PRM1_LODEL
ID PRM1_LODEL Reviewed; 659 AA.
AC A5DU71;
DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT 12-JUN-2007, sequence version 1.
DT 03-AUG-2022, entry version 55.
DE RecName: Full=Plasma membrane fusion protein PRM1;
GN Name=PRM1; ORFNames=LELG_00907;
OS Lodderomyces elongisporus (strain ATCC 11503 / CBS 2605 / JCM 1781 / NBRC
OS 1676 / NRRL YB-4239) (Yeast) (Saccharomyces elongisporus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Candida/Lodderomyces clade;
OC Lodderomyces.
OX NCBI_TaxID=379508;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 11503 / BCRC 21390 / CBS 2605 / JCM 1781 / NBRC 1676 / NRRL
RC YB-4239;
RX PubMed=19465905; DOI=10.1038/nature08064;
RA Butler G., Rasmussen M.D., Lin M.F., Santos M.A.S., Sakthikumar S.,
RA Munro C.A., Rheinbay E., Grabherr M., Forche A., Reedy J.L., Agrafioti I.,
RA Arnaud M.B., Bates S., Brown A.J.P., Brunke S., Costanzo M.C.,
RA Fitzpatrick D.A., de Groot P.W.J., Harris D., Hoyer L.L., Hube B.,
RA Klis F.M., Kodira C., Lennard N., Logue M.E., Martin R., Neiman A.M.,
RA Nikolaou E., Quail M.A., Quinn J., Santos M.C., Schmitzberger F.F.,
RA Sherlock G., Shah P., Silverstein K.A.T., Skrzypek M.S., Soll D.,
RA Staggs R., Stansfield I., Stumpf M.P.H., Sudbery P.E., Srikantha T.,
RA Zeng Q., Berman J., Berriman M., Heitman J., Gow N.A.R., Lorenz M.C.,
RA Birren B.W., Kellis M., Cuomo C.A.;
RT "Evolution of pathogenicity and sexual reproduction in eight Candida
RT genomes.";
RL Nature 459:657-662(2009).
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; CH981524; EDK42729.1; -; Genomic_DNA.
DR RefSeq; XP_001528387.1; XM_001528337.1.
DR AlphaFoldDB; A5DU71; -.
DR STRING; 379508.A5DU71; -.
DR PRIDE; A5DU71; -.
DR EnsemblFungi; EDK42729; EDK42729; LELG_00907.
DR GeneID; 5234756; -.
DR KEGG; lel:LELG_00907; -.
DR VEuPathDB; FungiDB:LELG_00907; -.
DR eggNOG; ENOG502QRP5; Eukaryota.
DR HOGENOM; CLU_010191_1_0_1; -.
DR InParanoid; A5DU71; -.
DR OMA; AYITSER; -.
DR OrthoDB; 1333210at2759; -.
DR Proteomes; UP000001996; 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_0000337284"
FT TOPO_DOM 1..21
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT TRANSMEM 22..42
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 43..95
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 96..116
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 117..285
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT TRANSMEM 286..306
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 307..367
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 368..388
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 389..543
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT TRANSMEM 544..564
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 565..659
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT CARBOHYD 132
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 184
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 209
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 220
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 249
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 281
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 403
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 424
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 446
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 516
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 659 AA; 73648 MW; 71855F7BD8E8B7B6 CRC64;
MLRNYLDLPE ILSQVYLNQY TILLVLVVVK LILLKESLID AISKQIINDA TCNDDNLQHI
LNGVHDAILK NIDKLQYSGI VFVVLILKTI RELTSFFIDL LLGTYVCLLT AVVVGTTEFA
FDASESIIQA VNVTVVAAAD EIEDGLRGLS NFINDLVTGF NAIRTFFTGS ASTSDADLYR
DRINLSLGNL KDKISIPSTV LMDIQNARNF SMNELENLNN ETQSLVNSPF NLVINKLDAI
KLEINRYDNS SLQPIQIRDA CLQTVNRVQD SQTVLIKVVE NVSKWFLIVL AIIIACSLAY
AFYIELRRWK RLSEFINEGD VADSEVGYRN EHNIYDNALL YTMIKRFGIS VNERVIWVIS
YMSSKMAGIV FAFGIIGIIS AVLQLLMIYF VQQAVDDEIS TMNNSNENFE MASSYIRSMN
NYINTTQSSI NDELFGDIID TSTKVNNTIA EFVDNLDSAV HSIFGESIIA SAVNTVVYCT
IGRKLEKIEA GCNWLAENVK IDIPEVPSEI LRELQNISFL QPQNLMENFK PILDLYRNSV
HLELLISLIF LAVWALQLII GLMILLARQG INASGAGGAG GAGGTGDAEG CDNYTDNKVI
LMRRVTPLQI GSPHSLTEKE RQLYQFPISK PRFDRSSDTL SSFYPPTSTP GRIEYPLHI
