LY9_MOUSE
ID LY9_MOUSE Reviewed; 654 AA.
AC Q01965; Q9ES29; Q9ES35; Q9ES36;
DT 01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT 20-JUN-2002, sequence version 2.
DT 03-AUG-2022, entry version 170.
DE RecName: Full=T-lymphocyte surface antigen Ly-9;
DE AltName: Full=Cell surface molecule Ly-9;
DE AltName: Full=Lymphocyte antigen 9;
DE AltName: Full=SLAM family member 3;
DE Short=SLAMF3;
DE AltName: Full=Signaling lymphocytic activation molecule 3;
DE AltName: CD_antigen=CD229;
DE Flags: Precursor;
GN Name=Ly9; Synonyms=Ly-9;
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 [GENOMIC DNA / MRNA], AND POLYMORPHISM.
RC STRAIN=129/Sv, BALB/cJ, and C57BL/6J; TISSUE=Spleen;
RX PubMed=10970093; DOI=10.1007/s002510000209;
RA Tovar V., de la Fuente M.A., Pizcueta P., Bosch J., Engel P.;
RT "Gene structure of the mouse leukocyte cell surface molecule Ly9.";
RL Immunogenetics 51:788-793(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 22-654, AND PROTEIN SEQUENCE OF 48-59.
RX PubMed=1506686;
RA Sandrin M.S., Gumley T.P., Henning M.M., Vaughan H.A., Gonez L.J.,
RA Trapani J.A., McKenzie I.F.C.;
RT "Isolation and characterization of cDNA clones for mouse Ly-9.";
RL J. Immunol. 149:1636-1641(1992).
RN [3]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-499, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA Thibault P.;
RT "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL Immunity 30:143-154(2009).
RN [4]
RP FUNCTION.
RX PubMed=19648922; DOI=10.1038/ni.1763;
RA Dong Z., Cruz-Munoz M.E., Zhong M.C., Chen R., Latour S., Veillette A.;
RT "Essential function for SAP family adaptors in the surveillance of
RT hematopoietic cells by natural killer cells.";
RL Nat. Immunol. 10:973-980(2009).
RN [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Spleen;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [6]
RP FUNCTION.
RX PubMed=23914190; DOI=10.3389/fimmu.2013.00225;
RA de Salort J., Cuenca M., Terhorst C., Engel P., Romero X.;
RT "Ly9 (CD229) cell-surface receptor is crucial for the development of
RT spontaneous autoantibody production to nuclear antigens.";
RL Front. Immunol. 4:225-225(2013).
RN [7]
RP FUNCTION.
RX PubMed=23225888; DOI=10.4049/jimmunol.1202435;
RA Sintes J., Cuenca M., Romero X., Bastos R., Terhorst C., Angulo A.,
RA Engel P.;
RT "Ly9 (CD229), a SLAM family receptor, negatively regulates the development
RT of thymic innate memory-like CD8+ T and invariant NKT cells.";
RL J. Immunol. 190:21-26(2013).
CC -!- FUNCTION: Self-ligand receptor of the signaling lymphocytic activation
CC molecule (SLAM) family. SLAM receptors triggered by homo- or
CC heterotypic cell-cell interactions are modulating the activation and
CC differentiation of a wide variety of immune cells and thus are involved
CC in the regulation and interconnection of both innate and adaptive
CC immune response. Activities are controlled by presence or absence of
CC small cytoplasmic adapter proteins, SH2D1A/SAP and/or SH2D1B/EAT-2
CC (PubMed:19648922). May participate in adhesion reactions between T
CC lymphocytes and accessory cells by homophilic interaction. Promotes T-
CC cell differentiation into a helper T-cell Th17 phenotype leading to
CC increased IL-17 secretion; the costimulatory activity requires SH2D1A.
CC Promotes recruitment of RORC to the IL-17 promoter (By similarity). May
CC be involved in the maintenance of peripheral cell tolerance by serving
CC as a negative regulator of the immune response. May disable
CC autoantibody responses and inhibit IFN-gamma secretion by CD4(+) T-
CC cells (PubMed:23914190). May negatively regulate the size of thymic
CC innate CD8(+) T-cells and the development of invariant natural killer T
CC (iNKT) cells (PubMed:23225888). Can promote natural killer (NK) cell
CC activation (PubMed:19648922). {ECO:0000250|UniProtKB:Q9HBG7,
CC ECO:0000269|PubMed:19648922, ECO:0000269|PubMed:23225888,
CC ECO:0000269|PubMed:23914190}.
CC -!- SUBUNIT: Interacts with SH2D1A and INPP5D. Interacts (via
CC phosphorylated cytoplasmic domain) with PTPN11; the interaction is
CC blocked by SH2D1A. {ECO:0000250|UniProtKB:Q9HBG7}.
