ID PRM1_CANAL Reviewed; 623 AA. AC Q59W55; A0A1D8PF36; DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot. DT 15-MAR-2017, sequence version 2. DT 22-FEB-2023, entry version 76. DE RecName: Full=Plasma membrane fusion protein PRM1; GN Name=PRM1; OrderedLocusNames=CAALFM_C111340WA; GN ORFNames=CaO19.669, CaO19.8286; OS Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast). OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes; OC Saccharomycetales; Debaryomycetaceae; Candida/Lodderomyces clade; Candida. OX NCBI_TaxID=237561; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=SC5314 / ATCC MYA-2876; RX PubMed=15123810; DOI=10.1073/pnas.0401648101; RA Jones T., Federspiel N.A., Chibana H., Dungan J., Kalman S., Magee B.B., RA Newport G., Thorstenson Y.R., Agabian N., Magee P.T., Davis R.W., RA Scherer S.; RT "The diploid genome sequence of Candida albicans."; RL Proc. Natl. Acad. Sci. U.S.A. 101:7329-7334(2004). RN [2] RP GENOME REANNOTATION. RC STRAIN=SC5314 / ATCC MYA-2876; RX PubMed=17419877; DOI=10.1186/gb-2007-8-4-r52; RA van het Hoog M., Rast T.J., Martchenko M., Grindle S., Dignard D., RA Hogues H., Cuomo C., Berriman M., Scherer S., Magee B.B., Whiteway M., RA Chibana H., Nantel A., Magee P.T.; RT "Assembly of the Candida albicans genome into sixteen supercontigs aligned RT on the eight chromosomes."; RL Genome Biol. 8:RESEARCH52.1-RESEARCH52.12(2007). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND GENOME REANNOTATION. RC STRAIN=SC5314 / ATCC MYA-2876; RX PubMed=24025428; DOI=10.1186/gb-2013-14-9-r97; RA Muzzey D., Schwartz K., Weissman J.S., Sherlock G.; RT "Assembly of a phased diploid Candida albicans genome facilitates allele- RT specific measurements and provides a simple model for repeat and indel RT structure."; RL Genome Biol. 14:RESEARCH97.1-RESEARCH97.14(2013). RN [4] RP INDUCTION. RX PubMed=16002644; DOI=10.1128/ec.4.7.1175-1190.2005; RA Zhao R., Daniels K.J., Lockhart S.R., Yeater K.M., Hoyer L.L., Soll D.R.; RT "Unique aspects of gene expression during Candida albicans mating and RT possible G(1) dependency."; RL Eukaryot. Cell 4:1175-1190(2005). RN [5] RP INDUCTION. RX PubMed=16400182; DOI=10.1128/ec.5.1.192-202.2006; RA Dignard D., Whiteway M.; RT "SST2, a regulator of G-protein signaling for the Candida albicans mating RT response pathway."; RL Eukaryot. Cell 5:192-202(2006). RN [6] RP INDUCTION. RX PubMed=16987174; DOI=10.1111/j.1365-2958.2006.05367.x; RA Bennett R.J., Johnson A.D.; RT "The role of nutrient regulation and the Gpa2 protein in the mating RT pheromone response of C. albicans."; RL Mol. Microbiol. 62:100-119(2006). 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 -!- INDUCTION: By pheromones during mating. {ECO:0000269|PubMed:16002644, CC ECO:0000269|PubMed:16400182, ECO:0000269|PubMed:16987174}. 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; CP017623; AOW26759.1; -; Genomic_DNA. DR RefSeq; XP_713802.2; XM_708709.2. DR AlphaFoldDB; Q59W55; -. DR STRING; 237561.Q59W55; -. DR GlyCosmos; Q59W55; 8 sites, No reported glycans. DR EnsemblFungi; C1_11340W_A-T; C1_11340W_A-T-p1; C1_11340W_A. DR GeneID; 3644549; -. DR KEGG; cal:CAALFM_C111340WA; -. DR CGD; CAL0000179626; PRM1. DR VEuPathDB; FungiDB:C1_11340W_A; -. DR eggNOG; ENOG502QRP5; Eukaryota. DR HOGENOM; CLU_010191_1_0_1; -. DR InParanoid; Q59W55; -. DR OrthoDB; 1424686at2759; -. DR PRO; PR:Q59W55; -. DR Proteomes; UP000000559; Chromosome 1. 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; PLASMA MEMBRANE FUSION PROTEIN PRM1; 1. DR PANTHER; PTHR31030:SF1; PLASMA MEMBRANE FUSION PROTEIN PRM1; 1. PE 2: Evidence at transcript level; KW Cell membrane; Conjugation; Glycoprotein; Membrane; Reference proteome; KW Transmembrane; Transmembrane helix. FT CHAIN 1..623 FT /note="Plasma membrane fusion protein PRM1" FT /id="PRO_0000337274" FT TOPO_DOM 1..19 FT /note="Extracellular" FT /evidence="ECO:0000250" FT TRANSMEM 20..40 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 41..92 FT /note="Cytoplasmic" FT /evidence="ECO:0000250" FT TRANSMEM 93..113 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 114..281 FT /note="Extracellular" FT /evidence="ECO:0000250" FT TRANSMEM 282..302 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 303..365 FT /note="Cytoplasmic" FT /evidence="ECO:0000250" FT TRANSMEM 366..386 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 387..537 FT /note="Extracellular" FT /evidence="ECO:0000250" FT TRANSMEM 538..558 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 559..623 FT /note="Cytoplasmic" FT /evidence="ECO:0000250" FT CARBOHYD 132 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 182 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 207 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 218 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 243 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 403 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 444 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 455 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" SQ SEQUENCE 623 AA; 70142 MW; 819D4CC01F6974BF CRC64; MFRNYLNLPE ILTQVYLNKY AILLILILIK LILLETSILD NLNSVLLDNS ICDNGEIQPV LNTVHYMIVD SLQTLEAAGI VSIILTLKVI KQLALFFIEL FFGTYICLLN AALKGSTEVA LDASEGVIRA VNATVVSATN DIESALKGLS SIINDLVTGF NAIKNMFTGS KSDPTQYQNK INITLGDLKS KIMIPSEVLT KLDNFKNSSL YGLSQLGNGT QTIVSTPFEL AIKKLNTMKS SYNFTTGAPS PINFREECLK DMSKLKDVQT DLAKLVEKIS KWLFIGLVLA MVGSILYVSY IQWRHWRRMD KFISETGIDK EVQFRNQYNI YNNFLIYTIV KRMGIELNER TIWMLSFMFS KISRNVFFFG IMGVVSVVAQ YILLNSVQSS MNNHIKSFDI TSNSTSMSAS TIYLRDMNTY IDDTQDKLNQ ELFSGIKEIS VSLNSTIVEF LDKLNETLSD IFGSTPLAGP INTVVYCTIG RKLEKVEKGL TWMNDNLNIN IPSISRDIED GLSHMTFLQP QSVLARANKI IDLYRKSILL ELYISLGLLG VWLFQIFVGS ATLTIRYWNS TRQGNNSYAI SSPHELSEQE KQVYGYPLSH PLIDGKDLTT SSSFYPTTEE KSK //