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Hepatitis A virus cellular receptor 2 homolog (HAVcr-2) (T-cell immunoglobulin and mucin domain-containing protein 3) (TIMD-3) (T-cell immunoglobulin mucin receptor 3) (TIM-3) (T-cell membrane protein 3)

 HAVR2_MOUSE             Reviewed;         281 AA.
Q8VIM0;
27-SEP-2005, integrated into UniProtKB/Swiss-Prot.
01-MAR-2002, sequence version 1.
22-NOV-2017, entry version 122.
RecName: Full=Hepatitis A virus cellular receptor 2 homolog;
Short=HAVcr-2;
AltName: Full=T-cell immunoglobulin and mucin domain-containing protein 3;
Short=TIMD-3;
AltName: Full=T-cell immunoglobulin mucin receptor 3;
Short=TIM-3;
AltName: Full=T-cell membrane protein 3;
Flags: Precursor;
Name=Havcr2; Synonyms=Tim3, Timd3;
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 [MRNA].
STRAIN=DBA/2J; TISSUE=Spleen;
PubMed=11725301; DOI=10.1038/ni739;
McIntire J.J., Umetsu S.E., Akbari O., Potter M., Kuchroo V.K.,
Barsh G.S., Freeman G.J., Umetsu D.T., DeKruyff R.H.;
"Identification of Tapr (an airway hyperreactivity regulatory locus)
and the linked Tim gene family.";
Nat. Immunol. 2:1109-1116(2001).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=C57BL/6J;
PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
Lindblad-Toh K., Eichler E.E., Ponting C.P.;
"Lineage-specific biology revealed by a finished genome assembly of
the mouse.";
PLoS Biol. 7:E1000112-E1000112(2009).
[3]
FUNCTION, AND TISSUE SPECIFICITY.
PubMed=11823861; DOI=10.1038/415536a;
Monney L., Sabatos C.A., Gaglia J.L., Ryu A., Waldner H., Chernova T.,
Manning S., Greenfield E.A., Coyle A.J., Sobel R.A., Freeman G.J.,
Kuchroo V.K.;
"Th1-specific cell surface protein Tim-3 regulates macrophage
activation and severity of an autoimmune disease.";
Nature 415:536-541(2002).
[4]
ALTERNATIVE SPLICING, FUNCTION, TISSUE SPECIFICITY, AND SUBCELLULAR
LOCATION.
PubMed=14556006; DOI=10.1038/ni988;
Sabatos C.A., Chakravarti S., Cha E., Schubart A., Sanchez-Fueyo A.,
Zheng X.X., Coyle A.J., Strom T.B., Freeman G.J., Kuchroo V.K.;
"Interaction of Tim-3 and Tim-3 ligand regulates T helper type 1
responses and induction of peripheral tolerance.";
Nat. Immunol. 4:1102-1110(2003).
[5]
FUNCTION, AND TISSUE SPECIFICITY.
PubMed=17620455; DOI=10.1182/blood-2006-11-058800;
Nakae S., Iikura M., Suto H., Akiba H., Umetsu D.T., Dekruyff R.H.,
Saito H., Galli S.J.;
"TIM-1 and TIM-3 enhancement of Th2 cytokine production by mast
cells.";
Blood 110:2565-2568(2007).
[6]
FUNCTION.
PubMed=18006747; DOI=10.1126/science.1148536;
Anderson A.C., Anderson D.E., Bregoli L., Hastings W.D., Kassam N.,
Lei C., Chandwaskar R., Karman J., Su E.W., Hirashima M., Bruce J.N.,
Kane L.P., Kuchroo V.K., Hafler D.A.;
"Promotion of tissue inflammation by the immune receptor Tim-3
expressed on innate immune cells.";
Science 318:1141-1143(2007).
[7]
PHOSPHATIDYLSERINE-BINDING, TISSUE SPECIFICITY, FUNCTION, AND
MUTAGENESIS OF GLN-62; ARG-112 AND 120-ASN-ASP-121.
PubMed=19224762; DOI=10.1182/blood-2008-10-185884;
Nakayama M., Akiba H., Takeda K., Kojima Y., Hashiguchi M., Azuma M.,
Yagita H., Okumura K.;
"Tim-3 mediates phagocytosis of apoptotic cells and cross-
presentation.";
Blood 113:3821-3830(2009).
