PRM1_ASPNC
ID PRM1_ASPNC Reviewed; 739 AA.
AC A2QJ14;
DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT 06-MAR-2007, sequence version 1.
DT 03-AUG-2022, entry version 60.
DE RecName: Full=Plasma membrane fusion protein prm1;
GN Name=prm1; ORFNames=An04g05460;
OS Aspergillus niger (strain CBS 513.88 / FGSC A1513).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Circumdati.
OX NCBI_TaxID=425011;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 513.88 / FGSC A1513 / ATCC MYA-4892;
RX PubMed=17259976; DOI=10.1038/nbt1282;
RA Pel H.J., de Winde J.H., Archer D.B., Dyer P.S., Hofmann G., Schaap P.J.,
RA Turner G., de Vries R.P., Albang R., Albermann K., Andersen M.R.,
RA Bendtsen J.D., Benen J.A.E., van den Berg M., Breestraat S., Caddick M.X.,
RA Contreras R., Cornell M., Coutinho P.M., Danchin E.G.J., Debets A.J.M.,
RA Dekker P., van Dijck P.W.M., van Dijk A., Dijkhuizen L., Driessen A.J.M.,
RA d'Enfert C., Geysens S., Goosen C., Groot G.S.P., de Groot P.W.J.,
RA Guillemette T., Henrissat B., Herweijer M., van den Hombergh J.P.T.W.,
RA van den Hondel C.A.M.J.J., van der Heijden R.T.J.M., van der Kaaij R.M.,
RA Klis F.M., Kools H.J., Kubicek C.P., van Kuyk P.A., Lauber J., Lu X.,
RA van der Maarel M.J.E.C., Meulenberg R., Menke H., Mortimer M.A.,
RA Nielsen J., Oliver S.G., Olsthoorn M., Pal K., van Peij N.N.M.E.,
RA Ram A.F.J., Rinas U., Roubos J.A., Sagt C.M.J., Schmoll M., Sun J.,
RA Ussery D., Varga J., Vervecken W., van de Vondervoort P.J.J., Wedler H.,
RA Woesten H.A.B., Zeng A.-P., van Ooyen A.J.J., Visser J., Stam H.;
RT "Genome sequencing and analysis of the versatile cell factory Aspergillus
RT niger CBS 513.88.";
RL Nat. Biotechnol. 25:221-231(2007).
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; AM270078; CAK38808.1; -; Genomic_DNA.
DR RefSeq; XP_001401910.1; XM_001401873.1.
DR AlphaFoldDB; A2QJ14; -.
DR PaxDb; A2QJ14; -.
DR PRIDE; A2QJ14; -.
DR EnsemblFungi; CAK38808; CAK38808; An04g05460.
DR GeneID; 4990953; -.
DR KEGG; ang:ANI_1_904184; -.
DR VEuPathDB; FungiDB:An04g05460; -.
DR HOGENOM; CLU_010191_1_0_1; -.
DR Proteomes; UP000006706; Chromosome 6L.
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..739
FT /note="Plasma membrane fusion protein prm1"
FT /id="PRO_0000337270"
FT TOPO_DOM 1..49
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT TRANSMEM 50..70
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 71..149
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 150..169
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 170..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..598
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT TRANSMEM 599..619
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 620..739
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT REGION 636..693
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 220
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 279
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 283
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 498
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 564
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 739 AA; 80532 MW; 94A9FE6F42640516 CRC64;
MLFSKSGRTI FPLLPPYGVQ DPNGVQGRVI PVHPDGSTPY LGLRARLSQV WLNRWTVLLL
LVLARVLMAA SSIKTDMNRA KSEALSACTS VESMGDAMVS MPHYLAEGVN ELTADGVNAA
IDGLKMLLML TLTGVEELVI FFVKVMYQTY LCLFTLVVHG VVDVGLSLIE DVTDVLNSTV
KTVAKDIAKV TETFEDDYNT LISKINGVAS LFGGSVPTLN ISSEIDKLEN VQLSSSIDKD
LQKINDSIPN FNEVMNFTEN VIRFPFDEVK KLVNESLGNY TFNASALPVP AKKTLTFCDK
NDGINSFFAG ATDIILTARK IFIAILVVAA IIACVPMAWQ EIRRWHTMKE RSQLVRKEAH
DPMDVVYIVS RPHTAAIGIK AASRFSNSRR QILVRWVIAY ATSPAALFVL LLALAGLLSC
LCQFILLSAV KRTVPELSNE VGDFAEEVVD VLQNTSAQWA NDANKVIQNV DDELNDHVFG
WVNTSTGALN DTLNTFVNKT IGVLNDTFGG TLLYEPLLDV FDCLVGLKVE SVQKGLTWVS
DHAHIDFPLL PNDTFSRGAE GSLNSSDASE SFLADAGDET SNKITEVVYK VISALEKALL
IEVIIASCIL LVWVINAMFG IIRALTLFWG RDKNRGEGGP APPNSRPNPG SGPDSHGFID
VPLTSLPSHR DADETAARSQ PAPRYEVATS QGSSAAVVSS ELEYPDEKVG FAGQRNALRV
DGVSDLRGSS YVEYGIEKY
