GLIT1_CAEEL
ID GLIT1_CAEEL Reviewed; 730 AA.
AC Q20826;
DT 16-OCT-2019, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 157.
DE RecName: Full=Neuroligin-like protein glit-1 {ECO:0000305};
DE AltName: Full=Gliotactin homolog {ECO:0000305|PubMed:29346364};
DE AltName: Full=Inactive esterase glit-1 {ECO:0000305};
DE Flags: Precursor;
GN Name=glit-1 {ECO:0000303|PubMed:29346364, ECO:0000312|WormBase:F55D10.3};
GN ORFNames=F55D10.3 {ECO:0000312|WormBase:F55D10.3};
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239 {ECO:0000312|Proteomes:UP000001940};
RN [1] {ECO:0000312|Proteomes:UP000001940}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2 {ECO:0000312|Proteomes:UP000001940};
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).
RN [2] {ECO:0000305}
RP FUNCTION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, AND MUTAGENESIS OF
RP PRO-113.
RX PubMed=29346364; DOI=10.1371/journal.pgen.1007106;
RA Offenburger S.L., Jongsma E., Gartner A.;
RT "Mutations in Caenorhabditis elegans neuroligin-like glit-1, the apoptosis
RT pathway and the calcium chaperone crt-1 increase dopaminergic
RT neurodegeneration after 6-OHDA treatment.";
RL PLoS Genet. 14:E1007106-E1007106(2018).
CC -!- FUNCTION: Probable neuronal cell surface protein thought to be involved
CC in cell-cell-interactions (Probable). Confers protection against
CC oxidative stress (PubMed:29346364). Plays a role in protecting
CC dopaminergic neurons against oxidative stress-induced neurodegeneration
CC (PubMed:29346364). {ECO:0000269|PubMed:29346364, ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Single-pass type I
CC membrane protein {ECO:0000255}.
CC -!- TISSUE SPECIFICITY: Expressed in the pharynx, intestine, and in several
CC cells in the head including dopaminergic neurons.
CC {ECO:0000269|PubMed:29346364}.
CC -!- DEVELOPMENTAL STAGE: Expressed in larvae and adults. Expressed in
CC dopaminergic neurons in L4 larvae. {ECO:0000269|PubMed:29346364}.
CC -!- SIMILARITY: Belongs to the type-B carboxylesterase/lipase family.
CC {ECO:0000305}.
CC -!- CAUTION: Although glit-1 contains an extracellular carboxylesterase-
CC like domain, the characteristic Ser-Glu-His catalytic triad present in
CC acetylcholinesterase is replaced by two Asp residues and an Arg,
CC suggesting that glit-1 lacks catalytic activity.
CC {ECO:0000305|PubMed:29346364}.
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DR EMBL; BX284606; CCD67089.1; -; Genomic_DNA.
DR PIR; T16455; T16455.
DR RefSeq; NP_508807.1; NM_076406.4.
DR AlphaFoldDB; Q20826; -.
DR SMR; Q20826; -.
DR STRING; 6239.F55D10.3; -.
DR ESTHER; caeel-f55d10.3; Gliotactin.
DR EPD; Q20826; -.
DR PaxDb; Q20826; -.
DR PeptideAtlas; Q20826; -.
DR EnsemblMetazoa; F55D10.3.1; F55D10.3.1; WBGene00018878.
DR GeneID; 180747; -.
DR KEGG; cel:CELE_F55D10.3; -.
DR UCSC; F55D10.3; c. elegans.
DR CTD; 180747; -.
DR WormBase; F55D10.3; CE04659; WBGene00018878; glit-1.
DR eggNOG; KOG1516; Eukaryota.
DR HOGENOM; CLU_380016_0_0_1; -.
DR InParanoid; Q20826; -.
DR OMA; VPVYMYV; -.
DR OrthoDB; 754103at2759; -.
DR PhylomeDB; Q20826; -.
DR Reactome; R-CEL-192456; Digestion of dietary lipid.
DR Reactome; R-CEL-6794361; Neurexins and neuroligins.
DR PRO; PR:Q20826; -.
DR Proteomes; UP000001940; Chromosome X.
DR Bgee; WBGene00018878; Expressed in pharyngeal muscle cell (C elegans) and 3 other tissues.
DR GO; GO:0009986; C:cell surface; IBA:GO_Central.
DR GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
DR GO; GO:0098793; C:presynapse; IEA:GOC.
DR GO; GO:0045202; C:synapse; IBA:GO_Central.
