GRLA_DICDI
ID GRLA_DICDI Reviewed; 798 AA.
AC Q55AP1;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 24-MAY-2005, sequence version 1.
DT 25-MAY-2022, entry version 90.
DE RecName: Full=Metabotropic glutamate receptor-like protein A;
DE Flags: Precursor;
GN Name=grlA; ORFNames=DDB_G0271684;
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.
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 [5]
RP DEVELOPMENTAL STAGE, SUBCELLULAR LOCATION, FUNCTION, AND DISRUPTION
RP PHENOTYPE.
RX PubMed=17950724; DOI=10.1016/j.ydbio.2007.08.055;
RA Prabhu Y., Mondal S., Eichinger L., Noegel A.A.;
RT "A GPCR involved in post aggregation events in Dictyostelium discoideum.";
RL Dev. Biol. 312:29-43(2007).
CC -!- FUNCTION: May play an important role in the terminal differentiation.
CC {ECO:0000269|PubMed:17950724}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane
CC protein {ECO:0000305}. Cytoplasm, cell cortex
CC {ECO:0000269|PubMed:17950724}. Cytoplasm, perinuclear region
CC {ECO:0000269|PubMed:17950724}.
CC -!- DEVELOPMENTAL STAGE: Expressed throughout growth and development and
CC shows increased levels during the post aggregation stages. Abundantly
CC expressed when fruiting body formation is close to completion.
CC {ECO:0000269|PubMed:17501984, ECO:0000269|PubMed:17950724}.
CC -!- DISRUPTION PHENOTYPE: Cells have tip formation delayed by 3 to 4 hours
CC and complete development with normally shaped fruiting bodies only
CC after 26-27 hour. Cells are able to form normally shaped mature
CC fruiting bodies, however with a lower number of produced spores.
CC {ECO:0000269|PubMed:17950724}.
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; AAFI02000006; EAL71532.1; -; Genomic_DNA.
DR RefSeq; XP_645481.1; XM_640389.1.
DR AlphaFoldDB; Q55AP1; -.
DR SMR; Q55AP1; -.
DR STRING; 44689.DDB0231963; -.
DR PaxDb; Q55AP1; -.
DR EnsemblProtists; EAL71532; EAL71532; DDB_G0271684.
DR GeneID; 8618109; -.
DR KEGG; ddi:DDB_G0271684; -.
DR dictyBase; DDB_G0271684; grlA.
DR eggNOG; KOG1055; Eukaryota.
DR HOGENOM; CLU_365408_0_0_1; -.
DR InParanoid; Q55AP1; -.
DR OMA; CRSRIWL; -.
DR PhylomeDB; Q55AP1; -.
DR PRO; PR:Q55AP1; -.
DR Proteomes; UP000002195; Chromosome 2.
DR GO; GO:0005938; C:cell cortex; IEA:UniProtKB-SubCell.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IDA:dictyBase.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005635; C:nuclear envelope; IDA:dictyBase.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:UniProtKB-SubCell.
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: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; IPR028082; Peripla_BP_I.
DR InterPro; IPR003760; PnrA-like.
DR Pfam; PF00003; 7tm_3; 1.
DR Pfam; PF02608; Bmp; 1.
DR SUPFAM; SSF53822; SSF53822; 1.
DR PROSITE; PS50259; G_PROTEIN_RECEP_F3_4; 1.
PE 2: Evidence at transcript level;
KW Coiled coil; Cytoplasm; G-protein coupled receptor; Glycoprotein; Membrane;
KW Receptor; Reference proteome; Signal; Transducer; Transmembrane;
KW Transmembrane helix.
FT SIGNAL 1..23
FT /evidence="ECO:0000255"
FT CHAIN 24..798
FT /note="Metabotropic glutamate receptor-like protein A"
FT /id="PRO_0000370346"
FT TOPO_DOM 24..388
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 389..409
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 410..419
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 420..440
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 441..447
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 448..468
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 469..494
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 495..515
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 516..545
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 546..566
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 567..580
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 581..601
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 602..609
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 610..630
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
FT TOPO_DOM 631..798
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 752..798
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 714..771
FT /evidence="ECO:0000255"
FT COMPBIAS 752..779
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 186
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 275
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 320
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 798 AA; 89613 MW; 46A919B1C49C547C CRC64;
MNKLKFLIIL FITFLFNLKY INSLKQCKIS VLLSGDWSDM GYNYQMNNAR IKAESALNLE
MSLCYKNLEV SIDLAKQAIE DSIKKGANFI VISSSVHTSI GYEYARLHRD KDIYWLIRGR
GRPVPDDLPK VAVINFNTHL LHYTLGLVSG YLTTSGTVGF ISPGPQILAL ANSNSFYLGA
LASRKNVTFL NAYTGSWYNP EVAYKASQML ISNGADFIGM SQDDMSVQKA LMDSGKMALG
ITGFSNRLIW GSDIALSYIT DWSDVFIKYA GHILNDTWPE YTDYYTTLAE GGSLLFDTFS
YRVPSEVQKL VSLEIEKLKN SSYQPFRCNP MYSQINLNFD SNGCANDMEF KNTKLLLKGT
DISKTINLGL YTIPIEFVDY SNSMKLGLTI VSGFCILFCI ISMVLVIMFR HAKIIKSASP
IFCLLILFGC IIIFSGCIIF SLSPTDGICG ARVWLLSIGY TIFLGSLLVK NWRIWLLFDN
PKLKKRSITN WKLYPFVAGI LAADVLILAL WQGLGDIRSE SRIGIDSLTK YQYANVCSSN
DQGSVALYIL LVFHGIKLLA ACFISFKIKA VDIEEFNESK PIASSIYIIT FCLFIVIPLM
VSPQSVASQV ITIVVCAIVT TLISISLLFG SKFYMMATQG LALNQTFATN TKSSSFSLSL
EKQKSKSNGL EFEDSDESEE KLPQIKNYSN SEIPNLQHNH SRLAHFSSDS CTSAEQDSKL
DLENQNDENE IENNQNNQNN IVEDCQKVEK LEKDENLEKD ENLEKDENLE KDNENQSIIQ
KKRLSKNFNQ SEIDPDDV
