ID   PRM1_AJECN              Reviewed;         736 AA.
AC   A6QWA0;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   21-AUG-2007, sequence version 1.
DT   03-AUG-2022, entry version 48.
DE   RecName: Full=Plasma membrane fusion protein PRM1;
GN   Name=PRM1; ORFNames=HCAG_01657;
OS   Ajellomyces capsulatus (strain NAm1 / WU24) (Darling's disease fungus)
OS   (Histoplasma capsulatum).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Onygenales; Ajellomycetaceae; Histoplasma;
OC   unclassified Histoplasma.
OX   NCBI_TaxID=2059318;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NAm1 / WU24;
RX   PubMed=19717792; DOI=10.1101/gr.087551.108;
RA   Sharpton T.J., Stajich J.E., Rounsley S.D., Gardner M.J., Wortman J.R.,
RA   Jordar V.S., Maiti R., Kodira C.D., Neafsey D.E., Zeng Q., Hung C.-Y.,
RA   McMahan C., Muszewska A., Grynberg M., Mandel M.A., Kellner E.M.,
RA   Barker B.M., Galgiani J.N., Orbach M.J., Kirkland T.N., Cole G.T.,
RA   Henn M.R., Birren B.W., Taylor J.W.;
RT   "Comparative genomic analyses of the human fungal pathogens Coccidioides
RT   and their relatives.";
RL   Genome Res. 19:1722-1731(2009).
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; CH476655; EDN03792.1; -; Genomic_DNA.
DR   RefSeq; XP_001544610.1; XM_001544560.1.
DR   AlphaFoldDB; A6QWA0; -.
DR   STRING; 339724.A6QWA0; -.
DR   EnsemblFungi; EDN03792; EDN03792; HCAG_01657.
DR   GeneID; 5451487; -.
DR   KEGG; aje:HCAG_01657; -.
DR   VEuPathDB; FungiDB:HCAG_01657; -.
DR   HOGENOM; CLU_010191_1_0_1; -.
DR   OMA; QTYLCLF; -.
DR   OrthoDB; 1333210at2759; -.
DR   Proteomes; UP000009297; 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..736
FT                   /note="Plasma membrane fusion protein PRM1"
FT                   /id="PRO_0000337265"
FT   TOPO_DOM        1..56
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000250"
FT   TRANSMEM        57..77
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        78..139
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000250"
FT   TRANSMEM        140..160
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        161..315
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000250"
FT   TRANSMEM        316..336
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        337..395
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000250"
FT   TRANSMEM        396..416
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        417..601
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000250"
FT   TRANSMEM        602..622
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        623..736
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000250"
FT   REGION          1..33
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          717..736
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CARBOHYD        228
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        254
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        452
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        481
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        503
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        550
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        565
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   736 AA;  81106 MW;  E4ABFA89A552305F CRC64;
     MKFSRFIPRS RTPGLPAYGE QEPNTFENGY RPSPPPGAIT PYLGLRSRLS QIWFNRWTIL
     LLLILARVLV AIGSLDGNLV SAKREALSAC SSVESVGSTM ASMPHYMAQG VNELTATGVE
     KAINGLMSML ELTVTGVEEI FVFFVNVMTQ TYLCLITLVV SGMMNAAIDV LKKATEFLDD
     ITGKLGNAIG DGISDFEDAI NGFGDVINMF GTKLPKLNLD GPIKELENLS LPDGLTDDLN
     KLKEKIPNFE DVNNFTNNAL RMPFELVKKL IRDEIDDYKF DRSVFPVPAK EQLQFCNEEG
     GIHSFFNKLA SLTSTAKKIF IGVLVVSAIL VCIPMAYREM RAWRGMKERS SLVRREAHDP
     MDVVYIVSRP FASAAGLKAA TWFSGHRRQV LARWVVAYVT SPPALFLLSL GVAGLFSCAC
     QAMLLTAVKK EVPSLTEQVG QFADKVFFAL NNASEQWAVG TNRVIDDTND DINQKVFGWV
     NQTTGSVNNT LNVFVDETSN VLNRTFGGTI LYEPIKDVLH CLIGLKIEGV QKALTWVSVH
     AKVDFPNLAN DTFSLRTLEK LSKDNDSNAD SFLMNPGDKT TDKISEVVQR VTDSVESGIR
     TEAIISAVII SIWFAVLLMA IVRALTLWYG ADKNRGDGSG DSEFPHPETL SRDAAGFSDI
     PLATPTHVSP GMADTSVPVY TTRPPAQAFN GGYNAEDYYQ EQKLGFAGQR ELRRDVEGHA
     RKSSYGEVEY TNDVKR