GRLH_DICDI
ID GRLH_DICDI Reviewed; 764 AA.
AC Q54SH8;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 24-MAY-2005, sequence version 1.
DT 03-AUG-2022, entry version 90.
DE RecName: Full=Metabotropic glutamate receptor-like protein H;
DE Flags: Precursor;
GN Name=grlH; ORFNames=DDB_G0282459;
OS Dictyostelium discoideum (Slime mold).
OC Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales;
OC Dictyosteliaceae; Dictyostelium.
OX NCBI_TaxID=44689;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AX4;
RX PubMed=15875012; DOI=10.1038/nature03481;
RA Eichinger L., Pachebat J.A., Gloeckner G., Rajandream M.A., Sucgang R.,
RA Berriman M., Song J., Olsen R., Szafranski K., Xu Q., Tunggal B.,
RA Kummerfeld S., Madera M., Konfortov B.A., Rivero F., Bankier A.T.,
RA Lehmann R., Hamlin N., Davies R., Gaudet P., Fey P., Pilcher K., Chen G.,
RA Saunders D., Sodergren E.J., Davis P., Kerhornou A., Nie X., Hall N.,
RA Anjard C., Hemphill L., Bason N., Farbrother P., Desany B., Just E.,
RA Morio T., Rost R., Churcher C.M., Cooper J., Haydock S., van Driessche N.,
RA Cronin A., Goodhead I., Muzny D.M., Mourier T., Pain A., Lu M., Harper D.,
RA Lindsay R., Hauser H., James K.D., Quiles M., Madan Babu M., Saito T.,
RA Buchrieser C., Wardroper A., Felder M., Thangavelu M., Johnson D.,
RA Knights A., Loulseged H., Mungall K.L., Oliver K., Price C., Quail M.A.,
RA Urushihara H., Hernandez J., Rabbinowitsch E., Steffen D., Sanders M.,
RA Ma J., Kohara Y., Sharp S., Simmonds M.N., Spiegler S., Tivey A.,
RA Sugano S., White B., Walker D., Woodward J.R., Winckler T., Tanaka Y.,
RA Shaulsky G., Schleicher M., Weinstock G.M., Rosenthal A., Cox E.C.,
RA Chisholm R.L., Gibbs R.A., Loomis W.F., Platzer M., Kay R.R.,
RA Williams J.G., Dear P.H., Noegel A.A., Barrell B.G., Kuspa A.;
RT "The genome of the social amoeba Dictyostelium discoideum.";
RL Nature 435:43-57(2005).
RN [2]
RP NOMENCLATURE.
RX PubMed=16735079; DOI=10.1016/j.ejcb.2006.04.003;
RA Prabhu Y., Eichinger L.;
RT "The Dictyostelium repertoire of seven transmembrane domain receptors.";
RL Eur. J. Cell Biol. 85:937-946(2006).
RN [3]
RP DEVELOPMENTAL STAGE.
RX PubMed=17501984; DOI=10.1186/1471-213x-7-44;
RA Prabhu Y., Mueller R., Anjard C., Noegel A.A.;
RT "GrlJ, a Dictyostelium GABAB-like receptor with roles in post-aggregation
RT development.";
RL BMC Dev. Biol. 7:44-44(2007).
RN [4]
RP INDUCTION [LARGE SCALE ANALYSIS].
RX PubMed=18559084; DOI=10.1186/1471-2164-9-291;
RA Sillo A., Bloomfield G., Balest A., Balbo A., Pergolizzi B., Peracino B.,
RA Skelton J., Ivens A., Bozzaro S.;
RT "Genome-wide transcriptional changes induced by phagocytosis or growth on
RT bacteria in Dictyostelium.";
RL BMC Genomics 9:291-291(2008).
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane
CC protein {ECO:0000305}.
CC -!- DEVELOPMENTAL STAGE: Increased levels found from the tight aggregation
CC stage onward. Levels stayed high during late development. Clear
CC expression at 24 hours when fruiting body formation is close to
CC completion. {ECO:0000269|PubMed:17501984}.
CC -!- INDUCTION: Down-regulated by phagocytic stimuli.
CC {ECO:0000269|PubMed:18559084}.
CC -!- SIMILARITY: In the N-terminal section; belongs to the BMP lipoprotein
CC family. {ECO:0000305}.
CC -!- SIMILARITY: In the C-terminal section; belongs to the G-protein coupled
CC receptor 3 family. GABA-B receptor subfamily. {ECO:0000305}.
