LOCUS       NP_001020238            1054 aa            linear   ROD 05-JUN-2024
DEFINITION  leucine-rich repeats and immunoglobulin-like domains protein 2
            isoform 1 precursor [Mus musculus].
ACCESSION   NP_001020238 XP_194114
VERSION     NP_001020238.1
DBSOURCE    REFSEQ: accession NM_001025067.2
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Mus musculus (house mouse)
  ORGANISM  Mus musculus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Mus; Mus.
REFERENCE   1  (residues 1 to 1054)
  AUTHORS   Li,Z.Q., Liao,W.J., Sun,B.L., Luo,Z.W., Zhong,N.S., Wu,J.B.,
            Liu,Z.L. and Liu,J.M.
  TITLE     LRIG2 regulates cell proliferation, migration and apoptosis of
            osteosarcoma
  JOURNAL   BMC Cancer 22 (1), 1029 (2022)
   PUBMED   36183058
  REMARK    GeneRIF: LRIG2 regulates cell proliferation, migration and
            apoptosis of osteosarcoma.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 1054)
  AUTHORS   Roberts,N.A., Hilton,E.N., Lopes,F.M., Singh,S., Randles,M.J.,
            Gardiner,N.J., Chopra,K., Coletta,R., Bajwa,Z., Hall,R.J.,
            Yue,W.W., Schaefer,F., Weber,S., Henriksson,R., Stuart,H.M.,
            Hedman,H., Newman,W.G. and Woolf,A.S.
  TITLE     Lrig2 and Hpse2, mutated in urofacial syndrome, pattern nerves in
            the urinary bladder
  JOURNAL   Kidney Int 95 (5), 1138-1152 (2019)
   PUBMED   30885509
  REMARK    GeneRIF: Mice with homozygous mutations in either Lrig2 or Hpse2
            had increased nerve density within the urinary bladder body and
            decreased nerve density around the urinary outflow tract.
            Observations provide evidence that a peripheral neuropathy is
            central to the pathobiology of functional bladder outlet
            obstruction in urofacial syndrome and emphasize the importance of
            LRIG2 and Hpse2 for nerve patterning in the urinary tract.
REFERENCE   3  (residues 1 to 1054)
  AUTHORS   van Erp,S., van den Heuvel,D.M.A., Fujita,Y., Robinson,R.A.,
            Hellemons,A.J.C.G.M., Adolfs,Y., Van Battum,E.Y., Blokhuis,A.M.,
            Kuijpers,M., Demmers,J.A.A., Hedman,H., Hoogenraad,C.C.,
            Siebold,C., Yamashita,T. and Pasterkamp,R.J.
  TITLE     Lrig2 Negatively Regulates Ectodomain Shedding of Axon Guidance
            Receptors by ADAM Proteases
  JOURNAL   Dev Cell 35 (5), 537-552 (2015)
   PUBMED   26651291
  REMARK    GeneRIF: Lrig2 has a role in negative regulation of ectodomain
            shedding of axon guidance receptors by ADAM17 protease
REFERENCE   4  (residues 1 to 1054)
  AUTHORS   Stuart,H.M., Roberts,N.A., Hilton,E.N., McKenzie,E.A., Daly,S.B.,
            Hadfield,K.D., Rahal,J.S., Gardiner,N.J., Tanley,S.W., Lewis,M.A.,
            Sites,E., Angle,B., Alves,C., Lourenco,T., Rodrigues,M., Calado,A.,
            Amado,M., Guerreiro,N., Serras,I., Beetz,C., Varga,R.E.,
            Silay,M.S., Darlow,J.M., Dobson,M.G., Barton,D.E., Hunziker,M.,
            Puri,P., Feather,S.A., Goodship,J.A., Goodship,T.H., Lambert,H.J.,
            Cordell,H.J., Saggar,A., Kinali,M., Lorenz,C., Moeller,K.,
            Schaefer,F., Bayazit,A.K., Weber,S., Newman,W.G. and Woolf,A.S.
  CONSRTM   UK VUR Study Group; 4C Study Group
  TITLE     Urinary tract effects of HPSE2 mutations
  JOURNAL   J Am Soc Nephrol 26 (4), 797-804 (2015)
   PUBMED   25145936
REFERENCE   5  (residues 1 to 1054)
  AUTHORS   Gu,Z., Imai,F., Kim,I.J., Fujita,H., Katayama,Ki., Mori,K.,
            Yoshihara,Y. and Yoshida,Y.
