PRM3_YEAST
ID PRM3_YEAST Reviewed; 133 AA.
AC Q08931; D6W3H6;
DT 28-NOV-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 121.
DE RecName: Full=Pheromone-regulated membrane protein 3;
GN Name=PRM3; OrderedLocusNames=YPL192C;
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=9169875;
RA Bussey H., Storms R.K., Ahmed A., Albermann K., Allen E., Ansorge W.,
RA Araujo R., Aparicio A., Barrell B.G., Badcock K., Benes V., Botstein D.,
RA Bowman S., Brueckner M., Carpenter J., Cherry J.M., Chung E.,
RA Churcher C.M., Coster F., Davis K., Davis R.W., Dietrich F.S., Delius H.,
RA DiPaolo T., Dubois E., Duesterhoeft A., Duncan M., Floeth M., Fortin N.,
RA Friesen J.D., Fritz C., Goffeau A., Hall J., Hebling U., Heumann K.,
RA Hilbert H., Hillier L.W., Hunicke-Smith S., Hyman R.W., Johnston M.,
RA Kalman S., Kleine K., Komp C., Kurdi O., Lashkari D., Lew H., Lin A.,
RA Lin D., Louis E.J., Marathe R., Messenguy F., Mewes H.-W., Mirtipati S.,
RA Moestl D., Mueller-Auer S., Namath A., Nentwich U., Oefner P., Pearson D.,
RA Petel F.X., Pohl T.M., Purnelle B., Rajandream M.A., Rechmann S.,
RA Rieger M., Riles L., Roberts D., Schaefer M., Scharfe M., Scherens B.,
RA Schramm S., Schroeder M., Sdicu A.-M., Tettelin H., Urrestarazu L.A.,
RA Ushinsky S., Vierendeels F., Vissers S., Voss H., Walsh S.V., Wambutt R.,
RA Wang Y., Wedler E., Wedler H., Winnett E., Zhong W.-W., Zollner A.,
RA Vo D.H., Hani J.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XVI.";
RL Nature 387:103-105(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 NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=17322287; DOI=10.1101/gr.6037607;
RA Hu Y., Rolfs A., Bhullar B., Murthy T.V.S., Zhu C., Berger M.F.,
RA Camargo A.A., Kelley F., McCarron S., Jepson D., Richardson A., Raphael J.,
RA Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F., Williamson J.,
RA Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G., Kolodner R.D.,
RA LaBaer J.;
RT "Approaching a complete repository of sequence-verified protein-encoding
RT clones for Saccharomyces cerevisiae.";
RL Genome Res. 17:536-543(2007).
RN [4]
RP NOMENCLATURE, AND INDUCTION.
RX PubMed=11062271; DOI=10.1083/jcb.151.3.719;
RA Heiman M.G., Walter P.;
RT "Prm1p, a pheromone-regulated multispanning membrane protein, facilitates
RT plasma membrane fusion during yeast mating.";
RL J. Cell Biol. 151:719-730(2000).
RN [5]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=12514182; DOI=10.1074/jbc.m212725200;
RA Beilharz T., Egan B., Silver P.A., Hofmann K., Lithgow T.;
RT "Bipartite signals mediate subcellular targeting of tail-anchored membrane
RT proteins in Saccharomyces cerevisiae.";
RL J. Biol. Chem. 278:8219-8223(2003).
RN [6]
RP SUBCELLULAR LOCATION.
RX PubMed=17996101; DOI=10.1186/1471-2121-8-47;
RA Hattier T., Andrulis E.D., Tartakoff A.M.;
RT "Immobility, inheritance and plasticity of shape of the yeast nucleus.";
RL BMC Cell Biol. 8:47-47(2007).
RN [7]
RP SUBCELLULAR LOCATION.
RX PubMed=18660802; DOI=10.1038/nature07212;
RA Shcheprova Z., Baldi S., Frei S.B., Gonnet G., Barral Y.;
RT "A mechanism for asymmetric segregation of age during yeast budding.";
RL Nature 454:728-734(2008).
RN [8]
RP FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH KAR5, AND MUTAGENESIS OF
RP TYR-106; GLY-108; GLY-112; PHE-114; LEU-115; THR-121 AND VAL-122.
RX PubMed=19297527; DOI=10.1091/mbc.e08-10-0987;
RA Shen S., Tobery C.E., Rose M.D.;
RT "Prm3p is a pheromone-induced peripheral nuclear envelope protein required
RT for yeast nuclear fusion.";
RL Mol. Biol. Cell 20:2438-2450(2009).
RN [9]
RP SUBCELLULAR LOCATION.
RX PubMed=19369416; DOI=10.1091/mbc.e08-12-1193;
RA Tartakoff A.M., Jaiswal P.;
RT "Nuclear fusion and genome encounter during yeast zygote formation.";
RL Mol. Biol. Cell 20:2932-2942(2009).
RN [10]
RP FUNCTION.
RX PubMed=19570912; DOI=10.1091/mbc.e09-02-0163;
RA Melloy P., Shen S., White E., Rose M.D.;
RT "Distinct roles for key karyogamy proteins during yeast nuclear fusion.";
RL Mol. Biol. Cell 20:3773-3782(2009).
RN [11]
RP INDUCTION.
RX PubMed=20584076; DOI=10.1111/j.1742-4658.2010.07728.x;
RA Su T.C., Tamarkina E., Sadowski I.;
RT "Organizational constraints on Ste12 cis-elements for a pheromone response
RT in Saccharomyces cerevisiae.";
RL FEBS J. 277:3235-3248(2010).
