ID   UIP3_YEAST              Reviewed;         235 AA.
AC   P39547; D6VPM9;
DT   01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1995, sequence version 1.
DT   03-AUG-2022, entry version 155.
DE   RecName: Full=ULP1-interacting protein 3;
DE   AltName: Full=DUP240 protein UIP3;
GN   Name=UIP3; OrderedLocusNames=YAR027W; ORFNames=FUN55;
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 204511 / S288c / AB972;
RA   Bussey H., Keng T., Storms R.K., Vo D., Zhong W., Fortin N., Barton A.B.,
RA   Kaback D.B., Clark M.W.;
RT   "Sequencing of chromosome I of Saccharomyces cerevisiae: analysis of the 52
RT   Kbp CDC15-FLO1-PHO11-YAR074 region.";
RL   Submitted (FEB-1994) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=7731988; DOI=10.1073/pnas.92.9.3809;
RA   Bussey H., Kaback D.B., Zhong W.-W., Vo D.H., Clark M.W., Fortin N.,
RA   Hall J., Ouellette B.F.F., Keng T., Barton A.B., Su Y., Davies C.J.,
RA   Storms R.K.;
RT   "The nucleotide sequence of chromosome I from Saccharomyces cerevisiae.";
RL   Proc. Natl. Acad. Sci. U.S.A. 92:3809-3813(1995).
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   SUBCELLULAR LOCATION, AND INTERACTION WITH ULP1.
RX   PubMed=11056382; DOI=10.1093/oxfordjournals.jbchem.a022807;
RA   Takahashi Y., Mizoi J., Toh-e A., Kikuchi Y.;
RT   "Yeast Ulp1, an Smt3-specific protease, associates with nucleoporins.";
RL   J. Biochem. 128:723-725(2000).
RN   [5]
RP   DISRUPTION PHENOTYPE.
RX   PubMed=12101299; DOI=10.1099/00221287-148-7-2111;
RA   Poirey R., Despons L., Leh V., Lafuente M.-J., Potier S., Souciet J.-L.,
RA   Jauniaux J.-C.;
RT   "Functional analysis of the Saccharomyces cerevisiae DUP240 multigene
RT   family reveals membrane-associated proteins that are not essential for cell
RT   viability.";
RL   Microbiology 148:2111-2123(2002).
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   UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-11 AND LYS-218, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY.
RC   STRAIN=SUB592;
RX   PubMed=12872131; DOI=10.1038/nbt849;
RA   Peng J., Schwartz D., Elias J.E., Thoreen C.C., Cheng D., Marsischky G.,
RA   Roelofs J., Finley D., Gygi S.P.;
RT   "A proteomics approach to understanding protein ubiquitination.";
RL   Nat. Biotechnol. 21:921-926(2003).
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).
RN   [9]
RP   UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-218, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=22106047; DOI=10.1002/pmic.201100166;
RA   Starita L.M., Lo R.S., Eng J.K., von Haller P.D., Fields S.;
RT   "Sites of ubiquitin attachment in Saccharomyces cerevisiae.";
RL   Proteomics 12:236-240(2012).
CC   -!- SUBUNIT: Interacts with ULP1. {ECO:0000269|PubMed:11056382}.
CC   -!- SUBCELLULAR LOCATION: Nucleus membrane {ECO:0000269|PubMed:11056382};
CC       Multi-pass membrane protein {ECO:0000269|PubMed:11056382}. Cell
CC       membrane {ECO:0000269|PubMed:11056382}; Multi-pass membrane protein
CC       {ECO:0000269|PubMed:11056382}.
CC   -!- DISRUPTION PHENOTYPE: Members of the DUP240 multigene family are
CC       specific to S.cerevisiae sensu strictu. Cells lacking all 10 DUP240
CC       proteins show no obvious alterations in mating, sporulation and cell
CC       growth. {ECO:0000269|PubMed:12101299}.
CC   -!- MISCELLANEOUS: Present with 1695 molecules/cell in log phase SD medium.
CC       {ECO:0000269|PubMed:14562106}.
CC   -!- SIMILARITY: Belongs to the DUP/COS family. {ECO:0000305}.
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DR   EMBL; L28920; AAC09489.1; -; Genomic_DNA.
DR   EMBL; BK006935; DAA06999.1; -; Genomic_DNA.
DR   PIR; S53479; S53479.
DR   RefSeq; NP_009414.1; NM_001178221.1.
DR   AlphaFoldDB; P39547; -.
DR   BioGRID; 31806; 105.
DR   DIP; DIP-2031N; -.
DR   IntAct; P39547; 54.
DR   MINT; P39547; -.
DR   STRING; 4932.YAR027W; -.
DR   iPTMnet; P39547; -.
DR   MaxQB; P39547; -.
DR   PaxDb; P39547; -.
DR   PRIDE; P39547; -.
DR   EnsemblFungi; YAR027W_mRNA; YAR027W; YAR027W.
DR   GeneID; 851279; -.
DR   KEGG; sce:YAR027W; -.
DR   SGD; S000000075; UIP3.
DR   VEuPathDB; FungiDB:YAR027W; -.
DR   eggNOG; ENOG502SSNW; Eukaryota.
DR   GeneTree; ENSGT00940000176285; -.
DR   HOGENOM; CLU_081384_0_1_1; -.
DR   InParanoid; P39547; -.
DR   OMA; KEWRIIA; -.
DR   BioCyc; YEAST:G3O-28878-MON; -.
DR   PRO; PR:P39547; -.
DR   Proteomes; UP000002311; Chromosome I.
DR   RNAct; P39547; protein.
DR   GO; GO:0000329; C:fungal-type vacuole membrane; HDA:SGD.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005635; C:nuclear envelope; IDA:SGD.
DR   GO; GO:0031965; C:nuclear membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   InterPro; IPR001142; DUP/COS.
DR   Pfam; PF00674; DUP; 1.
PE   1: Evidence at protein level;
KW   Cell membrane; Isopeptide bond; Membrane; Nucleus; Reference proteome;
KW   Transmembrane; Transmembrane helix; Ubl conjugation.
FT   CHAIN           1..235
FT                   /note="ULP1-interacting protein 3"
FT                   /id="PRO_0000207528"
FT   TRANSMEM        51..71
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        73..93
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   REGION          169..189
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CROSSLNK        11
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in ubiquitin)"
FT                   /evidence="ECO:0000269|PubMed:12872131"
FT   CROSSLNK        218
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in ubiquitin)"
FT                   /evidence="ECO:0007744|PubMed:22106047"
SQ   SEQUENCE   235 AA;  27117 MW;  9DBF29F9C2395AB2 CRC64;
     MQTPSENTDV KLDTLDEPSA HLIEENVALP EDTFNSYWSY ILNEIARCKP LMIMFLIPVC
     LVLLITFFHD IKGILVFLVI SLILSIIILL IGITAFVSET LNKGFIIKLL VEVITRKPAV
     GGKEWRIIAY NMNQYLFDHG IWHTPYYFFC EHRCHKFFKS LIKQTRSNAH LSSPTNGAEN
     TQSNTPAKEV SNEMVKPYIF SSDPVLEAYL IKAAEIHKEA EFEYWRKQYP EVDLP