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LRIG3_HUMAN
ID   LRIG3_HUMAN             Reviewed;        1119 AA.
AC   Q6UXM1; Q6UXL7; Q8NC72;
DT   16-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   03-AUG-2022, entry version 153.
DE   RecName: Full=Leucine-rich repeats and immunoglobulin-like domains protein 3;
DE            Short=LIG-3;
DE   Flags: Precursor;
GN   Name=LRIG3; Synonyms=LIG3; ORFNames=UNQ287/PRO326/PRO335;
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), 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] (ISOFORMS 1 AND 2).
RX   PubMed=12975309; DOI=10.1101/gr.1293003;
RA   Clark H.F., Gurney A.L., Abaya E., Baker K., Baldwin D.T., Brush J.,
RA   Chen J., Chow B., Chui C., Crowley C., Currell B., Deuel B., Dowd P.,
RA   Eaton D., Foster J.S., Grimaldi C., Gu Q., Hass P.E., Heldens S., Huang A.,
RA   Kim H.S., Klimowski L., Jin Y., Johnson S., Lee J., Lewis L., Liao D.,
RA   Mark M.R., Robbie E., Sanchez C., Schoenfeld J., Seshagiri S., Simmons L.,
RA   Singh J., Smith V., Stinson J., Vagts A., Vandlen R.L., Watanabe C.,
RA   Wieand D., Woods K., Xie M.-H., Yansura D.G., Yi S., Yu G., Yuan J.,
RA   Zhang M., Zhang Z., Goddard A.D., Wood W.I., Godowski P.J., Gray A.M.;
RT   "The secreted protein discovery initiative (SPDI), a large-scale effort to
RT   identify novel human secreted and transmembrane proteins: a bioinformatics
RT   assessment.";
RL   Genome Res. 13:2265-2270(2003).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 400-1119.
RX   PubMed=14702039; DOI=10.1038/ng1285;
RA   Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA   Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA   Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA   Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA   Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA   Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA   Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA   Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA   Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA   Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA   Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA   Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA   Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA   Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA   Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA   Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA   Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA   Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA   Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA   Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA   Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA   Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA   Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA   Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA   Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA   Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA   Isogai T., Sugano S.;
RT   "Complete sequencing and characterization of 21,243 full-length human
RT   cDNAs.";
RL   Nat. Genet. 36:40-45(2004).
CC   -!- FUNCTION: May play a role in craniofacial and inner ear morphogenesis
CC       during embryonic development. May act within the otic vesicle
CC       epithelium to control formation of the lateral semicircular canal in
CC       the inner ear, possibly by restricting the expression of NTN1 (By
CC       similarity). {ECO:0000250}.
CC   -!- SUBUNIT: Interacts with EGFR, ERBB2 and ERBB4 (in vitro).
CC       {ECO:0000250}.
CC   -!- INTERACTION:
CC       Q6UXM1; Q96JA1: LRIG1; NbExp=7; IntAct=EBI-9207843, EBI-2865191;
CC       Q6UXM1-1; Q9UPQ0-1: LIMCH1; NbExp=3; IntAct=EBI-25412632, EBI-25412679;
CC       Q6UXM1-1; Q8WWI1-3: LMO7; NbExp=3; IntAct=EBI-25412632, EBI-4400717;
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Single-pass type I
CC       membrane protein {ECO:0000250}. Cytoplasmic vesicle membrane
CC       {ECO:0000250}; Single-pass type I membrane protein {ECO:0000250}.
CC       Note=Detected in cytoplasmic vesicles when coexpressed with ERBB4.
CC       {ECO:0000250}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q6UXM1-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q6UXM1-2; Sequence=VSP_015097;
CC   -!- TISSUE SPECIFICITY: Widely expressed. {ECO:0000269|PubMed:15203213}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAC11295.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR   EMBL; AY505340; AAR98629.1; -; mRNA.
DR   EMBL; AY358288; AAQ88655.1; -; mRNA.
DR   EMBL; AY358295; AAQ88662.1; -; mRNA.
DR   EMBL; AK074921; BAC11295.1; ALT_INIT; mRNA.