[8]
FUNCTION.
PubMed=20937702; DOI=10.1084/jem.20100687;
Jayaraman P., Sada-Ovalle I., Beladi S., Anderson A.C., Dardalhon V.,
Hotta C., Kuchroo V.K., Behar S.M.;
"Tim3 binding to galectin-9 stimulates antimicrobial immunity.";
J. Exp. Med. 207:2343-2354(2010).
[9]
FUNCTION, INTERACTION WITH PIK3R1; PIK3R2 AND FYN, MUTAGENESIS OF
TYR-256 AND TYR-263, PHOSPHORYLATION, AND GLYCOSYLATION.
PubMed=21807895; DOI=10.1128/MCB.05297-11;
Lee J., Su E.W., Zhu C., Hainline S., Phuah J., Moroco J.A.,
Smithgall T.E., Kuchroo V.K., Kane L.P.;
"Phosphotyrosine-dependent coupling of Tim-3 to T-cell receptor
signaling pathways.";
Mol. Cell. Biol. 31:3963-3974(2011).
[10]
FUNCTION, INTERACTION WITH HMGB1, AND INVOLVEMENT IN CHEMOTHERAPY.
PubMed=22842346; DOI=10.1038/ni.2376;
Chiba S., Baghdadi M., Akiba H., Yoshiyama H., Kinoshita I.,
Dosaka-Akita H., Fujioka Y., Ohba Y., Gorman J.V., Colgan J.D.,
Hirashima M., Uede T., Takaoka A., Yagita H., Jinushi M.;
"Tumor-infiltrating DCs suppress nucleic acid-mediated innate immune
responses through interactions between the receptor TIM-3 and the
alarmin HMGB1.";
Nat. Immunol. 13:832-842(2012).
[11]
FUNCTION, INTERACTION WITH BAG6, AND MUTAGENESIS OF TYR-256 AND
TYR-263.
PubMed=22863785; DOI=10.1038/nm.2871;
Rangachari M., Zhu C., Sakuishi K., Xiao S., Karman J., Chen A.,
Angin M., Wakeham A., Greenfield E.A., Sobel R.A., Okada H.,
McKinnon P.J., Mak T.W., Addo M.M., Anderson A.C., Kuchroo V.K.;
"Bat3 promotes T cell responses and autoimmunity by repressing Tim-3-
mediated cell death and exhaustion.";
Nat. Med. 18:1394-1400(2012).
[12]
FUNCTION, AND TISSUE SPECIFICITY.
PubMed=24567532; DOI=10.4049/jimmunol.1302290;
Gorman J.V., Starbeck-Miller G., Pham N.L., Traver G.L., Rothman P.B.,
Harty J.T., Colgan J.D.;
"Tim-3 directly enhances CD8 T cell responses to acute Listeria
monocytogenes infection.";
J. Immunol. 192:3133-3142(2014).
[13]
FUNCTION, AND TISSUE SPECIFICITY.
PubMed=25337993; DOI=10.1371/journal.pone.0110585;
Hou H., Liu W., Wu S., Lu Y., Peng J., Zhu Y., Lu Y., Wang F., Sun Z.;
"Tim-3 negatively mediates natural killer cell function in LPS-induced
endotoxic shock.";
PLoS ONE 9:E110585-E110585(2014).
[14]
X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS) OF 29-233 IN COMPLEX WITH
PHOSPHATIDYLSERINE, DISULFIDE BOND, FUNCTION, DOMAIN, AND MUTAGENESIS
OF TRP-53; 60-TRP--GLN-62; 118-LEU-MET-119 AND 120-ASN-ASP-121.
