LRIG3_MOUSE
ID LRIG3_MOUSE Reviewed; 1117 AA.
AC Q6P1C6; Q6ZPE6; Q8BRF0; Q8BS51; Q8C5E4;
DT 16-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 147.
DE RecName: Full=Leucine-rich repeats and immunoglobulin-like domains protein 3;
DE Short=LIG-3;
DE Flags: Precursor;
GN Name=Lrig3; Synonyms=Kiaa3016;
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], AND TISSUE SPECIFICITY.
RX PubMed=15203213; DOI=10.1016/j.ygeno.2004.01.013;
RA Guo D., Holmlund C., Henriksson R., Hedman H.;
RT "The LRIG gene family has three vertebrate paralogs widely expressed in
RT human and mouse tissues and a homolog in Ascidiacea.";
RL Genomics 84:157-165(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Eye;
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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-79 AND 718-1117.
RC STRAIN=C57BL/6J; TISSUE=Embryo, and Embryonic testis;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 254-1117.
RX PubMed=12693553; DOI=10.1093/dnares/10.1.35;
RA Okazaki N., Kikuno R., Ohara R., Inamoto S., Aizawa H., Yuasa S.,
RA Nakajima D., Nagase T., Ohara O., Koga H.;
RT "Prediction of the coding sequences of mouse homologues of KIAA gene: II.
RT The complete nucleotide sequences of 400 mouse KIAA-homologous cDNAs
RT identified by screening of terminal sequences of cDNA clones randomly
RT sampled from size-fractionated libraries.";
RL DNA Res. 10:35-48(2003).
RN [5]
RP DISRUPTION PHENOTYPE, FUNCTION, AND DEVELOPMENTAL STAGE.
RX PubMed=19004851; DOI=10.1242/dev.029330;
RA Abraira V.E., Del Rio T., Tucker A.F., Slonimsky J., Keirnes H.L.,
RA Goodrich L.V.;
RT "Cross-repressive interactions between Lrig3 and netrin 1 shape the
RT architecture of the inner ear.";
RL Development 135:4091-4099(2008).
RN [6]
RP DISRUPTION PHENOTYPE, FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH
RP EGFR; ERBB2 AND ERBB4.
RX PubMed=20126551; DOI=10.1371/journal.pone.0008981;
RA Abraira V.E., Satoh T., Fekete D.M., Goodrich L.V.;
RT "Vertebrate Lrig3-ErbB interactions occur in vitro but are unlikely to play
RT a role in Lrig3-dependent inner ear morphogenesis.";
RL PLoS ONE 5:E8981-E8981(2010).
RN [7]
RP X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) OF 490-600.
RG Joint center for structural genomics (JCSG);
RT "Crystal structure of an immunoglobulin I-set domain of LRIG3 protein
RT (LRIG3) from Mus musculus at 1.70 A resolution.";
RL Submitted (JUL-2011) to the PDB data bank.
CC -!- FUNCTION: Plays a role in craniofacial and inner ear morphogenesis
CC during embryonic development. Acts within the otic vesicle epithelium
CC to control formation of the lateral semicircular canal in the inner
CC ear, possibly by restricting the expression of NTN1.
CC {ECO:0000269|PubMed:19004851, ECO:0000269|PubMed:20126551}.
CC -!- SUBUNIT: Interacts with EGFR, ERBB2 and ERBB4 (in vitro).
CC {ECO:0000269|PubMed:20126551}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:20126551};
CC Single-pass type I membrane protein {ECO:0000269|PubMed:20126551}.
CC Cytoplasmic vesicle membrane {ECO:0000269|PubMed:20126551}; Single-pass
CC type I membrane protein {ECO:0000269|PubMed:20126551}. Note=Detected in
CC cytoplasmic vesicles when coexpressed with ERBB4.
CC -!- TISSUE SPECIFICITY: Widely expressed. {ECO:0000269|PubMed:15203213}.
CC -!- DEVELOPMENTAL STAGE: Detected in the lateral wall of the otic vesicle
CC at 10.5 dpc. Enriched in lateral pouch epithelium at 12.5 dpc.
CC {ECO:0000269|PubMed:19004851}.
CC -!- DISRUPTION PHENOTYPE: Mice display circling and head tossing behavior,
CC due to a defect in inner ear morphogenesis. In mutants, fusion of the
CC canal pouches starts earlier than normal and involves an abnormally
CC large region, leading to truncation of the lateral semicircular canal
CC in the inner ear. Nevertheless, hearing seems to be normal. Mutant mice
CC also display craniofacial deformities, and especially a dramatically
CC shortened snout. {ECO:0000269|PubMed:19004851,
CC ECO:0000269|PubMed:20126551}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAC32175.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=BAC98291.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AY505341; AAR98630.1; -; mRNA.
