PRM1_ASHGO
ID PRM1_ASHGO Reviewed; 643 AA.
AC Q751Z0;
DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 83.
DE RecName: Full=Plasma membrane fusion protein PRM1;
GN Name=PRM1; OrderedLocusNames=AFR685C;
OS Ashbya gossypii (strain ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056)
OS (Yeast) (Eremothecium gossypii).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Eremothecium.
OX NCBI_TaxID=284811;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056;
RX PubMed=15001715; DOI=10.1126/science.1095781;
RA Dietrich F.S., Voegeli S., Brachat S., Lerch A., Gates K., Steiner S.,
RA Mohr C., Poehlmann R., Luedi P., Choi S., Wing R.A., Flavier A.,
RA Gaffney T.D., Philippsen P.;
RT "The Ashbya gossypii genome as a tool for mapping the ancient Saccharomyces
RT cerevisiae genome.";
RL Science 304:304-307(2004).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056;
RX PubMed=23749448; DOI=10.1534/g3.112.002881;
RA Dietrich F.S., Voegeli S., Kuo S., Philippsen P.;
RT "Genomes of Ashbya fungi isolated from insects reveal four mating-type
RT loci, numerous translocations, lack of transposons, and distinct gene
RT duplications.";
RL G3 (Bethesda) 3:1225-1239(2013).
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}.
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; AE016819; AAS54057.1; -; Genomic_DNA.
DR RefSeq; NP_986233.1; NM_212369.1.
DR AlphaFoldDB; Q751Z0; -.
DR SMR; Q751Z0; -.
DR STRING; 33169.AAS54057; -.
DR EnsemblFungi; AAS54057; AAS54057; AGOS_AFR685C.
DR GeneID; 4622522; -.
DR KEGG; ago:AGOS_AFR685C; -.
DR eggNOG; ENOG502QRP5; Eukaryota.
DR HOGENOM; CLU_010191_1_0_1; -.
DR InParanoid; Q751Z0; -.
DR OMA; QTYLCLF; -.
DR Proteomes; UP000000591; Chromosome VI.
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..643
FT /note="Plasma membrane fusion protein PRM1"
FT /id="PRO_0000337266"
FT TOPO_DOM 1..16
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT TRANSMEM 17..37
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 38..104
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 105..125
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 126..296
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT TRANSMEM 297..317
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 318..410
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 411..431
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 432..608
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT TRANSMEM 609..629
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 630..643
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT CARBOHYD 135
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 145
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 198
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 232
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 253
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 474
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 496
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 643 AA; 70916 MW; C602F3DB4B0CA348 CRC64;
MYATQPYLEL RERLSQIWIN RYTLLLMLCM VKILLFTSSL RFSLNNSKVH VLEECSNIEH
YYNILRNGTP HYMGKMGNYL VAHALEATVE SLLALLTSLA TVVEVVAHFM IELWLGTYAC
LLFSAAHGAV EVATNVTEKV IGVANKTLIA AANELDNGLD GLSKVLNKII ETGTKVSHLF
KDDDEEHASP EGQFKKINLT IASLRTVKIP ESVNDKLRSL AEKTPDFEDV KNKTKGLVSI
PFQTLKNEIN GINATSMLKN RKLMSVPPID MGDAADGVCS ANRDGIESVY RNLNSALIYS
LVATAVSLAI VALLCLIPAA WHEYRQWERL SALRDHERTV DCKDPFADTH SSASASTASS
TRCDVIQNYQ GVFHRAPTLI GEWVARHTAH TQEGALRIQW LLAYVLSPRA LVPLALGLAG
VLVCGCQFLI IHALRIQLAS TSTRDSLQRL ETDTAGLVAH DLSRWADSTN AYINGTEASV
NAGLLGWVTT ATTALNTTVA ALLADIDSTV DRAFADTPLH RPMVTVVSCV IGNKLRAIEA
GLTWTHDHVR IALPRIHTAR LRDAVAEPDL PTHPAYTAVL QSLSDRLRHS VDRVLHQCCA
AVRIELYVSL ALLGLWILQT PLGLAMLLFK SHCRRRNLRR RVP