DR   CCDS; CCDS44933.1; -. [Q6UXM1-2]
DR   CCDS; CCDS8960.1; -. [Q6UXM1-1]
DR   RefSeq; NP_001129523.1; NM_001136051.2. [Q6UXM1-2]
DR   RefSeq; NP_700356.2; NM_153377.4. [Q6UXM1-1]
DR   AlphaFoldDB; Q6UXM1; -.
DR   SMR; Q6UXM1; -.
DR   BioGRID; 125712; 53.
DR   IntAct; Q6UXM1; 10.
DR   STRING; 9606.ENSP00000326759; -.
DR   GlyGen; Q6UXM1; 12 sites.
DR   iPTMnet; Q6UXM1; -.
DR   PhosphoSitePlus; Q6UXM1; -.
DR   BioMuta; LRIG3; -.
DR   DMDM; 73621176; -.
DR   EPD; Q6UXM1; -.
DR   jPOST; Q6UXM1; -.
DR   MassIVE; Q6UXM1; -.
DR   MaxQB; Q6UXM1; -.
DR   PaxDb; Q6UXM1; -.
DR   PeptideAtlas; Q6UXM1; -.
DR   PRIDE; Q6UXM1; -.
DR   ProteomicsDB; 67636; -. [Q6UXM1-1]
DR   ProteomicsDB; 67637; -. [Q6UXM1-2]
DR   Antibodypedia; 2484; 153 antibodies from 25 providers.
DR   DNASU; 121227; -.
DR   Ensembl; ENST00000320743.8; ENSP00000326759.3; ENSG00000139263.12. [Q6UXM1-1]
DR   Ensembl; ENST00000379141.8; ENSP00000368436.4; ENSG00000139263.12. [Q6UXM1-2]
DR   GeneID; 121227; -.
DR   KEGG; hsa:121227; -.
DR   MANE-Select; ENST00000320743.8; ENSP00000326759.3; NM_153377.5; NP_700356.2.
DR   UCSC; uc001sqr.5; human. [Q6UXM1-1]
DR   CTD; 121227; -.
DR   DisGeNET; 121227; -.
DR   GeneCards; LRIG3; -.
DR   HGNC; HGNC:30991; LRIG3.
DR   HPA; ENSG00000139263; Low tissue specificity.
DR   MIM; 608870; gene.
DR   neXtProt; NX_Q6UXM1; -.
DR   OpenTargets; ENSG00000139263; -.
DR   PharmGKB; PA134864136; -.
DR   VEuPathDB; HostDB:ENSG00000139263; -.
DR   eggNOG; KOG0619; Eukaryota.
DR   eggNOG; KOG4194; Eukaryota.
DR   GeneTree; ENSGT00940000157098; -.
DR   InParanoid; Q6UXM1; -.
DR   OMA; WIIEDQS; -.
DR   OrthoDB; 161719at2759; -.
DR   PhylomeDB; Q6UXM1; -.
DR   TreeFam; TF325380; -.
DR   PathwayCommons; Q6UXM1; -.
DR   SignaLink; Q6UXM1; -.
DR   SIGNOR; Q6UXM1; -.
DR   BioGRID-ORCS; 121227; 11 hits in 1071 CRISPR screens.
DR   ChiTaRS; LRIG3; human.
DR   GenomeRNAi; 121227; -.
DR   Pharos; Q6UXM1; Tbio.
DR   PRO; PR:Q6UXM1; -.
DR   Proteomes; UP000005640; Chromosome 12.
DR   RNAct; Q6UXM1; protein.
DR   Bgee; ENSG00000139263; Expressed in calcaneal tendon and 147 other tissues.
DR   ExpressionAtlas; Q6UXM1; baseline and differential.
DR   Genevisible; Q6UXM1; HS.
DR   GO; GO:0030659; C:cytoplasmic vesicle membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0031012; C:extracellular matrix; IBA:GO_Central.
DR   GO; GO:0005615; C:extracellular space; HDA: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:0032474; P:otolith morphogenesis; IEA:Ensembl.
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; 3.
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   Alternative splicing; Cell membrane; Cytoplasmic vesicle;
KW   Developmental protein; Disulfide bond; Glycoprotein; Immunoglobulin domain;
KW   Leucine-rich repeat; Membrane; Reference proteome; Repeat; Signal;
KW   Transmembrane; Transmembrane helix.
