PRM9_YEAST
ID PRM9_YEAST Reviewed; 298 AA.
AC P39551; D6VPN2;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1995, sequence version 1.
DT 03-AUG-2022, entry version 140.
DE RecName: Full=Pheromone-regulated membrane protein 9;
DE AltName: Full=DUP240 protein PRM9;
GN Name=PRM9; OrderedLocusNames=YAR031W; ORFNames=FUN58;
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 NOMENCLATURE.
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 SUBCELLULAR LOCATION.
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 INTERACTION WITH PRM8.
RX PubMed=12925749; DOI=10.1091/mbc.e02-11-0736;
RA Sandmann T., Herrmann J.M., Dengjel J., Schwarz H., Spang A.;
RT "Suppression of coatomer mutants by a new protein family with COPI and
RT COPII binding motifs in Saccharomyces cerevisiae.";
RL Mol. Biol. Cell 14:3097-3113(2003).
RN [7]
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 [8]
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).
CC -!- FUNCTION: May be involved in endoplasmic reticulum exit trafficking of
CC proteins.
CC -!- SUBUNIT: Interacts with PRM8. Binds to COPII coated vesicles (By
CC similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:12101299};
CC Multi-pass membrane protein {ECO:0000269|PubMed:12101299}.
CC -!- MISCELLANEOUS: Present with 259 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- MISCELLANEOUS: Members of the DUP240 multigene family are specific to
CC S.cerevisiae sensu strictu. Cells lacking all 10 DUP240 proteins show
CC no obvious alterations in mating, sporulation and cell growth.
CC -!- SIMILARITY: Belongs to the DUP/COS family. {ECO:0000305}.
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DR EMBL; L28920; AAC09493.1; -; Genomic_DNA.
DR EMBL; BK006935; DAA07002.1; -; Genomic_DNA.
DR PIR; S53483; S53483.
DR RefSeq; NP_009418.1; NM_001178224.1.
DR AlphaFoldDB; P39551; -.
DR BioGRID; 31809; 78.
DR DIP; DIP-1757N; -.
DR IntAct; P39551; 4.
DR MINT; P39551; -.
DR STRING; 4932.YAR031W; -.
DR MaxQB; P39551; -.
DR PaxDb; P39551; -.
DR PRIDE; P39551; -.
DR EnsemblFungi; YAR031W_mRNA; YAR031W; YAR031W.
DR GeneID; 851282; -.
DR KEGG; sce:YAR031W; -.
DR SGD; S000000078; PRM9.
DR VEuPathDB; FungiDB:YAR031W; -.
DR eggNOG; ENOG502SSNW; Eukaryota.
DR GeneTree; ENSGT00940000176285; -.
DR HOGENOM; CLU_081384_0_0_1; -.
DR InParanoid; P39551; -.
DR OMA; NTEFCVA; -.
DR BioCyc; YEAST:G3O-28881-MON; -.
DR PRO; PR:P39551; -.
DR Proteomes; UP000002311; Chromosome I.
DR RNAct; P39551; protein.
DR GO; GO:0005783; C:endoplasmic reticulum; IPI:SGD.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IDA:SGD.
DR GO; GO:0016192; P:vesicle-mediated transport; IEA:UniProtKB-KW.
DR InterPro; IPR001142; DUP/COS.
DR Pfam; PF00674; DUP; 1.
PE 1: Evidence at protein level;
KW Cell membrane; ER-Golgi transport; Membrane; Reference proteome;
KW Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..298
FT /note="Pheromone-regulated membrane protein 9"
FT /id="PRO_0000207524"
FT TOPO_DOM 1..111
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 112..132
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 133..137
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 138..158
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 159..298
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 235..262
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 297..298
FT /note="COPII binding"
FT /evidence="ECO:0000250"
FT COMPBIAS 238..262
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 298 AA; 35073 MW; 2CCB50B4D73DAB71 CRC64;
MSPQYHFYFV SFRNLVLNEK CLRSKKQVMK SFNWYKTDRY FDPHNILQHH SRAIEKTRYK
LGMQTSSEST DAKSDFLDEP SAYLIEKNVA LPKDIFGSYL SYWIYEVTRH KAAVILLVLI
VTSILLLVFF YNTEFCVAFE ILLFSFCFPG TCMVVIAFSE PIGDREFKVK LLMEIITRKP
AVKGKEWRTI TYKMNQYLFD HGLWDTPYYF YRDEDCHRYF LSLIKGRTFK KQKESSASNV
KDAQSNDETA GTPNEAAESS SFSAGPNFIK LLTKAAEIEQ QFQKEYWRQE YPGVDEFF
