ISLR2_MOUSE
ID ISLR2_MOUSE Reviewed; 745 AA.
AC Q5RKR3; C8XPY9; Q6ZPQ3;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 21-DEC-2004, sequence version 1.
DT 03-AUG-2022, entry version 141.
DE RecName: Full=Immunoglobulin superfamily containing leucine-rich repeat protein 2;
DE AltName: Full=Leucine-rich repeat domain and immunoglobulin domain-containing axon extension protein;
DE Flags: Precursor;
GN Name=Islr2; Synonyms=Kiaa1465, Linx;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBUNIT, INTERACTION WITH NTRK1,
RP SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND DISRUPTION PHENOTYPE.
RC STRAIN=C57BL/6J;
RX PubMed=19755105; DOI=10.1016/j.neuron.2009.07.031;
RA Mandai K., Guo T., StHillaire C., Meabon J.S., Kanning K.C., Bothwell M.,
RA Ginty D.D.;
RT "LIG family receptor tyrosine kinase-associated proteins modulate growth
RT factor signals during neural development.";
RL Neuron 63:614-627(2009).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Fetal brain;
RX PubMed=14621295; DOI=10.1093/dnares/10.4.167;
RA Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S.,
RA Saga Y., Nagase T., Ohara O., Koga H.;
RT "Prediction of the coding sequences of mouse homologues of KIAA gene: III.
RT The complete nucleotide sequences of 500 mouse KIAA-homologous cDNAs
RT identified by screening of terminal sequences of cDNA clones randomly
RT sampled from size-fractionated libraries.";
RL DNA Res. 10:167-180(2003).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Brain;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-719 AND SER-720, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
CC -!- FUNCTION: Required for axon extension during neural development.
CC {ECO:0000269|PubMed:19755105}.
CC -!- SUBUNIT: Homomultimer. Interacts with NTRK1/TrkA.
CC {ECO:0000269|PubMed:19755105}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:19755105};
CC Single-pass membrane protein {ECO:0000269|PubMed:19755105}.
CC -!- TISSUE SPECIFICITY: At 11.5 dpc, expressed in spinal nerves, their
CC roots and the ventral spinal cord. At 12.5 dpc, detected in the ventral
CC spinal cord, dorsal root ganglia (DRG), dorsal and ventral roots and
CC sympathetic chain ganglia. At 12.5 dpc, expressed in almost all motor
CC neurons which also express RET and in almost all DRG sensory neurons
CC which also express NTRK1. At 18.5 dpc, expressed only in a subset of
CC NTRK1-expressing neurons but still expressed in nearly all RET-
CC expressing neurons. {ECO:0000269|PubMed:19755105}.
CC -!- DISRUPTION PHENOTYPE: Sensory and motor neuron axonal projection
CC defects. {ECO:0000269|PubMed:19755105}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAC98177.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; EU497918; ACC99423.1; -; mRNA.
DR EMBL; AK129367; BAC98177.1; ALT_INIT; mRNA.
DR EMBL; BC059068; AAH59068.1; -; mRNA.
DR EMBL; BC096531; AAH96531.1; -; mRNA.
DR CCDS; CCDS23238.1; -.
DR RefSeq; NP_001155007.1; NM_001161535.1.
DR RefSeq; NP_001155008.1; NM_001161536.1.
DR RefSeq; NP_001155009.1; NM_001161537.1.
DR RefSeq; NP_001155010.1; NM_001161538.1.
DR RefSeq; NP_001155011.1; NM_001161539.1.
DR RefSeq; NP_001155012.1; NM_001161540.1.
DR RefSeq; NP_001155013.1; NM_001161541.1.
DR RefSeq; NP_796167.2; NM_177193.5.
DR RefSeq; XP_006511292.1; XM_006511229.3.
DR RefSeq; XP_006511293.1; XM_006511230.2.
DR RefSeq; XP_006511294.1; XM_006511231.3.
DR RefSeq; XP_006511295.1; XM_006511232.3.
DR RefSeq; XP_006511296.1; XM_006511233.2.
DR RefSeq; XP_006511297.1; XM_006511234.3.
DR AlphaFoldDB; Q5RKR3; -.
DR SMR; Q5RKR3; -.
DR BioGRID; 236117; 1.
DR STRING; 10090.ENSMUSP00000130879; -.
DR GlyConnect; 2380; 3 N-Linked glycans (2 sites).
DR GlyGen; Q5RKR3; 7 sites, 3 N-linked glycans (2 sites).
DR iPTMnet; Q5RKR3; -.
DR PhosphoSitePlus; Q5RKR3; -.
DR SwissPalm; Q5RKR3; -.
DR MaxQB; Q5RKR3; -.
DR PaxDb; Q5RKR3; -.
DR PRIDE; Q5RKR3; -.
DR ProteomicsDB; 269103; -.
DR Antibodypedia; 26861; 84 antibodies from 20 providers.
DR DNASU; 320563; -.
DR Ensembl; ENSMUST00000114144; ENSMUSP00000109781; ENSMUSG00000051243.
DR Ensembl; ENSMUST00000163897; ENSMUSP00000130322; ENSMUSG00000051243.
DR Ensembl; ENSMUST00000165276; ENSMUSP00000129328; ENSMUSG00000051243.
DR Ensembl; ENSMUST00000170421; ENSMUSP00000127228; ENSMUSG00000051243.