CC -!- SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane protein.
CC Cell membrane {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Lymphocytes.
CC -!- DOMAIN: The ITSMs (immunoreceptor tyrosine-based switch motifs) with
CC the consensus sequence T-X-Y-X-X-[VI] present in SLAM family receptors
CC have overlapping specificity for activating and inhibitory SH2 domain-
CC containing binding partners. Especially they mediate the interaction
CC with the SH2 domain of SH2D1A and SH2D1B. A 'three-pronged' mechanism
CC is proposed involving threonine (position -2), phosphorylated tyrosine
CC (position 0) and valine/isoleucine (position +3).
CC {ECO:0000250|UniProtKB:Q13291}.
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DR EMBL; AF244131; AAG14997.1; -; mRNA.
DR EMBL; AF244130; AAG14996.1; -; mRNA.
DR EMBL; AF246701; AAG13268.2; -; Genomic_DNA.
DR EMBL; AF245117; AAG13268.2; JOINED; Genomic_DNA.
DR EMBL; AF245506; AAG13268.2; JOINED; Genomic_DNA.
DR EMBL; AF245118; AAG13268.2; JOINED; Genomic_DNA.
DR EMBL; AF245507; AAG13268.2; JOINED; Genomic_DNA.
DR EMBL; AF245508; AAG13268.2; JOINED; Genomic_DNA.
DR EMBL; AF245509; AAG13268.2; JOINED; Genomic_DNA.
DR EMBL; AF245510; AAG13268.2; JOINED; Genomic_DNA.
DR EMBL; AF246699; AAG13268.2; JOINED; Genomic_DNA.
DR EMBL; AF246700; AAG13268.2; JOINED; Genomic_DNA.
DR EMBL; M84412; AAA39468.1; -; mRNA.
DR CCDS; CCDS35779.1; -.
DR RefSeq; NP_001264897.1; NM_001277968.1.
DR RefSeq; NP_032560.2; NM_008534.3.
DR AlphaFoldDB; Q01965; -.
DR IntAct; Q01965; 4.
DR STRING; 10090.ENSMUSP00000069319; -.
DR GlyGen; Q01965; 8 sites.
DR iPTMnet; Q01965; -.
DR PhosphoSitePlus; Q01965; -.
DR SwissPalm; Q01965; -.
DR EPD; Q01965; -.
DR jPOST; Q01965; -.
DR MaxQB; Q01965; -.
DR PaxDb; Q01965; -.
DR PRIDE; Q01965; -.
DR ProteomicsDB; 290200; -.
DR ABCD; Q01965; 14 sequenced antibodies.
DR Antibodypedia; 20495; 671 antibodies from 39 providers.
DR DNASU; 17085; -.
DR Ensembl; ENSMUST00000068878; ENSMUSP00000069319; ENSMUSG00000004707.
DR GeneID; 17085; -.
DR KEGG; mmu:17085; -.
DR UCSC; uc007dou.2; mouse.
DR CTD; 4063; -.
DR MGI; MGI:96885; Ly9.
DR VEuPathDB; HostDB:ENSMUSG00000004707; -.
DR eggNOG; ENOG502SGRG; Eukaryota.
DR GeneTree; ENSGT01030000234540; -.
DR HOGENOM; CLU_035502_0_0_1; -.
DR InParanoid; Q01965; -.
DR OMA; ICPGPER; -.
DR OrthoDB; 990343at2759; -.
DR PhylomeDB; Q01965; -.
DR TreeFam; TF334964; -.
DR BioGRID-ORCS; 17085; 2 hits in 72 CRISPR screens.
DR ChiTaRS; Ly9; mouse.
DR PRO; PR:Q01965; -.
DR Proteomes; UP000000589; Chromosome 1.
DR RNAct; Q01965; protein.
DR Bgee; ENSMUSG00000004707; Expressed in peripheral lymph node and 45 other tissues.
DR ExpressionAtlas; Q01965; baseline and differential.
DR Genevisible; Q01965; MM.
DR GO; GO:0009986; C:cell surface; IDA:MGI.
DR GO; GO:0009897; C:external side of plasma membrane; IBA:GO_Central.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; ISO:MGI.
DR GO; GO:0007155; P:cell adhesion; IEA:UniProtKB-KW.
DR GO; GO:0045087; P:innate immune response; IEA:UniProtKB-KW.
DR GO; GO:0032740; P:positive regulation of interleukin-17 production; ISO:MGI.
DR GO; GO:0042110; P:T cell activation; IBA:GO_Central.
DR GO; GO:0072540; P:T-helper 17 cell lineage commitment; ISO:MGI.
DR Gene3D; 2.60.40.10; -; 4.
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 Pfam; PF13895; Ig_2; 1.
