ID   GPRM_ASPFC              Reviewed;         497 AA.
AC   B0YCP1;
DT   23-FEB-2022, integrated into UniProtKB/Swiss-Prot.
DT   08-APR-2008, sequence version 1.
DT   03-AUG-2022, entry version 39.
DE   RecName: Full=G protein-coupled receptor gprM {ECO:0000303|PubMed:30914505};
GN   Name=gprM {ECO:0000303|PubMed:30914505}; ORFNames=AFUB_090880;
OS   Neosartorya fumigata (strain CEA10 / CBS 144.89 / FGSC A1163) (Aspergillus
OS   fumigatus).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Fumigati.
OX   NCBI_TaxID=451804;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CEA10 / CBS 144.89 / FGSC A1163;
RX   PubMed=18404212; DOI=10.1371/journal.pgen.1000046;
RA   Fedorova N.D., Khaldi N., Joardar V.S., Maiti R., Amedeo P., Anderson M.J.,
RA   Crabtree J., Silva J.C., Badger J.H., Albarraq A., Angiuoli S., Bussey H.,
RA   Bowyer P., Cotty P.J., Dyer P.S., Egan A., Galens K., Fraser-Liggett C.M.,
RA   Haas B.J., Inman J.M., Kent R., Lemieux S., Malavazi I., Orvis J.,
RA   Roemer T., Ronning C.M., Sundaram J.P., Sutton G., Turner G., Venter J.C.,
RA   White O.R., Whitty B.R., Youngman P., Wolfe K.H., Goldman G.H.,
RA   Wortman J.R., Jiang B., Denning D.W., Nierman W.C.;
RT   "Genomic islands in the pathogenic filamentous fungus Aspergillus
RT   fumigatus.";
RL   PLoS Genet. 4:E1000046-E1000046(2008).
RN   [2]
RP   FUNCTION, DISRUPTION PHENOTYPE, AND INTERACTION WITH GPAA.
RX   PubMed=30914505; DOI=10.1128/mbio.00215-19;
RA   Manfiolli A.O., Siqueira F.S., Dos Reis T.F., Van Dijck P., Schrevens S.,
RA   Hoefgen S., Foege M., Strassburger M., de Assis L.J., Heinekamp T.,
RA   Rocha M.C., Janevska S., Brakhage A.A., Malavazi I., Goldman G.H.,
RA   Valiante V.;
RT   "Mitogen-activated protein kinase cross-talk interaction modulates the
RT   production of melanins in Aspergillus fumigatus.";
RL   MBio 10:0-0(2019).
CC   -!- FUNCTION: G protein-coupled receptor that plays a role in conidiation
CC       and regulation of the biosynthesis of secondary metabolites such as
CC       dihydroxynaphthalene (DHN)-melanin, via interaction with the G-protein
CC       complex alpha subunit gpaA. {ECO:0000269|PubMed:30914505}.
CC   -!- SUBUNIT: Interacts with gpaA. {ECO:0000269|PubMed:30914505}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass membrane
CC       protein {ECO:0000255}.
CC   -!- DISRUPTION PHENOTYPE: Leads to a strong increase of
CC       dihydroxynaphthalene (DHN)-melanin production.
CC       {ECO:0000269|PubMed:30914505}.
CC   -!- SIMILARITY: Belongs to the G-protein coupled receptor GPR1/git3 family.
CC       {ECO:0000305}.
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DR   EMBL; DS499601; EDP48372.1; -; Genomic_DNA.
DR   EnsemblFungi; EDP48372; EDP48372; AFUB_090880.
DR   VEuPathDB; FungiDB:AFUB_090880; -.
DR   HOGENOM; CLU_026939_1_0_1; -.
DR   PhylomeDB; B0YCP1; -.
DR   Proteomes; UP000001699; Unassembled WGS sequence.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
PE   1: Evidence at protein level;
KW   Cell membrane; Glycoprotein; Membrane; Transmembrane; Transmembrane helix.
FT   CHAIN           1..497
FT                   /note="G protein-coupled receptor gprM"
FT                   /id="PRO_0000454889"
FT   TRANSMEM        66..86
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        98..118
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        138..158
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        179..199
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        221..241
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        293..313
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        357..377
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   REGION          428..497
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CARBOHYD        3
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        259
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        421
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ   SEQUENCE   497 AA;  54927 MW;  BDDBA08403177FF2 CRC64;
     MTNRTSLNGR CPVPFLQEDL FPPTGGFIGG RYCQPVGDIS CCLPCPIVSW TYGDGLFGKA
     SSASWISVAI LPLCIFLLVS YAVLPVKFTH RHYLSVCFTL GICFMEASKI AFIIPLGVKP
     DQCYNQITPN DMHSSLSCAF TGSLLLLGGW MVVVWSFLRT VAFHLQVCWE VILGPKFMWG
     ALIFGWVVPA VGLTVMLILT GVSFRFGTVC HINIDGALQD YWIPIISFAV AALILQLATM
     AYCIHVYVKS LFDTDSTTNS SGLPSYSASV RTVSARQAYR RIRRVLQLQW RGVTLVLIII
     ANVIFFSVTF IELDSSLKPT AENMEKALPW VACLAATNGD REKCDPEAAK FRPSEGLLLA
     VLVLLSLVGF WNFILFARPS IFHGWVDFFQ NKFGTGDGRL EFVSADARTR LGDTRSYEML
     NSTGLPSYKS PSPMVRSPSP ARMGGTKSPE NGHFGRDARY VRPSMSFSSP RPPSAPQGRG
     WDPKTTFAPA VYREYDD