ID   PRM1_ASPTN              Reviewed;         725 AA.
AC   Q0CQS4;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   17-OCT-2006, sequence version 1.
DT   03-AUG-2022, entry version 60.
DE   RecName: Full=Plasma membrane fusion protein prm1;
GN   Name=prm1; ORFNames=ATEG_03960;
OS   Aspergillus terreus (strain NIH 2624 / FGSC A1156).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Circumdati.
OX   NCBI_TaxID=341663;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NIH 2624 / FGSC A1156;
RA   Birren B.W., Lander E.S., Galagan J.E., Nusbaum C., Devon K., Henn M.,
RA   Ma L.-J., Jaffe D.B., Butler J., Alvarez P., Gnerre S., Grabherr M.,
RA   Kleber M., Mauceli E.W., Brockman W., Rounsley S., Young S.K., LaButti K.,
RA   Pushparaj V., DeCaprio D., Crawford M., Koehrsen M., Engels R.,
RA   Montgomery P., Pearson M., Howarth C., Larson L., Luoma S., White J.,
RA   Alvarado L., Kodira C.D., Zeng Q., Oleary S., Yandava C., Denning D.W.,
RA   Nierman W.C., Milne T., Madden K.;
RT   "Annotation of the Aspergillus terreus NIH2624 genome.";
RL   Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
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; CH476598; EAU35762.1; -; Genomic_DNA.
DR   RefSeq; XP_001213138.1; XM_001213138.1.
DR   AlphaFoldDB; Q0CQS4; -.
DR   SMR; Q0CQS4; -.
DR   STRING; 341663.Q0CQS4; -.
DR   EnsemblFungi; EAU35762; EAU35762; ATEG_03960.
DR   GeneID; 4318375; -.
DR   VEuPathDB; FungiDB:ATEG_03960; -.
DR   eggNOG; ENOG502QRP5; Eukaryota.
DR   HOGENOM; CLU_010191_1_0_1; -.
DR   OMA; QTYLCLF; -.
DR   OrthoDB; 1333210at2759; -.
DR   Proteomes; UP000007963; 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..725
FT                   /note="Plasma membrane fusion protein prm1"
FT                   /id="PRO_0000337272"
FT   TOPO_DOM        1..53
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000250"
FT   TRANSMEM        54..74
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        75..136
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000250"
FT   TRANSMEM        137..157
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        158..318
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000250"
FT   TRANSMEM        319..339
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        340..394
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000250"
FT   TRANSMEM        395..417
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        418..602
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000250"
FT   TRANSMEM        603..623
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        624..725
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        176
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        244
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        273
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        278
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        482
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        489
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        504
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        551
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   725 AA;  78670 MW;  36E4B9D1103333AE CRC64;
     MLFSRPGRSI FPLLPPYGAH DPNGGRRIIP LNPDGITPYL GLRSRLSQVW LNRWTILLLL
     VLARVLIAVA GMQSDMGSAK REALSACTSV ESMGSAMVSM PHYLSQGVNE LTAAGVEKAV
     SALKTMLLLT ITGVEELILF FIKVMYQTYL CLFTMVVRGS VHLALGVVED AADFLNSTVK
     SIGQDIHKSV DSFESSLNSF IDDINGIASA LLGEIPKLDI SDKLDKLDSL SLPSSIDSTI
     DKVNNSIPTF DEVDKYVTNI LRTPFEEVKR LVNGSLSNYT FDRSALPVPA KEQLSFCDGS
     DGINSFFDKV AHITTTARTI FIAVLIIAAV LVCVPVGWQE IRRWRTMKER SQLVHKDAHD
     PMDVVYIVSR PYTAATGVKA ASRFSNSRRQ ILVRWVIAYA TSPPALFVLC LALAGLFSCL
     CQYILLKAVE RTVPELTSEV GQFAGKVVDK LQDTSAKWAA DANSAIADTN TDLNKNIFGW
     VNTSTTAVND TLDAFVEKTT GVLNDTFGDT VLSGPVQEVY DCLIGLKVEA VQKALTWVHD
     HAHIDFPLLP NDTFSRGAAD SISDGSSNPS DSFLADADDQ TSNKITEVVF RVTDKIEEGI
     RTETVISAVI LLVWVVNALI GVLRALSLFW SRERTRGEGG GGAPMPAAPA DSHGFVDVPL
     TAIPDVASHS QPAPRYEGPA PALAVSRDIP YGDEKLGSVG QKALHVDGIS DLRGSSYVEY
     GMEKR