DR EMBL; BC065142; AAH65142.1; -; mRNA.
DR EMBL; AK044994; BAC32175.1; ALT_INIT; mRNA.
DR EMBL; AK078783; BAC37394.1; -; mRNA.
DR EMBL; AK129481; BAC98291.1; ALT_FRAME; mRNA.
DR CCDS; CCDS24219.1; -.
DR RefSeq; NP_796126.4; NM_177152.5.
DR PDB; 3SO5; X-ray; 1.70 A; A/B=490-600.
DR PDBsum; 3SO5; -.
DR AlphaFoldDB; Q6P1C6; -.
DR SMR; Q6P1C6; -.
DR STRING; 10090.ENSMUSP00000074360; -.
DR GlyGen; Q6P1C6; 7 sites.
DR iPTMnet; Q6P1C6; -.
DR PhosphoSitePlus; Q6P1C6; -.
DR PaxDb; Q6P1C6; -.
DR PRIDE; Q6P1C6; -.
DR ProteomicsDB; 252675; -.
DR Antibodypedia; 2484; 153 antibodies from 25 providers.
DR DNASU; 320398; -.
DR Ensembl; ENSMUST00000074807; ENSMUSP00000074360; ENSMUSG00000020105.
DR GeneID; 320398; -.
DR KEGG; mmu:320398; -.
DR UCSC; uc007hhc.2; mouse.
DR CTD; 121227; -.
DR MGI; MGI:2443955; Lrig3.
DR VEuPathDB; HostDB:ENSMUSG00000020105; -.
DR eggNOG; KOG0619; Eukaryota.
DR eggNOG; KOG4194; Eukaryota.
DR GeneTree; ENSGT00940000157098; -.
DR HOGENOM; CLU_000288_18_24_1; -.
DR InParanoid; Q6P1C6; -.
DR OMA; WIIEDQS; -.
DR OrthoDB; 161719at2759; -.
DR PhylomeDB; Q6P1C6; -.
DR TreeFam; TF325380; -.
DR BioGRID-ORCS; 320398; 2 hits in 74 CRISPR screens.
DR ChiTaRS; Lrig3; mouse.
DR PRO; PR:Q6P1C6; -.
DR Proteomes; UP000000589; Chromosome 10.
DR RNAct; Q6P1C6; protein.
DR Bgee; ENSMUSG00000020105; Expressed in manus and 199 other tissues.
DR Genevisible; Q6P1C6; MM.
DR GO; GO:0030659; C:cytoplasmic vesicle membrane; IEA:UniProtKB-SubCell.
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:0032474; P:otolith morphogenesis; IGI: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 SMART; SM00409; IG; 3.
DR SMART; SM00408; IGc2; 3.
DR SMART; SM00369; LRR_TYP; 14.
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 3D-structure; Cell membrane; Cytoplasmic vesicle; Developmental protein;
KW Disulfide bond; Glycoprotein; Immunoglobulin domain; Leucine-rich repeat;
KW Membrane; Reference proteome; Repeat; Signal; Transmembrane;
KW Transmembrane helix.
FT SIGNAL 1..24
FT /evidence="ECO:0000255"
FT CHAIN 25..1117
FT /note="Leucine-rich repeats and immunoglobulin-like domains
FT protein 3"
FT /id="PRO_0000014832"
FT TRANSMEM 810..830
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 38..74
FT /note="LRRNT"
FT REPEAT 75..98
FT /note="LRR 1"
FT REPEAT 99..120
FT /note="LRR 2"
FT REPEAT 122..143
FT /note="LRR 3"
FT REPEAT 146..168
FT /note="LRR 4"
FT REPEAT 169..189
FT /note="LRR 5"
FT REPEAT 193..214
FT /note="LRR 6"
FT REPEAT 216..237
FT /note="LRR 7"
FT REPEAT 240..261
FT /note="LRR 8"
FT REPEAT 264..285
FT /note="LRR 9"
FT REPEAT 288..309
FT /note="LRR 10"
FT REPEAT 312..333
FT /note="LRR 11"
FT REPEAT 336..357
FT /note="LRR 12"
FT REPEAT 360..382
FT /note="LRR 13"
FT REPEAT 387..408
FT /note="LRR 14"
FT REPEAT 411..432
FT /note="LRR 15"
FT DOMAIN 444..495
FT /note="LRRCT"
FT DOMAIN 499..598
FT /note="Ig-like C2-type 1"
FT DOMAIN 603..692
FT /note="Ig-like C2-type 2"
FT DOMAIN 697..783
FT /note="Ig-like C2-type 3"
FT REGION 1019..1093
