LAG3_MOUSE
ID LAG3_MOUSE Reviewed; 521 AA.
AC Q61790; Q0VBL2;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 167.
DE RecName: Full=Lymphocyte activation gene 3 protein {ECO:0000303|PubMed:8921170};
DE Short=LAG-3 {ECO:0000303|PubMed:8921170};
DE AltName: Full=Activation-induced cytidine deaminase-linked autoimmunity protein {ECO:0000303|PubMed:21300912};
DE Short=Aida {ECO:0000303|PubMed:21300912};
DE AltName: CD_antigen=CD223 {ECO:0000303|PubMed:12209638};
DE Contains:
DE RecName: Full=Secreted lymphocyte activation gene 3 protein {ECO:0000305};
DE Short=sLAG-3 {ECO:0000303|PubMed:15557174, ECO:0000303|PubMed:17245433};
DE Flags: Precursor;
GN Name=Lag3 {ECO:0000312|MGI:MGI:106588};
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].
RC STRAIN=BALB/cJ; TISSUE=Thymus;
RX PubMed=8921170; DOI=10.1006/abio.1996.0382;
RA Mastrangeli R., Micangeli E., Donini S.;
RT "Cloning of murine LAG-3 by magnetic bead bound homologous probes and PCR
RT (gene-capture PCR).";
RL Anal. Biochem. 241:93-102(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], SUBCELLULAR LOCATION, AND DISRUPTION PHENOTYPE.
RC STRAIN=BALB/cJ; TISSUE=Thymus;
RX PubMed=8602528; DOI=10.1126/science.272.5260.405;
RA Miyazaki T., Dierich A., Benoist C., Mathis D.;
RT "Independent modes of natural killing distinguished in mice lacking Lag3.";
RL Science 272:405-408(1996).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC 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 [4]
RP FUNCTION, TISSUE SPECIFICITY, AND INTERACTION WITH MHC-II.
RX PubMed=12209638;
RX DOI=10.1002/1521-4141(200208)32:8<2255::aid-immu2255>3.0.co;2-a;
RA Workman C.J., Rice D.S., Dugger K.J., Kurschner C., Vignali D.A.;
RT "Phenotypic analysis of the murine CD4-related glycoprotein, CD223 (LAG-
RT 3).";
RL Eur. J. Immunol. 32:2255-2263(2002).
RN [5]
RP FUNCTION (SECRETED LYMPHOCYTE ACTIVATION GENE 3 PROTEIN).
RX PubMed=11937541; DOI=10.4049/jimmunol.168.8.3874;
RA Andreae S., Piras F., Burdin N., Triebel F.;
RT "Maturation and activation of dendritic cells induced by lymphocyte
RT activation gene-3 (CD223).";
RL J. Immunol. 168:3874-3880(2002).
RN [6]
RP FUNCTION, INTERACTION WITH MHC-II, DOMAIN, AND MUTAGENESIS OF ARG-94;
RP TYR-95; ARG-121 AND LYS-490.
RX PubMed=12421911; DOI=10.4049/jimmunol.169.10.5392;
RA Workman C.J., Dugger K.J., Vignali D.A.;
RT "Molecular analysis of the negative regulatory function of lymphocyte
RT activation gene-3.";
RL J. Immunol. 169:5392-5395(2002).
RN [7]
RP FUNCTION, AND DOMAIN.
RX PubMed=12672063; DOI=10.1002/eji.200323382;
RA Workman C.J., Vignali D.A.;
RT "The CD4-related molecule, LAG-3 (CD223), regulates the expansion of
RT activated T cells.";
RL Eur. J. Immunol. 33:970-979(2003).
RN [8]
RP FUNCTION, AND TISSUE SPECIFICITY.
RX PubMed=15485628; DOI=10.1016/j.immuni.2004.08.010;
RA Huang C.T., Workman C.J., Flies D., Pan X., Marson A.L., Zhou G.,
RA Hipkiss E.L., Ravi S., Kowalski J., Levitsky H.I., Powell J.D.,
RA Pardoll D.M., Drake C.G., Vignali D.A.;
RT "Role of LAG-3 in regulatory T cells.";
RL Immunity 21:503-513(2004).
RN [9]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=15100286; DOI=10.4049/jimmunol.172.9.5450;
RA Workman C.J., Cauley L.S., Kim I.J., Blackman M.A., Woodland D.L.,
RA Vignali D.A.;
RT "Lymphocyte activation gene-3 (CD223) regulates the size of the expanding T
RT cell population following antigen activation in vivo.";
RL J. Immunol. 172:5450-5455(2004).