DR GO; GO:0042043; F:neurexin family protein binding; IBA:GO_Central.
DR GO; GO:0038023; F:signaling receptor activity; IBA:GO_Central.
DR GO; GO:0072756; P:cellular response to paraquat; IMP:UniProtKB.
DR GO; GO:0007268; P:chemical synaptic transmission; IBA:GO_Central.
DR GO; GO:0050804; P:modulation of chemical synaptic transmission; IBA:GO_Central.
DR GO; GO:1903204; P:negative regulation of oxidative stress-induced neuron death; IMP:UniProtKB.
DR GO; GO:1902883; P:negative regulation of response to oxidative stress; IMP:UniProtKB.
DR GO; GO:0007158; P:neuron cell-cell adhesion; IBA:GO_Central.
DR GO; GO:0097104; P:postsynaptic membrane assembly; IBA:GO_Central.
DR GO; GO:0097105; P:presynaptic membrane assembly; IBA:GO_Central.
DR GO; GO:0048488; P:synaptic vesicle endocytosis; IBA:GO_Central.
DR Gene3D; 3.40.50.1820; -; 1.
DR InterPro; IPR029058; AB_hydrolase.
DR InterPro; IPR002018; CarbesteraseB.
DR InterPro; IPR019819; Carboxylesterase_B_CS.
DR Pfam; PF00135; COesterase; 1.
DR SUPFAM; SSF53474; SSF53474; 1.
DR PROSITE; PS00941; CARBOXYLESTERASE_B_2; 1.
PE 1: Evidence at protein level;
KW Cell membrane; Glycoprotein; Membrane; Reference proteome; Signal;
KW Transmembrane; Transmembrane helix.
FT SIGNAL 1..18
FT /evidence="ECO:0000255"
FT CHAIN 19..730
FT /note="Neuroligin-like protein glit-1"
FT /evidence="ECO:0000255"
FT /id="PRO_5004199260"
FT TOPO_DOM 19..663
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 664..684
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 685..730
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT CARBOHYD 103
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 320
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 445
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 512
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 557
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 564
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 604
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT MUTAGEN 113
FT /note="P->L: In gt1981; in larvae, enhances
FT neurodegeneration of CEP and DEP dopaminergic neurons
FT induced by the oxidative stress agent 6-hydroxydopamine (6-
FT OHDA). Increases expression of oxidative stress genes in
FT response to paraquat and hydrogen peroxide. Increases
FT paralysis induced by high dopamine levels. No defect in
FT dopamine signaling and intestinal permeability. Reduced
FT lifespan and slower development in response to oxidative
FT agent paraquat."
FT /evidence="ECO:0000269|PubMed:29346364"
SQ SEQUENCE 730 AA; 82993 MW; 866F417AC58E270D CRC64;
MFTGTIFNSL FTLPLVISQF VPPPTRPVDL WDPFKTTTTP FPHGGVNQGL NRDEVVVRLP
LGDIVGKEVH LHNLPWTIHK DPTEELPKDG THFDPNPLKP KNNITVFTFL GVPYAEPPTS
QRRFKPPQQL TVFPGKQPYL AFNYAASCAQ DVEKSPSPFV DHPYPFMVDE DCLYLNIFSP
DISKNAQTTY PVIVFFHGGN FQTGSANEWP AHGLASRGMV VVTVNYRLGA FGFMSMGDSE
TGNYGLQDQR LALEFVKNNI VTFGGDPQAV TVVGHDAGAA SIGFHMQSPY SRHLFRSAAT
MSGAEVSYHS YIGKTALAFN NTMKLGRYAG CTQAVAQHRW DCILTRSTGD IIDATRNIPI
EYNRYLFMPT VDGKYLPGNP LWTLVNAPSG ETSIMSPVPM LIGMNAQDGS EVVLEDRRLG
EFSQFNDVDH EYLKSYSLEY CYRHNYSMNR EATADAILSK YTFWPDRAAA WAIKENFIQF
ATDAYYTAPM QLSSHLHSSS GSRVFQYVNN YNFSRQHPNL LFIPDWMGVC RDCDLYLMFG
YPFLPDELRP IGLRGINFTD TDRNASRTFS NIIRRFSYHQ NPNFQFDGSW AAYEPRRHWY
INFNYTHEED WKIPGTLARD YRYQDVAFWN EYIPALVNYM TTTFSPENVA YRREIMVFKW
ITGVNVIIIA LLIVLAGAFG YMVWGNKEDE EAAYKAENHQ LVEYRDTGHS VSDATISSRT
RSPRSRITNL
