SOL1_CAEEL
ID SOL1_CAEEL Reviewed; 594 AA.
AC Q93212;
DT 16-FEB-2004, integrated into UniProtKB/Swiss-Prot.
DT 16-FEB-2004, sequence version 3.
DT 03-AUG-2022, entry version 138.
DE RecName: Full=Suppressor of lurcher protein 1;
DE Flags: Precursor;
GN Name=sol-1; ORFNames=C15A11.3;
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBCELLULAR LOCATION, DEVELOPMENTAL
RP STAGE, INTERACTION WITH GLR-1, AND MUTAGENESIS OF GLY-323.
RX PubMed=14749834; DOI=10.1038/nature02244;
RA Zheng Y., Mellem J.E., Brockie P.J., Madsen D.M., Maricq A.V.;
RT "SOL-1 is a CUB-domain protein required for GLR-1 glutamate receptor
RT function in C. elegans.";
RL Nature 427:451-457(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2;
RX PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG The C. elegans sequencing consortium;
RT "Genome sequence of the nematode C. elegans: a platform for investigating
RT biology.";
RL Science 282:2012-2018(1998).
CC -!- FUNCTION: Accessory protein required for glutamate-gated currents. May
CC participate in the gating of non-NMDA (N-methyl-D-aspartate) ionotropic
CC glutamate receptors such as glr-1. {ECO:0000269|PubMed:14749834}.
CC -!- SUBUNIT: Interacts with glr-1. {ECO:0000269|PubMed:14749834}.
CC -!- INTERACTION:
CC Q93212; P34299: glr-1; NbExp=2; IntAct=EBI-15564914, EBI-15564936;
CC -!- SUBCELLULAR LOCATION: Postsynaptic cell membrane {ECO:0000305}; Single-
CC pass type I membrane protein {ECO:0000305}. Synapse
CC {ECO:0000269|PubMed:14749834}. Note=Colocalizes with glr-1 at the cell
CC surface. Enriched at postsynaptic membranes.
CC -!- TISSUE SPECIFICITY: Widely expressed in the nervous system. Also
CC expressed in neurons that do not express glr-1.
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DR EMBL; AY387697; AAR26326.1; -; mRNA.
DR EMBL; Z79694; CAB01962.3; -; Genomic_DNA.
DR PIR; T19292; T19292.
DR RefSeq; NP_492088.3; NM_059687.6.
DR AlphaFoldDB; Q93212; -.
DR SMR; Q93212; -.
DR BioGRID; 37935; 2.
DR DIP; DIP-61096N; -.
DR IntAct; Q93212; 1.
DR STRING; 6239.C15A11.3; -.
DR TCDB; 8.A.47.1.4; the neuropilin and tolloid-like (neto) family.
DR PaxDb; Q93212; -.
DR EnsemblMetazoa; C15A11.3.1; C15A11.3.1; WBGene00004944.
DR GeneID; 172493; -.
DR KEGG; cel:CELE_C15A11.3; -.
DR UCSC; C15A11.3; c. elegans.
DR CTD; 172493; -.
DR WormBase; C15A11.3; CE36685; WBGene00004944; sol-1.
DR eggNOG; ENOG502RY9C; Eukaryota.
DR GeneTree; ENSGT00970000196453; -.
DR HOGENOM; CLU_020044_2_0_1; -.
DR InParanoid; Q93212; -.
DR OMA; FHTDWNM; -.
DR OrthoDB; 359110at2759; -.
DR PhylomeDB; Q93212; -.
DR Reactome; R-CEL-196791; Vitamin D (calciferol) metabolism.
DR PRO; PR:Q93212; -.
DR Proteomes; UP000001940; Chromosome I.
DR Bgee; WBGene00004944; Expressed in pharyngeal muscle cell (C elegans) and 3 other tissues.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0008328; C:ionotropic glutamate receptor complex; IPI:WormBase.
DR GO; GO:0032589; C:neuron projection membrane; IDA:WormBase.
