ASI3_YEAST
ID ASI3_YEAST Reviewed; 676 AA.
AC P53983; D6W1G9;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 21-SEP-2011, sequence version 2.
DT 03-AUG-2022, entry version 140.
DE RecName: Full=Probable ERAD-associated E3 ubiquitin-protein ligase ASI1;
DE EC=2.3.2.27;
DE AltName: Full=Amino acid sensor-independent protein 3;
GN Name=ASI3; OrderedLocusNames=YNL008C; ORFNames=N2874;
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=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 [2]
RP GENOME REANNOTATION, AND SEQUENCE REVISION.
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 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, GLYCOSYLATION, AND INTERACTION WITH ASI1.
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 -!- 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:11454748};
CC -!- SUBUNIT: Component of the Asi complex, which contains ASI1, ASI2 and
CC ASI3 (PubMed:25236469). Interacts directly with ASI1 (PubMed:17085444).
CC {ECO:0000269|PubMed:17085444, ECO:0000269|PubMed:25236469}.
CC -!- INTERACTION:
CC P53983; P54074: ASI1; NbExp=5; IntAct=EBI-28603, EBI-27241;
CC -!- SUBCELLULAR LOCATION: Nucleus inner membrane
CC {ECO:0000269|PubMed:14562095, ECO:0000269|PubMed:17085444}; Multi-pass
CC membrane protein {ECO:0000269|PubMed:14562095,
CC ECO:0000269|PubMed:17085444}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; Z71284; CAA95868.1; -; Genomic_DNA.
DR EMBL; Z71283; CAA95867.1; -; Genomic_DNA.
DR EMBL; BK006947; DAA10535.2; -; Genomic_DNA.
DR PIR; S62919; S62919.
DR RefSeq; NP_014390.2; NM_001182847.2.
DR AlphaFoldDB; P53983; -.
DR BioGRID; 35817; 123.
DR ComplexPortal; CPX-3248; Asi ubiquitin ligase complex.
DR DIP; DIP-5065N; -.
DR IntAct; P53983; 9.
DR MINT; P53983; -.
DR STRING; 4932.YNL008C; -.
DR MaxQB; P53983; -.
DR PaxDb; P53983; -.
DR PRIDE; P53983; -.
DR EnsemblFungi; YNL008C_mRNA; YNL008C; YNL008C.
DR GeneID; 855724; -.
DR KEGG; sce:YNL008C; -.
DR SGD; S000004953; ASI3.
DR VEuPathDB; FungiDB:YNL008C; -.
DR eggNOG; ENOG502S2K4; Eukaryota.
DR GeneTree; ENSGT00940000176791; -.
DR HOGENOM; CLU_026112_0_0_1; -.
DR InParanoid; P53983; -.
DR OMA; CLSHCIE; -.
DR BioCyc; YEAST:G3O-33050-MON; -.
DR PRO; PR:P53983; -.
DR Proteomes; UP000002311; Chromosome XIV.
DR RNAct; P53983; 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:0004842; F:ubiquitin-protein transferase activity; IGI: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.
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..676
FT /note="Probable ERAD-associated E3 ubiquitin-protein ligase
FT ASI1"
FT /id="PRO_0000203467"
FT TOPO_DOM 1..78
FT /note="Perinuclear space"
FT /evidence="ECO:0000305|PubMed:16847258"
FT TRANSMEM 79..99
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 100..126
FT /note="Nuclear"
FT /evidence="ECO:0000305|PubMed:16847258"
FT TRANSMEM 127..147
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 148..156
FT /note="Perinuclear space"
FT /evidence="ECO:0000305|PubMed:16847258"
FT TRANSMEM 157..177
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 178..181
FT /note="Nuclear"
FT /evidence="ECO:0000305|PubMed:16847258"
FT TRANSMEM 182..202
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 203..277
FT /note="Perinuclear space"
FT /evidence="ECO:0000305|PubMed:16847258"
FT TRANSMEM 278..298
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 299..676
FT /note="Nuclear"
FT /evidence="ECO:0000269|PubMed:16847258"
FT ZN_FING 624..664
FT /note="RING-type; atypical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
FT CARBOHYD 24
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 34
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 46
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 66
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CONFLICT 1..15
FT /note="MSTNILQHVKQLLHN -> MLSNCSIT (in Ref. 1; CAA95867/
FT CAA95868)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 676 AA; 77649 MW; 58ECCEA014034A3B CRC64;
MSTNILQHVK QLLHNRDVFS FFHNKTGNLN YLDNTTQKPE VFVSPNSTIV SAPTLDSFQA
LMEKGNFTTL QLAKVGIRMF FSYSVSKYAV LCFSTAIILN RLTVMSSLRS NSTNIRLPLW
SKTLLHLVAT LSLVKALLQI LSQFGLMHEL HVSDTDFYAL SVYLFVALSD CIEIFISSTT
NVPSLICSDF SIWGLSLNLY IISKMPAGQQ HIGDNVELLG AVFHRLVIHL VELFHIRAYR
LCGEVILNAG FFTAFVTRTY LNGLDFINIC LIHNYFPGFF YISTILLASI GIFLKALFTS
NPFRSLYSRY KNLEKWWRSN NYNGEEEFNE IALSLCLLLT SNDYKIFKKS DNVKSVDEVA
AFSNSYVVSG HLNQLQSTPE DLLSRKEMTT DSQLPGFART YLGLFELVRT IILTYSRLLK
NLLWSKNFES SIDKKPRVGK RKKRDLNKYV TEKNYKKFLY KPDVKELNIE SDLRSLELLL
PEDDSSKDYF PPRKIDESVS DEEFDSDMES QLIIDEEKEL THLSSNAVDS DDLEEIAWNI
SMWSILNYEM DVHNKVNGPL TRSQYGKRNP QGVLVDVVIE RLLHHTNSRY MYKRLNMKDD
DKLEFKFDFA FDSCDEVEEM DLSCLICKVN KRNIVTWPCR CLALCDDCRI SLGYKGFATC
VSCDSEVKGY SKLNIV
