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T-lymphocyte surface antigen Ly-9 (Cell surface molecule Ly-9) (Lymphocyte antigen 9) (SLAM family member 3) (SLAMF3) (Signaling lymphocytic activation molecule 3) (CD antigen CD229)

 LY9_MOUSE               Reviewed;         654 AA.
Q01965; Q9ES29; Q9ES35; Q9ES36;
01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
20-JUN-2002, sequence version 2.
12-SEP-2018, entry version 148.
RecName: Full=T-lymphocyte surface antigen Ly-9;
AltName: Full=Cell surface molecule Ly-9;
AltName: Full=Lymphocyte antigen 9;
AltName: Full=SLAM family member 3;
Short=SLAMF3;
AltName: Full=Signaling lymphocytic activation molecule 3;
AltName: CD_antigen=CD229;
Flags: Precursor;
Name=Ly9; Synonyms=Ly-9;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], AND POLYMORPHISM.
STRAIN=129/Sv, BALB/cJ, and C57BL/6J; TISSUE=Spleen;
PubMed=10970093; DOI=10.1007/s002510000209;
Tovar V., de la Fuente M.A., Pizcueta P., Bosch J., Engel P.;
"Gene structure of the mouse leukocyte cell surface molecule Ly9.";
Immunogenetics 51:788-793(2000).
[2]
NUCLEOTIDE SEQUENCE [MRNA] OF 22-654, AND PROTEIN SEQUENCE OF 48-59.
PubMed=1506686;
Sandrin M.S., Gumley T.P., Henning M.M., Vaughan H.A., Gonez L.J.,
Trapani J.A., McKenzie I.F.C.;
"Isolation and characterization of cDNA clones for mouse Ly-9.";
J. Immunol. 149:1636-1641(1992).
[3]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-499, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
Thibault P.;
"The phagosomal proteome in interferon-gamma-activated macrophages.";
Immunity 30:143-154(2009).
[4]
FUNCTION.
PubMed=19648922; DOI=10.1038/ni.1763;
Dong Z., Cruz-Munoz M.E., Zhong M.C., Chen R., Latour S.,
Veillette A.;
"Essential function for SAP family adaptors in the surveillance of
hematopoietic cells by natural killer cells.";
Nat. Immunol. 10:973-980(2009).
[5]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Spleen;
PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
"A tissue-specific atlas of mouse protein phosphorylation and
expression.";
Cell 143:1174-1189(2010).
[6]
FUNCTION.
PubMed=23914190; DOI=10.3389/fimmu.2013.00225;
de Salort J., Cuenca M., Terhorst C., Engel P., Romero X.;
"Ly9 (CD229) cell-surface receptor is crucial for the development of
spontaneous autoantibody production to nuclear antigens.";
Front. Immunol. 4:225-225(2013).
[7]
FUNCTION.
PubMed=23225888; DOI=10.4049/jimmunol.1202435;
Sintes J., Cuenca M., Romero X., Bastos R., Terhorst C., Angulo A.,
Engel P.;
"Ly9 (CD229), a SLAM family receptor, negatively regulates the
development of thymic innate memory-like CD8+ T and invariant NKT
cells.";
J. Immunol. 190:21-26(2013).
-!- FUNCTION: Self-ligand receptor of the signaling lymphocytic
activation molecule (SLAM) family. SLAM receptors triggered by
homo- or heterotypic cell-cell interactions are modulating the
activation and differentiation of a wide variety of immune cells
and thus are involved in the regulation and interconnection of
both innate and adaptive immune response. Activities are
controlled by presence or absence of small cytoplasmic adapter
proteins, SH2D1A/SAP and/or SH2D1B/EAT-2 (PubMed:19648922). May
participate in adhesion reactions between T lymphocytes and
accessory cells by homophilic interaction. Promotes T-cell
differentiation into a helper T-cell Th17 phenotype leading to
increased IL-17 secretion; the costimulatory activity requires
SH2D1A. Promotes recruitment of RORC to the IL-17 promoter (By
similarity). May be involved in the maintenance of peripheral cell
tolerance by serving as a negative regulator of the immune
response. May disable autoantibody responses and inhibit IFN-gamma
secretion by CD4(+) T-cells (PubMed:23914190). May negatively
regulate the size of thymic innate CD8(+) T-cells and the
development of invariant natural killer T (iNKT) cells
(PubMed:23225888). Can promote natural killer (NK) cell activation
(PubMed:19648922). {ECO:0000250|UniProtKB:Q9HBG7,
ECO:0000269|PubMed:19648922, ECO:0000269|PubMed:23225888,
ECO:0000269|PubMed:23914190}.