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1019..1038
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1073..1093
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 156
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 274
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 442
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 469
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 688
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 729
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1014
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 520..581
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 624..676
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 718..767
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT CONFLICT 467
FT /note="F -> L (in Ref. 1; AAR98630)"
FT /evidence="ECO:0000305"
FT CONFLICT 561..571
FT /note="Missing (in Ref. 4; BAC98291)"
FT /evidence="ECO:0000305"
FT CONFLICT 1054
FT /note="S -> F (in Ref. 4; BAC98291)"
FT /evidence="ECO:0000305"
FT TURN 491..494
FT /evidence="ECO:0007829|PDB:3SO5"
FT STRAND 500..503
FT /evidence="ECO:0007829|PDB:3SO5"
FT STRAND 508..511
FT /evidence="ECO:0007829|PDB:3SO5"
FT STRAND 516..525
FT /evidence="ECO:0007829|PDB:3SO5"
FT STRAND 531..535
FT /evidence="ECO:0007829|PDB:3SO5"
FT STRAND 545..551
FT /evidence="ECO:0007829|PDB:3SO5"
FT HELIX 554..556
FT /evidence="ECO:0007829|PDB:3SO5"
FT STRAND 560..568
FT /evidence="ECO:0007829|PDB:3SO5"
FT HELIX 573..575
FT /evidence="ECO:0007829|PDB:3SO5"
FT STRAND 580..585
FT /evidence="ECO:0007829|PDB:3SO5"
FT STRAND 588..591
FT /evidence="ECO:0007829|PDB:3SO5"
FT STRAND 597..600
FT /evidence="ECO:0007829|PDB:3SO5"
SQ SEQUENCE 1117 AA; 122688 MW; 107A1B6960BF6A37 CRC64;
MGAPGLRAAT AALGLLLCAG LGRAGPAGSG GHGAPGQLLD DDAQRPCPAA CHCLGDLLDC
SRRRLVRLPD PLPAWVTRLD LSHNRLSFIQ TSSLSHLQSL QEVKLNNNEL ETIPNLGSIS
ANIRQLSLAG NAIDKILPEQ LEAFQSLETL DLSNNNISEL RTAFPPLQLK YLYINNNRVS
SMEPGYFDNL ASTLLVLKLN RNRISAIPPK MFKLPQLQHL ELNRNKIKNV DGLTFQGLGA
LKSLKMQRNG VTKLMDGAFW GLSNMEVLQL DHNNLTEITK GWLYGLLMLR ELHLSQNAIN
RISPDAWEFC QKLSELDLTF NHLSRLDDSS FLGLSLLNAL HIGNNKVSYI ADCAFRGLTS
LKTLDLRNNE ISWTIEDMSG AFSGLDRLRQ LILQGNRIRS ITKKAFAGLD TLEHLDLSGN
AIMSLQSNAF SQMKKLQQLH LNTSSLLCDC QLRWLPQWVA ENNFQSFVNA SCAHPQLLKG
RSIFTVSPDG FVCDDFPKPQ ITVQPETQSA IKGSDVSFTC SAASSSDSPM TFAWKKDNEA
LQDAEMENYA HLRAQGGELM EYTTILRLRN VEFTSEGKYQ CVISNHFGSS YSVKAKLTIN
MLPSFTKTPM DLTIRAGAMA RLECAAVGHP APQIAWQKDG GTDFPAARER RMHVMPEDDV
FFIVDVKIED IGVYSCTAQN SAGSVSANAT LTVLETPSFL RPLLDRTVTK GETAVLQCIA
GGSPPPRLNW TKDDSPLVVT ERHFFAAGNQ LLIIVDSDVS DAGKYTCEMS NTLGTERGNV
RLSVIPTPTC DSPHMTAPSL DGDGWATVGV VIIAVVCCVV GTSLVWVVII YHTRRRNEDC
SITNTDETNL PADIPSYLSS QGTLADRQDG YISSESGSHH QFVTSSGGGF FLPQHDGAGT
CHFDDSSEAD VEAASDPFLC PFVGSTGPVY LQGNLYSPDP FEVYLPGCSS DPRTALMDHC
ESSYVKQDRF SCARPSEEPC ERSLKSIPWP HSRKLTDSTY PPNEGHTVQT LCLNKSSVDF
STGPEPGSAT SSNSFMGTFG KPLRRPHLDA FSSSAQPPDC QPRPCHGKSL SSPELDSESE
ENDKERTDFR EENHRCTYQQ IFHTYRTPDC QPCDSDT
