LRIG2_MOUSE
ID LRIG2_MOUSE Reviewed; 1054 AA.
AC Q52KR2; Q69ZY8;
DT 16-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT 24-MAY-2005, sequence version 1.
DT 03-AUG-2022, entry version 141.
DE RecName: Full=Leucine-rich repeats and immunoglobulin-like domains protein 2;
DE Short=LIG-2;
DE Flags: Precursor;
GN Name=Lrig2; Synonyms=Kiaa0806;
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 [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Fetal brain;
RX PubMed=15368895; DOI=10.1093/dnares/11.3.205;
RA Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S.,
RA Saga Y., Seino S., Nishimura M., Kaisho T., Hoshino K., Kitamura H.,
RA Nagase T., Ohara O., Koga H.;
RT "Prediction of the coding sequences of mouse homologues of KIAA gene: IV.
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. 11:205-218(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
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 [3]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-905, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=15592455; DOI=10.1038/nbt1046;
RA Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H.,
RA Zha X.-M., Polakiewicz R.D., Comb M.J.;
RT "Immunoaffinity profiling of tyrosine phosphorylation in cancer cells.";
RL Nat. Biotechnol. 23:94-101(2005).
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Single-pass type I
CC membrane protein {ECO:0000250}. Cytoplasm {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q52KR2-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q52KR2-2; Sequence=VSP_014993, VSP_057113;
CC -!- MISCELLANEOUS: [Isoform 2]: May be due to a competing acceptor splice
CC site. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAD32308.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AK173030; BAD32308.1; ALT_INIT; mRNA.
DR EMBL; BC094228; AAH94228.1; -; mRNA.
DR CCDS; CCDS17701.1; -. [Q52KR2-1]
DR RefSeq; NP_001020238.1; NM_001025067.2. [Q52KR2-1]
DR RefSeq; NP_001297627.1; NM_001310698.1.
DR AlphaFoldDB; Q52KR2; -.
DR SMR; Q52KR2; -.
DR BioGRID; 234657; 3.
DR IntAct; Q52KR2; 1.
DR STRING; 10090.ENSMUSP00000035999; -.
DR GlyGen; Q52KR2; 13 sites.
DR iPTMnet; Q52KR2; -.
DR PhosphoSitePlus; Q52KR2; -.
DR MaxQB; Q52KR2; -.
DR PaxDb; Q52KR2; -.
DR PRIDE; Q52KR2; -.
DR ProteomicsDB; 252673; -. [Q52KR2-1]
DR ProteomicsDB; 252674; -. [Q52KR2-2]
DR Antibodypedia; 2748; 143 antibodies from 19 providers.
DR DNASU; 269473; -.
DR Ensembl; ENSMUST00000046316; ENSMUSP00000035999; ENSMUSG00000032913. [Q52KR2-1]
DR Ensembl; ENSMUST00000199070; ENSMUSP00000142373; ENSMUSG00000032913. [Q52KR2-2]
DR GeneID; 269473; -.
DR KEGG; mmu:269473; -.
DR UCSC; uc008que.1; mouse. [Q52KR2-1]
DR UCSC; uc012cvk.1; mouse. [Q52KR2-2]
DR CTD; 9860; -.
DR MGI; MGI:2443718; Lrig2.
DR VEuPathDB; HostDB:ENSMUSG00000032913; -.
DR eggNOG; KOG4194; Eukaryota.
DR GeneTree; ENSGT00940000158791; -.
DR HOGENOM; CLU_000288_18_24_1; -.
DR InParanoid; Q52KR2; -.
DR OMA; MSCHRLQ; -.
DR OrthoDB; 161719at2759; -.
DR PhylomeDB; Q52KR2; -.
DR TreeFam; TF325380; -.
DR BioGRID-ORCS; 269473; 2 hits in 72 CRISPR screens.
DR ChiTaRS; Lrig2; mouse.