-!- SUBUNIT: Interacts with SH2D1A and INPP5D. Interacts (via
phosphorylated cytoplasmic domain) with PTPN11; the interaction is
blocked by SH2D1A. {ECO:0000250|UniProtKB:Q9HBG7}.
-!- SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane
protein. Cell membrane {ECO:0000305}.
-!- TISSUE SPECIFICITY: Lymphocytes.
-!- DOMAIN: The ITSMs (immunoreceptor tyrosine-based switch motifs)
with the consensus sequence T-X-Y-X-X-[VI] present in SLAM family
receptors have overlapping specificity for activating and
inhibitory SH2 domain-containing binding partners. Especially they
mediate the interaction with the SH2 domain of SH2D1A and SH2D1B.
A 'three-pronged' mechanism is proposed involving threonine
(position -2), phosphorylated tyrosine (position 0) and
valine/isoleucine (position +3). {ECO:0000250|UniProtKB:Q13291}.
-----------------------------------------------------------------------
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Distributed under the Creative Commons Attribution (CC BY 4.0) License
-----------------------------------------------------------------------
EMBL; AF244131; AAG14997.1; -; mRNA.
EMBL; AF244130; AAG14996.1; -; mRNA.
EMBL; AF246701; AAG13268.2; -; Genomic_DNA.
EMBL; AF245117; AAG13268.2; JOINED; Genomic_DNA.
EMBL; AF245506; AAG13268.2; JOINED; Genomic_DNA.
EMBL; AF245118; AAG13268.2; JOINED; Genomic_DNA.
EMBL; AF245507; AAG13268.2; JOINED; Genomic_DNA.
EMBL; AF245508; AAG13268.2; JOINED; Genomic_DNA.
EMBL; AF245509; AAG13268.2; JOINED; Genomic_DNA.
EMBL; AF245510; AAG13268.2; JOINED; Genomic_DNA.
EMBL; AF246699; AAG13268.2; JOINED; Genomic_DNA.
EMBL; AF246700; AAG13268.2; JOINED; Genomic_DNA.
EMBL; M84412; AAA39468.1; -; mRNA.
CCDS; CCDS35779.1; -.
RefSeq; NP_001264897.1; NM_001277968.1.
RefSeq; NP_032560.2; NM_008534.3.
UniGene; Mm.560; -.
ProteinModelPortal; Q01965; -.
IntAct; Q01965; 4.
STRING; 10090.ENSMUSP00000069319; -.
iPTMnet; Q01965; -.
PhosphoSitePlus; Q01965; -.
SwissPalm; Q01965; -.
EPD; Q01965; -.
MaxQB; Q01965; -.
PaxDb; Q01965; -.
PRIDE; Q01965; -.
Ensembl; ENSMUST00000068878; ENSMUSP00000069319; ENSMUSG00000004707.
GeneID; 17085; -.
KEGG; mmu:17085; -.
UCSC; uc007dou.2; mouse.
CTD; 4063; -.
MGI; MGI:96885; Ly9.
eggNOG; ENOG410JJ3F; Eukaryota.
eggNOG; ENOG410ZAYK; LUCA.
GeneTree; ENSGT00530000063114; -.
HOGENOM; HOG000013143; -.
HOVERGEN; HBG030765; -.
InParanoid; Q01965; -.
KO; K06570; -.
OMA; YHAYVCS; -.
OrthoDB; EOG091G0KKU; -.
PhylomeDB; Q01965; -.
TreeFam; TF334964; -.
ChiTaRS; Ly9; mouse.
PRO; PR:Q01965; -.
Proteomes; UP000000589; Chromosome 1.
Bgee; ENSMUSG00000004707; Expressed in 42 organ(s), highest expression level in bone marrow macrophage.
