NLR1_CAEEL
ID NLR1_CAEEL Reviewed; 1180 AA.
AC Q19617;
DT 07-APR-2021, integrated into UniProtKB/Swiss-Prot.
DT 06-FEB-2007, sequence version 3.
DT 03-AUG-2022, entry version 174.
DE RecName: Full=Neurexin like receptor 1 {ECO:0000312|WormBase:F20B10.1};
DE Flags: Precursor;
GN Name=nlr-1 {ECO:0000312|WormBase:F20B10.1};
GN ORFNames=F20B10.1 {ECO:0000312|WormBase:F20B10.1};
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 TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RX PubMed=21055481; DOI=10.1016/j.gep.2010.10.008;
RA Haklai-Topper L., Soutschek J., Sabanay H., Scheel J., Hobert O., Peles E.;
RT "The neurexin superfamily of Caenorhabditis elegans.";
RL Gene Expr. Patterns 11:144-150(2011).
RN [3] {ECO:0000305}
RP FUNCTION, INTERACTION WITH F-ACTIN, SUBCELLULAR LOCATION, TISSUE
RP SPECIFICITY, DEVELOPMENTAL STAGE, AND DISRUPTION PHENOTYPE.
RX PubMed=33238150; DOI=10.1016/j.devcel.2020.10.020;
RA Meng L., Yan D.;
RT "NLR-1/CASPR Anchors F-Actin to Promote Gap Junction Formation.";
RL Dev. Cell 55:574-587(2020).
CC -!- FUNCTION: Required for gap junction formation, playing a role in
CC anchoring the cytoskeletal component F-actin to the membrane of
CC adjacent cells and thus facilitating the formation of gap junction
CC channels in embryonic cells, muscle cells and neuronal cells
CC (PubMed:33238150). Plays a role in maintaining gap junction activity to
CC promote pharyngeal muscle contraction (PubMed:33238150).
CC {ECO:0000269|PubMed:33238150}.
CC -!- SUBUNIT: Interacts (via the intracellular domain) with F-actin; the
CC interaction is required for anchoring F-actin at the membrane for gap
CC junction formation. {ECO:0000269|PubMed:33238150}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305|PubMed:33238150};
CC Single-pass type I membrane protein {ECO:0000255}. Cell junction, gap
CC junction {ECO:0000269|PubMed:33238150}. Note=Partially co-localizes
CC with F-actin at gap junctions between EA and EP endodermal precursor
CC cells in embryos. {ECO:0000269|PubMed:33238150}.
CC -!- TISSUE SPECIFICITY: Highly expressed in pharyngeal g1 and g2 gland
CC cells, pharyngeal muscle cells and the unilateral GABAergic RIS
CC interneuron (at protein level) (PubMed:21055481). Expressed in pm5
CC pharyngeal muscle cells and the nerve ring (PubMed:33238150).
CC {ECO:0000269|PubMed:21055481, ECO:0000269|PubMed:33238150}.
CC -!- DEVELOPMENTAL STAGE: Expressed during all stages of larval development
CC and adulthood (at protein level) (PubMed:21055481). Expressed during
CC embryogenesis (PubMed:33238150). Expressed in EA and EP endodermal
CC precursor cells at the 16-24 cell stage of embryogenesis
CC (PubMed:33238150). {ECO:0000269|PubMed:21055481,
CC ECO:0000269|PubMed:33238150}.