RN [10]
RP PROTEOLYTIC CLEAVAGE, AND SUBCELLULAR LOCATION (SECRETED LYMPHOCYTE
RP ACTIVATION GENE 3 PROTEIN).
RX PubMed=15557174; DOI=10.4049/jimmunol.173.11.6806;
RA Li N., Workman C.J., Martin S.M., Vignali D.A.;
RT "Biochemical analysis of the regulatory T cell protein lymphocyte
RT activation gene-3 (LAG-3; CD223).";
RL J. Immunol. 173:6806-6812(2004).
RN [11]
RP FUNCTION.
RX PubMed=15634887; DOI=10.4049/jimmunol.174.2.688;
RA Workman C.J., Vignali D.A.;
RT "Negative regulation of T cell homeostasis by lymphocyte activation gene-3
RT (CD223).";
RL J. Immunol. 174:688-695(2005).
RN [12]
RP PROTEOLYTIC CLEAVAGE, AND SUBCELLULAR LOCATION (SECRETED LYMPHOCYTE
RP ACTIVATION GENE 3 PROTEIN).
RX PubMed=17245433; DOI=10.1038/sj.emboj.7601520;
RA Li N., Wang Y., Forbes K., Vignali K.M., Heale B.S., Saftig P.,
RA Hartmann D., Black R.A., Rossi J.J., Blobel C.P., Dempsey P.J.,
RA Workman C.J., Vignali D.A.;
RT "Metalloproteases regulate T-cell proliferation and effector function via
RT LAG-3.";
RL EMBO J. 26:494-504(2007).
RN [13]
RP FUNCTION, AND TISSUE SPECIFICITY.
RX PubMed=19201841; DOI=10.4049/jimmunol.0800185;
RA Workman C.J., Wang Y., El Kasmi K.C., Pardoll D.M., Murray P.J.,
RA Drake C.G., Vignali D.A.;
RT "LAG-3 regulates plasmacytoid dendritic cell homeostasis.";
RL J. Immunol. 182:1885-1891(2009).
RN [14]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=21300912; DOI=10.1084/jem.20100466;
RA Okazaki T., Okazaki I.M., Wang J., Sugiura D., Nakaki F., Yoshida T.,
RA Kato Y., Fagarasan S., Muramatsu M., Eto T., Hioki K., Honjo T.;
RT "PD-1 and LAG-3 inhibitory co-receptors act synergistically to prevent
RT autoimmunity in mice.";
RL J. Exp. Med. 208:395-407(2011).
RN [15]
RP DISRUPTION PHENOTYPE.
RX PubMed=21873518; DOI=10.4049/jimmunol.1100714;
RA Bettini M., Szymczak-Workman A.L., Forbes K., Castellaw A.H., Selby M.,
RA Pan X., Drake C.G., Korman A.J., Vignali D.A.;
RT "Accelerated autoimmune diabetes in the absence of LAG-3.";
RL J. Immunol. 187:3493-3498(2011).
RN [16]
RP FUNCTION, AND INTERACTION WITH FGL1.
RX PubMed=30580966; DOI=10.1016/j.cell.2018.11.010;
RA Wang J., Sanmamed M.F., Datar I., Su T.T., Ji L., Sun J., Chen L., Chen Y.,
RA Zhu G., Yin W., Zheng L., Zhou T., Badri T., Yao S., Zhu S., Boto A.,
RA Sznol M., Melero I., Vignali D.A.A., Schalper K., Chen L.;
RT "Fibrinogen-like protein 1 is a major immune inhibitory ligand of LAG-3.";
RL Cell 0:0-0(2018).
RN [17]
RP INTERACTION WITH MHC-II.
RX PubMed=30349037; DOI=10.1038/s41590-018-0217-9;
RA Maruhashi T., Okazaki I.M., Sugiura D., Takahashi S., Maeda T.K.,
RA Shimizu K., Okazaki T.;
RT "LAG-3 inhibits the activation of CD4+ T cells that recognize stable pMHCII
RT through its conformation-dependent recognition of pMHCII.";
RL Nat. Immunol. 19:1415-1426(2018).
CC -!- FUNCTION: Lymphocyte activation gene 3 protein: Inhibitory receptor on
CC antigen activated T-cells (PubMed:12209638, PubMed:12421911,
CC PubMed:12672063, PubMed:15100286, PubMed:15634887, PubMed:30580966).
CC Delivers inhibitory signals upon binding to ligands, such as FGL1
CC (PubMed:30580966). FGL1 constitutes a major ligand of LAG3 and is
CC responsible for LAG3 T-cell inhibitory function (PubMed:30580966).