CC -!- FUNCTION: Required for the fusion of nuclear envelopes during mating,
CC ensuring proper karyogamy. Plays a role in the initiation of outer
CC nuclear envelope fusion. {ECO:0000269|PubMed:12514182,
CC ECO:0000269|PubMed:19297527, ECO:0000269|PubMed:19570912}.
CC -!- SUBUNIT: Interacts with KAR5. {ECO:0000269|PubMed:19297527}.
CC -!- SUBCELLULAR LOCATION: Nucleus outer membrane; Single-pass membrane
CC protein; Cytoplasmic side. Cytoplasm, cytoskeleton, microtubule
CC organizing center, spindle pole body.
CC -!- INDUCTION: By pheromone. Expression is controlled by the STE12
CC transcription factor that binds to pheromone-response cis-elements
CC (PREs) in the promoter of target genes. {ECO:0000269|PubMed:11062271,
CC ECO:0000269|PubMed:20584076}.
CC -!- CAUTION: Was originally shown to be localized in the inner nuclear
CC membrane by using a truncated protein (PubMed:12514182). Was used as an
CC inner nuclear membrane marker (PubMed:17996101, PubMed:18660802 and
CC PubMed:19369416). However, more recent studies showed that it is
CC localized in the nuclear outer membrane, which is consistent with a
CC function in the initiation of nuclear fusion (PubMed:19297527 and
CC PubMed:19570912). {ECO:0000305|PubMed:12514182}.
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DR EMBL; Z73548; CAA97905.1; -; Genomic_DNA.
DR EMBL; AY693130; AAT93149.1; -; Genomic_DNA.
DR EMBL; BK006949; DAA11242.1; -; Genomic_DNA.
DR PIR; S65211; S65211.
DR RefSeq; NP_015132.1; NM_001184006.1.
DR AlphaFoldDB; Q08931; -.
DR BioGRID; 35991; 55.
DR DIP; DIP-1699N; -.
DR IntAct; Q08931; 7.
DR MINT; Q08931; -.
DR STRING; 4932.YPL192C; -.
DR PaxDb; Q08931; -.
DR PRIDE; Q08931; -.
DR EnsemblFungi; YPL192C_mRNA; YPL192C; YPL192C.
DR GeneID; 855909; -.
DR KEGG; sce:YPL192C; -.
DR SGD; S000006113; PRM3.
DR VEuPathDB; FungiDB:YPL192C; -.
DR HOGENOM; CLU_1897414_0_0_1; -.
DR InParanoid; Q08931; -.
DR BioCyc; YEAST:G3O-34085-MON; -.
DR PRO; PR:Q08931; -.
DR Proteomes; UP000002311; Chromosome XVI.
DR RNAct; Q08931; protein.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0031316; C:extrinsic component of nuclear outer membrane; IDA: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:0034399; C:nuclear periphery; HDA:SGD.
DR GO; GO:0005816; C:spindle pole body; IDA:SGD.
DR GO; GO:0000742; P:karyogamy involved in conjugation with cellular fusion; IMP:SGD.
DR GO; GO:0048288; P:nuclear membrane fusion involved in karyogamy; IMP:SGD.
PE 1: Evidence at protein level;
KW Cytoplasm; Cytoskeleton; Membrane; Nucleus; Reference proteome;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..133
FT /note="Pheromone-regulated membrane protein 3"
FT /id="PRO_0000262749"
FT TOPO_DOM 1..104
FT /note="Nuclear"
FT /evidence="ECO:0000255"
FT TRANSMEM 105..127
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 128..133
FT /note="Perinuclear space"
FT /evidence="ECO:0000255"
FT REGION 36..100
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 69..75
FT /note="Bipartite nuclear localization signal"
FT COMPBIAS 67..83
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 84..98
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MUTAGEN 106
FT /note="Y->H: In pmr3-7; leads to mislocalization and
FT decreases nuclear fusion efficiency when temperature
FT rises."
FT /evidence="ECO:0000269|PubMed:19297527"
FT MUTAGEN 108
FT /note="G->S: In pmr3-1; decreases nuclear fusion
FT efficiency."
FT /evidence="ECO:0000269|PubMed:19297527"
FT MUTAGEN 112
FT /note="G->S: In pmr3-8; leads to mislocalization and
FT decreases nuclear fusion efficiency."
FT /evidence="ECO:0000269|PubMed:19297527"
FT MUTAGEN 114
FT /note="F->S: In pmr3-3; leads to mislocalization and
FT decreases nuclear fusion efficiency."
FT /evidence="ECO:0000269|PubMed:19297527"
FT MUTAGEN 115
FT /note="L->R: In pmr3-5; leads to mislocalization and
FT decreases nuclear fusion efficiency."
FT /evidence="ECO:0000269|PubMed:19297527"
FT MUTAGEN 121
FT /note="T->A: In pmr3-6; leads to mislocalization."
FT /evidence="ECO:0000269|PubMed:19297527"
FT MUTAGEN 122
FT /note="V->D: In pmr3-2; leads to mislocalization and
FT decreases nuclear fusion efficiency."
FT /evidence="ECO:0000269|PubMed:19297527"
SQ SEQUENCE 133 AA; 14428 MW; EEC7EC604F06C2B1 CRC64;
MTAMKEDNAA LITLKKNNDQ EKLRVHKLTD ASSNSADGFV INKAKNGGPL NKKSLVNNEQ
HIKKAVSPGR VRKHKTTTSS TKSRTKSKKK DASESKVQRE NKGSFYQGAI FGSFLGAAVT
TVLSNLAVKA LQN
