IGLR2_CAEEL
ID IGLR2_CAEEL Reviewed; 773 AA.
AC P34595;
DT 01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT 11-JUL-2002, sequence version 2.
DT 03-AUG-2022, entry version 147.
DE RecName: Full=Immunoglobulin domain and leucine-rich repeat-containing protein 2 {ECO:0000305};
DE Flags: Precursor;
GN Name=iglr-2 {ECO:0000312|WormBase:ZC262.3a};
GN ORFNames=ZC262.3 {ECO:0000312|WormBase:ZC262.3a};
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 [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2;
RX PubMed=7906398; DOI=10.1038/368032a0;
RA Wilson R., Ainscough R., Anderson K., Baynes C., Berks M., Bonfield J.,
RA Burton J., Connell M., Copsey T., Cooper J., Coulson A., Craxton M.,
RA Dear S., Du Z., Durbin R., Favello A., Fraser A., Fulton L., Gardner A.,
RA Green P., Hawkins T., Hillier L., Jier M., Johnston L., Jones M.,
RA Kershaw J., Kirsten J., Laisster N., Latreille P., Lightning J., Lloyd C.,
RA Mortimore B., O'Callaghan M., Parsons J., Percy C., Rifken L., Roopra A.,
RA Saunders D., Shownkeen R., Sims M., Smaldon N., Smith A., Smith M.,
RA Sonnhammer E., Staden R., Sulston J., Thierry-Mieg J., Thomas K.,
RA Vaudin M., Vaughan K., Waterston R., Watson A., Weinstock L.,
RA Wilkinson-Sproat J., Wohldman P.;
RT "2.2 Mb of contiguous nucleotide sequence from chromosome III of C.
RT elegans.";
RL Nature 368:32-38(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND ALTERNATIVE SPLICING.
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).
RN [3]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-114; ASN-204; ASN-361 AND
RP ASN-379, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC STRAIN=Bristol N2;
RX PubMed=17761667; DOI=10.1074/mcp.m600392-mcp200;
RA Kaji H., Kamiie J., Kawakami H., Kido K., Yamauchi Y., Shinkawa T.,
RA Taoka M., Takahashi N., Isobe T.;
RT "Proteomics reveals N-linked glycoprotein diversity in Caenorhabditis
RT elegans and suggests an atypical translocation mechanism for integral
RT membrane proteins.";
RL Mol. Cell. Proteomics 6:2100-2109(2007).
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass type I
CC membrane protein {ECO:0000305}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=a;
CC IsoId=P34595-1; Sequence=Displayed;
CC Name=b;
CC IsoId=P34595-2; Sequence=VSP_002450, VSP_002451;
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DR EMBL; FO081113; CCD69194.1; -; Genomic_DNA.
DR EMBL; FO081113; CCD69195.1; -; Genomic_DNA.
DR PIR; S44883; S44883.
DR RefSeq; NP_498833.1; NM_066432.5.
DR RefSeq; NP_498834.1; NM_066433.6. [P34595-1]
DR AlphaFoldDB; P34595; -.
DR SMR; P34595; -.
DR BioGRID; 41379; 1.
DR STRING; 6239.ZC262.3a; -.
DR iPTMnet; P34595; -.
DR EPD; P34595; -.
DR PaxDb; P34595; -.
DR PeptideAtlas; P34595; -.
DR PRIDE; P34595; -.
DR EnsemblMetazoa; ZC262.3.1; ZC262.3.1; WBGene00022580. [P34595-1]
DR EnsemblMetazoa; ZC262.3.2; ZC262.3.2; WBGene00022580. [P34595-1]
DR GeneID; 176175; -.
DR KEGG; cel:CELE_ZC262.3; -.
DR UCSC; ZC262.3a; c. elegans. [P34595-1]
DR CTD; 176175; -.
DR WormBase; ZC262.3a; CE27345; WBGene00022580; iglr-2. [P34595-1]
DR WormBase; ZC262.3b; CE29616; WBGene00022580; iglr-2. [P34595-2]
DR eggNOG; KOG0619; Eukaryota.
DR GeneTree; ENSGT00390000006493; -.
DR HOGENOM; CLU_020438_0_0_1; -.
DR InParanoid; P34595; -.
DR OMA; KSALWWI; -.
DR OrthoDB; 334902at2759; -.
DR PhylomeDB; P34595; -.
DR PRO; PR:P34595; -.
DR Proteomes; UP000001940; Chromosome III.
DR Bgee; WBGene00022580; Expressed in embryo and 4 other tissues.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005840; C:ribosome; IEA:InterPro.
DR GO; GO:0003735; F:structural constituent of ribosome; IEA:InterPro.
DR GO; GO:0006412; P:translation; IEA:InterPro.
DR Gene3D; 2.60.40.10; -; 1.
DR Gene3D; 3.80.10.10; -; 2.
