLYCOSYLATION AT ASN-2; ASN-19 AND ASN-29,
RP TOPOLOGY, AND MUTAGENESIS OF CYS-583 AND CYS-585.
RX PubMed=16735580; DOI=10.1083/jcb.200601011;
RA Boban M., Zargari A., Andreasson C., Heessen S., Thyberg J.,
RA Ljungdahl P.O.;
RT "Asi1 is an inner nuclear membrane protein that restricts promoter access
RT of two latent transcription factors.";
RL J. Cell Biol. 173:695-707(2006).
RN [6]
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 [7]
RP FUNCTION, SUBCELLULAR LOCATION, GLYCOSYLATION AT ASN-2; ASN-19 AND ASN-29,
RP AND INTERACTION WITH ASI3.
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 [8]
RP FUNCTION, CATALYTIC ACTIVITY, 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).
RN [9]
RP SUBCELLULAR LOCATION.
RX PubMed=27831485; DOI=10.1083/jcb.201607043;
RA Smoyer C.J., Katta S.S., Gardner J.M., Stoltz L., McCroskey S.,
RA Bradford W.D., McClain M., Smith S.E., Slaughter B.D., Unruh J.R.,
RA Jaspersen S.L.;
RT "Analysis of membrane proteins localizing to the inner nuclear envelope in
RT living cells.";
RL J. Cell Biol. 215:575-590(2016).
CC -!- FUNCTION: E3 ubiquitin-protein ligase which transfers ubiquitin to
CC substrates promoting their degradation. Part of the nuclear inner
CC membrane (INM)-specific branch of the ER-associated degradation (ERAD)
CC pathway, required for the elimination of misfolded proteins in the INM,
CC a specialized ER subdomain. Required for ERG11 degradation
CC (PubMed:25236469). Negative regulator of SPS-sensor signaling. Together
CC with ASI2 and ASI3, prevents the unprocessed precursor forms of STP1
CC and STP2 that escape cytoplasmic anchoring from inducing SPS-sensor-
CC regulated genes in the absence of inducing signals (PubMed:16735580,
CC PubMed:17085444). Controls amino acid permease (AAP) gene expression in
CC response to amino acid availability, a process mediated by the
CC transcription factors STP1 and STP1 (PubMed:11454748).
CC {ECO:0000269|PubMed:11454748, ECO:0000269|PubMed:16735580,
CC ECO:0000269|PubMed:17085444, ECO:0000269|PubMed:25236469}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine +
CC [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-
CC cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine.;
CC EC=2.3.2.27; Evidence={ECO:0000305|PubMed:25236469};
CC -!- SUBUNIT: Component of the Asi complex, which contains ASI1, ASI2 and
CC ASI3 (PubMed:25236469). Interacts directly with ASI3 (PubMed:17085444).
CC {ECO:0000269|PubMed:17085444, ECO:0000269|PubMed:25236469}.
CC -!- INTERACTION:
CC P54074; P53983: ASI3; NbExp=5; IntAct=EBI-27241, EBI-28603;
CC -!- SUBCELLULAR LOCATION: Nucleus inner membrane
CC {ECO:0000269|PubMed:14562095, ECO:0000269|PubMed:16735580,
CC ECO:0000269|PubMed:17085444, ECO:0000269|PubMed:27831485}; Multi-pass
CC membrane protein {ECO:0000269|PubMed:14562095,
CC ECO:0000269|PubMed:16735580, ECO:0000269|PubMed:17085444}.
CC -!- PTM: Glycosylation is not required for ASI1 function.
CC {ECO:0000269|PubMed:16735580, ECO:0000269|PubMed:17085444}.
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DR EMBL; Z49702; CAA89757.1; -; Genomic_DNA.
DR EMBL; Z49273; CAA89268.1; -; Genomic_DNA.
DR EMBL; BK006946; DAA10016.1; -; Genomic_DNA.
DR PIR; S54581; S54581.
DR RefSeq; NP_013837.1; NM_001182619.1.
DR AlphaFoldDB; P54074; -.
DR BioGRID; 35296; 96.
DR ComplexPortal; CPX-3248; Asi ubiquitin ligase complex.
DR DIP; DIP-7733N; -.
DR IntAct; P54074; 3.
DR STRING; 4932.YMR119W; -.
DR iPTMnet; P54074; -.
DR MaxQB; P54074; -.
DR PaxDb; P54074; -.
DR PRIDE; P54074; -.
DR EnsemblFungi; YMR119W_mRNA; YMR119W; YMR119W.
DR GeneID; 855147; -.
DR KEGG; sce:YMR119W; -.
DR SGD; S000004725; ASI1.
DR VEuPathDB; FungiDB:YMR119W; -.
DR eggNOG; ENOG502QV7Y; Eukaryota.
DR GeneTree; ENSGT00940000176791; -.
DR HOGENOM; CLU_026112_0_0_1; -.