CC Following TCR engagement, LAG3 associates with CD3-TCR in the
CC immunological synapse and directly inhibits T-cell activation
CC (PubMed:12209638, PubMed:12421911, PubMed:12672063, PubMed:15100286,
CC PubMed:15634887). May inhibit antigen-specific T-cell activation in
CC synergy with PDCD1/PD-1, possibly by acting as a coreceptor for
CC PDCD1/PD-1 (PubMed:21300912). Negatively regulates the proliferation,
CC activation, effector function and homeostasis of both CD8(+) and CD4(+)
CC T-cells (PubMed:12209638, PubMed:12421911, PubMed:12672063,
CC PubMed:15100286, PubMed:15634887). Also mediates immune tolerance:
CC constitutively expressed on a subset of regulatory T-cells (Tregs) and
CC contributes to their suppressive function (PubMed:15485628). Also acts
CC as a negative regulator of plasmacytoid dendritic cell (pDCs)
CC activation (PubMed:19201841). Binds MHC class II (MHC-II); the precise
CC role of MHC-II-binding is however unclear (PubMed:12209638,
CC PubMed:12421911, PubMed:15634887). {ECO:0000269|PubMed:12209638,
CC ECO:0000269|PubMed:12421911, ECO:0000269|PubMed:12672063,
CC ECO:0000269|PubMed:15100286, ECO:0000269|PubMed:15485628,
CC ECO:0000269|PubMed:15634887, ECO:0000269|PubMed:19201841,
CC ECO:0000269|PubMed:21300912, ECO:0000269|PubMed:30580966}.
CC -!- FUNCTION: [Secreted lymphocyte activation gene 3 protein]: May function
CC as a ligand for MHC class II (MHC-II) on antigen-presenting cells
CC (APC), promoting APC activation/maturation and driving Th1 immune
CC response. {ECO:0000269|PubMed:11937541}.
CC -!- SUBUNIT: Interacts with MHC class II (MHC-II); selectively recognizes
CC stable complexes of peptide and MHC-II (PubMed:12209638,
CC PubMed:12421911, PubMed:30349037). Interacts with FGL1 (via the
CC Fibrinogen C-terminal domain) (PubMed:30580966).
CC {ECO:0000269|PubMed:12209638, ECO:0000269|PubMed:12421911,
CC ECO:0000269|PubMed:30349037, ECO:0000269|PubMed:30580966}.
CC -!- SUBCELLULAR LOCATION: [Lymphocyte activation gene 3 protein]: Cell
CC membrane {ECO:0000269|PubMed:8602528}; Single-pass type I membrane
CC protein {ECO:0000255}.
CC -!- SUBCELLULAR LOCATION: [Secreted lymphocyte activation gene 3 protein]:
CC Secreted {ECO:0000269|PubMed:15557174, ECO:0000269|PubMed:17245433}.
CC Note=Produced following cleavage of the main chain.
CC {ECO:0000269|PubMed:17245433}.
CC -!- TISSUE SPECIFICITY: Primarily expressed in activated CD4(+) and CD8(+)
CC T-cells (PubMed:12209638). Also expressed in a subset of regulatory T-
CC cells (Tregs), such as natural CD4(+)CD25(+) Tregs (PubMed:15485628).
CC Also expressed on plasmacytoid dendritic cells (pDCs)
CC (PubMed:19201841). {ECO:0000269|PubMed:12209638,
CC ECO:0000269|PubMed:15485628, ECO:0000269|PubMed:19201841}.
CC -!- DOMAIN: [Lymphocyte activation gene 3 protein]: The KIEELE motif is
CC required for interaction with downstream signaling molecules.
CC {ECO:0000269|PubMed:12421911, ECO:0000269|PubMed:12672063}.
CC -!- PTM: [Lymphocyte activation gene 3 protein]: Proteolytically cleaved by
CC ADAM10 and ADAM17 within the connecting peptide region, leading to
CC release of Secreted lymphocyte activation gene 3 protein (sLAG-3)
CC (PubMed:17245433). ADAM10 mediates constitutive cleavage, but cleavage
CC increases following T-cell activation, whereas shedding by ADAM17 is
CC induced by TCR signaling in a PRKCQ-dependent manner (PubMed:17245433).
CC {ECO:0000269|PubMed:17245433}.
CC -!- DISRUPTION PHENOTYPE: Mice develop normally but show minor defects in
CC the natural killer (NK) cells (PubMed:8602528). They are however prone
CC to development of autoimmune diseases, such as autoimmune diabetes on a
CC permissive genetic background (PubMed:21300912, PubMed:21873518).
