PRM8_YEAST
ID PRM8_YEAST Reviewed; 237 AA.
AC P53174; D6VU88;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 149.
DE RecName: Full=Pheromone-regulated membrane protein 8;
DE AltName: Full=DUP240 protein PRM8;
DE AltName: Full=Protein DUP1;
GN Name=PRM8; Synonyms=DUP1; OrderedLocusNames=YGL053W;
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 204508 / S288c;
RX PubMed=9234674;
RX DOI=10.1002/(sici)1097-0061(199707)13:9<861::aid-yea125>3.0.co;2-9;
RA Feuermann M., de Montigny J., Potier S., Souciet J.-L.;
RT "The characterization of two new clusters of duplicated genes suggests a
RT 'Lego' organization of the yeast Saccharomyces cerevisiae chromosomes.";
RL Yeast 13:861-869(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169869;
RA Tettelin H., Agostoni-Carbone M.L., Albermann K., Albers M., Arroyo J.,
RA Backes U., Barreiros T., Bertani I., Bjourson A.J., Brueckner M.,
RA Bruschi C.V., Carignani G., Castagnoli L., Cerdan E., Clemente M.L.,
RA Coblenz A., Coglievina M., Coissac E., Defoor E., Del Bino S., Delius H.,
RA Delneri D., de Wergifosse P., Dujon B., Durand P., Entian K.-D., Eraso P.,
RA Escribano V., Fabiani L., Fartmann B., Feroli F., Feuermann M.,
RA Frontali L., Garcia-Gonzalez M., Garcia-Saez M.I., Goffeau A.,
RA Guerreiro P., Hani J., Hansen M., Hebling U., Hernandez K., Heumann K.,
RA Hilger F., Hofmann B., Indge K.J., James C.M., Klima R., Koetter P.,
RA Kramer B., Kramer W., Lauquin G., Leuther H., Louis E.J., Maillier E.,
RA Marconi A., Martegani E., Mazon M.J., Mazzoni C., McReynolds A.D.K.,
RA Melchioretto P., Mewes H.-W., Minenkova O., Mueller-Auer S., Nawrocki A.,
RA Netter P., Neu R., Nombela C., Oliver S.G., Panzeri L., Paoluzi S.,
RA Plevani P., Portetelle D., Portillo F., Potier S., Purnelle B., Rieger M.,
RA Riles L., Rinaldi T., Robben J., Rodrigues-Pousada C.,
RA Rodriguez-Belmonte E., Rodriguez-Torres A.M., Rose M., Ruzzi M.,
RA Saliola M., Sanchez-Perez M., Schaefer B., Schaefer M., Scharfe M.,
RA Schmidheini T., Schreer A., Skala J., Souciet J.-L., Steensma H.Y.,
RA Talla E., Thierry A., Vandenbol M., van der Aart Q.J.M., Van Dyck L.,
RA Vanoni M., Verhasselt P., Voet M., Volckaert G., Wambutt R., Watson M.D.,
RA Weber N., Wedler E., Wedler H., Wipfli P., Wolf K., Wright L.F.,
RA Zaccaria P., Zimmermann M., Zollner A., Kleine K.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome VII.";
RL Nature 387:81-84(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 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 [5]
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 [6]
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 [7]
RP SUBCELLULAR LOCATION, AND INTERACTION WITH PRM9.
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 [8]
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 [9]
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 PRM9. Binds to SEC23/24 of COPII coated
CC vesicles. {ECO:0000269|PubMed:12925749}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane
CC protein {ECO:0000305}. Endoplasmic reticulum
CC {ECO:0000269|PubMed:12101299, ECO:0000269|PubMed:12925749}.
CC -!- MISCELLANEOUS: Present with 1254 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; Z72575; CAA96755.1; -; Genomic_DNA.
DR EMBL; AY693004; AAT93023.1; -; Genomic_DNA.
DR EMBL; BK006941; DAA08049.1; -; Genomic_DNA.
DR PIR; S64057; S64057.
DR RefSeq; NP_011462.1; NM_001180918.1.
DR AlphaFoldDB; P53174; -.
DR BioGRID; 33195; 72.
DR DIP; DIP-4067N; -.
DR IntAct; P53174; 18.
DR MINT; P53174; -.
DR STRING; 4932.YGL053W; -.
DR MaxQB; P53174; -.
DR PaxDb; P53174; -.
DR PRIDE; P53174; -.
DR EnsemblFungi; YGL053W_mRNA; YGL053W; YGL053W.
DR GeneID; 852828; -.
DR KEGG; sce:YGL053W; -.
DR SGD; S000003021; PRM8.
DR VEuPathDB; FungiDB:YGL053W; -.
DR eggNOG; ENOG502SSNW; Eukaryota.
DR GeneTree; ENSGT00940000176285; -.
DR HOGENOM; CLU_081384_0_1_1; -.
DR InParanoid; P53174; -.
DR OMA; FHDNENC; -.
DR BioCyc; YEAST:G3O-30562-MON; -.
DR ChiTaRS; PRM8; yeast.
DR PRO; PR:P53174; -.
DR Proteomes; UP000002311; Chromosome VII.
DR RNAct; P53174; protein.
DR GO; GO:0005783; C:endoplasmic reticulum; IDA:SGD.
DR GO; GO:0016021; C:integral component of membrane; ISM:SGD.
DR GO; GO:0005886; C:plasma membrane; IMP: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 Endoplasmic reticulum; ER-Golgi transport; Membrane; Reference proteome;
KW Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..237
FT /note="Pheromone-regulated membrane protein 8"
FT /id="PRO_0000207523"
FT TOPO_DOM 1..47
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 48..68
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 69..74
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 75..95
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 96..237
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 174..201
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 236..237
FT /note="COPII binding"
FT COMPBIAS 177..201
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 237 AA; 27250 MW; 565C4A3B5067269A CRC64;
MQTPSENTNA KSDSLDEPGA YLIEENVALP KDIFHSYLSY WIYEAAHCTP VMLLSLVIGV
LISIIILFHD NENCVGVSVG FLLIFSGILV IVLILRFGPQ ISDEDFKCKL LMEIITRKPT
VKGKEWRTIT YKMNQYLFDN DLWNTPYYFY RDEDCHRYFL SLIKGRTFKK QKESSASNVK
DAQSNDETAG TPNEAAESSS FSAGPNFIKL LTKAAEIEQQ FQKEYWRQEY PGVDEFF
