PRM1_ASPFC
ID PRM1_ASPFC Reviewed; 740 AA.
AC B0Y6V2;
DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT 08-APR-2008, sequence version 1.
DT 03-AUG-2022, entry version 51.
DE RecName: Full=Plasma membrane fusion protein prm1;
GN Name=prm1; ORFNames=AFUB_068240;
OS Neosartorya fumigata (strain CEA10 / CBS 144.89 / FGSC A1163) (Aspergillus
OS fumigatus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Fumigati.
OX NCBI_TaxID=451804;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CEA10 / CBS 144.89 / FGSC A1163;
RX PubMed=18404212; DOI=10.1371/journal.pgen.1000046;
RA Fedorova N.D., Khaldi N., Joardar V.S., Maiti R., Amedeo P., Anderson M.J.,
RA Crabtree J., Silva J.C., Badger J.H., Albarraq A., Angiuoli S., Bussey H.,
RA Bowyer P., Cotty P.J., Dyer P.S., Egan A., Galens K., Fraser-Liggett C.M.,
RA Haas B.J., Inman J.M., Kent R., Lemieux S., Malavazi I., Orvis J.,
RA Roemer T., Ronning C.M., Sundaram J.P., Sutton G., Turner G., Venter J.C.,
RA White O.R., Whitty B.R., Youngman P., Wolfe K.H., Goldman G.H.,
RA Wortman J.R., Jiang B., Denning D.W., Nierman W.C.;
RT "Genomic islands in the pathogenic filamentous fungus Aspergillus
RT fumigatus.";
RL PLoS Genet. 4:E1000046-E1000046(2008).
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; DS499598; EDP50487.1; -; Genomic_DNA.
DR AlphaFoldDB; B0Y6V2; -.
DR EnsemblFungi; EDP50487; EDP50487; AFUB_068240.
DR VEuPathDB; FungiDB:AFUB_068240; -.
DR HOGENOM; CLU_010191_1_0_1; -.
DR PhylomeDB; B0Y6V2; -.
DR Proteomes; UP000001699; 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; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..740
FT /note="Plasma membrane fusion protein prm1"
FT /id="PRO_0000337268"
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; 80104 MW; D3B89AE3865A34CF 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
MAVSNTNTDA RSMPPPAPAP RYEASTSTVV ASRAVPVSST HHEDEKLGFA GERQYGSALK
VDGAADLRGS SYVEYDMEKR