ID   PRM1_CHAGB              Reviewed;         722 AA.
AC   Q2GMW8;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   21-MAR-2006, sequence version 1.
DT   03-AUG-2022, entry version 53.
DE   RecName: Full=Plasma membrane fusion protein PRM1;
GN   Name=PRM1; ORFNames=CHGG_10686;
OS   Chaetomium globosum (strain ATCC 6205 / CBS 148.51 / DSM 1962 / NBRC 6347 /
OS   NRRL 1970) (Soil fungus).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Sordariomycetidae; Sordariales; Chaetomiaceae; Chaetomium.
OX   NCBI_TaxID=306901;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 6205 / CBS 148.51 / DSM 1962 / NBRC 6347 / NRRL 1970;
RX   PubMed=25720678; DOI=10.1128/genomea.00021-15;
RA   Cuomo C.A., Untereiner W.A., Ma L.-J., Grabherr M., Birren B.W.;
RT   "Draft genome sequence of the cellulolytic fungus Chaetomium globosum.";
RL   Genome Announc. 3:E0002115-E0002115(2015).
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; CH408035; EAQ84282.1; -; Genomic_DNA.
DR   RefSeq; XP_001228613.1; XM_001228612.1.
DR   AlphaFoldDB; Q2GMW8; -.
DR   SMR; Q2GMW8; -.
DR   STRING; 38033.XP_001228613.1; -.
DR   EnsemblFungi; EAQ84282; EAQ84282; CHGG_10686.
DR   GeneID; 4396372; -.
DR   eggNOG; ENOG502QRP5; Eukaryota.
DR   HOGENOM; CLU_010191_1_0_1; -.
DR   InParanoid; Q2GMW8; -.
DR   OMA; QTYLCLF; -.
DR   OrthoDB; 1333210at2759; -.
DR   Proteomes; UP000001056; Unassembled WGS sequence.
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..722
FT                   /note="Plasma membrane fusion protein PRM1"
FT                   /id="PRO_0000337276"
FT   TOPO_DOM        1..60
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000250"
FT   TRANSMEM        61..81
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        82..143
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000250"
FT   TRANSMEM        144..164
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        165..326
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000250"
FT   TRANSMEM        327..347
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        348..413
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000250"
FT   TRANSMEM        414..434
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        435..604
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000250"
FT   TRANSMEM        605..625
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        626..722
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000250"
FT   REGION          636..722
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        668..683
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        701..722
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CARBOHYD        252
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        263
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        281
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        307
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        491
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        497
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        567
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   722 AA;  78655 MW;  F36B161B62D7A3BB CRC64;
     MFYNEKTGAV PPVPSNLNAN TWHTVDLQPA PQLQPHAHTA PTVTPYLGLR ARLSQLWFNR
     WTILLILVLV RVLILTAGLN DNIGDAKTKA LSACTKVEDI GSAMASMPHY LSVGVNSMAA
     DGITKTVSGM VKMLMMILTG VENLILFIIN MYVGTYACLI AALIHGGLDV SVKVVEGATK
     VMNDAIGTIT GQITESISDV QDAINKIPDT ISSFLGGVDF DLPKIDITKN LDDLENIKIN
     SNELVRDIVA LNKTIPTFDQ VENFTKNAIA IPFNFLKEQV NSSFGSYKFD DSVFPVAEKQ
     ALSFCSNNSF LNDFFETLFN VVRTAKIAFC VAIPILAVLA IVGMGYLEIQ RWRREKQRSR
     EFTERGYDPM DVVYLSSRPV TGGFGLWLSA KFKSVKKQLL VRWTIAYGTS LPALFVLSLA
     FAGLFSCLCQ FIILRSIQKE APALANQVGD FAGDVVGTLQ QVSTNWADDA NGVIIKLQDD
     INDDMFGWVS NATTAVNDTL NTFDDEIDKA ITAVFKDTIL FNTARNLVGC LITRKIETVQ
     EGLTWVHDNA HVTLPLFAND VFSQGANNSV NGDSDLTSFL ASPSSVTTDE ITSAVNQVIT
     KLEHGIVQEA LISTALLLVY VIVVLSGAVR ALVASAQKEK TRGEGGEQYG VKAPGSRGSS
     SASSGNSDNH HYHHHHDNSA PSDFDRKGVI YAGSVKRGRP GPERWPSHAR KSSYPEVEGP
     DH