GRLJ_DICDI
ID GRLJ_DICDI Reviewed; 783 AA.
AC Q75JT4; Q559S6;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 25-MAY-2022, entry version 93.
DE RecName: Full=Metabotropic glutamate receptor-like protein J;
DE Flags: Precursor;
GN Name=grlJ; ORFNames=DDB_G0272150;
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=12097910; DOI=10.1038/nature00847;
RA Gloeckner G., Eichinger L., Szafranski K., Pachebat J.A., Bankier A.T.,
RA Dear P.H., Lehmann R., Baumgart C., Parra G., Abril J.F., Guigo R.,
RA Kumpf K., Tunggal B., Cox E.C., Quail M.A., Platzer M., Rosenthal A.,
RA Noegel A.A.;
RT "Sequence and analysis of chromosome 2 of Dictyostelium discoideum.";
RL Nature 418:79-85(2002).
RN [2]
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 [3]
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 [4]
RP DEVELOPMENTAL STAGE, SUBCELLULAR LOCATION, DISRUPTION PHENOTYPE, AND
RP FUNCTION.
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).
CC -!- FUNCTION: May act during the development and be a negative regulator.
CC {ECO:0000269|PubMed:17501984}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:17501984}.
CC Membrane {ECO:0000269|PubMed:17501984}; Multi-pass membrane protein
CC {ECO:0000269|PubMed:17501984}. Endoplasmic reticulum membrane
CC {ECO:0000269|PubMed:17501984}. Golgi apparatus membrane
CC {ECO:0000269|PubMed:17501984}. Nucleus envelope
CC {ECO:0000269|PubMed:17501984}. Note=May also localize to internal
CC membranes.
CC -!- DEVELOPMENTAL STAGE: Expressed throughout growth and development with a
CC strong increase in early and late development.
CC {ECO:0000269|PubMed:17501984}.
CC -!- DISRUPTION PHENOTYPE: Cells show precocious development. Alterations
CC are also noted at the slug stage and in spore formation. Slugs are
CC longer and break apart several times on their way to culmination
CC forming smaller but proportionate fruiting bodies. Spores from fruiting
CC bodies are malformed and less viable, although the spore
CC differentiation factors are synthesized and sensed normally. Mutant
CC completes development 6 hours earlier. {ECO:0000269|PubMed:17501984}.
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; AAFI02000008; EAL71227.1; -; Genomic_DNA.
DR RefSeq; XP_645258.1; XM_640166.1.
DR AlphaFoldDB; Q75JT4; -.
DR SMR; Q75JT4; -.
DR PaxDb; Q75JT4; -.
DR EnsemblProtists; EAL71227; EAL71227; DDB_G0272150.
DR GeneID; 8618425; -.
DR KEGG; ddi:DDB_G0272150; -.
DR dictyBase; DDB_G0272150; grlJ.
DR eggNOG; KOG1055; Eukaryota.
DR HOGENOM; CLU_365408_0_0_1; -.
DR InParanoid; Q75JT4; -.
DR OMA; WININKL; -.
DR PhylomeDB; Q75JT4; -.
DR PRO; PR:Q75JT4; -.
DR Proteomes; UP000002195; Chromosome 2.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005635; C:nuclear envelope; IEA:UniProtKB-SubCell.
DR GO; GO:0031090; C:organelle membrane; IDA:dictyBase.
DR GO; GO:0005886; C:plasma membrane; IDA:dictyBase.
DR GO; GO:0004930; F:G protein-coupled receptor activity; IEA:UniProtKB-KW.
DR GO; GO:1902610; P:response to N-phenylthiourea; IMP:dictyBase.
DR GO; GO:0031153; P:slug development involved in sorocarp development; IMP:dictyBase.
DR GO; GO:0030587; P:sorocarp development; IMP:dictyBase.
DR GO; GO:0030435; P:sporulation resulting in formation of a cellular spore; 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 Cell membrane; Coiled coil; Endoplasmic reticulum;
KW G-protein coupled receptor; Glycoprotein; Golgi apparatus; Membrane;
KW Nucleus; Receptor; Reference proteome; Signal; Transducer; Transmembrane;
KW Transmembrane helix.
FT SIGNAL 1..20
FT /evidence="ECO:0000255"
FT CHAIN 21..783
FT /note="Metabotropic glutamate receptor-like protein J"
FT /id="PRO_0000370353"
FT TOPO_DOM 21..383
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 384..404
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 405..415
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 416..436
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 437..443
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 444..464
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 465..489
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 490..510
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 511..538
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 539..559
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 560..575
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 576..596
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 597..604
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 605..625
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
FT TOPO_DOM 626..783
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 647..696
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 731..783
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 56..85
FT /evidence="ECO:0000255"
FT COMPBIAS 647..672
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 731..747
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 748..762
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 763..783
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 181
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 196
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 256
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 282
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 315
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 441
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 783 AA; 87581 MW; 91F1EC8FB92390D7 CRC64;
MKILLYIAII LSFFSLITIS SECKIAVLLS GSPNDLGYNY LMNEARVKAE SELKLDFSIY
YENLEESMEE AEKAFQDALH KGANLIVVGS FVHVGLGLKY AALTKDQDIY WIIRGNKRPN
PDLPHVVILN FNSFELHYLL GYFSGLMTKT GIVGFVAPGP DVNTISTDNS FYLGAKYARP
NITFLNVYVQ SWYNPNVSYS AAKMLIKNGA DLIGMSQDDM SCQKAMMDSG LIGIGATGYP
THLLFGGNVG VSYITNWTNL YVKYAQHVLN DDWPDYSSYF TNLSREDSIF IDDYSYKVPI
DIQNLVNDEI QRLKNTSYIP YRSDPYLAQL GIPFDSKGLL VEDQFRANKK LLKGDSISKV
IDFGQYSIPI EFIDYPNSLK YGVTIVSGVC IFICLVCMTL VVVFKKARVI KSSSPAFLLL
ILLGCCIIFA ACILFAQSPT NQTCSARIWL LSLGYTLFLG NLLVKNWRIW LLFDNPKLKK
RAITNWKLYP WVFAILAIDV MILAIWQGLG NINAESRIGY DSLTQYQYKN VCSSDDQGSI
ALYLLLVFHG LVLLVACFIS FKIKVVDIEE FNESKPITTS VYIITFCLFI VIPLMVSPQS
LTSQTTIICV CAIVTTLISM LLLFGSKFYK MATQGLAINE TFATSTKSSS KSSKSSYGKD
NPNPNAINFG EDDTSDETSE EKHKSPKQKS VNFSNKSNSH LAVFTSDEET SKTSKLSIDF
ENSSKDISID QLQQQKQQPI NTNGDLENKS NDKIDDDNDN SSVLSKRISN QQNGETEIDS
NNV
