PRM1_PICGU
ID PRM1_PICGU Reviewed; 630 AA.
AC A5DJ60;
DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT 10-FEB-2009, sequence version 2.
DT 03-AUG-2022, entry version 56.
DE RecName: Full=Plasma membrane fusion protein PRM1;
GN Name=PRM1; ORFNames=PGUG_03311;
OS Meyerozyma guilliermondii (strain ATCC 6260 / CBS 566 / DSM 6381 / JCM 1539
OS / NBRC 10279 / NRRL Y-324) (Yeast) (Candida guilliermondii).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Meyerozyma.
OX NCBI_TaxID=294746;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 6260 / CBS 566 / DSM 6381 / JCM 1539 / NBRC 10279 / NRRL Y-324;
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; CH408158; EDK39213.2; -; Genomic_DNA.
DR RefSeq; XP_001483930.1; XM_001483880.1.
DR AlphaFoldDB; A5DJ60; -.
DR STRING; 4929.XP_001483930.1; -.
DR EnsemblFungi; EDK39213; EDK39213; PGUG_03311.
DR GeneID; 5125809; -.
DR KEGG; pgu:PGUG_03311; -.
DR VEuPathDB; FungiDB:PGUG_03311; -.
DR eggNOG; ENOG502QRP5; Eukaryota.
DR HOGENOM; CLU_010191_1_0_1; -.
DR InParanoid; A5DJ60; -.
DR OMA; QTYLCLF; -.
DR OrthoDB; 1333210at2759; -.
DR Proteomes; UP000001997; 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..630
FT /note="Plasma membrane fusion protein PRM1"
FT /id="PRO_0000337287"
FT TOPO_DOM 1..37
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT TRANSMEM 38..58
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 59..108
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 109..129
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 130..302
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT TRANSMEM 303..323
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 324..376
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 377..397
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 398..566
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT TRANSMEM 567..587
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 588..630
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT CARBOHYD 158
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 202
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 236
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 252
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 279
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 465
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 476
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 630 AA; 70527 MW; 6BA32DB88A4690FE CRC64;
MFHFFLKYHF FLFISMAPRY YLTLSQVCSQ VWCNKYTIAF VLLAVKVYTF SLILRSTLDH
LMDLVDTINV SLDQFASTAT NFPAQLTQLT NKLIAEQLQQ LKSNFKLSLL LLVSVIRALI
GFYMEIFLGT FTCLLDAAAQ ASVNFALDSA QATLKCLNTT IVSVTSEVES GLESISSFIE
NSINTVSSLF TNGKKPSVTS INLSLGKLRN LQIPGSVTNE LDSFRLNLDE FDNLKNSTIN
LLTAPLTHFD KNVSGSDLFG PIDSSKMVVA NYGPSAAKNV TFDLTEVKNS IVDFKNDAAK
IASIMIIVLA SLSVIAMIAL VFVERRNFVK RDIFVISVRE KSSPLAIGNA LETYQNRTIY
YMAKLKVNPR YYWICNYLTS KYAMVVIIIG LVGVISFTLQ YRLLLSVKNK LKNLIDTVSS
PEQTKQLQAS LSQYTAQTNN YIEAQSKALN QNLLGWYMKA STNVNDTLTD ILHQINSTIH
TVTGNTALSK PFEVVVYCVI GRKIVAVTKG ITWLNEHLVI DLPQLPVDLF KDVTEAAPLR
YGKQLETQMV KATNSLEHML FIELYVALGF VGIWVIFIVM GIIFMFFPKK RTIGSPKLLT
KTEKEEYIFP LSSFNTSSSV YSTLNDRPIS
