PRM1_DEBHA
ID PRM1_DEBHA Reviewed; 645 AA.
AC Q6BPF8;
DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT 16-DEC-2008, sequence version 2.
DT 03-AUG-2022, entry version 73.
DE RecName: Full=Plasma membrane fusion protein PRM1;
GN Name=PRM1; OrderedLocusNames=DEHA2E13948g;
OS Debaryomyces hansenii (strain ATCC 36239 / CBS 767 / BCRC 21394 / JCM 1990
OS / NBRC 0083 / IGC 2968) (Yeast) (Torulaspora hansenii).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Debaryomyces.
OX NCBI_TaxID=284592;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 36239 / CBS 767 / BCRC 21394 / JCM 1990 / NBRC 0083 / IGC 2968;
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; CR382137; CAG88154.2; -; Genomic_DNA.
DR RefSeq; XP_459912.2; XM_459912.1.
DR AlphaFoldDB; Q6BPF8; -.
DR STRING; 4959.XP_459912.2; -.
DR EnsemblFungi; CAG88154; CAG88154; DEHA2E13948g.
DR GeneID; 2901980; -.
DR KEGG; dha:DEHA2E13948g; -.
DR VEuPathDB; FungiDB:DEHA2E13948g; -.
DR eggNOG; ENOG502QRP5; Eukaryota.
DR HOGENOM; CLU_010191_1_0_1; -.
DR InParanoid; Q6BPF8; -.
DR OMA; QTYLCLF; -.
DR OrthoDB; 1333210at2759; -.
DR Proteomes; UP000000599; Chromosome E.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0043332; C:mating projection tip; IEA:InterPro.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
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..645
FT /note="Plasma membrane fusion protein PRM1"
FT /id="PRO_0000337280"
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..102
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 103..123
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 124..289
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT TRANSMEM 290..310
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 311..378
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 379..399
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 400..568
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT TRANSMEM 569..589
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 590..645
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT REGION 624..645
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 142
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 192
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 226
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 426
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 462
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 473
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 514
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 525
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 533
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 547
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 645 AA; 73033 MW; 7EEE306265B151B1 CRC64;
MKKQFLNYYE ILSQVWFNKY TIILVLMTIK IYLFTNSILS NLTNFKAYTE SICTSLDTYS
TVIASLPEQL SKVINHMVAS TLNSMKMQSL KMLMTIITII KSLIVFYIDI FLGTYICILT
AAIGGTVDFA LDSTQSVLKS VNETIISVSE DIQDGLNGLS KVINTLLSGV DKVKSFFTNQ
DTDSTEYVDK VNLSIKALQN IKIPNSVLTD IDNFKDKVPD FNELQNTSKL VSKPFEIITQ
ELNESAHFKN ITVDQLKLAS TPPVNFCSNS LDIDKFYSNL AKKVQFTSNI IIIVLLIMAM
FAIASLVVVE YFKWRKSQRM INEILADKNQ ESYFVSTRNI MNKYNSSLIY YIEKFVTIPP
SRKDNLYWLL SYITTPYSLT VLIIGLAGLF TVMLQFIILQ IILKSFKSLT TELTGFKTQI
ITLMDNATSS YIKETNSYIG SQQKSINDEL FGNIRTASTS VNSTINDFLM KMNTTINSVF
ANTPFSKPVN TLVYCTIGRK LIKIEQGLTW IVENLSVSLP QLPKNLTEDF MTNYSKDNHG
IHKLTDNVTS GITFLLDTYK KSLLIELYIS SAILGIWILQ IIIGLTLIWY RSSSNCKARK
PEKIQGEPTI GNPKPLTTEQ RKEYGYPHID PFNEKVDASS SIYSL