CC -!- DISRUPTION PHENOTYPE: RNAi-mediated knockdown results in abherrent inx-
CC 3-positive gap junction formation along the adjoining membranes of EA
CC and EP endodermal precursor cells at the 16-24 cell stage of
CC embryogenesis, and in adult pharyngeal muscles (PubMed:33238150). The
CC inx-3-positive gap junctions are increased in number, are randomly
CC positioned at irregular intervals on either the EA and EP cells and,
CC although they are along the membrane, they are not on the membrane
CC (PubMed:33238150). Furthermore, F-actin does not accumulate at the gap
CC junction formation plaque in between the EA and EP adjoining membrane,
CC but randomly forms patches along the membrane (PubMed:33238150). RNAi-
CC mediated knockdown does not affect the expression of inx-3
CC (PubMed:33238150). RNAi-mediated knockdown impairs gap junction
CC function in pharyngeal muscles which disrupts the synchronized muscle
CC contraction between the pharyngeal metacorpus and terminal bulbs and
CC thereby decreases the pharyngeal pumping rate (PubMed:33238150). RNAi-
CC mediated knockdown in the nerve ring results in uncoordinated movements
CC (also known as an unc phenotype), decreased locomotion and defective
CC unc-9-positive gap junction formation and morphology (PubMed:33238150).
CC {ECO:0000269|PubMed:33238150}.
CC -!- SIMILARITY: Belongs to the neurexin family. {ECO:0000305}.
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DR EMBL; BX284604; CAA93465.2; -; Genomic_DNA.
DR PIR; T21133; T21133.
DR RefSeq; NP_502312.2; NM_069911.4.
DR AlphaFoldDB; Q19617; -.
DR SMR; Q19617; -.
DR DIP; DIP-26832N; -.
DR STRING; 6239.F20B10.1; -.
DR EPD; Q19617; -.
DR PaxDb; Q19617; -.
DR EnsemblMetazoa; F20B10.1.1; F20B10.1.1; WBGene00003772.
DR GeneID; 178167; -.
DR KEGG; cel:CELE_F20B10.1; -.
DR UCSC; F20B10.1; c. elegans.
DR CTD; 178167; -.
DR WormBase; F20B10.1; CE40647; WBGene00003772; nlr-1.
DR eggNOG; KOG3516; Eukaryota.
DR GeneTree; ENSGT00940000160532; -.
DR HOGENOM; CLU_273234_0_0_1; -.
DR InParanoid; Q19617; -.
DR OMA; YDGPLCS; -.
DR OrthoDB; 338397at2759; -.
DR PhylomeDB; Q19617; -.
DR PRO; PR:Q19617; -.
DR Proteomes; UP000001940; Chromosome IV.
DR Bgee; WBGene00003772; Expressed in pharyngeal muscle cell (C elegans) and 3 other tissues.
DR GO; GO:0005921; C:gap junction; IDA:UniProtKB.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0051015; F:actin filament binding; IDA:UniProtKB.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0005243; F:gap junction channel activity; IMP:UniProtKB.
DR GO; GO:1903598; P:positive regulation of gap junction assembly; IMP:UniProtKB.
DR GO; GO:1903746; P:positive regulation of pharyngeal pumping; IMP:UniProtKB.
DR CDD; cd00110; LamG; 2.
DR InterPro; IPR013320; ConA-like_dom_sf.
DR InterPro; IPR001881; EGF-like_Ca-bd_dom.
DR InterPro; IPR000742; EGF-like_dom.
DR InterPro; IPR000152; EGF-type_Asp/Asn_hydroxyl_site.
DR InterPro; IPR001791; Laminin_G.
DR Pfam; PF00008; EGF; 1.
DR Pfam; PF02210; Laminin_G_2; 2.
DR SMART; SM00181; EGF; 2.
DR SMART; SM00179; EGF_CA; 2.
DR SMART; SM00282; LamG; 2.
DR SUPFAM; SSF49899; SSF49899; 4.
DR PROSITE; PS00010; ASX_HYDROXYL; 1.
DR PROSITE; PS00022; EGF_1; 1.
DR PROSITE; PS01186; EGF_2; 1.
DR PROSITE; PS50026; EGF_3; 2.
DR PROSITE; PS50025; LAM_G_DOMAIN; 2.
PE 1: Evidence at protein level;
KW Cell junction; Cell membrane; Disulfide bond; EGF-like domain;
KW Gap junction; Glycoprotein; Membrane; Receptor; Reference proteome; Repeat;
KW Signal; Transmembrane; Transmembrane helix.