DR SMART; SM00409; IG; 2.
DR SUPFAM; SSF48726; SSF48726; 4.
DR PROSITE; PS50835; IG_LIKE; 2.
PE 1: Evidence at protein level;
KW Adaptive immunity; Cell adhesion; Cell membrane; Direct protein sequencing;
KW Disulfide bond; Glycoprotein; Immunity; Immunoglobulin domain;
KW Innate immunity; Membrane; Phosphoprotein; Reference proteome; Repeat;
KW Signal; Transmembrane; Transmembrane helix.
FT SIGNAL 1..47
FT /evidence="ECO:0000269|PubMed:1506686"
FT CHAIN 48..654
FT /note="T-lymphocyte surface antigen Ly-9"
FT /id="PRO_0000014852"
FT TOPO_DOM 48..453
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 454..474
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 475..654
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 48..158
FT /note="Ig-like V-type 1"
FT DOMAIN 159..243
FT /note="Ig-like C2-type 1"
FT DOMAIN 250..362
FT /note="Ig-like V-type 2"
FT DOMAIN 353..453
FT /note="Ig-like C2-type 2"
FT REGION 292..319
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 517..557
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 628..654
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 599..604
FT /note="ITSM 1 (atypical)"
FT /evidence="ECO:0000250|UniProtKB:Q13291"
FT MOTIF 623..628
FT /note="ITSM 2"
FT /evidence="ECO:0000250|UniProtKB:Q13291"
FT COMPBIAS 295..317
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 522..537
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 499
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:19144319"
FT MOD_RES 601
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:Q9HBG7"
FT CARBOHYD 68
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 231
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 284
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 390
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 412
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 423
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 434
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 172..242
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 178..222
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 376..445
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 382..426
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT VARIANT 10
FT /note="D -> G (in Ly9-1)"
FT VARIANT 14
FT /note="G -> S (in Ly9-1)"
FT VARIANT 79
FT /note="I -> T (in Ly9-1)"
FT VARIANT 91
FT /note="F -> S (in Ly9-1)"
FT VARIANT 130
FT /note="H -> Y (in Ly9-1)"
FT VARIANT 139
FT /note="I -> T (in Ly9-1)"
FT VARIANT 362
FT /note="P -> S"
FT VARIANT 366
FT /note="K -> N (in Ly9-1)"
FT VARIANT 377
FT /note="E -> K (in Ly9-1)"
FT VARIANT 550
FT /note="M -> I (in Ly9-1)"
FT VARIANT 592
FT /note="G -> E (in Ly9-1)"
FT CONFLICT 283
FT /note="F -> L (in Ref. 2; AAA39468)"
FT /evidence="ECO:0000305"
FT CONFLICT 499
FT /note="T -> P (in Ref. 2; AAA39468)"
FT /evidence="ECO:0000305"
FT CONFLICT 560
FT /note="V -> L (in Ref. 2; AAA39468)"
FT /evidence="ECO:0000305"
FT CONFLICT 647..654
FT /note="TPTYENFT -> SPYL (in Ref. 2; AAA39468)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 654 AA; 73143 MW; 1CBBE99708AE8EE7 CRC64;
MADLKRYWCD WALGPLSENP RMSQQQIFSP ILWIPLLFLL MGLGASGKET PPTVISGMLG
GSVTFSLNIS KDAEIEHIIW NCPPKALALV FYKKDITILD KGYNGRLKVS EDGYSLYMSN
LTKSDSGSYH AQINQKNVIL TTNKEFTLHI YEKLQKPQII VESVTPSDTD SCTFTLICTV
KGTKDSVQYS WTREDTHLNT YDGSHTLRVS QSVCDPDLPY TCKAWNPVSQ NSSQPVRIWQ
FCTGASRRKT AAGKTVVGIL GEPVTLPLEF RATRATKNVV WVFNTSVISQ ERRGAATADS
RRKPKGSEER RVRTSDQDQS LKISQLKMED AGPYHAYVCS EASRDPSVRH FTLLVYKRLE
KPSVTKSPVH MMNGICEVVL TCSVDGGGNN VTYTWMPLQN KAVMSQGKSH LNVSWESGEH
LPNFTCTAHN PVSNSSSQFS SGTICSGPER NKRFWLLLLL VLLLLMLIGG YFILRKKKQC
SSLATRYRQA EVPAEIPETP TGHGQFSVLS QRYEKLDMSA KTTRHQPTPT SDTSSESSAT
TEEDDEKTRM HSTANSRNQV YDLVTHQDIA HALAYEGQVE YEAITPYDKV DGSMDEEDMA
YIQVSLNVQG ETPLPQKKED SNTIYCSVQK PKKTAQTPQQ DAESPETPTY ENFT