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DR EMBL; AAFI02000047; EAL66089.1; -; Genomic_DNA.
DR RefSeq; XP_640061.1; XM_634969.1.
DR AlphaFoldDB; Q54SH8; -.
DR SMR; Q54SH8; -.
DR STRING; 44689.DDB0231982; -.
DR PaxDb; Q54SH8; -.
DR EnsemblProtists; EAL66089; EAL66089; DDB_G0282459.
DR GeneID; 8623589; -.
DR KEGG; ddi:DDB_G0282459; -.
DR dictyBase; DDB_G0282459; grlH.
DR eggNOG; KOG1055; Eukaryota.
DR HOGENOM; CLU_365408_0_0_1; -.
DR InParanoid; Q54SH8; -.
DR OMA; WRSEDAN; -.
DR PhylomeDB; Q54SH8; -.
DR PRO; PR:Q54SH8; -.
DR Proteomes; UP000002195; Chromosome 3.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IEA:InterPro.
DR GO; GO:0004930; F:G protein-coupled receptor activity; IEA:UniProtKB-KW.
DR GO; GO:0090630; P:activation of GTPase activity; IMP:dictyBase.
DR GO; GO:1903669; P:positive regulation of chemorepellent activity; IMP:dictyBase.
DR InterPro; IPR017978; GPCR_3_C.
DR InterPro; IPR003760; PnrA-like.
DR Pfam; PF00003; 7tm_3; 1.
DR Pfam; PF02608; Bmp; 1.
DR PROSITE; PS50259; G_PROTEIN_RECEP_F3_4; 1.
PE 2: Evidence at transcript level;
KW G-protein coupled receptor; Glycoprotein; Membrane; Receptor;
KW Reference proteome; Signal; Transducer; Transmembrane; Transmembrane helix.
FT SIGNAL 1..20
FT /evidence="ECO:0000255"
FT CHAIN 21..764
FT /note="Metabotropic glutamate receptor-like protein H"
FT /id="PRO_0000370352"
FT TOPO_DOM 21..393
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 394..414
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 415..427
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 428..448
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 449..464
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 465..485
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 486..500
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 501..521
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 522..552
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 553..573
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 574..587
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 588..608
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 609..617
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 618..638
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
FT TOPO_DOM 639..764
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 664..764
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 664..699
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 703..719
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 745..764
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 72
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 260
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 278
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 344
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 379
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 547
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 764 AA; 84896 MW; 708A26FEC2B9657C CRC64;
MKNILKILIL ILICINKINC LDGDGKQFRM IMLLSANVND MGFNNMMNQG RIGVSKNLQI
EDSRLIVVDG ENDTKALVEP ILQNEDIDFV ICSSQGHTVA CKYFADKYLK HPTVKTQFLI
RGSGSSTANL IQFNYNFASC NYMSGYFAGL HTKTNKIGFL SPGAPKVNDA WVYAFWLGAK
QVNPKIQFFY YNVGAFLNPD ASERATNDLL ERGCDVIGNT LDDFSSGITI MSKGYRTIGT
NGFPQKLIYG EKILYSYAYN WTKLFLPIAM SVKAGITNNT NGYGDFNLDE SKNFFNIEYS
YGVSTDTINR MNQQITFLKS NSRFTHPYYC NEYLPEYTKK NNLNLSTSPT VNNLICIDHS
TFLKINPPFP GMTYLGIYNI SLVEVEFSQS IQNGFSITTG ILIGITILMM IGIIKYSKTP
SMRSASPIFL NFILAGGIIV YIGIIVWVGP MSTHSCNARL WLVTLGFSTL IGSLVVKNFR
IWLIFDNPEL KSIKITNYQL FPWVGACLVI NIILMAILTS VGDLKQIDAM NIDSLGKYEY
MKVCKMNSSG ASTLYTILAY FAALLLVGVF VSWKIRIVDI LEFNESGAIA NTLYAISFCL
FVIVPLMISP QDMQSETIIL CTTGLFITTA ALLIIFIPKF WRVFRKGAND SEINFNKKKS
SSVATARAES GSKGSNGNAS SGNRTNRRGN VVSGDFTDDS ESSVGDENQK EKEKIKDDVA
NVTSGAVLAE FTDEASDTDN NEFNDIELSE QPPSIIVNDS ENNN