DR InterPro; IPR007110; Ig-like_dom.
DR InterPro; IPR036179; Ig-like_dom_sf.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR001611; Leu-rich_rpt.
DR InterPro; IPR032675; LRR_dom_sf.
DR InterPro; IPR001648; Ribosomal_S18.
DR PANTHER; PTHR13479; PTHR13479; 1.
DR SUPFAM; SSF48726; SSF48726; 1.
DR PROSITE; PS50835; IG_LIKE; 1.
DR PROSITE; PS51450; LRR; 4.
PE 1: Evidence at protein level;
KW Alternative splicing; Disulfide bond; Glycoprotein; Immunoglobulin domain;
KW Leucine-rich repeat; Membrane; Reference proteome; Repeat; Signal;
KW Transmembrane; Transmembrane helix.
FT SIGNAL 1..20
FT /evidence="ECO:0000255"
FT CHAIN 21..773
FT /note="Immunoglobulin domain and leucine-rich repeat-
FT containing protein 2"
FT /evidence="ECO:0000305"
FT /id="PRO_0000072708"
FT TOPO_DOM 21..493
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 494..514
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 515..773
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REPEAT 52..73
FT /note="LRR 1"
FT /evidence="ECO:0000255"
FT REPEAT 74..96
FT /note="LRR 2"
FT /evidence="ECO:0000255"
FT REPEAT 97..120
FT /note="LRR 3"
FT /evidence="ECO:0000255"
FT REPEAT 122..144
FT /note="LRR 4"
FT /evidence="ECO:0000255"
FT REPEAT 145..167
FT /note="LRR 5"
FT /evidence="ECO:0000255"
FT REPEAT 168..191
FT /note="LRR 6"
FT /evidence="ECO:0000255"
FT REPEAT 206..230
FT /note="LRR 7"
FT /evidence="ECO:0000255"
FT REPEAT 233..251
FT /note="LRR 8"
FT /evidence="ECO:0000255"
FT REPEAT 252..275
FT /note="LRR 9"
FT /evidence="ECO:0000255"
FT REPEAT 296..319
FT /note="LRR 10"
FT /evidence="ECO:0000255"
FT DOMAIN 349..479
FT /note="Ig-like"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT REGION 725..773
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 734..765
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 114
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:17761667"
FT CARBOHYD 204
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:17761667"
FT CARBOHYD 361
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:17761667"
FT CARBOHYD 379
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:17761667"
FT DISULFID 396..463
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT VAR_SEQ 587..624
FT /note="FQNYKAAQVDAVHSHLDAMRDGYNNQLGRVREYGSKRA -> LNHFVCLSIT
FT IPKSVPSSSDLSFLFAISPKTLTYHLQE (in isoform b)"
FT /evidence="ECO:0000305"
FT /id="VSP_002450"
FT VAR_SEQ 625..773
FT /note="Missing (in isoform b)"
FT /evidence="ECO:0000305"
FT /id="VSP_002451"
SQ SEQUENCE 773 AA; 89054 MW; 0F4966385F8111EE CRC64;
MRKFVFFVVA ILIQIHTTTS QRNRSSSPSG FLDLQLEKCP QVLGCRCVRD STRNIQCFSI
DESKLLEIQK IYGSNIQRLE LHNWQHDQLN FDIFAPFPQL EHIILRDGDL ESLNGTVIHP
TLKVLSIENS ELTSSSEVCR LLSIFPKIQS LSLSKNYFEK FECDTSNTKL KILDLSQNRI
SHLEVPNTLR VLNVSRNRLT SFENISTKLT DLDISFNKLS LWPSFDDWKF PNLRSLSAIK
LDLQTGFQLD APLLNSLNID GASLRYLNFH QILTPKLKKF SARYLTELRN IAGRLPSTVT
DVAFTDTMLR TLPADFIPMS STNHMQKVSF DFSTNQLLCD KCLLQWSLPV YAQTSIRKDC
NLTREEIESA SCKIGVVAND TGIQYGKYEK PTAISCFSYG VPSPKISWWR FRPAEKLGSY
DPITDEISYT NVSETMKESY EIQSGGSLLI RSPNRSHVER YVCVVENEYG KDYGIYHFRL
DYLDWYSYDV FNSVFWGGLA TSLIVCLISF LLNITWILTR KSALWWIQRA ERLSRVRKMV
EAMEKYRVRQ MESLHEKYTK RVQIVRDNYH QQVEALRVSY ASQQEKFQNY KAAQVDAVHS
HLDAMRDGYN NQLGRVREYG SKRAEQLWES YERQVNRMRT FSLQHRLKMM RQYKVKQRYV
NKLLESLQAT SPEVQLENEE KVRAALEIPD DLATIDGSMD TPSRLSRSSS FHSLPEYVID
EQGNVRPGII PTNAPSIRFT TKPTTSSISN EASTSSPSSS GAHRSPDSPP EKR