  TITLE     Expression of the immunoglobulin superfamily cell adhesion
            molecules in the developing spinal cord and dorsal root ganglion
  JOURNAL   PLoS One 10 (3), e0121550 (2015)
   PUBMED   25826454
  REMARK    Publication Status: Online-Only
REFERENCE   6  (residues 1 to 1054)
  AUTHORS   Rondahl,V., Holmlund,C., Karlsson,T., Wang,B., Faraz,M.,
            Henriksson,R. and Hedman,H.
  TITLE     Lrig2-deficient mice are protected against PDGFB-induced glioma
  JOURNAL   PLoS One 8 (9), e73635 (2013)
   PUBMED   24023893
  REMARK    GeneRIF: phenotype of Lrig2E12-/- mice showed that Lrig2 was a
            promoter of PDGFB-induced glioma
            Publication Status: Online-Only
REFERENCE   7  (residues 1 to 1054)
  AUTHORS   Homma,S., Shimada,T., Hikake,T. and Yaginuma,H.
  TITLE     Expression pattern of LRR and Ig domain-containing protein (LRRIG
            protein) in the early mouse embryo
  JOURNAL   Gene Expr Patterns 9 (1), 1-26 (2009)
   PUBMED   18848646
REFERENCE   8  (residues 1 to 1054)
  AUTHORS   Blackshaw,S., Harpavat,S., Trimarchi,J., Cai,L., Huang,H.,
            Kuo,W.P., Weber,G., Lee,K., Fraioli,R.E., Cho,S.H., Yung,R.,
            Asch,E., Ohno-Machado,L., Wong,W.H. and Cepko,C.L.
  TITLE     Genomic analysis of mouse retinal development
  JOURNAL   PLoS Biol 2 (9), E247 (2004)
   PUBMED   15226823
REFERENCE   9  (residues 1 to 1054)
  AUTHORS   Okazaki,N., F-Kikuno,R., Ohara,R., Inamoto,S., Koseki,H.,
            Hiraoka,S., Saga,Y., Seino,S., Nishimura,M., Kaisho,T., Hoshino,K.,
            Kitamura,H., Nagase,T., Ohara,O. and Koga,H.
  TITLE     Prediction of the coding sequences of mouse homologues of KIAA
            gene: IV. The complete nucleotide sequences of 500 mouse
            KIAA-homologous cDNAs identified by screening of terminal sequences
            of cDNA clones randomly sampled from size-fractionated libraries
  JOURNAL   DNA Res 11 (3), 205-218 (2004)
   PUBMED   15368895
REFERENCE   10 (residues 1 to 1054)
  AUTHORS   Stryke,D., Kawamoto,M., Huang,C.C., Johns,S.J., King,L.A.,
            Harper,C.A., Meng,E.C., Lee,R.E., Yee,A., L'Italien,L.,
            Chuang,P.T., Young,S.G., Skarnes,W.C., Babbitt,P.C. and Ferrin,T.E.
  TITLE     BayGenomics: a resource of insertional mutations in mouse embryonic
            stem cells
  JOURNAL   Nucleic Acids Res 31 (1), 278-281 (2003)
   PUBMED   12520002
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            BY205369.1, BC094228.1 and CN532345.1.
            
            On Jun 30, 2005 this sequence version replaced XP_194114.3.
