ID   PRM1_ASPFU              Reviewed;         740 AA.
AC   Q4WQ14;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2005, sequence version 1.
DT   25-MAY-2022, entry version 78.
DE   RecName: Full=Plasma membrane fusion protein prm1;
GN   Name=prm1; ORFNames=AFUA_4G11210;
OS   Neosartorya fumigata (strain ATCC MYA-4609 / Af293 / CBS 101355 / FGSC
OS   A1100) (Aspergillus fumigatus).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Fumigati.
OX   NCBI_TaxID=330879;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100;
RX   PubMed=16372009; DOI=10.1038/nature04332;
RA   Nierman W.C., Pain A., Anderson M.J., Wortman J.R., Kim H.S., Arroyo J.,
RA   Berriman M., Abe K., Archer D.B., Bermejo C., Bennett J.W., Bowyer P.,
RA   Chen D., Collins M., Coulsen R., Davies R., Dyer P.S., Farman M.L.,
RA   Fedorova N., Fedorova N.D., Feldblyum T.V., Fischer R., Fosker N.,
RA   Fraser A., Garcia J.L., Garcia M.J., Goble A., Goldman G.H., Gomi K.,
RA   Griffith-Jones S., Gwilliam R., Haas B.J., Haas H., Harris D.E.,
RA   Horiuchi H., Huang J., Humphray S., Jimenez J., Keller N., Khouri H.,
RA   Kitamoto K., Kobayashi T., Konzack S., Kulkarni R., Kumagai T., Lafton A.,
RA   Latge J.-P., Li W., Lord A., Lu C., Majoros W.H., May G.S., Miller B.L.,
RA   Mohamoud Y., Molina M., Monod M., Mouyna I., Mulligan S., Murphy L.D.,
RA   O'Neil S., Paulsen I., Penalva M.A., Pertea M., Price C., Pritchard B.L.,
RA   Quail M.A., Rabbinowitsch E., Rawlins N., Rajandream M.A., Reichard U.,
RA   Renauld H., Robson G.D., Rodriguez de Cordoba S., Rodriguez-Pena J.M.,
RA   Ronning C.M., Rutter S., Salzberg S.L., Sanchez M., Sanchez-Ferrero J.C.,
RA   Saunders D., Seeger K., Squares R., Squares S., Takeuchi M., Tekaia F.,
RA   Turner G., Vazquez de Aldana C.R., Weidman J., White O., Woodward J.R.,
RA   Yu J.-H., Fraser C.M., Galagan J.E., Asai K., Machida M., Hall N.,
RA   Barrell B.G., Denning D.W.;
RT   "Genomic sequence of the pathogenic and allergenic filamentous fungus
RT   Aspergillus fumigatus.";
RL   Nature 438:1151-1156(2005).
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; AAHF01000005; EAL89670.1; -; Genomic_DNA.
DR   RefSeq; XP_751708.1; XM_746615.1.
DR   AlphaFoldDB; Q4WQ14; -.
DR   STRING; 746128.CADAFUBP00006644; -.
DR   EnsemblFungi; EAL89670; EAL89670; AFUA_4G11210.
DR   GeneID; 3509053; -.
DR   KEGG; afm:AFUA_4G11210; -.
DR   VEuPathDB; FungiDB:Afu4g11210; -.
DR   eggNOG; ENOG502QRP5; Eukaryota.
DR   HOGENOM; CLU_010191_1_0_1; -.
DR   InParanoid; Q4WQ14; -.
DR   OMA; QTYLCLF; -.
DR   OrthoDB; 1333210at2759; -.
DR   Proteomes; UP000002530; Chromosome 4.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0043332; C:mating projection tip; IBA:GO_Central.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0032220; P:plasma membrane fusion involved in cytogamy; IBA:GO_Central.
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..740
FT                   /note="Plasma membrane fusion protein prm1"
FT                   /id="PRO_0000337269"
FT   TOPO_DOM        1..54
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000250"
FT   TRANSMEM        55..75
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        76..137
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000250"
FT   TRANSMEM        138..158
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        159..320
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000250"
FT   TRANSMEM        321..341
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        342..397
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000250"
FT   TRANSMEM        398..418
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        419..603
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000250"
FT   TRANSMEM        604..624
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        625..740
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        177
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        222
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        245
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        256
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        274
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        454
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        483
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        490
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        505
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        552
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        566
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   740 AA;  80074 MW;  E6FF7846C1AA34D0 CRC64;
     MLFSRSGRSI FPLLPPYAAH APNPNQGHII ALPPDGLTPY LGLRARLSQV WINRWTILLL
     LVLVRVLLAA SGLQADMSTA KREALSACTS VESMGSSMAS MPHYLSQGVN ELTATGVEKA
     VSGLKSMLML TITGVEELVL FIIKVLYQTY LCLFTLAVRG SVHVAVGVIK EAADFLNSTV
     KEVGDDIGKA VSTFESAFNK FLDGVNTVAS AFGASVPTLD LNSSISTLEN LQLPSSIDQG
     LDKLNSSLPT FDEVNNFTQT VLRTPFEEVK KLVNESLGTY TFDRSLLPVP AKEQLTFCEG
     SNGIDSFFDS VTDLVMKARK IFIAILIVAA TLACVPMAWQ EIRRWRSMKE RSQLVRKEAH
     DPMDVVYIVS RPYTAAAGIK AASRFSNSRR QILVRWAIAY ATTPAALFVL CLGVAGLLSC
     LCQYLLLQAV EKTVPELSTQ VGAFADKVVD SLQNASAEWA NDANGVIGHM SQDLNENVFG
     WVNTSTTALN DTLNTFVDKT TGVLNDTFGG TLLYEPLMDV FGCLIGLKVQ GIQKGLTWVH
     DHAHIDFPLL PNDTFSRGAA ASISSNSSNP SDSFLADAGD QTSNKITEVV IRVVNKVEDG
     IRTETIISGV IILIWVFIAL IGIVRALTLF WVRDRNRGEG GGARVNHHLS DAGGFIDVPL
     TAVSNTNTDA RSMPPPAPAP RYEASTSTVV ASRAVPVSST HHEDEKLGFA GERQYGSALK
     VDGAADLRGS SYVEYDMEKR