PRM1_CANAL
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 25-MAY-2022, entry version 73.
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}.
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DR EMBL; CP017623; AOW26759.1; -; Genomic_DNA.
DR RefSeq; XP_713802.2; XM_708709.2.
DR AlphaFoldDB; Q59W55; -.
DR STRING; 237561.Q59W55; -.
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; 1333210at2759; -.
DR PRO; PR:Q59W55; -.
DR Proteomes; UP000000559; Chromosome 1.
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 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