PRM1_BOTFB
ID PRM1_BOTFB Reviewed; 794 AA.
AC A6SEV8;
DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT 21-AUG-2007, sequence version 1.
DT 03-AUG-2022, entry version 60.
DE RecName: Full=Plasma membrane fusion protein prm1;
GN Name=prm1; ORFNames=BC1G_10779;
OS Botryotinia fuckeliana (strain B05.10) (Noble rot fungus) (Botrytis
OS cinerea).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC Helotiales; Sclerotiniaceae; Botrytis.
OX NCBI_TaxID=332648;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=B05.10;
RX PubMed=21876677; DOI=10.1371/journal.pgen.1002230;
RA Amselem J., Cuomo C.A., van Kan J.A.L., Viaud M., Benito E.P., Couloux A.,
RA Coutinho P.M., de Vries R.P., Dyer P.S., Fillinger S., Fournier E.,
RA Gout L., Hahn M., Kohn L., Lapalu N., Plummer K.M., Pradier J.-M.,
RA Quevillon E., Sharon A., Simon A., ten Have A., Tudzynski B., Tudzynski P.,
RA Wincker P., Andrew M., Anthouard V., Beever R.E., Beffa R., Benoit I.,
RA Bouzid O., Brault B., Chen Z., Choquer M., Collemare J., Cotton P.,
RA Danchin E.G., Da Silva C., Gautier A., Giraud C., Giraud T., Gonzalez C.,
RA Grossetete S., Gueldener U., Henrissat B., Howlett B.J., Kodira C.,
RA Kretschmer M., Lappartient A., Leroch M., Levis C., Mauceli E.,
RA Neuveglise C., Oeser B., Pearson M., Poulain J., Poussereau N.,
RA Quesneville H., Rascle C., Schumacher J., Segurens B., Sexton A., Silva E.,
RA Sirven C., Soanes D.M., Talbot N.J., Templeton M., Yandava C., Yarden O.,
RA Zeng Q., Rollins J.A., Lebrun M.-H., Dickman M.;
RT "Genomic analysis of the necrotrophic fungal pathogens Sclerotinia
RT sclerotiorum and Botrytis cinerea.";
RL PLoS Genet. 7:E1002230-E1002230(2011).
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; CH476923; EDN32463.1; -; Genomic_DNA.
DR RefSeq; XP_001550235.1; XM_001550185.1.
DR AlphaFoldDB; A6SEV8; -.
DR PRIDE; A6SEV8; -.
DR OMA; QTYLCLF; -.
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..794
FT /note="Plasma membrane fusion protein prm1"
FT /id="PRO_0000337273"
FT TOPO_DOM 1..66
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT TRANSMEM 67..87
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 88..149
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 150..170
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 171..332
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT TRANSMEM 333..353
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 354..421
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 422..442
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 443..622
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT TRANSMEM 623..643
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 644..794
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT REGION 9..30
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 756..794
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 13..30
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 756..771
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 21
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 189
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 259
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 270
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 288
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 469
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 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 520
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 580
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 794 AA; 86418 MW; 547576E18F21D78D CRC64;
MDAFKGYIAS QKIQHSHAPS NDSSINSGHE MHPYGVNRNI NAAPADDYYT PYLGLRARLS
QTWINRWTVL LLLIIVRLLI SLAGIKGDVA SAKTEALSAC SSVENVGSAM ASMPHYLSQG
VNSMAAAGIT KAVNGMMQML YMSLTGVEEI VLFVIHMMTS TYMCLITLAI TGSLQVAIQM
IEDVGAFMNK SIDTITGDMS SGLKSFEDDL NGFLSKINIG GIFGSSTSPP TIDLSSEINK
LNSIQIDPTT MDADLAKLNA SLPTFEQVQN FTDNIIKLPF EEVKKLVNES MIAYKFDDSV
FPVPQKKSLT FCSDNTAIQD FFVGLVKTLD TAKKIILIVL VIAAILACIP MAFREIWGWR
VMQIQAALLK SRSYTNEMDI LYQAHRPYTS QFGLKLSRRF KGQKNQILAR WFIAYATSIP
ALFVLALGLA GLFTCLCQFI VLKTLEKEIP ALTAEVGDFA EHVVKALNNA SESWALGANS
VINNTNTEIN DNVFGWVNTT TGAINETLNV FTDEMTKALN VTFGGTILYK PIMGVFECLV
GLKIAGIEKG LTWVSDNAHV EFPEFQPDVF SLGAAASLSN TTADDNFLAN PATSTTDEIT
NAVVKVGKKL EAVIRQEALI STALVAIYFV IVLIGLVHVI IGMCGRDKSR GEGGSAPTPL
YRNTDVEAPN QHLPEISREK FGTSGNDGWH QEHMRAGGDP ITRMPFGGGD GAADDLPYNG
APAPTYEASI APTERLGVVP AGRVNTNRGP WVRDEKSREL WEADDMQRRA TSSYGHLEGG
DEKSSGWGVP PRRI