DR Ensembl; ENSMUST00000215950; ENSMUSP00000149095; ENSMUSG00000051243.
DR GeneID; 320563; -.
DR KEGG; mmu:320563; -.
DR UCSC; uc009pwm.2; mouse.
DR CTD; 57611; -.
DR MGI; MGI:2444277; Islr2.
DR VEuPathDB; HostDB:ENSMUSG00000051243; -.
DR eggNOG; KOG0619; Eukaryota.
DR GeneTree; ENSGT00940000162846; -.
DR HOGENOM; CLU_400948_0_0_1; -.
DR InParanoid; Q5RKR3; -.
DR OMA; YSVCLTY; -.
DR OrthoDB; 282791at2759; -.
DR PhylomeDB; Q5RKR3; -.
DR BioGRID-ORCS; 320563; 5 hits in 71 CRISPR screens.
DR ChiTaRS; Islr2; mouse.
DR PRO; PR:Q5RKR3; -.
DR Proteomes; UP000000589; Chromosome 9.
DR RNAct; Q5RKR3; protein.
DR Bgee; ENSMUSG00000051243; Expressed in cortical plate and 111 other tissues.
DR ExpressionAtlas; Q5RKR3; baseline and differential.
DR Genevisible; Q5RKR3; MM.
DR GO; GO:0009986; C:cell surface; 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:0007399; P:nervous system development; IEA:UniProtKB-KW.
DR GO; GO:0045773; P:positive regulation of axon extension; IMP:UniProtKB.
DR Gene3D; 2.60.40.10; -; 1.
DR Gene3D; 3.80.10.10; -; 1.
DR InterPro; IPR000483; Cys-rich_flank_reg_C.
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; IPR003591; Leu-rich_rpt_typical-subtyp.
DR InterPro; IPR032675; LRR_dom_sf.
DR Pfam; PF13855; LRR_8; 2.
DR SMART; SM00369; LRR_TYP; 4.
DR SMART; SM00082; LRRCT; 1.
DR SUPFAM; SSF48726; SSF48726; 1.
DR PROSITE; PS50835; IG_LIKE; 1.
DR PROSITE; PS51450; LRR; 5.
PE 1: Evidence at protein level;
KW Cell membrane; Developmental protein; Disulfide bond; Glycoprotein;
KW Immunoglobulin domain; Leucine-rich repeat; Membrane; Neurogenesis;
KW Phosphoprotein; Reference proteome; Repeat; Signal; Transmembrane;
KW Transmembrane helix.
FT SIGNAL 1..19
FT /evidence="ECO:0000255"
FT CHAIN 20..745
FT /note="Immunoglobulin superfamily containing leucine-rich
FT repeat protein 2"
FT /id="PRO_0000317499"
FT TOPO_DOM 20..589
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 590..610
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 611..745
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 20..51
FT /note="LRRNT"
FT REPEAT 52..73
FT /note="LRR 1"
FT REPEAT 76..97
FT /note="LRR 2"
FT REPEAT 100..123
FT /note="LRR 3"
FT REPEAT 124..145
FT /note="LRR 4"
FT REPEAT 148..169
FT /note="LRR 5"
FT DOMAIN 181..232
FT /note="LRRCT"
FT DOMAIN 233..372
FT /note="Ig-like"
FT REGION 290..328
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 376..423
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 654..697
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 668..684
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 719
FT /note="Phosphotyrosine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 720
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT CARBOHYD 52
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 73
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 121
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 338
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 365
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 474
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 563
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 260..356
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT CONFLICT 460
FT /note="G -> D (in Ref. 2; BAC98177)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 745 AA; 79758 MW; D224B2F1B6DE8B28 CRC64;
MGPFGALCLA WALLGVVRAC PEPCACVDKY AHQFADCAYK ELREVPEGLP ANVTTLSLSA
NKITVLRRGA FVNVTQVTSL WLAHSEVRTV ESGALAVLSQ LKNLDLSHNL ISNFPWSDLR
NLSALQLLKM NHNRLGSLPR DALGALPDLR SLRINNNRLR TLEPGTFDAL SALSHLQLYH
NPFHCSCGLV WLQAWAASTR VSLPEPDSIA CASPPELQGV PVHRLPALPC APPSVRLSAE
PPPEAPGTPL RAGLAFMLHC VAEGHPTPRL QWQLQIPGGT VVLVPPVLSK EEDGGDKVED
GEGDGDEDLP TQTEAPTPTP APAWPAPPAT PRFLALANGS LLVPLLSAKE AGIYTCRAHN
ELGTNSTSLR VTVAAAGPPK HAPGTGEEPD AQVPTSERKA TTKGRSNSVL PFKPEGKTKG
QGLARVSVLG EIEAELEETD EGEQMEGQIP ADPMGEKHCG HGDPSRYVSN HAFNQSSDLK
PHVFELGVIA LDVAEREARV QLTPLAARWG PGPDGASGAR RPGRRPLRLL YLCPAGGGTA
VQWSRVEEGV NAYWFRGLRP GTNYSVCLAL AGEACHVQVV FSTKKELPSL LVIVTVSVFL
LVLATVPLLG AACCHLLAKH PGKPYRLILR PQAPDPMEKR IAADFDPRAS YLESEKSYPA
RGEAGGEEPE EVPEEGLDED VEQGDPSGDL QREESLAGCS LVESQSKANQ EEFEAGSEYS
DRLPLGAEAV NIAQEINGNY RQTAG