FT   SIGNAL          1..24
FT                   /evidence="ECO:0000255"
FT   CHAIN           25..1119
FT                   /note="Leucine-rich repeats and immunoglobulin-like domains
FT                   protein 3"
FT                   /id="PRO_0000014831"
FT   TRANSMEM        810..830
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          38..74
FT                   /note="LRRNT"
FT   REPEAT          75..96
FT                   /note="LRR 1"
FT   REPEAT          99..120
FT                   /note="LRR 2"
FT   REPEAT          122..142
FT                   /note="LRR 3"
FT   REPEAT          146..167
FT                   /note="LRR 4"
FT   REPEAT          168..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          1073..1093
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1076..1093
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CARBOHYD        122
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
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        515
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        905
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        987
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        999
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        1016
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   VAR_SEQ         1..79
FT                   /note="MSAPSLRARAAGLGLLLCAVLGRAGRSDSGGRGELGQPSGVAAERPCPTTCR
FT                   CLGDLLDCSRKRLARLPEPLPSWVARL -> MVDVLLLFSLCLLFHISRP (in
FT                   isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:12975309"
FT                   /id="VSP_015097"
SQ   SEQUENCE   1119 AA;  123434 MW;  EB3B6A391F3C8713 CRC64;
     MSAPSLRARA AGLGLLLCAV LGRAGRSDSG GRGELGQPSG VAAERPCPTT CRCLGDLLDC
     SRKRLARLPE PLPSWVARLD LSHNRLSFIK ASSMSHLQSL REVKLNNNEL ETIPNLGPVS
     ANITLLSLAG NRIVEILPEH LKEFQSLETL DLSSNNISEL QTAFPALQLK YLYLNSNRVT
     SMEPGYFDNL ANTLLVLKLN RNRISAIPPK MFKLPQLQHL ELNRNKIKNV DGLTFQGLGA
     LKSLKMQRNG VTKLMDGAFW GLSNMEILQL DHNNLTEITK GWLYGLLMLQ ELHLSQNAIN
     RISPDAWEFC QKLSELDLTF NHLSRLDDSS FLGLSLLNTL HIGNNRVSYI ADCAFRGLSS
     LKTLDLKNNE ISWTIEDMNG AFSGLDKLRR LILQGNRIRS ITKKAFTGLD ALEHLDLSDN
     AIMSLQGNAF SQMKKLQQLH LNTSSLLCDC QLKWLPQWVA ENNFQSFVNA SCAHPQLLKG
     RSIFAVSPDG FVCDDFPKPQ ITVQPETQSA IKGSNLSFIC SAASSSDSPM TFAWKKDNEL
     LHDAEMENYA HLRAQGGEVM EYTTILRLRE VEFASEGKYQ CVISNHFGSS YSVKAKLTVN
     MLPSFTKTPM DLTIRAGAMA RLECAAVGHP APQIAWQKDG GTDFPAARER RMHVMPEDDV
     FFIVDVKIED IGVYSCTAQN SAGSISANAT LTVLETPSFL RPLLDRTVTK GETAVLQCIA
     GGSPPPKLNW TKDDSPLVVT ERHFFAAGNQ LLIIVDSDVS DAGKYTCEMS NTLGTERGNV
     RLSVIPTPTC DSPQMTAPSL DDDGWATVGV VIIAVVCCVV GTSLVWVVII YHTRRRNEDC
     SITNTDETNL PADIPSYLSS QGTLADRQDG YVSSESGSHH QFVTSSGAGF FLPQHDSSGT
     CHIDNSSEAD VEAATDLFLC PFLGSTGPMY LKGNVYGSDP FETYHTGCSP DPRTVLMDHY
     EPSYIKKKEC YPCSHPSEES CERSFSNISW PSHVRKLLNT SYSHNEGPGM KNLCLNKSSL
     DFSANPEPAS VASSNSFMGT FGKALRRPHL DAYSSFGQPS DCQPRAFYLK AHSSPDLDSG
     SEEDGKERTD FQEENHICTF KQTLENYRTP NFQSYDLDT
 
 
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