PRM1_NEOFI
ID PRM1_NEOFI Reviewed; 742 AA.
AC A1CWM3;
DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 1.
DT 03-AUG-2022, entry version 66.
DE RecName: Full=Plasma membrane fusion protein prm1;
GN Name=prm1; ORFNames=NFIA_105130;
OS Neosartorya fischeri (strain ATCC 1020 / DSM 3700 / CBS 544.65 / FGSC A1164
OS / JCM 1740 / NRRL 181 / WB 181) (Aspergillus fischerianus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Fumigati.
OX NCBI_TaxID=331117;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 1020 / DSM 3700 / CBS 544.65 / FGSC A1164 / JCM 1740 / NRRL 181
RC / WB 181;
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; DS027685; EAW25025.1; -; Genomic_DNA.
DR RefSeq; XP_001266922.1; XM_001266921.1.
DR AlphaFoldDB; A1CWM3; -.
DR STRING; 36630.CADNFIAP00010015; -.
DR EnsemblFungi; EAW25025; EAW25025; NFIA_105130.
DR GeneID; 4593990; -.
DR KEGG; nfi:NFIA_105130; -.
DR VEuPathDB; FungiDB:NFIA_105130; -.
DR eggNOG; ENOG502QRP5; Eukaryota.
DR HOGENOM; CLU_010191_1_0_1; -.
DR OMA; QTYLCLF; -.
DR OrthoDB; 1333210at2759; -.
DR Proteomes; UP000006702; 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..742
FT /note="Plasma membrane fusion protein prm1"
FT /id="PRO_0000337285"
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..395
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 396..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..742
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 742 AA; 80335 MW; 44AA08B8D926F976 CRC64;
MLFSRSGRSI FPLLPPYAAH APNPNQGHII TLPPDGLTPY LGLRARLSQV WINRWTILLL
LVLVRVLLAA SGLQADMSTA KREALSACTS VESMGSSMAS MPHYLSQGVN ELTASGVEKA
VSGLKSMLML TITGVEELVL FIIKVLYQTY LCLFTLAVRG SVHVAVGVIE EAADFLNSTV
KEVGDDIGKA VSTFESAFNK FLDGVNTVAS AFGASVPTLD LNSSISALEN LQLPSSIDKG
LDKLNSSLPT FDEVNNFTQT VLRTPFEEVK KLVNESLGTY TFDRSLLPVP AKEQLTFCEG
NNGIDSFFDS VTDLVMTARK IFIAVLIVAA TLACVPMAWQ EIRRWRSMKE RSQLVRKEAH
DPMDVVYIVS RPYTAAAGIK AASRFSNSRR QILVRWAVAY ATTPAALFVL CLGVAGLLSC
LCQYLLLQAV EKTVPELSTQ VGAFADKVVD SLQNASAEWA NDANGVIGHM NQDLNENVFG
WVNTSTTALN DTLNTFVDKT TGVLNDTFGG TLLYEPLMDV FECLIGLKVQ GIQKGLTWVH
DHAHIDFPLL PNDTFSRGAA ASISSNSSNP SDSFLADAGD QTSNKITEVV IRVVNKVEDG
VRTETIISAV IILIWVFIAL VGIVRALSLF WVRDRNRGEG GGARVNRHES DAGGFIDVPL
TAIPNTNTDA RSMPTPAPAP APRYEASTST VVASRAVPVS STHHEDEKLG FAGERQYGSA
LKVDGAADLR GSSYVEYDME KR