ID   PRM1_PICST              Reviewed;         620 AA.
AC   A3LNK7;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   20-MAY-2008, sequence version 3.
DT   03-AUG-2022, entry version 57.
DE   RecName: Full=Plasma membrane fusion protein PRM1;
GN   Name=PRM1; ORFNames=PICST_54949;
OS   Scheffersomyces stipitis (strain ATCC 58785 / CBS 6054 / NBRC 10063 / NRRL
OS   Y-11545) (Yeast) (Pichia stipitis).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Debaryomycetaceae; Scheffersomyces.
OX   NCBI_TaxID=322104;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 58785 / CBS 6054 / NBRC 10063 / NRRL Y-11545;
RX   PubMed=17334359; DOI=10.1038/nbt1290;
RA   Jeffries T.W., Grigoriev I.V., Grimwood J., Laplaza J.M., Aerts A.,
RA   Salamov A., Schmutz J., Lindquist E., Dehal P., Shapiro H., Jin Y.-S.,
RA   Passoth V., Richardson P.M.;
RT   "Genome sequence of the lignocellulose-bioconverting and xylose-fermenting
RT   yeast Pichia stipitis.";
RL   Nat. Biotechnol. 25:319-326(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; CP000496; ABN64874.2; ALT_TERM; Genomic_DNA.
DR   RefSeq; XP_001382903.2; XM_001382866.1.
DR   AlphaFoldDB; A3LNK7; -.
DR   SMR; A3LNK7; -.
DR   STRING; 4924.XP_001382903.2; -.
DR   EnsemblFungi; ABN64874; ABN64874; PICST_54949.
DR   GeneID; 4837481; -.
DR   KEGG; pic:PICST_54949; -.
DR   eggNOG; ENOG502QRP5; Eukaryota.
DR   HOGENOM; CLU_010191_1_0_1; -.
DR   InParanoid; A3LNK7; -.
DR   OrthoDB; 1333210at2759; -.
DR   Proteomes; UP000002258; Chromosome 2.
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..620
FT                   /note="Plasma membrane fusion protein PRM1"
FT                   /id="PRO_0000337288"
FT   TOPO_DOM        1..19
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000250"
FT   TRANSMEM        20..40
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        41..86
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000250"
FT   TRANSMEM        87..107
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        108..274
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000250"
FT   TRANSMEM        275..295
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        296..352
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000250"
FT   TRANSMEM        353..373
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        374..534
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000250"
FT   TRANSMEM        535..555
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        556..620
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        130
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        169
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        190
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        215
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        235
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        267
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        396
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        432
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        443
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        484
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   620 AA;  69307 MW;  5F5057D6629625F5 CRC64;
     MPYLNFAERI SQVYLNKYTL ALVLVTIKVY LFQKTLVAAV RNIPDFSDCS VDELPTKVSV
     MIRNMVENNL NSFTYSTLAL LHVAAKSILN LIWFAVEMLL GTYTCLFKAA IVGTSDFAAD
     TSEMVVKGLN TTIVEITHDI QSGLDGLSSI LNKVVSTASK VADFFTGNNN SDSPDQYQKS
     ISLSLGKLTN LSIPSSVLGE INKIRIDPDF SSVENSTKKL IEEPFTSLTN QWNQNETLSL
     GGVKFPLLQP LSVCDIGSKS IQELSHNLST SVEMAAKIVI IILAICAVLV MVPLIYDEWR
     KWNREERIIG NLVNQNTHYY FDLREAFSNL LHPYLRFLPK SWLSTYVFSN YSISFLLVGL
     LGLFVVFLQY IILRILIKKA KGTDIDTSQM TKELSNMTSV YLSQIDSYFQ KQEDNINDKL
     FGSVKSTSSK INSTLHEFMS TLNDTVNSIF SNTPFSGPVN TIVYCTIGRK IDKVESGLTW
     INDNLSVKIP NINKKQLSDN LKSVISESDS SAGSVFAKGV QKTIAMYKSN LFLEFVISIS
     LVGVWVMQLL IGVIIAVTKS HLKRRRLGSL TSSLDKTRIS SPKELTKEEK LQYGYGFSVT
     NPYEVQRYSS KLSGTKIYNT