PRM1_ASPCL
ID PRM1_ASPCL Reviewed; 736 AA.
AC A1CI53;
DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT 20-MAY-2008, sequence version 2.
DT 03-AUG-2022, entry version 56.
DE RecName: Full=Plasma membrane fusion protein prm1;
GN Name=prm1; ORFNames=ACLA_050300;
OS Aspergillus clavatus (strain ATCC 1007 / CBS 513.65 / DSM 816 / NCTC 3887 /
OS NRRL 1 / QM 1276 / 107).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Fumigati.
OX NCBI_TaxID=344612;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 1007 / CBS 513.65 / DSM 816 / NCTC 3887 / NRRL 1;
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 -!- SEQUENCE CAUTION:
CC Sequence=EAW10558.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; DS027054; EAW10558.1; ALT_INIT; Genomic_DNA.
DR RefSeq; XP_001271984.1; XM_001271983.1.
DR AlphaFoldDB; A1CI53; -.
DR STRING; 5057.CADACLAP00004915; -.
DR EnsemblFungi; EAW10558; EAW10558; ACLA_050300.
DR GeneID; 4703769; -.
DR KEGG; act:ACLA_050300; -.
DR eggNOG; ENOG502QRP5; Eukaryota.
DR OrthoDB; 1333210at2759; -.
DR Proteomes; UP000006701; 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..736
FT /note="Plasma membrane fusion protein prm1"
FT /id="PRO_0000337267"
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..736
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT REGION 638..675
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
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 736 AA; 79649 MW; 0E4FD5A0AB718CD1 CRC64;
MLFSRSGHSI FPLLPPYAAH APTTNQGHII TMPPDGLTPY LGLRARLSQV WINRWTILLL
LVLVRVLMAA SGLQADMGTA KREALSACSS VESMGSSMAS MPHYLSQGVN ELTASGVETA
VSGLKSMLML TVTGVEELVL FIIKVLYQTY LCLFTLAVRG SVHVAVGVIK DAADFLNSTV
KEVGDDIGKV VSTFEDGFNK FLDSVNSVAS VFGGSVPTLD LNSSISTLEN LQLPSSIDKG
LDKLNNSLPT FDEVNNFTQT VLRTPFEEVK KLVNQSLGTY TFDRSLLPIP AKEQLKFCEG
NDGIDSFFDN VGDLVMTARK IFIAVLILAA VLACIPMAWQ EIRRWRSMKE RSQLVRKEAH
DPMDIVYIVS RPYTAAAGIK AASRFSNSRR QILVRWAIAY ATTPAALFVL CLGIAGLFSC
LCQYLLLHAV EKTVPELSTQ VGAFADKVVD KLENASAAWA NDANGVIGHM NQDLNQNVFG
WVNTSTTALN DTLNTFVDKT TGVLNETFGG TILYEPLMDV FGCLIGLKVA GIQKGLTWVH
DHAHIDFPLL PNDTFSRGAA ASIASNNSDA SDSFLADAGD QTSNKITEVV IRVVDKVEEG
IRMETIISTA ILLLWVFIAL VGIVRALTLF WMRDRSRGEG GGAPSTSHHT SDAGGFDDVP
LTAIPNPSAH SAPAPRYEAT ISTVVASRAI PTSNSFQHQD EKMGFAGERQ YGSALKVDGA
PDLRGSAYVE YGVEKH
