ISN1_YEAST
ID ISN1_YEAST Reviewed; 450 AA.
AC Q99312; D6W2L2;
DT 08-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 146.
DE RecName: Full=IMP-specific 5'-nucleotidase 1 {ECO:0000303|PubMed:8141771};
DE EC=3.1.3.99 {ECO:0000269|PubMed:12735798, ECO:0000269|PubMed:8141771};
GN Name=ISN1; OrderedLocusNames=YOR155C; ORFNames=O3548;
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=S288c / FY1678;
RX PubMed=9046089;
RX DOI=10.1002/(sici)1097-0061(199701)13:1<73::aid-yea52>3.0.co;2-m;
RA Bordonne R., Camasses A., Madania A., Poch O., Tarassov I.A., Winsor B.,
RA Martin R.P.;
RT "Analysis of a 35.6 kb region on the right arm of Saccharomyces cerevisiae
RT chromosome XV.";
RL Yeast 13:73-83(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169874;
RA Dujon B., Albermann K., Aldea M., Alexandraki D., Ansorge W., Arino J.,
RA Benes V., Bohn C., Bolotin-Fukuhara M., Bordonne R., Boyer J., Camasses A.,
RA Casamayor A., Casas C., Cheret G., Cziepluch C., Daignan-Fornier B.,
RA Dang V.-D., de Haan M., Delius H., Durand P., Fairhead C., Feldmann H.,
RA Gaillon L., Galisson F., Gamo F.-J., Gancedo C., Goffeau A., Goulding S.E.,
RA Grivell L.A., Habbig B., Hand N.J., Hani J., Hattenhorst U., Hebling U.,
RA Hernando Y., Herrero E., Heumann K., Hiesel R., Hilger F., Hofmann B.,
RA Hollenberg C.P., Hughes B., Jauniaux J.-C., Kalogeropoulos A.,
RA Katsoulou C., Kordes E., Lafuente M.J., Landt O., Louis E.J., Maarse A.C.,
RA Madania A., Mannhaupt G., Marck C., Martin R.P., Mewes H.-W., Michaux G.,
RA Paces V., Parle-McDermott A.G., Pearson B.M., Perrin A., Pettersson B.,
RA Poch O., Pohl T.M., Poirey R., Portetelle D., Pujol A., Purnelle B.,
RA Ramezani Rad M., Rechmann S., Schwager C., Schweizer M., Sor F., Sterky F.,
RA Tarassov I.A., Teodoru C., Tettelin H., Thierry A., Tobiasch E.,
RA Tzermia M., Uhlen M., Unseld M., Valens M., Vandenbol M., Vetter I.,
RA Vlcek C., Voet M., Volckaert G., Voss H., Wambutt R., Wedler H.,
RA Wiemann S., Winsor B., Wolfe K.H., Zollner A., Zumstein E., Kleine K.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XV.";
RL Nature 387:98-102(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, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT,
RP COFACTOR, AND SUBSTRATE SPECIFICITY.
RX PubMed=8141771; DOI=10.1042/bj2980593;
RA Itoh R.;
RT "Purification and some properties of an IMP-specific 5'-nucleotidase from
RT yeast.";
RL Biochem. J. 298:593-598(1994).
RN [5]
RP FUNCTION, CATALYTIC ACTIVITY, IDENTIFICATION BY MASS SPECTROMETRY, AND
RP DOMAIN.
RX PubMed=12735798; DOI=10.1186/1471-2091-4-4;
RA Itoh R., Saint-Marc C., Chaignepain S., Katahira R., Schmitter J.-M.,
RA Daignan-Fornier B.;
RT "The yeast ISN1 (YOR155c) gene encodes a new type of IMP-specific 5'-
RT nucleotidase.";
RL BMC Biochem. 4:4-4(2003).
RN [6]
RP LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX PubMed=14562106; DOI=10.1038/nature02046;
RA Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N.,
RA O'Shea E.K., Weissman J.S.;
RT "Global analysis of protein expression in yeast.";
RL Nature 425:737-741(2003).
RN [7]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=18407956; DOI=10.1074/mcp.m700468-mcp200;
RA Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
RT "A multidimensional chromatography technology for in-depth phosphoproteome
RT analysis.";
RL Mol. Cell. Proteomics 7:1389-1396(2008).
RN [8]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19779198; DOI=10.1126/science.1172867;
RA Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.;
RT "Global analysis of Cdk1 substrate phosphorylation sites provides insights
RT into evolution.";
RL Science 325:1682-1686(2009).