            
            Transcript Variant: This variant (1) represents the longer
            transcript and encodes the longer isoform (1).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC094228.1, SRR10223971.4256.1
                                           [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMN00849374,
                                           SAMN00849375 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..1054
                     /organism="Mus musculus"
                     /strain="C57BL/6"
                     /db_xref="taxon:10090"
                     /chromosome="3"
                     /map="3 45.62 cM"
     Protein         1..1054
                     /product="leucine-rich repeats and immunoglobulin-like
                     domains protein 2 isoform 1 precursor"
                     /note="leucine-rich repeats and immunoglobulin-like
                     domains protein 2"
                     /calculated_mol_wt=113716
     sig_peptide     1..39
                     /note="/evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q52KR2.1)"
                     /calculated_mol_wt=4165
     mat_peptide     40..1054
                     /product="Leucine-rich repeats and immunoglobulin-like
                     domains protein 2. /id=PRO_0000014830"
                     /note="propagated from UniProtKB/Swiss-Prot (Q52KR2.1)"
                     /calculated_mol_wt=113716
     Region          53..75
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275378"
     Region          72..462
                     /region_name="LRR"
                     /note="Leucine-rich repeat (LRR) protein [Transcription];
                     COG4886"
                     /db_xref="CDD:443914"
     Region          75..96
                     /region_name="LRR 1"
                     /note="propagated from UniProtKB/Swiss-Prot (Q52KR2.1)"
     Site            90
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q52KR2.1)"
     Region          97..118
                     /region_name="LRR 2"
                     /note="propagated from UniProtKB/Swiss-Prot (Q52KR2.1)"
     Region          98..120
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          120..141
                     /region_name="LRR 3"
                     /note="propagated from UniProtKB/Swiss-Prot (Q52KR2.1)"
     Site            120
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q52KR2.1)"
     Region          121..144
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          144..165
                     /region_name="LRR 4"
                     /note="propagated from UniProtKB/Swiss-Prot (Q52KR2.1)"
     Region          145..167
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          167..188
                     /region_name="LRR 5"
                     /note="propagated from UniProtKB/Swiss-Prot (Q52KR2.1)"
     Region          168..192
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Site            172
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q52KR2.1)"
     Site            188
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q52KR2.1)"
     Region          192..213
                     /region_name="LRR 6"
                     /note="propagated from UniProtKB/Swiss-Prot (Q52KR2.1)"
     Region          193..215
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          215..236
                     /region_name="LRR 7"
                     /note="propagated from UniProtKB/Swiss-Prot (Q52KR2.1)"
     Region          216..239
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          239..260
                     /region_name="LRR 8"
                     /note="propagated from UniProtKB/Swiss-Prot (Q52KR2.1)"
     Region          240..263
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          263..284
                     /region_name="LRR 9"
                     /note="propagated from UniProtKB/Swiss-Prot (Q52KR2.1)"
     Region          264..287
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Site            273
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q52KR2.1)"
     Region          287..308
                     /region_name="LRR 10"
                     /note="propagated from UniProtKB/Swiss-Prot (Q52KR2.1)"
     Region          288..311
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          311..332
                     /region_name="LRR 11"
                     /note="propagated from UniProtKB/Swiss-Prot (Q52KR2.1)"
     Region          312..335
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          335..356
                     /region_name="LRR 12"
                     /note="propagated from UniProtKB/Swiss-Prot (Q52KR2.1)"
     Region          336..359
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          359..381
                     /region_name="LRR 13"
                     /note="propagated from UniProtKB/Swiss-Prot (Q52KR2.1)"
     Region          360..384
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          386..407
                     /region_name="LRR 14"
                     /note="propagated from UniProtKB/Swiss-Prot (Q52KR2.1)"
     Region          387..410
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          410..431
                     /region_name="LRR 15"
                     /note="propagated from UniProtKB/Swiss-Prot (Q52KR2.1)"
     Region          411..430
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Site            440
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q52KR2.1)"
     Region          444..492
                     /region_name="LRRCT"
                     /note="Leucine rich repeat C-terminal domain; smart00082"
                     /db_xref="CDD:214507"
     Site            467
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q52KR2.1)"