CC Knockout NOD mice exhibit accelerated, invasive insulitis,
CC corresponding to increased CD4(+) and CD8(+) T-cell islet infiltration
CC and intraislet proliferation (PubMed:21873518). T-cells display a delay
CC in cell cycle arrest following stimulation with the superantigen
CC staphylococcal enterotoxin-B resulting in increased T-cell expansion
CC and splenomegaly (PubMed:15100286). Mice lacking both Lag3 and
CC Pdcd1/PD-1 die of severe myocarditis before 10 weeks of age in BALB/c
CC mice (PubMed:21300912). {ECO:0000269|PubMed:15100286,
CC ECO:0000269|PubMed:21300912, ECO:0000269|PubMed:21873518,
CC ECO:0000269|PubMed:8602528}.
CC -!- SIMILARITY: Belongs to the LAG3 family. {ECO:0000305}.
CC -!- CAUTION: An initial knockout experiment in mouse reported only minor
CC phenotype with no development of spontaneous disease, arguing against a
CC significant role in controlling T-cell activation (PubMed:8602528).
CC However, subsequent analysis showed that knockout mice develop
CC autoimmune diseases caused by T-cell activation (PubMed:21873518).
CC {ECO:0000269|PubMed:21873518, ECO:0000269|PubMed:8602528}.
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DR EMBL; X98113; CAA66794.1; -; mRNA.
DR EMBL; BC120591; AAI20592.1; -; mRNA.
DR CCDS; CCDS20536.1; -.
DR RefSeq; NP_032505.1; NM_008479.2.
DR AlphaFoldDB; Q61790; -.
DR STRING; 10090.ENSMUSP00000032217; -.
DR GlyGen; Q61790; 5 sites.
DR iPTMnet; Q61790; -.
DR PhosphoSitePlus; Q61790; -.
DR EPD; Q61790; -.
DR PaxDb; Q61790; -.
DR PRIDE; Q61790; -.
DR ProteomicsDB; 264907; -.
DR Antibodypedia; 2267; 1053 antibodies from 38 providers.
DR DNASU; 16768; -.
DR Ensembl; ENSMUST00000032217; ENSMUSP00000032217; ENSMUSG00000030124.
DR GeneID; 16768; -.
DR KEGG; mmu:16768; -.
DR UCSC; uc009dsl.2; mouse.
DR CTD; 3902; -.
DR MGI; MGI:106588; Lag3.
DR VEuPathDB; HostDB:ENSMUSG00000030124; -.
DR eggNOG; ENOG502S2HD; Eukaryota.
DR GeneTree; ENSGT01050000244846; -.
DR HOGENOM; CLU_041154_1_0_1; -.
DR InParanoid; Q61790; -.
DR OMA; LWVAPVE; -.
DR OrthoDB; 862925at2759; -.
DR PhylomeDB; Q61790; -.
DR TreeFam; TF335942; -.
DR Reactome; R-MMU-2132295; MHC class II antigen presentation.
DR BioGRID-ORCS; 16768; 7 hits in 78 CRISPR screens.
DR PRO; PR:Q61790; -.
DR Proteomes; UP000000589; Chromosome 6.
DR RNAct; Q61790; protein.
DR Bgee; ENSMUSG00000030124; Expressed in thymus and 57 other tissues.
DR Genevisible; Q61790; MM.
DR GO; GO:0009897; C:external side of plasma membrane; IDA:MGI.
DR GO; GO:0005576; C:extracellular region; IDA:UniProtKB.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0042289; F:MHC class II protein binding; IDA:UniProtKB.
DR GO; GO:0004888; F:transmembrane signaling receptor activity; IDA:UniProtKB.
DR GO; GO:0002250; P:adaptive immune response; IEA:UniProtKB-KW.
DR GO; GO:0007166; P:cell surface receptor signaling pathway; IDA:UniProtKB.
DR GO; GO:0042267; P:natural killer cell mediated cytotoxicity; IDA:MGI.
DR GO; GO:0032703; P:negative regulation of interleukin-2 production; IDA:MGI.
DR GO; GO:0045590; P:negative regulation of regulatory T cell differentiation; IMP:UniProtKB.
DR GO; GO:0050868; P:negative regulation of T cell activation; IDA:UniProtKB.
DR GO; GO:0002270; P:plasmacytoid dendritic cell activation; IMP:UniProtKB.
DR GO; GO:0045954; P:positive regulation of natural killer cell mediated cytotoxicity; IDA:MGI.
DR GO; GO:0050776; P:regulation of immune response; IDA:UniProtKB.