DR GO; GO:0005886; C:plasma membrane; IDA:WormBase.
DR GO; GO:0045211; C:postsynaptic membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0045202; C:synapse; IDA:WormBase.
DR GO; GO:0016247; F:channel regulator activity; IDA:WormBase.
DR GO; GO:0008344; P:adult locomotory behavior; IMP:UniProtKB.
DR GO; GO:0006972; P:hyperosmotic response; IMP:WormBase.
DR GO; GO:0051968; P:positive regulation of synaptic transmission, glutamatergic; IDA:WormBase.
DR GO; GO:0040012; P:regulation of locomotion; IGI:WormBase.
DR GO; GO:0001966; P:thigmotaxis; IMP:WormBase.
DR CDD; cd00041; CUB; 2.
DR Gene3D; 2.60.120.290; -; 4.
DR InterPro; IPR000859; CUB_dom.
DR InterPro; IPR035914; Sperma_CUB_dom_sf.
DR Pfam; PF00431; CUB; 3.
DR SMART; SM00042; CUB; 4.
DR SUPFAM; SSF49854; SSF49854; 4.
DR PROSITE; PS01180; CUB; 4.
PE 1: Evidence at protein level;
KW Cell membrane; Disulfide bond; Glycoprotein; Membrane;
KW Postsynaptic cell membrane; Reference proteome; Repeat; Signal; Synapse;
KW Transmembrane; Transmembrane helix.
FT SIGNAL 1..23
FT /evidence="ECO:0000255"
FT CHAIN 24..594
FT /note="Suppressor of lurcher protein 1"
FT /id="PRO_0000022383"
FT TOPO_DOM 24..571
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 572..592
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 593..594
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 28..147
FT /note="CUB 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00059"
FT DOMAIN 162..272
FT /note="CUB 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00059"
FT DOMAIN 286..417
FT /note="CUB 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00059"
FT DOMAIN 435..554
FT /note="CUB 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00059"
FT CARBOHYD 34
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 151
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 187
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 345
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 355
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 440
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 83..109
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00059"
FT DISULFID 162..188
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00059"
FT DISULFID 286..317
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00059"
FT DISULFID 435..464
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00059"
FT MUTAGEN 323
FT /note="G->R: In ak66; induces delayed reaction times; when
FT exposed to a drop of hyperosmotic solution."
FT /evidence="ECO:0000269|PubMed:14749834"
SQ SEQUENCE 594 AA; 68233 MW; D5897E3CAB2DEB89 CRC64;
MCRRAEDLVL LLIPILFGYF SHASEHECKC VLFNVTSGNF HSPEFPAPLE GVPCLFYHFQ
APPDHIIRLT FDVFQLPPRI GVCSSSIMLF DHSTDGLIEF GERADFEFCG KEISSGRQFF
SKDQHFLLQI SSGKESSRGF RGSFLAIPKK NFTSDAVEMA ECSYRVEKQK AIIYSPDYPY
YYPSKVNCTY HIPQRKGFQI VVNSIVMDIG RDAILQIFES VEGKFEKRLI EMVTSVQKSI
YVSSTSSLLI YFSAGNNDVE RAVGFVIELQ YSNAVWSQSP ETASECQLNI NSENFKEGQL
SSDKIGRFTS SSLPTKCQIV LQGYPNEKIS VKFTHFNLYV PDNKNVTKRC TEVDNLSADV
RVGSRLSRID EWCGKRAPPN LMSSSNLLQL EYNTKSSKAI RESTNDDIGF RLDYKFHTDW
NMGNMKAKVD KKKECRFSFN SSEHTNGKLW SANYPGLYPR NLYCEYIFHG RNDQVVHIHF
EYFDIEGFNQ CDETTQSDYI LFSNYQTHDR TNRRFCGKTA PKGPILSESN YFRMIFSTND
IFDATGFYAH YQFITQEKSQ ISRVKLTISS SQTPFSSFFL VILLFTFRYI ANIF
