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PRM1_SCHPO
ID   PRM1_SCHPO              Reviewed;         703 AA.
AC   Q9P771;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   03-AUG-2022, entry version 96.
DE   RecName: Full=Plasma membrane fusion protein prm1;
GN   Name=prm1; ORFNames=SPAP7G5.03;
OS   Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC   Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC   Schizosaccharomyces.
OX   NCBI_TaxID=284812;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=972 / ATCC 24843;
RX   PubMed=11859360; DOI=10.1038/nature724;
RA   Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA   Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA   Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.,
RA   Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S.,
RA   Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S.,
RA   Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D.,
RA   Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P.,
RA   Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K.,
RA   O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M.,
RA   Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N.,
RA   Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A.,
RA   Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R.,
RA   Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M.,
RA   Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A.,
RA   Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A.,
RA   Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H.,
RA   Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S.,
RA   Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C.,
RA   Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A.,
RA   Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M.,
RA   del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S.,
RA   Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R.,
RA   Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G.,
RA   Nurse P.;
RT   "The genome sequence of Schizosaccharomyces pombe.";
RL   Nature 415:871-880(2002).
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; CU329670; CAB88270.1; -; Genomic_DNA.
DR   RefSeq; NP_594313.1; NM_001019736.2.
DR   AlphaFoldDB; Q9P771; -.
DR   SMR; Q9P771; -.
DR   BioGRID; 279248; 3.
DR   STRING; 4896.SPAP7G5.03.1; -.
DR   TCDB; 9.B.63.1.2; the yeast pheromone-induced plasma membrane mating cell fusion protein (prm1) family.
DR   iPTMnet; Q9P771; -.
DR   PaxDb; Q9P771; -.
DR   EnsemblFungi; SPAP7G5.03.1; SPAP7G5.03.1:pep; SPAP7G5.03.
DR   GeneID; 2542800; -.
DR   KEGG; spo:SPAP7G5.03; -.
DR   PomBase; SPAP7G5.03; prm1.
DR   VEuPathDB; FungiDB:SPAP7G5.03; -.
DR   eggNOG; ENOG502QRP5; Eukaryota.
DR   HOGENOM; CLU_010191_1_0_1; -.
DR   InParanoid; Q9P771; -.
DR   OMA; QTYLCLF; -.
DR   PhylomeDB; Q9P771; -.
DR   PRO; PR:Q9P771; -.
DR   Proteomes; UP000002485; Chromosome I.
DR   GO; GO:0005737; C:cytoplasm; HDA:PomBase.
DR   GO; GO:0005887; C:integral component of plasma membrane; ISO:PomBase.
DR   GO; GO:0043332; C:mating projection tip; IDA:PomBase.
DR   GO; GO:0032220; P:plasma membrane fusion involved in cytogamy; IMP:PomBase.
DR   GO; GO:0097036; P:regulation of plasma membrane sterol distribution; IMP:PomBase.
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..703
FT                   /note="Plasma membrane fusion protein prm1"
FT                   /id="PRO_0000337289"
FT   TOPO_DOM        1..14
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000250"
FT   TRANSMEM        15..35
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        36..102
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000250"
FT   TRANSMEM        103..123
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        124..285
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000250"
FT   TRANSMEM        286..306
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        307..375
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000250"
FT   TRANSMEM        376..396
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        397..566
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000250"
FT   TRANSMEM        567..587
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        588..703
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        142
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        185
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        196
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        221
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        256
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        423
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        430
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        459
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        470
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        510
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        530
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        542
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        545
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   703 AA;  78740 MW;  B6925C68B6BC3DA0 CRC64;
     MASSYLSLAA RLSQCWISPW SLCCLYILMQ FFLFTKDLNT KIGDFVNDEQ ATCNYIQEKV
     DILLDSPSLI ANAAVRVAKD GIQSTVKIIL SGISDSLIAA ENVFIFFIEF SYGTYLCLIQ
     LAIDGILDAV ADVGEEIGTA VNDTLHAIAD EIEDTVSSLN EVFQSAEDSL EKVASWLGED
     INLPNVSIPE IQSLRNFTLS SSYDTEFEKL KAGVNFDSAI NATKAAISKP FSSARNLILE
     KVSNYSFDTS MVSSPNKTHV VVCSTDDLTA ISSFILSSIY KIRKVVIISL LIIIAGLFLI
     SSIYEIWKWC RIRHKAFLLD EHIRSNKFED TRDLISYIES PISWNLKYFI SALPLPCFLS
     VQLRWFITYI FHPPAAMILF ISCTSFISGI LQLVLLNNIR EDGSVISALA QNSFHKVESA
     LANVSVAWAN STNQIILKNQ ENINNNMFGS IHNTTLSLNS TLNTFMNELN SSMTSAFGDT
     FLASTVQNVM NCLLYRKIEN FEEVLTWVYN KSHIELPLLP TDILSKSIDN QTIYSSLYSS
     LNSSNSTVSF SGIFDRVEKS VISELNFSFL FFLLWLLICA FGLIGVLSSW LKSLFLSLLD
     LVIPNPKENI TLPVQSLAFP VTKSCRPPPI PPRESHVYDF QNFQYEEDDC IDYKRSLGLI
     SLSSDLAIDI PISPAIISDI QFNSITTESE ETTYLLKEKQ DRY
 
 
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