PRM1_COCIM
ID PRM1_COCIM Reviewed; 746 AA.
AC Q1E7G6; A0A0D6K9Q4; J3KJL2;
DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT 11-JUL-2006, sequence version 1.
DT 03-AUG-2022, entry version 62.
DE RecName: Full=Plasma membrane fusion protein PRM1;
GN Name=PRM1; ORFNames=CIMG_01497;
OS Coccidioides immitis (strain RS) (Valley fever fungus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Onygenales; Onygenaceae; Coccidioides.
OX NCBI_TaxID=246410;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RS;
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).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=RS;
RX PubMed=20516208; DOI=10.1101/gr.103911.109;
RA Neafsey D.E., Barker B.M., Sharpton T.J., Stajich J.E., Park D.J.,
RA Whiston E., Hung C.-Y., McMahan C., White J., Sykes S., Heiman D.,
RA Young S., Zeng Q., Abouelleil A., Aftuck L., Bessette D., Brown A.,
RA FitzGerald M., Lui A., Macdonald J.P., Priest M., Orbach M.J.,
RA Galgiani J.N., Kirkland T.N., Cole G.T., Birren B.W., Henn M.R.,
RA Taylor J.W., Rounsley S.D.;
RT "Population genomic sequencing of Coccidioides fungi reveals recent
RT hybridization and transposon control.";
RL Genome Res. 20:938-946(2010).
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; GG704911; EAS36143.1; -; Genomic_DNA.
DR RefSeq; XP_001247726.1; XM_001247725.1.
DR AlphaFoldDB; Q1E7G6; -.
DR SMR; Q1E7G6; -.
DR STRING; 246410.Q1E7G6; -.
DR EnsemblFungi; EAS36143; EAS36143; CIMG_01497.
DR GeneID; 4567659; -.
DR KEGG; cim:CIMG_01497; -.
DR VEuPathDB; FungiDB:CIMG_01497; -.
DR InParanoid; Q1E7G6; -.
DR OMA; QTYLCLF; -.
DR OrthoDB; 1333210at2759; -.
DR Proteomes; UP000001261; 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..746
FT /note="Plasma membrane fusion protein PRM1"
FT /id="PRO_0000337277"
FT TOPO_DOM 1..50
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT TRANSMEM 51..71
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 72..138
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 139..159
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 160..323
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT TRANSMEM 324..344
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 345..398
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 399..421
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 422..606
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT TRANSMEM 607..627
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 628..746
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT REGION 1..32
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 682..708
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 15..32
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 178
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 248
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 277
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 457
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 486
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 493
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 508
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 555
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 570
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 746 AA; 81308 MW; 073168FCA584F593 CRC64;
MQFSRFIPRS SPGLPPYGAH DPPMMQNPAP TTAPPGAITP YLGFKARLSQ IWINKWTILL
LLVLARVLIA VTGLNDNMAS AKREALSACT SVESMGSAMA SMPHYMSKGV NELTASGVER
AVNGLMSMLL LTVTGVEEVV VFFVNVLTQT YLCLITLAVS GSLHVALKVV EDAADFLNKT
LADVTEGIEK GVDGFEDKIN DFLKGINSIT SAFGGEKDPP KLDIGGDLDK LKEIRLPSSL
DEGLKKINDS IPTFDEVNKF ANDAIRYPFK EVKKLINQSL EEYKFDRSVF PVPQKEKLSF
CGDNDGINSF FGKIGSIIST AKKIFIAVLI AGAVAACVPM ALLEIRRWRH MKERASLVQK
NDHDPMDVVY IVSRPYTSTA GLKIASWFKP GRRQVLVRWI VAYATTTPAL FLLALGIAGL
FSCACQAILL HAVKKEVPGL TNEVSQFADK VVMSLNNASE QWAISTNRVI ADTNDDINQK
VFGWVNTSTT SINDTLNVFV DKTSDVLNDT FGGTILHGPI KDVLYCLIGL KIQGIQKALT
WVYDHAHVDF PNMPNDTFSL GAVESIANDN KSDPESFLAS PGDKTADAIT HVVVRVTEAI
ENAIRTEALI STFLIALWFA ILLIAVLRAL TLAFRRDKPR GEGGIDATYH PPAPRAAHAV
GSMEMSDFYN VPLTGVPNAN GDGGLAPKYS TTPHVRGGSR GSDTDEEEYQ AQKLGYAGQR
DYEAALNREM CRESSCGQVM YGSEKR