FT SIGNAL 1..20
FT /evidence="ECO:0000255"
FT CHAIN 21..1180
FT /note="Neurexin like receptor 1"
FT /evidence="ECO:0000255"
FT /id="PRO_5004187349"
FT TOPO_DOM 21..1108
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 1109..1129
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1130..1180
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT DOMAIN 124..290
FT /note="Laminin G-like 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00122"
FT DOMAIN 444..481
FT /note="EGF-like 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 695..863
FT /note="Laminin G-like 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00122"
FT DOMAIN 859..896
FT /note="EGF-like 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT REGION 1142..1180
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 229
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 302
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 336
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 355
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 436
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 522
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 636
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 933
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 949
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 978
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 997
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 1011
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 1052
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT DISULFID 267..290
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00122"
FT DISULFID 448..459
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 453..469
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 471..480
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 863..874
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 868..883
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 885..895
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
SQ SEQUENCE 1180 AA; 131154 MW; AB91A1B71FE73E5B CRC64;
MSGLCLVLLL SIFAVSQSSG ECSDVSFSSV ASKLDGLKRV TRLSVSGHIS AYHVKVSISD
DDFQLVRLSN GNPLVLYSTL SNTPSWTHVD FLATEVRIFP AFEQATEDVR GPLLILTICD
YDTPITAFDD SSYTVEAHHA GLVSMYENDL CVVFRTYRSG VFFFSMADQG DVLIAQIIHG
TVHVIFDFGS LTPSRISAGK ALDDGRWHEM RWLHQFDSVQ LSIDGVLLNQ TAPTGLYRKL
DLHSVVHIGG RPNDDFSQGI ETTFTGCIAR LQLNNADLLQ LSPNEVHNQC QMPKPPSFTL
HNSSRAVLPF TFLPFSFEFR IVPINGPLVT LFDAENGTLV DVVIDEESKL HLVSNITKFK
QAANPAIDVA DGAWHSFSLR IRGVRMEIDI DGYTVLWLEG HEVRRVSQRL SNFILSASGC
YRSVTIDLTS VRVDGNVTRG ECTFQEKCLP NPCENGGGCV QSALDDYVCN CKEGYKGKNC
HTTDLPHSCE EWVFTKGNKQ KAVQGRKVLI DIDGGGEMQP INVTCKTERD EIGIDGVSTI
LEHDLLRPMI VTGDNKPGAV RYSLTYGIST EQMDRLVEGF EACSQFMRYT CRGGARLMTQ
GDERSPSSWY STRSDKHGLQ WGEAPPYSRM CSCAINGSCL HNRMCNCDSG EDSTDEGVNP
YSQLLPVTGL FLGGTTKSSS IEVEIGPLKC RNRATFDPVT FSNRNAKLSG AQTFNQRTFD
VSLHVKFSHS QMSILSWHST DDLHWFHLYV NDGKIVGEVV NGGESQQIVS EHRYDDGKFH
AIYWEADSTG MFLKVDGQRK SVKTSFILPT VYMWIVGSRT EKGSTGFAGV IRNVHLCGVE
LALGQYARKE TERGVAIGDD GYCRPDLCQN GGQCVDKYDG YVCDCSMTPF GGSDCTKEYG
MMVPAGSSIQ IPWQNPAHQA MCHRIAIQTT SRNTTILRSK ALFADSTFNM TVDDNGNLQM
MAYDGFFFHF KRQSKRHNLS DDIMHDISFC ASKHHFNVSV DGMQVITIEG NWTFFESFNV
WHFLDENFEG CVSRIQTGSA FPLKNPKTAR LNYSGKIRFG TCPIEAVSRQ QMYDFNPQPD
LISSTIKTST EDIKIFSVSQ NKQDLVSKAI IGGGILALSL FILCMSSLIC YMRSRPEGVY
KTNETGENCS PSRSEEPLVH NTTSNNNNNP TYASNKEYFC