DR GO; GO:0042110; P:T cell activation; IDA:MGI.
DR Gene3D; 2.60.40.10; -; 3.
DR InterPro; IPR007110; Ig-like_dom.
DR InterPro; IPR036179; Ig-like_dom_sf.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR003599; Ig_sub.
DR InterPro; IPR015621; IL-1_rcpt_fam.
DR InterPro; IPR013151; Immunoglobulin.
DR PANTHER; PTHR11890; PTHR11890; 1.
DR Pfam; PF00047; ig; 1.
DR SMART; SM00409; IG; 3.
DR SUPFAM; SSF48726; SSF48726; 3.
DR PROSITE; PS50835; IG_LIKE; 2.
PE 1: Evidence at protein level;
KW Adaptive immunity; Cell membrane; Disulfide bond; Glycoprotein; Immunity;
KW Immunoglobulin domain; Membrane; Reference proteome; Repeat; Secreted;
KW Signal; Transmembrane; Transmembrane helix.
FT SIGNAL 1..23
FT /evidence="ECO:0000255"
FT CHAIN 24..521
FT /note="Lymphocyte activation gene 3 protein"
FT /id="PRO_0000014632"
FT CHAIN 24..422
FT /note="Secreted lymphocyte activation gene 3 protein"
FT /evidence="ECO:0000305|PubMed:15557174"
FT /id="PRO_0000446643"
FT TOPO_DOM 24..442
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 443..463
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 464..521
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 37..163
FT /note="Ig-like V-type"
FT /evidence="ECO:0000255"
FT DOMAIN 165..246
FT /note="Ig-like C2-type 1"
FT /evidence="ECO:0000255"
FT DOMAIN 258..341
FT /note="Ig-like C2-type 2"
FT /evidence="ECO:0000255"
FT DOMAIN 345..412
FT /note="Ig-like C2-type 3"
FT /evidence="ECO:0000255"
FT REGION 37..246
FT /note="Interaction with FGL1"
FT /evidence="ECO:0000250|UniProtKB:P18627"
FT REGION 422..442
FT /note="Connecting peptide"
FT /evidence="ECO:0000305|PubMed:15557174"
FT REGION 493..521
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 493..518
FT /note="13 X 2 AA tandem repeats of E-X"
FT MOTIF 490..495
FT /note="KIEELE motif"
FT /evidence="ECO:0000269|PubMed:12421911"
FT CARBOHYD 184
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 244
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 309
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 337
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 381
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 44..156
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 185..235
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 276..327
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 363..405
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT MUTAGEN 94
FT /note="R->E: Decreased binding to MHC class II."
FT /evidence="ECO:0000269|PubMed:12421911"
FT MUTAGEN 95
FT /note="Y->F: No significant effect on MHC class II-
FT binding."
FT /evidence="ECO:0000269|PubMed:12421911"
FT MUTAGEN 121
FT /note="R->A: No significant effect on MHC class II-
FT binding."
FT /evidence="ECO:0000269|PubMed:12421911"
FT MUTAGEN 490
FT /note="K->A: Abolished ability to inhibit T-cell
FT activation."
FT /evidence="ECO:0000269|PubMed:12421911"
SQ SEQUENCE 521 AA; 56978 MW; 64C29C40EB780E48 CRC64;
MREDLLLGFL LLGLLWEAPV VSSGPGKELP VVWAQEGAPV HLPCSLKSPN LDPNFLRRGG
VIWQHQPDSG QPTPIPALDL HQGMPSPRQP APGRYTVLSV APGGLRSGRQ PLHPHVQLEE
RGLQRGDFSL WLRPALRTDA GEYHATVRLP NRALSCSLRL RVGQASMIAS PSGVLKLSDW
VLLNCSFSRP DRPVSVHWFQ GQNRVPVYNS PRHFLAETFL LLPQVSPLDS GTWGCVLTYR
DGFNVSITYN LKVLGLEPVA PLTVYAAEGS RVELPCHLPP GVGTPSLLIA KWTPPGGGPE
LPVAGKSGNF TLHLEAVGLA QAGTYTCSIH LQGQQLNATV TLAVITVTPK SFGLPGSRGK
LLCEVTPASG KERFVWRPLN NLSRSCPGPV LEIQEARLLA ERWQCQLYEG QRLLGATVYA
AESSSGAHSA RRISGDLKGG HLVLVLILGA LSLFLLVAGA FGFHWWRKQL LLRRFSALEH
GIQPFPAQRK IEELERELET EMGQEPEPEP EPQLEPEPRQ L
