PRM1_SCLS1
ID PRM1_SCLS1 Reviewed; 795 AA.
AC A7F9L8;
DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT 11-SEP-2007, sequence version 1.
DT 25-MAY-2022, entry version 54.
DE RecName: Full=Plasma membrane fusion protein prm1;
GN Name=prm1; ORFNames=SS1G_14299;
OS Sclerotinia sclerotiorum (strain ATCC 18683 / 1980 / Ss-1) (White mold)
OS (Whetzelinia sclerotiorum).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC Helotiales; Sclerotiniaceae; Sclerotinia.
OX NCBI_TaxID=665079;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 18683 / 1980 / Ss-1;
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}.
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DR EMBL; CH476652; EDO00429.1; -; Genomic_DNA.
DR RefSeq; XP_001584686.1; XM_001584636.1.
DR AlphaFoldDB; A7F9L8; -.
DR STRING; 665079.A7F9L8; -.
DR GeneID; 5480744; -.
DR KEGG; ssl:SS1G_14299; -.
DR VEuPathDB; FungiDB:sscle_16g111210; -.
DR InParanoid; A7F9L8; -.
DR OMA; QTYLCLF; -.
DR Proteomes; UP000001312; Unassembled WGS sequence.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0043332; C:mating projection tip; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0032220; P:plasma membrane fusion involved in cytogamy; IBA:GO_Central.
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..795
FT /note="Plasma membrane fusion protein prm1"
FT /id="PRO_0000337290"
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..330
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT TRANSMEM 331..351
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 352..421
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 422..442
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 443..616
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT TRANSMEM 617..637
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 638..795
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT REGION 11..37
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 736..795
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 750..766
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
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 795 AA; 86696 MW; BF4B4B1F704D8ECA CRC64;
MDAFRGYLAA QKGQHNQAAS NNPPFHSDHE MHHYGAHPNT NAAPADDYYT PYLGLRARLS
QTWINRWTIL LLLIIVRLLI SLSTINGDIA SAKTEALSAC TSVENVGSAM ASMPHYLSQG
VNSMAAAGIT KAVNGMMEML YLTLTGVEEI VLFVIHMMTS TYMCLITLAI TGSLQVAIQM
IEDVGAFMNK SIDTITGDMS SGLKSFEDDL NGFLSKINIG GIFGSSTSPP KIDLSSEINK
LNSIQIDPST MDADLAKLNA SLPTFDQVQN FTDSIIKLPF EEVKKLVNES KIGYKFDDSV
FPVPQKKSLT FCSDNTAIQD FFIGLVKTLN IAKKIMLIVL IIAAILACVP MAYREIWGWR
SMQRRAALLK AHNYTNELDI LYQAHRPYTS QFGLKLSRRF KGQKNQILAR WFIAYATSIP
ALFVLALGMA GLFTCLCQFI ILRTIEKEIP ALAAEVGDFA EHVVQALNNA SEAWALGANS
VINNTNTDIN ENVFGWVNTT TGAINETLNV FTDEMTKALN VTFGGTILYK PIMGVFECLV
GLKVAGIEKG LTWVSDHAHV EFPEFQPDVF SLGAAASLTN STADDNFLAN PATSTTDEIT
DAVVKVGKKL EAVIKQEALI SASLVIVYFV IVFIGFVRVV IGMCGRDKSR AEGGSGPGTL
YRNGFPHQHL PVIREEKFGS NASDGWHEEH MRAGGDTIRM PFGGDGAADD LPYDGAPAPK
YEASIAPVTT EMGSERLGVV PGGRANTNRG PWVRDEKGRE GWEADDAQMR ATSSYGFLEN
GDEKSSGWGL PPRRV
