PRM1_NEUCR
ID PRM1_NEUCR Reviewed; 764 AA.
AC Q7S130;
DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT 15-DEC-2003, sequence version 1.
DT 25-MAY-2022, entry version 79.
DE RecName: Full=Plasma membrane fusion protein prm-1;
GN Name=prm-1; ORFNames=NCU09337;
OS Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 /
OS FGSC 987).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Sordariomycetidae; Sordariales; Sordariaceae; Neurospora.
OX NCBI_TaxID=367110;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987;
RX PubMed=12712197; DOI=10.1038/nature01554;
RA Galagan J.E., Calvo S.E., Borkovich K.A., Selker E.U., Read N.D.,
RA Jaffe D.B., FitzHugh W., Ma L.-J., Smirnov S., Purcell S., Rehman B.,
RA Elkins T., Engels R., Wang S., Nielsen C.B., Butler J., Endrizzi M.,
RA Qui D., Ianakiev P., Bell-Pedersen D., Nelson M.A., Werner-Washburne M.,
RA Selitrennikoff C.P., Kinsey J.A., Braun E.L., Zelter A., Schulte U.,
RA Kothe G.O., Jedd G., Mewes H.-W., Staben C., Marcotte E., Greenberg D.,
RA Roy A., Foley K., Naylor J., Stange-Thomann N., Barrett R., Gnerre S.,
RA Kamal M., Kamvysselis M., Mauceli E.W., Bielke C., Rudd S., Frishman D.,
RA Krystofova S., Rasmussen C., Metzenberg R.L., Perkins D.D., Kroken S.,
RA Cogoni C., Macino G., Catcheside D.E.A., Li W., Pratt R.J., Osmani S.A.,
RA DeSouza C.P.C., Glass N.L., Orbach M.J., Berglund J.A., Voelker R.,
RA Yarden O., Plamann M., Seiler S., Dunlap J.C., Radford A., Aramayo R.,
RA Natvig D.O., Alex L.A., Mannhaupt G., Ebbole D.J., Freitag M., Paulsen I.,
RA Sachs M.S., Lander E.S., Nusbaum C., Birren B.W.;
RT "The genome sequence of the filamentous fungus Neurospora crassa.";
RL Nature 422:859-868(2003).
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; CM002237; EAA29058.1; -; Genomic_DNA.
DR RefSeq; XP_958294.1; XM_953201.2.
DR AlphaFoldDB; Q7S130; -.
DR STRING; 5141.EFNCRP00000009097; -.
DR EnsemblFungi; EAA29058; EAA29058; NCU09337.
DR GeneID; 3874441; -.
DR KEGG; ncr:NCU09337; -.
DR VEuPathDB; FungiDB:NCU09337; -.
DR HOGENOM; CLU_010191_1_0_1; -.
DR InParanoid; Q7S130; -.
DR OMA; QTYLCLF; -.
DR Proteomes; UP000001805; Chromosome 6, Linkage Group II.
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..764
FT /note="Plasma membrane fusion protein prm-1"
FT /id="PRO_0000337286"
FT TOPO_DOM 1..61
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT TRANSMEM 62..82
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 83..149
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 150..170
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 171..334
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT TRANSMEM 335..355
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 356..424
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 425..445
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 446..624
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT TRANSMEM 625..645
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 646..764
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT REGION 653..701
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 735..754
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 271
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 315
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 479
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 508
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 527
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 764 AA; 82997 MW; 9DB5348943BDFAF9 CRC64;
MVYNEKNGGG IPPVPLSLNT ATPWQNVNLH NDQQTEPQLK SHPDTDPRIT PYLGLRARLS
QLWFNRWTIL LILVLIRVII LTANLKENLG DAKAKALSAC TKVEDVGSAM ASMPYYMSKG
VNVMAAGSMQ KAVEAMASVL KMILTGVQAI IMFVINMYIG TFACLVAAFI HGGLHVATAV
VEGATKVMND AISSITKGIT DDMKSFQSAI DKARDFINSG IGLISKDIQL PTINIDSHIR
DLQGIKINAN GVVNGLDVLD QKIPTFDEAK NLTESALAIP FNLVKGKIDT AFSEFTIEPT
IFPTAEKQAL SFCSNNSFLN DFFESLITLV YKAKIAFLVV IIILALLAIF VMGYIEYRGF
KRERERAARM DANAFNSQDA IYIASRRWTA DGGMRLAKWW TKDTDSKNYL LIRWAFAYAT
SLPALFVLSL AVAGMLSCLF QWVLLRQIEK KAPELAAQVG DFAGDVVGTL KQVSNNWANS
SNAVVANMES DINSDLFGWV REATESVNNT LTVLDDQIDH ALVAVFNGTV LLDTARDVVG
CLIGRKIDAV QDGLTWVHDH AKVTLPRFDD DIFSAGAAQS MGSDGDLSSF LAKPGAVTTD
EINEAVGKVI RSLRNGVIQE ALITLGLFLT YVIVVLIGVM GALIGWATPG KTRGEGGQQF
GGRPPSFHNH NGFDPALAPS NAMVGNPASP HYQNEKFGGG GGMHDVASPA YEEVVYAGRV
PVGNTRELIT RYPSHQRTSS YPTVESPDPM PHGDEKVPGY FTPI