CC -!- FUNCTION: IMP-specific 5'-nucleotidase involved in IMP (inosine 5'-
CC phosphate) degradation. {ECO:0000269|PubMed:12735798,
CC ECO:0000269|PubMed:8141771}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + IMP = inosine + phosphate; Xref=Rhea:RHEA:27718,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:17596, ChEBI:CHEBI:43474,
CC ChEBI:CHEBI:58053; EC=3.1.3.99;
CC Evidence={ECO:0000269|PubMed:12735798, ECO:0000269|PubMed:8141771};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000269|PubMed:8141771};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC pH dependence:
CC Optimum pH is 6-6.5. {ECO:0000269|PubMed:8141771};
CC -!- SUBUNIT: Homotetramer. {ECO:0000269|PubMed:8141771}.
CC -!- MISCELLANEOUS: Present with 1590 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the ISN1 family. {ECO:0000305}.
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DR EMBL; U55020; AAC49641.1; -; Genomic_DNA.
DR EMBL; Z75063; CAA99361.1; -; Genomic_DNA.
DR EMBL; BK006948; DAA10928.1; -; Genomic_DNA.
DR PIR; S67043; S67043.
DR RefSeq; NP_014798.3; NM_001183574.3.
DR AlphaFoldDB; Q99312; -.
DR SMR; Q99312; -.
DR BioGRID; 34551; 50.
DR DIP; DIP-4027N; -.
DR IntAct; Q99312; 4.
DR MINT; Q99312; -.
DR STRING; 4932.YOR155C; -.
DR iPTMnet; Q99312; -.
DR MaxQB; Q99312; -.
DR PaxDb; Q99312; -.
DR PRIDE; Q99312; -.
DR EnsemblFungi; YOR155C_mRNA; YOR155C; YOR155C.
DR GeneID; 854326; -.
DR KEGG; sce:YOR155C; -.
DR SGD; S000005681; ISN1.
DR VEuPathDB; FungiDB:YOR155C; -.
DR eggNOG; ENOG502QR24; Eukaryota.
DR HOGENOM; CLU_031816_1_0_1; -.
DR OMA; FKARLAC; -.
DR BioCyc; MetaCyc:MON3O-10; -.
DR BioCyc; YEAST:MON3O-10; -.
DR BRENDA; 3.1.3.99; 984.
DR PRO; PR:Q99312; -.
DR Proteomes; UP000002311; Chromosome XV.
DR RNAct; Q99312; protein.
DR GO; GO:0050483; F:IMP 5'-nucleotidase activity; IDA:SGD.
DR GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR GO; GO:0006190; P:inosine salvage; IMP:SGD.
DR GO; GO:0071590; P:nicotinamide riboside biosynthetic process; IMP:SGD.
DR GO; GO:0071592; P:nicotinic acid riboside biosynthetic process; IMP:SGD.
DR GO; GO:0009117; P:nucleotide metabolic process; IEA:UniProtKB-KW.
DR InterPro; IPR036412; HAD-like_sf.
DR InterPro; IPR009453; ISN1.
DR PANTHER; PTHR28213; PTHR28213; 1.
DR Pfam; PF06437; ISN1; 1.
DR PIRSF; PIRSF028836; ISN1; 1.
DR SUPFAM; SSF56784; SSF56784; 1.
PE 1: Evidence at protein level;
KW Hydrolase; Magnesium; Nucleotide metabolism; Reference proteome.
FT CHAIN 1..450
FT /note="IMP-specific 5'-nucleotidase 1"
FT /id="PRO_0000084257"
SQ SEQUENCE 450 AA; 51330 MW; E0F3033FF2C18F07 CRC64;
MSSRYRVEYH LKSHRKDEFI DWVKGLLASP FVLHAVSHEG DYNDDLATTQ RVRSQYADIF
KDIEGLIKDK IEFDSRNMSQ DEIEDGASSQ SLNILGQSRL NLLVPSIGTF FTELPLEQAF
LWEDSQRAIS ARRMVAPSFN DIRHILNTAQ IFHFKKQENL HNGKVLRLVT FDGDVTLYED
GGSLVYTNPV IPYILKLLRC GINVGIVTAA GYDEAGTYEN RLKGLIVALH DSTDIPVSQK
QNLTIMGGES SYLFRYYEDP EEDNFGFRQI DKEEWLLPRM KAWSLEDVEK TLDFAERTLN
RLRKRLNLPS EISIIRKVRA VGIVPGERYD EASKRQVPVK LDREQLEEIV LTLQNTLESF
APSRRIQFSC FDGGSDVWCD IGGKDLGVRS LQQFYNPESP IQPSETLHVG DQFAPVGSAN
DFKARLAGCT LWIASPQETV NYLHRLLETD