     Region          496..583
                     /region_name="Ig_3"
                     /note="Immunoglobulin domain; pfam13927"
                     /db_xref="CDD:464046"
     Site            513
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q52KR2.1)"
     Site            570
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q52KR2.1)"
     Site            588
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q52KR2.1)"
     Region          602..692
                     /region_name="IgI_LRIG1-like"
                     /note="Immunoglobulin (Ig)-like ectodomain of the LRIG1
                     (Leucine-rich Repeats And Immunoglobulin-like Domains
                     Protein 1) and similar proteins; member of the I-set of
                     IgSF domains; cd05763"
                     /db_xref="CDD:409420"
     Region          602..605
                     /region_name="Ig strand A"
                     /note="Ig strand A [structural motif]"
                     /db_xref="CDD:409420"
     Region          609..613
                     /region_name="Ig strand A'"
                     /note="Ig strand A' [structural motif]"
                     /db_xref="CDD:409420"
     Region          616..625
                     /region_name="Ig strand B"
                     /note="Ig strand B [structural motif]"
                     /db_xref="CDD:409420"
     Region          631..636
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:409420"
     Region          639..641
                     /region_name="Ig strand C'"
                     /note="Ig strand C' [structural motif]"
                     /db_xref="CDD:409420"
     Region          649..653
                     /region_name="Ig strand D"
                     /note="Ig strand D [structural motif]"
                     /db_xref="CDD:409420"
     Region          657..664
                     /region_name="Ig strand E"
                     /note="Ig strand E [structural motif]"
                     /db_xref="CDD:409420"
     Region          670..678
                     /region_name="Ig strand F"
                     /note="Ig strand F [structural motif]"
                     /db_xref="CDD:409420"
     Region          681..692
                     /region_name="Ig strand G"
                     /note="Ig strand G [structural motif]"
                     /db_xref="CDD:409420"
     Site            686
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q52KR2.1)"
     Region          695..782
                     /region_name="I-set"
                     /note="Immunoglobulin I-set domain; pfam07679"
                     /db_xref="CDD:400151"
     Region          712..716
                     /region_name="Ig strand B"
                     /note="Ig strand B [structural motif]"
                     /db_xref="CDD:409353"
     Region          725..729
                     /region_name="Ig strand C"
                     /note="Ig strand C [structural motif]"
                     /db_xref="CDD:409353"
     Site            727
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q52KR2.1)"
     Region          748..752
                     /region_name="Ig strand E"
                     /note="Ig strand E [structural motif]"
                     /db_xref="CDD:409353"
     Region          762..767
                     /region_name="Ig strand F"
                     /note="Ig strand F [structural motif]"
                     /db_xref="CDD:409353"
     Region          775..778
                     /region_name="Ig strand G"
                     /note="Ig strand G [structural motif]"
                     /db_xref="CDD:409353"
     Site            807..827
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q52KR2.1)"
     Site            905
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0007744|PubMed:15592455; propagated from
                     UniProtKB/Swiss-Prot (Q52KR2.1)"
     Site            1024
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (Q52KR2.1)"
     CDS             1..1054
                     /gene="Lrig2"
                     /gene_synonym="4632419I10Rik; LIG-2"
                     /coded_by="NM_001025067.2:228..3392"
                     /note="isoform 1 precursor is encoded by transcript
                     variant 1"
                     /db_xref="CCDS:CCDS17701.1"
                     /db_xref="GeneID:269473"
                     /db_xref="MGI:MGI:2443718"
ORIGIN      
        1 maaaprgiwe qrrlgcglgp larllilaqa lrllpaarag lcpapcacrl plldcsrrkl
       61 papswralsg plpsdissld lshnrlsnwn ntlesqtlqe vkmnynelte ipyfgeptpn
      121 itllslvhnl ipeinaeafe lysalesldl ssniiseikt ssfprmslky lnlsnnrist
      181 leagcfdnls dsllvvklnr nrismippkv fklphlqfle lkrnrikive gltfqgldsl
      241 rslkmqrngi sklkdgaffg lnnmeelele hnnltgvnkg wlyglrmlqq lymsqnaiek
      301 ispdawefcq rlseldlsyn qltrldesaf vglsllerln lgdnrvthia dgvfrflsnl
      361 qtldlrnndi swaiedasea fsglksltkl ilqgnriksv tqkafigles leyldlnnna
      421 imsiqenafs qthlkglvln tssllcdchl kwllqwlvdn nfhhsvnvsc ahpewlagqs
      481 ilnvdlkdfv cddflkpqir thpestialr gvnvtltcta vsssdspmst iwrkdseily
      541 dvdienfvry rqqdgealey tsvlrlfsvn ftdegkyqci vtnhfgsnys qkakltvnem
      601 psflktpmdl tirtgamarl ecaaeghptp qiswqkdggt dfpaarerrm hvmpeddvff
      661 ianvkiedmg iyscmaqnia gglsanaslt vletpsfirp ledktvtrge tavlqciagg
      721 spaprlnwtk ddgpllvter hffaaanqll iivdagleda gkytclmsnt lgterghiyl
      781 nvisspncds sqssighedd gwttvgivii vvvccvvgts liwviviyhm rrknedysit
      841 nteelnlpad ipsylssqgt lsepqegysn seagshqqlm ppangythrg tdggagtrvi
      901 csdcydnani ysrtreycpy tyiaeedvld qalsslmvqm pketflshpp qdaanlesli
      961 psaerepaaf ptnhermten lpfsqrssei fqrplwnmnr elgllpfsqq pvlespelte
     1021 rdpncsspvt crrlhdhafd fsrtriiqdg tegt
//