PubMed=20083673; DOI=10.4049/jimmunol.0903059;
DeKruyff R.H., Bu X., Ballesteros A., Santpiago C., Chim Y.L.,
Lee H.H., Karisola P., Pichavant M., Kaplan G.G., Umetsu D.T.,
Freeman G.J., Casasnovas J.M.;
"T cell/transmembrane, Ig, and mucin-3 allelic variants differentially
recognize phosphatidylserine and mediate phagocytosis of apoptotic
cells.";
J. Immunol. 184:1918-1930(2010).
-!- FUNCTION: Cell surface receptor implicated in modulating innate
and adaptive immune responses. Generally accepted to have an
inhibiting function. Reports on stimulating functions suggest that
the activity may be influenced by the cellular context and/or the
respective ligand (PubMed:18006747). Regulates macrophage
activation (PubMed:11823861). Inhibits T-helper type 1 lymphocyte
(Th1)-mediated auto- and alloimmune responses and promotes
immunological tolerance (PubMed:14556006, PubMed:18006747). In
CD8+ cells attenuates TCR-induced signaling, specifically by
blocking NF-kappaB and NFAT promoter activities resulting in the
loss of IL-2 secretion. The function may implicate its association
with LCK proposed to impair phosphorylation of TCR subunits (By
similarity). In contrast, shown to activate TCR-induced signaling
in T-cells probably implicating ZAP70, LCP2, LCK and FYN
(PubMed:21807895). Expressed on Treg cells can inhibit Th17 cell
responses (By similarity). Receptor for LGALS9. Binding to LGALS9
is believed to result in suppression of T-cell responses; the
resulting apoptosis of antigen-specific cells may implicate HAVCR2
phosphorylation and disruption of its association with BAG6
(PubMed:22863785). Binding to LGALS9 is proposed to be involved in
innate immune response to intracellular pathogens. Expressed on
Th1 cells interacts with LGALS9 expressed on Mycobacterium
tuberculosis-infected macrophages to stimulate antibactericidal
activity including IL-1 beta secretion and to restrict
intracellular bacterial growth (PubMed:20937702). However, the
function as receptor for LGALS9 has been challenged (By
similarity). Also reported to enhance CD8+ T-cell responses to an
acute infection such as by Listeria monocytogenes
(PubMed:24567532). Receptor for phosphatidylserine (PtSer); PtSer-
binding is calcium-dependent (PubMed:20083673). May recognize
PtSer on apoptotic cells leading to their phagocytosis. Mediates
the engulfment of apoptotic cells by dendritic cells
(PubMed:19224762). Expressed on T-cells, promotes conjugation but
not engulfment of apoptotic cells (PubMed:20083673). Expressed on
dendritic cells (DCs) positively regulates innate immune response
and in synergy with Toll-like receptors promotes secretion of TNF-
alpha (PubMed:18006747). In tumor-imfiltrating DCs suppresses
nucleic acid-mediated innate immune repsonse by interaction with
HMGB1 and interfering with nucleic acid-sensing and trafficking of
nucleid acids to endosomes (PubMed:22842346). Can enhance mast
cell production of Th2 cytokines Il-4, IL-6 and IL-13
(PubMed:17620455). Expressed on natural killer (NK) cells acts as
a coreceptor to enhance IFN-gamma production in response to
LGALS9. In contrast, shown to suppress NK cell-mediated
cytotoxicity (By similarity). Negatively regulates NK cell
function in LPS-induced endotoxic shock (PubMed:25337993).
{ECO:0000250|UniProtKB:Q8TDQ0, ECO:0000269|PubMed:11823861,
ECO:0000269|PubMed:14556006, ECO:0000269|PubMed:17620455,
ECO:0000269|PubMed:18006747, ECO:0000269|PubMed:19224762,
ECO:0000269|PubMed:20083673, ECO:0000269|PubMed:20937702,
ECO:0000269|PubMed:21807895, ECO:0000269|PubMed:22842346,
ECO:0000269|PubMed:24567532, ECO:0000269|PubMed:25337993,
ECO:0000305|PubMed:22863785}.
-!- SUBUNIT: Interacts with HMGB1; impairs HMGB1 binding to B-DNA and
likely HMGB1-mediated innate immume response (PubMed:22842346).
Interacts with BAG6 (PubMed:22863785). Interacts (phosphorylated)
with PIK3R1 and PIK3R2. Interacts (not dependent on its
phosphorylation status) with FYN (PubMed:21807895). Interacts (in
basal state T-cells) with VAV1; AKT1/2, LCP2, ZAP70, SYK, PIK3R1,
FYN, SH3BP2 and SH2D2A. Interacts (in activated T-cells) with LCK
and PLCG (By similarity). {ECO:0000250|UniProtKB:Q8TDQ0,
ECO:0000269|PubMed:21807895, ECO:0000269|PubMed:22842346,
ECO:0000269|PubMed:22863785}.