CleanEx; MM_LY9; -.
ExpressionAtlas; Q01965; baseline and differential.
Genevisible; Q01965; MM.
GO; GO:0009986; C:cell surface; IDA:MGI.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0005886; C:plasma membrane; ISO:MGI.
GO; GO:0007155; P:cell adhesion; IEA:UniProtKB-KW.
GO; GO:0045087; P:innate immune response; IEA:UniProtKB-KW.
GO; GO:0032740; P:positive regulation of interleukin-17 production; ISO:MGI.
GO; GO:0072540; P:T-helper 17 cell lineage commitment; ISO:MGI.
Gene3D; 2.60.40.10; -; 4.
InterPro; IPR007110; Ig-like_dom.
InterPro; IPR036179; Ig-like_dom_sf.
InterPro; IPR013783; Ig-like_fold.
InterPro; IPR003599; Ig_sub.
Pfam; PF13895; Ig_2; 1.
SMART; SM00409; IG; 2.
SUPFAM; SSF48726; SSF48726; 4.
PROSITE; PS50835; IG_LIKE; 2.
1: Evidence at protein level;
Adaptive immunity; Cell adhesion; Cell membrane; Complete proteome;
Direct protein sequencing; Disulfide bond; Glycoprotein; Immunity;
Immunoglobulin domain; Innate immunity; Membrane; Phosphoprotein;
Polymorphism; Reference proteome; Repeat; Signal; Transmembrane;
Transmembrane helix.
SIGNAL 1 47 {ECO:0000269|PubMed:1506686}.
CHAIN 48 654 T-lymphocyte surface antigen Ly-9.
/FTId=PRO_0000014852.
TOPO_DOM 48 453 Extracellular. {ECO:0000255}.
TRANSMEM 454 474 Helical. {ECO:0000255}.
TOPO_DOM 475 654 Cytoplasmic. {ECO:0000255}.
DOMAIN 48 158 Ig-like V-type 1.
DOMAIN 159 243 Ig-like C2-type 1.
DOMAIN 250 362 Ig-like V-type 2.
DOMAIN 353 453 Ig-like C2-type 2.
MOTIF 599 604 ITSM 1 (atypical).
{ECO:0000250|UniProtKB:Q13291}.
MOTIF 623 628 ITSM 2. {ECO:0000250|UniProtKB:Q13291}.
MOD_RES 499 499 Phosphothreonine.
{ECO:0000244|PubMed:19144319}.
MOD_RES 601 601 Phosphotyrosine.
{ECO:0000250|UniProtKB:Q9HBG7}.
CARBOHYD 68 68 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 120 120 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 231 231 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 284 284 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 390 390 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 412 412 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 423 423 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 434 434 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 172 242 {ECO:0000255|PROSITE-ProRule:PRU00114}.
DISULFID 178 222 {ECO:0000255|PROSITE-ProRule:PRU00114}.
DISULFID 376 445 {ECO:0000255|PROSITE-ProRule:PRU00114}.
DISULFID 382 426 {ECO:0000255|PROSITE-ProRule:PRU00114}.
VARIANT 10 10 D -> G (in Ly9-1).
VARIANT 14 14 G -> S (in Ly9-1).
VARIANT 79 79 I -> T (in Ly9-1).
VARIANT 91 91 F -> S (in Ly9-1).
VARIANT 130 130 H -> Y (in Ly9-1).
VARIANT 139 139 I -> T (in Ly9-1).
VARIANT 362 362 P -> S.
VARIANT 366 366 K -> N (in Ly9-1).
VARIANT 377 377 E -> K (in Ly9-1).
VARIANT 550 550 M -> I (in Ly9-1).
VARIANT 592 592 G -> E (in Ly9-1).
CONFLICT 283 283 F -> L (in Ref. 2; AAA39468).
{ECO:0000305}.
CONFLICT 499 499 T -> P (in Ref. 2; AAA39468).
{ECO:0000305}.
CONFLICT 560 560 V -> L (in Ref. 2; AAA39468).
{ECO:0000305}.
CONFLICT 647 654 TPTYENFT -> SPYL (in Ref. 2; AAA39468).
{ECO:0000305}.
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


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