PRM1_EMENI
ID PRM1_EMENI Reviewed; 739 AA.
AC Q5B1G6; C8VFY4;
DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT 26-APR-2005, sequence version 1.
DT 25-MAY-2022, entry version 79.
DE RecName: Full=Plasma membrane fusion protein prm1;
GN Name=prm1; ORFNames=AN5614;
OS Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 /
OS M139) (Aspergillus nidulans).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Nidulantes.
OX NCBI_TaxID=227321;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139;
RX PubMed=16372000; DOI=10.1038/nature04341;
RA Galagan J.E., Calvo S.E., Cuomo C., Ma L.-J., Wortman J.R., Batzoglou S.,
RA Lee S.-I., Bastuerkmen M., Spevak C.C., Clutterbuck J., Kapitonov V.,
RA Jurka J., Scazzocchio C., Farman M.L., Butler J., Purcell S., Harris S.,
RA Braus G.H., Draht O., Busch S., D'Enfert C., Bouchier C., Goldman G.H.,
RA Bell-Pedersen D., Griffiths-Jones S., Doonan J.H., Yu J., Vienken K.,
RA Pain A., Freitag M., Selker E.U., Archer D.B., Penalva M.A., Oakley B.R.,
RA Momany M., Tanaka T., Kumagai T., Asai K., Machida M., Nierman W.C.,
RA Denning D.W., Caddick M.X., Hynes M., Paoletti M., Fischer R., Miller B.L.,
RA Dyer P.S., Sachs M.S., Osmani S.A., Birren B.W.;
RT "Sequencing of Aspergillus nidulans and comparative analysis with A.
RT fumigatus and A. oryzae.";
RL Nature 438:1105-1115(2005).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139;
RX PubMed=19146970; DOI=10.1016/j.fgb.2008.12.003;
RA Wortman J.R., Gilsenan J.M., Joardar V., Deegan J., Clutterbuck J.,
RA Andersen M.R., Archer D., Bencina M., Braus G., Coutinho P., von Dohren H.,
RA Doonan J., Driessen A.J., Durek P., Espeso E., Fekete E., Flipphi M.,
RA Estrada C.G., Geysens S., Goldman G., de Groot P.W., Hansen K.,
RA Harris S.D., Heinekamp T., Helmstaedt K., Henrissat B., Hofmann G.,
RA Homan T., Horio T., Horiuchi H., James S., Jones M., Karaffa L.,
RA Karanyi Z., Kato M., Keller N., Kelly D.E., Kiel J.A., Kim J.M.,
RA van der Klei I.J., Klis F.M., Kovalchuk A., Krasevec N., Kubicek C.P.,
RA Liu B., Maccabe A., Meyer V., Mirabito P., Miskei M., Mos M., Mullins J.,
RA Nelson D.R., Nielsen J., Oakley B.R., Osmani S.A., Pakula T., Paszewski A.,
RA Paulsen I., Pilsyk S., Pocsi I., Punt P.J., Ram A.F., Ren Q., Robellet X.,
RA Robson G., Seiboth B., van Solingen P., Specht T., Sun J.,
RA Taheri-Talesh N., Takeshita N., Ussery D., vanKuyk P.A., Visser H.,
RA van de Vondervoort P.J., de Vries R.P., Walton J., Xiang X., Xiong Y.,
RA Zeng A.P., Brandt B.W., Cornell M.J., van den Hondel C.A., Visser J.,
RA Oliver S.G., Turner G.;
RT "The 2008 update of the Aspergillus nidulans genome annotation: a community
RT effort.";
RL Fungal Genet. Biol. 46:S2-13(2009).
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; AACD01000098; EAA62707.1; -; Genomic_DNA.
DR EMBL; BN001305; CBF81547.1; -; Genomic_DNA.
DR RefSeq; XP_663218.1; XM_658126.1.
DR AlphaFoldDB; Q5B1G6; -.
DR STRING; 162425.CADANIAP00003456; -.
DR TCDB; 9.B.63.1.3; the yeast pheromone-induced plasma membrane mating cell fusion protein (prm1) family.
DR PRIDE; Q5B1G6; -.
DR EnsemblFungi; CBF81547; CBF81547; ANIA_05614.
DR EnsemblFungi; EAA62707; EAA62707; AN5614.2.
DR GeneID; 2871905; -.
DR KEGG; ani:AN5614.2; -.
DR VEuPathDB; FungiDB:AN5614; -.
DR eggNOG; ENOG502QRP5; Eukaryota.
DR HOGENOM; CLU_010191_1_0_1; -.
DR InParanoid; Q5B1G6; -.
DR OMA; QTYLCLF; -.
DR OrthoDB; 1333210at2759; -.
DR Proteomes; UP000000560; Chromosome V.
DR Proteomes; UP000005890; 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..739
FT /note="Plasma membrane fusion protein prm1"
FT /id="PRO_0000337281"
FT TOPO_DOM 1..52
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT TRANSMEM 53..73
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 74..135
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 136..156
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 157..320
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT TRANSMEM 321..341
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 342..394
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 395..417
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 418..600
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT TRANSMEM 601..621
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 622..739
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT REGION 634..697
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 658..681
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 175
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 244
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 273
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 309
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 453
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 482
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 489
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 504
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 551
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 739 AA; 79983 MW; 52348FC182584DC5 CRC64;
MIFSRSARSI FPLLPPYGAH DPQGGRAVPL QPDDITPYMG LRARLSQIWM NRWTILLLLV
LVRVLIAIAS LNTNMDSARR EALSACTSVE SMGSAMASMP HYSARGINEL TASGVETAVS
ALKTMLTLVV SGVEELIVFF IKMMYQTYLC LITMAVRGTV DVGVGLLKDA SDFLNSTIKS
IGEGISDATQ TFEDGLNKFV DGINIVGSVF GGDEVPDLDL SSFIEDLENA QLPSSIDDGL
DKLNDSVPTF DEVSEFVENI IRTPFDEVKK LINESMGTFT FDRDTLPVPA KKQLSFCKGS
DGIDSFFNNV SDIAETAKKV FIAVLVIAAV LVCFPMAWQE IRRWRAQKER SQLVRKEAHD
PLDVVYIVSR PYSAAAGIKA ASRFSNSRRQ ILVRWVIAYA TSPSALFVLS LAIAGLFACL
CQYLLLRAVE EAVPELSAEV GAFADKVVAS LDNTSAEWAL SANSAIGDIN TELNDKVFGW
VNSTTTGVND TLNTFVDKTT GVLNDTFGGT LLYDPLKDVF DCLIGLKIAG IQRGLTWVHD
NAHIDFPELS NDTFSRGAAE SLSDDNSSES FLSDAGASTS NKITEVVFRV TSAIESGIAT
EALISGAILL IWFLNLLFGL IRALSLFRSH DRNRGDGGPG PAANLDPNDG FSDVPLTAIP
NPHTTAHSAA DSQSRSQPVP EYEPPSRNFA SAGPPAAVTA QTTYEDEKLG FAGQRRNALK
VSVIDARASS YPEFGDEKR