DR PRO; PR:Q52KR2; -.
DR Proteomes; UP000000589; Chromosome 3.
DR RNAct; Q52KR2; protein.
DR Bgee; ENSMUSG00000032913; Expressed in spermatocyte and 231 other tissues.
DR ExpressionAtlas; Q52KR2; baseline and differential.
DR Genevisible; Q52KR2; MM.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0031012; C:extracellular matrix; IBA:GO_Central.
DR GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR GO; GO:0030426; C:growth cone; IDA:MGI.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0097708; C:intracellular vesicle; IDA:MGI.
DR GO; GO:0016020; C:membrane; IDA:MGI.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005102; F:signaling receptor binding; IPI:MGI.
DR GO; GO:0060384; P:innervation; IGI:MGI.
DR GO; GO:0006509; P:membrane protein ectodomain proteolysis; IMP:MGI.
DR GO; GO:0048681; P:negative regulation of axon regeneration; IMP:MGI.
DR GO; GO:0051045; P:negative regulation of membrane protein ectodomain proteolysis; IMP:MGI.
DR GO; GO:0010977; P:negative regulation of neuron projection development; IGI:MGI.
DR GO; GO:2000010; P:positive regulation of protein localization to cell surface; IMP:MGI.
DR GO; GO:0034394; P:protein localization to cell surface; IMP:MGI.
DR GO; GO:0048679; P:regulation of axon regeneration; IGI:MGI.
DR GO; GO:2001222; P:regulation of neuron migration; IGI:MGI.
DR GO; GO:0010640; P:regulation of platelet-derived growth factor receptor signaling pathway; IGI:MGI.
DR GO; GO:0007605; P:sensory perception of sound; IMP:MGI.
DR Gene3D; 2.60.40.10; -; 3.
DR Gene3D; 3.80.10.10; -; 2.
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; IPR013098; Ig_I-set.
DR InterPro; IPR003599; Ig_sub.
DR InterPro; IPR003598; Ig_sub2.
DR InterPro; IPR001611; Leu-rich_rpt.
DR InterPro; IPR003591; Leu-rich_rpt_typical-subtyp.
DR InterPro; IPR032675; LRR_dom_sf.
DR Pfam; PF07679; I-set; 2.
DR Pfam; PF13855; LRR_8; 4.
DR Pfam; PF01463; LRRCT; 1.
DR SMART; SM00409; IG; 3.
DR SMART; SM00408; IGc2; 3.
DR SMART; SM00369; LRR_TYP; 12.
DR SMART; SM00082; LRRCT; 1.
DR SUPFAM; SSF48726; SSF48726; 3.
DR PROSITE; PS50835; IG_LIKE; 3.
DR PROSITE; PS51450; LRR; 15.
PE 1: Evidence at protein level;
KW Alternative splicing; Cell membrane; Cytoplasm; Disulfide bond;
KW Glycoprotein; Immunoglobulin domain; Leucine-rich repeat; Membrane;
KW Phosphoprotein; Reference proteome; Repeat; Signal; Transmembrane;
KW Transmembrane helix.
