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PRM1_YARLI
ID   PRM1_YARLI              Reviewed;         690 AA.
AC   Q6C6L1;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   16-AUG-2004, sequence version 1.
DT   25-MAY-2022, entry version 74.
DE   RecName: Full=Plasma membrane fusion protein PRM1;
GN   Name=PRM1; OrderedLocusNames=YALI0E08580g;
OS   Yarrowia lipolytica (strain CLIB 122 / E 150) (Yeast) (Candida lipolytica).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Dipodascaceae; Yarrowia.
OX   NCBI_TaxID=284591;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CLIB 122 / E 150;
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; CR382131; CAG79290.1; -; Genomic_DNA.
DR   RefSeq; XP_503701.1; XM_503701.1.
DR   AlphaFoldDB; Q6C6L1; -.
DR   STRING; 4952.CAG79290; -.
DR   EnsemblFungi; CAG79290; CAG79290; YALI0_E08580g.
DR   GeneID; 2912494; -.
DR   KEGG; yli:YALI0E08580g; -.
DR   VEuPathDB; FungiDB:YALI0_E08580g; -.
DR   HOGENOM; CLU_010191_1_0_1; -.
DR   InParanoid; Q6C6L1; -.
DR   OMA; QTYLCLF; -.
DR   Proteomes; UP000001300; Chromosome E.
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   3: Inferred from homology;
KW   Cell membrane; Conjugation; Glycoprotein; Membrane; Reference proteome;
KW   Transmembrane; Transmembrane helix.
FT   CHAIN           1..690
FT                   /note="Plasma membrane fusion protein PRM1"
FT                   /id="PRO_0000337293"
FT   TOPO_DOM        1..39
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000250"
FT   TRANSMEM        40..60
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        61..111
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000250"
FT   TRANSMEM        112..132
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        133..308
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000250"
FT   TRANSMEM        309..329
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        330..403
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000250"
FT   TRANSMEM        404..424
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        425..586
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000250"
FT   TRANSMEM        587..607
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        608..690
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        162
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        265
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        273
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        456
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        485
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   690 AA;  77376 MW;  5938DB34B6EC122B CRC64;
     MAMSLASQIK LWWNTQNSPT EHSSIPLLKA RLSQTWLNKW TIGLLLVSIK LWMFKMSLSG
     QLDGAESNSE RSCSALERSV SKMMSIPHYT ATGMNHVIAT AIQKFVSGLI KMVLLIITGV
     QELLIFAVNM LISTYTCLIT LVVQGAVSLA VDTSKHVISF VNDTISTVVP EIEKGLNGLA
     DGLNTATNAF VDLGNLITGK QAEEYTGQID FVKLQLDGLK NVSIPASVNE KLDSVKDKVP
     DFETVKNEIE SLIRKPFQTI SKSMNETLAT PLNVSDSLKV PALKSAQFCK DANIPEVYAK
     LNSGLNTGLK VIISLLLILA LIMIVPVAWS EWRLWRYHEE LWVEQSTVDV KQEKRHAFHT
     VLFQAQHKYV TMVKQKLAWG KKLYQRNLSQ WYWAYILYPY MLTLLLVGLF GILAFLLQLG
     LLSILKSGLQ SLTVPTSEVG ADVTETVVRE IETWKNDTNL FLNSQETHIN KNLLGWVVDS
     TSTVNTTLST FIDTMNNGID SVFKDTPLHG AVQGVTKCLV TLKLQKVADG MGWVSDNAHV
     TLPRIDKELM SHQDIEQEAS EKADYVSDGI ARIIKTVEKL LFTELYIALA CLGIWLFMCL
     IALVYVLIKS RDRTTNFEPS RELKFDMVDT SRDINVPRVL PPQITIPKPA LFMRNHIPSP
     ATDPFEEYPI RRNKSSSWLF NLKSPVLRKS
 
 
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