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 27-MAR-2024, entry version 162.
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; 57.
DR IntAct; Q6UXM1; 10.
DR STRING; 9606.ENSP00000326759; -.
DR GlyCosmos; Q6UXM1; 12 sites, No reported glycans.
DR GlyGen; Q6UXM1; 13 sites, 1 O-linked glycan (1 site).
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; 9606-ENSP00000326759; -.
DR PeptideAtlas; Q6UXM1; -.
DR ProteomicsDB; 67636; -. [Q6UXM1-1]
DR ProteomicsDB; 67637; -. [Q6UXM1-2]
DR Antibodypedia; 2484; 169 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 AGR; HGNC:30991; -.
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; 5405965at2759; -.
DR PhylomeDB; Q6UXM1; -.
DR TreeFam; TF325380; -.
DR PathwayCommons; Q6UXM1; -.
DR SignaLink; Q6UXM1; -.
DR SIGNOR; Q6UXM1; -.
DR BioGRID-ORCS; 121227; 11 hits in 1151 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 149 other cell types or 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:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0032474; P:otolith morphogenesis; IEA:Ensembl.
DR CDD; cd05763; IgI_LRIG1-like; 1.
DR Gene3D; 2.60.40.10; Immunoglobulins; 3.
DR Gene3D; 3.80.10.10; Ribonuclease Inhibitor; 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 PANTHER; PTHR45842:SF23; IG-LIKE DOMAIN-CONTAINING PROTEIN; 1.
DR PANTHER; PTHR45842; SYNAPTIC ADHESION-LIKE MOLECULE SALM; 1.
DR Pfam; PF07679; I-set; 2.
DR Pfam; PF13927; Ig_3; 1.
DR Pfam; PF00560; LRR_1; 1.
DR Pfam; PF13855; LRR_8; 3.
DR SMART; SM00409; IG; 3.
DR SMART; SM00408; IGc2; 3.
DR SMART; SM00365; LRR_SD22; 7.
DR SMART; SM00369; LRR_TYP; 14.
DR SMART; SM00082; LRRCT; 1.
DR SUPFAM; SSF48726; Immunoglobulin; 3.
DR SUPFAM; SSF52058; L domain-like; 1.
DR SUPFAM; SSF52047; RNI-like; 1.
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
//
