ID   PRM1_VANPO              Reviewed;         659 AA.
AC   A7TRZ7;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   02-OCT-2007, sequence version 1.
DT   03-AUG-2022, entry version 58.
DE   RecName: Full=Plasma membrane fusion protein PRM1;
GN   Name=PRM1; ORFNames=Kpol_388p9;
OS   Vanderwaltozyma polyspora (strain ATCC 22028 / DSM 70294 / BCRC 21397 / CBS
OS   2163 / NBRC 10782 / NRRL Y-8283 / UCD 57-17) (Kluyveromyces polysporus).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Vanderwaltozyma.
OX   NCBI_TaxID=436907;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 22028 / DSM 70294 / BCRC 21397 / CBS 2163 / NBRC 10782 / NRRL
RC   Y-8283 / UCD 57-17;
RX   PubMed=17494770; DOI=10.1073/pnas.0608218104;
RA   Scannell D.R., Frank A.C., Conant G.C., Byrne K.P., Woolfit M., Wolfe K.H.;
RT   "Independent sorting-out of thousands of duplicated gene pairs in two yeast
RT   species descended from a whole-genome duplication.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:8397-8402(2007).
CC   -!- FUNCTION: Involved in cell fusion during mating by stabilizing the
CC       plasma membrane fusion event. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Multi-pass membrane
CC       protein {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the PRM1 family. {ECO:0000305}.
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DR   EMBL; DS480492; EDO14965.1; -; Genomic_DNA.
DR   RefSeq; XP_001642823.1; XM_001642773.1.
DR   AlphaFoldDB; A7TRZ7; -.
DR   STRING; 436907.A7TRZ7; -.
DR   PRIDE; A7TRZ7; -.
DR   EnsemblFungi; EDO14965; EDO14965; Kpol_388p9.
DR   GeneID; 5543008; -.
DR   KEGG; vpo:Kpol_388p9; -.
DR   eggNOG; ENOG502QRP5; Eukaryota.
DR   HOGENOM; CLU_010191_1_0_1; -.
DR   InParanoid; A7TRZ7; -.
DR   OMA; QTYLCLF; -.
DR   OrthoDB; 1333210at2759; -.
DR   PhylomeDB; A7TRZ7; -.
DR   Proteomes; UP000000267; Unassembled WGS sequence.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0043332; C:mating projection tip; IEA:InterPro.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   InterPro; IPR026777; PRM1.
DR   PANTHER; PTHR31030; PTHR31030; 1.
PE   3: Inferred from homology;
KW   Cell membrane; Conjugation; Glycoprotein; Membrane; Reference proteome;
KW   Transmembrane; Transmembrane helix.
FT   CHAIN           1..659
FT                   /note="Plasma membrane fusion protein PRM1"
FT                   /id="PRO_0000337292"
FT   TOPO_DOM        1..17
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000250"
FT   TRANSMEM        18..38
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        39..106
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000250"
FT   TRANSMEM        107..127
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        128..305
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000250"
FT   TRANSMEM        306..326
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        327..431
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000250"
FT   TRANSMEM        432..452
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        453..632
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000250"
FT   TRANSMEM        633..653
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        654..659
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        136
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        146
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        203
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        237
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        258
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        461
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        473
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        518
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        537
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        572
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        591
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        592
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        595
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   659 AA;  74343 MW;  C079DA6084132891 CRC64;
     MIKYNPAYLN LNERLSQIWL NKYTILFILA AFKLLFFSTS LRNALDVSKS YILSNCGTID
     TMYSKTLNST PHYIGVFGNY LINKALIQTV KTSLSTVSLL VYASEEILEF MVDFYLGTYE
     CLLVAAIDGT VDTAVNATEK LIGFVNGSVG SIANDLDDGL NDLSKIINKA ISAAEKVGSL
     FSDDDDDDDD DSSSSSKNIA SVNLTIKALR NLYIPSSIND KLEKISDSTP TFDEVKNSTK
     NLIGIPFEKI RKEIKSINTT NIVGDPDVLY VPPINDNSNY QGICSANKNH ITSFFYSMDH
     LLKVATIVCI VLLLIGAVVV LFPEFLEEFK LWKRLTQLRE FYWYNKDLYP SSSELETINQ
     EVKDPFNDKK NIIPDQFDVI AGYQTCFNPW HTRIVNFIEK IITYFNRSSF QNESNKRRRQ
     WIVAYVASER ALFILGIGML AFFVSILQLI IITLLKRTFD NNSNMININS IANSSAVHSL
     KDDVSTWSNQ VNLYIKQTEG NLNHQVFGWI EDSTESLNNT VTHMINGIDD TLADIFNGTL
     LYNPMKTVVS CVIENKLYTI EKSLTWIHNK ANVTLPRING DDINNLLSSS NNSTNATGSN
     NLATELFEDV IDDSKKIINK VIQTYHKSII YEMIISLVFI GIWSSQIPIA LVIARFKNF