PRM1_KLULA
ID PRM1_KLULA Reviewed; 643 AA.
AC Q6CUV7;
DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT 16-AUG-2004, sequence version 1.
DT 03-AUG-2022, entry version 80.
DE RecName: Full=Plasma membrane fusion protein PRM1;
GN Name=PRM1; OrderedLocusNames=KLLA0C01936g;
OS Kluyveromyces lactis (strain ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 /
OS NRRL Y-1140 / WM37) (Yeast) (Candida sphaerica).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Kluyveromyces.
OX NCBI_TaxID=284590;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 / NRRL Y-1140 / WM37;
RX PubMed=15229592; DOI=10.1038/nature02579;
RA Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S., Lafontaine I.,
RA de Montigny J., Marck C., Neuveglise C., Talla E., Goffard N., Frangeul L.,
RA Aigle M., Anthouard V., Babour A., Barbe V., Barnay S., Blanchin S.,
RA Beckerich J.-M., Beyne E., Bleykasten C., Boisrame A., Boyer J.,
RA Cattolico L., Confanioleri F., de Daruvar A., Despons L., Fabre E.,
RA Fairhead C., Ferry-Dumazet H., Groppi A., Hantraye F., Hennequin C.,
RA Jauniaux N., Joyet P., Kachouri R., Kerrest A., Koszul R., Lemaire M.,
RA Lesur I., Ma L., Muller H., Nicaud J.-M., Nikolski M., Oztas S.,
RA Ozier-Kalogeropoulos O., Pellenz S., Potier S., Richard G.-F.,
RA Straub M.-L., Suleau A., Swennen D., Tekaia F., Wesolowski-Louvel M.,
RA Westhof E., Wirth B., Zeniou-Meyer M., Zivanovic Y., Bolotin-Fukuhara M.,
RA Thierry A., Bouchier C., Caudron B., Scarpelli C., Gaillardin C.,
RA Weissenbach J., Wincker P., Souciet J.-L.;
RT "Genome evolution in yeasts.";
RL Nature 430:35-44(2004).
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; CR382123; CAH01133.1; -; Genomic_DNA.
DR RefSeq; XP_452282.1; XM_452282.1.
DR AlphaFoldDB; Q6CUV7; -.
DR SMR; Q6CUV7; -.
DR STRING; 28985.XP_452282.1; -.
DR EnsemblFungi; CAH01133; CAH01133; KLLA0_C01936g.
DR GeneID; 2892642; -.
DR KEGG; kla:KLLA0_C01936g; -.
DR eggNOG; ENOG502QRP5; Eukaryota.
DR HOGENOM; CLU_010191_1_0_1; -.
DR InParanoid; Q6CUV7; -.
DR OMA; AYITSER; -.
DR Proteomes; UP000000598; Chromosome C.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0043332; C:mating projection tip; IEA:EnsemblFungi.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0032220; P:plasma membrane fusion involved in cytogamy; IEA:EnsemblFungi.
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..643
FT /note="Plasma membrane fusion protein PRM1"
FT /id="PRO_0000337282"
FT TOPO_DOM 1..21
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT TRANSMEM 22..42
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 43..103
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 104..124
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 125..296
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT TRANSMEM 297..317
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 318..405
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 406..426
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 427..606
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT TRANSMEM 607..627
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 628..643
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT CARBOHYD 133
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 143
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 195
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 229
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 250
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 277
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 293
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 447
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 466
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 488
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 507
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 549
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 560
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 565
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 576
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 643 AA; 72208 MW; BD06CA1FC607BB4D CRC64;
MGHIYLKLNE RLSQIWCNKY TIIILVMMVK ILLFIKMLSN GFENIMDYTM ENCRNIDYYY
SKYVNSSPHY MGLMGNFLIQ KSMEQSVALS LKSISLLVSV SENVIDFMID LWLGTWVCLI
VSAIDGSVDV ATNATESVID LVNGTVSSVA DEIDDGLSGL TKVVNKVLSA VNDIQNFFKG
NDDESDINDQ VKKVNLTING LRTLSIPSSI DDKLVKLSAN TPDFDTVKNK TKQAIAVPFD
IIRNEIKSIN ASKLVGDPQY LEVPAIDTSG VKICSDNKSE INEVFDTIRK VFNASTMTIL
IVFILAALSL IVYNAWAEWR QWIRLKRFRD QYRHQTIMLK NPFDDMADEK VPQNVDILET
YHLVFNRYQS GFGRWLSRRI SSKLETQRNI QWLVTYLTSS TSLTLLALGL CGILMCCVQF
AIIAIISNKI NGKETEKMMT SMSTAMNDTV QQGMTDWSKS ANLYINDTET QINRQVFGWI
QNTTDTVNGT VTDLIEDIDN AISKAFNGTI LYKPMDTVMQ CVIGNKLEAI STALTWVHNT
AQVNLPRVNG SELYQQLQQN LTDSNSTTSS TAELPNSTSI ATQLKDNLIS AANKILSQYK
NTVVIELIVS SVFLALYFFQ IPVAGIILAA QKHKSKHNNQ NRP