FT SIGNAL 1..39
FT /evidence="ECO:0000255"
FT CHAIN 40..1054
FT /note="Leucine-rich repeats and immunoglobulin-like domains
FT protein 2"
FT /id="PRO_0000014830"
FT TRANSMEM 807..827
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 40..74
FT /note="LRRNT"
FT REPEAT 75..96
FT /note="LRR 1"
FT REPEAT 97..118
FT /note="LRR 2"
FT REPEAT 120..141
FT /note="LRR 3"
FT REPEAT 144..165
FT /note="LRR 4"
FT REPEAT 167..188
FT /note="LRR 5"
FT REPEAT 192..213
FT /note="LRR 6"
FT REPEAT 215..236
FT /note="LRR 7"
FT REPEAT 239..260
FT /note="LRR 8"
FT REPEAT 263..284
FT /note="LRR 9"
FT REPEAT 287..308
FT /note="LRR 10"
FT REPEAT 311..332
FT /note="LRR 11"
FT REPEAT 335..356
FT /note="LRR 12"
FT REPEAT 359..381
FT /note="LRR 13"
FT REPEAT 386..407
FT /note="LRR 14"
FT REPEAT 410..431
FT /note="LRR 15"
FT DOMAIN 442..493
FT /note="LRRCT"
FT DOMAIN 497..596
FT /note="Ig-like C2-type 1"
FT DOMAIN 601..690
FT /note="Ig-like C2-type 2"
FT DOMAIN 695..784
FT /note="Ig-like C2-type 3"
FT MOD_RES 905
FT /note="Phosphotyrosine"
FT /evidence="ECO:0007744|PubMed:15592455"
FT CARBOHYD 90
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 120
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 172
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 188
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 273
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 440
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 467
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 513
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 570
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 588
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 686
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 727
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1024
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 518..579
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 622..674
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 716..765
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT VAR_SEQ 79..436
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15368895"
FT /id="VSP_014993"
FT VAR_SEQ 843..849
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15368895"
FT /id="VSP_057113"
SQ SEQUENCE 1054 AA; 117863 MW; 334B7250E2DF168E CRC64;
MAAAPRGIWE QRRLGCGLGP LARLLILAQA LRLLPAARAG LCPAPCACRL PLLDCSRRKL
PAPSWRALSG PLPSDISSLD LSHNRLSNWN NTLESQTLQE VKMNYNELTE IPYFGEPTPN
ITLLSLVHNL IPEINAEAFE LYSALESLDL SSNIISEIKT SSFPRMSLKY LNLSNNRIST
LEAGCFDNLS DSLLVVKLNR NRISMIPPKV FKLPHLQFLE LKRNRIKIVE GLTFQGLDSL
RSLKMQRNGI SKLKDGAFFG LNNMEELELE HNNLTGVNKG WLYGLRMLQQ LYMSQNAIEK
ISPDAWEFCQ RLSELDLSYN QLTRLDESAF VGLSLLERLN LGDNRVTHIA DGVFRFLSNL
QTLDLRNNDI SWAIEDASEA FSGLKSLTKL ILQGNRIKSV TQKAFIGLES LEYLDLNNNA
IMSIQENAFS QTHLKGLVLN TSSLLCDCHL KWLLQWLVDN NFHHSVNVSC AHPEWLAGQS
ILNVDLKDFV CDDFLKPQIR THPESTIALR GVNVTLTCTA VSSSDSPMST IWRKDSEILY
DVDIENFVRY RQQDGEALEY TSVLRLFSVN FTDEGKYQCI VTNHFGSNYS QKAKLTVNEM
PSFLKTPMDL TIRTGAMARL ECAAEGHPTP QISWQKDGGT DFPAARERRM HVMPEDDVFF
IANVKIEDMG IYSCMAQNIA GGLSANASLT VLETPSFIRP LEDKTVTRGE TAVLQCIAGG
SPAPRLNWTK DDGPLLVTER HFFAAANQLL IIVDAGLEDA GKYTCLMSNT LGTERGHIYL
NVISSPNCDS SQSSIGHEDD GWTTVGIVII VVVCCVVGTS LIWVIVIYHM RRKNEDYSIT
NTEELNLPAD IPSYLSSQGT LSEPQEGYSN SEAGSHQQLM PPANGYTHRG TDGGAGTRVI
CSDCYDNANI YSRTREYCPY TYIAEEDVLD QALSSLMVQM PKETFLSHPP QDAANLESLI
PSAEREPAAF PTNHERMTEN LPFSQRSSEI FQRPLWNMNR ELGLLPFSQQ PVLESPELTE
RDPNCSSPVT CRRLHDHAFD FSRTRIIQDG TEGT