DR InParanoid; P54074; -.
DR OMA; CFALCED; -.
DR BioCyc; YEAST:G3O-32814-MON; -.
DR PRO; PR:P54074; -.
DR Proteomes; UP000002311; Chromosome XIII.
DR RNAct; P54074; protein.
DR GO; GO:0097658; C:Asi complex; IDA: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:0034399; C:nuclear periphery; HDA:SGD.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0061630; F:ubiquitin protein ligase activity; IBA:GO_Central.
DR GO; GO:0004842; F:ubiquitin-protein transferase activity; IMP:SGD.
DR GO; GO:0071230; P:cellular response to amino acid stimulus; IMP:SGD.
DR GO; GO:0016567; P:protein ubiquitination; IBA:GO_Central.
DR GO; GO:0036369; P:transcription factor catabolic process; IMP:SGD.
DR GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IMP:SGD.
DR Gene3D; 3.30.40.10; -; 1.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
PE 1: Evidence at protein level;
KW Glycoprotein; Membrane; Metal-binding; Nucleus; Reference proteome;
KW Transferase; Transmembrane; Transmembrane helix; Zinc; Zinc-finger.
FT CHAIN 1..624
FT /note="ERAD-associated E3 ubiquitin-protein ligase ASI1"
FT /id="PRO_0000203295"
FT TOPO_DOM 1..69
FT /note="Perinuclear space"
FT /evidence="ECO:0000269|PubMed:16735580,
FT ECO:0000305|PubMed:16847258"
FT TRANSMEM 70..90
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 91..116
FT /note="Nuclear"
FT /evidence="ECO:0000269|PubMed:16735580,
FT ECO:0000305|PubMed:16847258"
FT TRANSMEM 117..137
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 138..152
FT /note="Perinuclear space"
FT /evidence="ECO:0000269|PubMed:16735580,
FT ECO:0000305|PubMed:16847258"
FT TRANSMEM 153..173
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 174..209
FT /note="Nuclear"
FT /evidence="ECO:0000305|PubMed:16735580,
FT ECO:0000305|PubMed:16847258"
FT TRANSMEM 210..230
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 231..273
FT /note="Perinuclear space"
FT /evidence="ECO:0000269|PubMed:16735580,
FT ECO:0000305|PubMed:16847258"
FT TRANSMEM 274..294
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 295..624
FT /note="Nuclear"
FT /evidence="ECO:0000269|PubMed:16735580,
FT ECO:0000269|PubMed:16847258"
FT ZN_FING 568..608
FT /note="RING-type; atypical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
FT REGION 467..490
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 2
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:16735580,
FT ECO:0000269|PubMed:17085444"
FT CARBOHYD 19
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:16735580,
FT ECO:0000269|PubMed:17085444"
FT CARBOHYD 29
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:16735580,
FT ECO:0000269|PubMed:17085444"
FT MUTAGEN 583
FT /note="C->S: In ASI1-21HA; when associated with S-585;
FT abolishes function."
FT /evidence="ECO:0000269|PubMed:16735580"
FT MUTAGEN 585
FT /note="C->S: In ASI1-21HA; when associated with S-583;
FT abolishes function."
FT /evidence="ECO:0000269|PubMed:16735580"
SQ SEQUENCE 624 AA; 71444 MW; E2F5149F89A09655 CRC64;
MNSSTSSENV FINSFSYLNQ TSQAVISGNS TFANVINFPY RLGLSFIGAV NLQYEQTVKS
EEIPPTLRSV FDTIGFFFSP YAIFCFVIAI VLNRFVVFYA VLNNGSRRTL PLWLSNVFHV
SAVVVLAMVS LGPLTLGKDF KILGDPAFAQ EKFLLNIFYA FAYSYCVETI FTIMRNSSPL
EGTDYSLFEL SIQFYTMTNN NTKFLDSPDY IIDCSMAILS RILIHLVEIF RLRNYRLLFS
TIMNLCHICY LGIRVKQGGW KSLPFSVKFR HFPKLFSVSI ICLSLLIFKL SCLIRWDPFG
KSRNSCELLQ FYPLSRNWKK YLNYTGEEDF SAMATKFALL LCSGTELMEK GIRREFPAIN
IPDNVNEKFF ISGYLNELSK PYKENTSISF PKKNSSILKQ RFFLMFPKSI IWIMKKLVGQ
VFFGFRDNKD EDIPDNDPSK MLKITKTNSL NNSAGHKEDI ELELLNTSDD EYSEDYEPSE
VESLGDSDEE NLEEDSLIFN ETRDALLDLF SSEDNEVHTD YNWIMSTSRI LQQKLLSDKT
LTRASILDTK LSEVDETFGT ESDFDLSCAV CKVNERNTVL WPCRCFAICE DCRISLGLRG
FSTCVCCRSK VHGYCKVHPV SDSK