-!- INTERACTION:
P63158:Hmgb1; NbExp=4; IntAct=EBI-6665112, EBI-6665811;
O08573-2:Lgals9; NbExp=4; IntAct=EBI-6665112, EBI-11316797;
-!- SUBCELLULAR LOCATION: Isoform 1: Membrane {ECO:0000305}; Single-
pass type I membrane protein {ECO:0000305}. Cell junction
{ECO:0000250|UniProtKB:Q8TDQ0}. Note=Localizes to the
immunological synapse between CD8+ T-cells and target cells.
{ECO:0000250|UniProtKB:Q8TDQ0}.
-!- SUBCELLULAR LOCATION: Isoform 2: Secreted
{ECO:0000269|PubMed:14556006}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1; Synonyms=Tim-3L, flTim-3;
IsoId=Q8VIM0-1; Sequence=Displayed;
Name=2; Synonyms=sTim-3;
IsoId=Q8VIM0-2; Sequence=VSP_058116;
-!- TISSUE SPECIFICITY: Expressed in T-helper type 1 lymphocytes. Not
expressed by naive T-cells but up-regulated as they differentiate
into T-helper-1 cells. Also expressed by differentiated type 1
CD8+ cytotoxic T-cells. Expressed on peritoneal exudate
macrophages, monocytes, and splenic dendritic cells (DCs).
Expression on natural killer (NK) cells is inversely associated
with IFN-gamma production during the initial 24 h of LPS-induced
endotoxic shock. Expressed on mast cells.
{ECO:0000269|PubMed:11823861, ECO:0000269|PubMed:14556006,
ECO:0000269|PubMed:17620455, ECO:0000269|PubMed:19224762,
ECO:0000269|PubMed:24567532, ECO:0000269|PubMed:25337993}.
-!- DOMAIN: The Ig-like V-type (immunoglobulin-like) domain mediates
binding to PtSer involving a Ca(2+) ion.
{ECO:0000269|PubMed:20083673}.
-!- PTM: Phosphorylated on tyrosine residues; modestly increased after
TCR/CD28 stimulation. Can be phosphorylated in the cytoplasmatic
domain by FYN (PubMed:21807895). Phosphorylation at Tyr-256 is
increased by stimulation with ligand LGALS9 (By similarity).
{ECO:0000250|UniProtKB:Q8TDQ0, ECO:0000269|PubMed:21807895}.
-!- PTM: N-glycosylated. {ECO:0000269|PubMed:21807895}.
-!- POLYMORPHISM: Polymorphic differences between BALB/c and HBA
alleles in the Ig-like V-type domain are the reason for distinct
binding affinities for PtSer. The HBA2 allele binds PtSer
approximately 50% less than BALB/c. {ECO:0000269|PubMed:20083673}.
-!- MISCELLANEOUS: Belongs to the T-cell and airway phenotype
regulator (Tapr) locus, a single chromosomal region that confers
reduced T-helper type 2 responsiveness and protects against airway
hyperactivity (AHR), the hallmark of human asthma.
-!- MISCELLANEOUS: In vivo administration of antibody to HAVCR2
enhances the clinical and pathological severity of experimental
autoimmune encephalomyelitis (EAE), a Th1-dependent autoimmune
disease and increases the number and activation level of
macrophages.
-!- MISCELLANEOUS: Endogenous expression on dendritic cells is
proposed to act as a negative regulator of chemotherapy-induced
antitumor responses. {ECO:0000269|PubMed:22842346}.
-!- SIMILARITY: Belongs to the immunoglobulin superfamily. TIM family.
{ECO:0000305}.
-!- CAUTION: Experimental results based on the injection of
HAVCR2/TIM-3 antibodies or use of HAVCR2/TIM-3-Fc fusion proteins
can reflect changes in the activity of several cell types and
pathways as HAVCR2/TIM-3 is expressed by multiple immune cell
types. {ECO:0000305}.
-!- WEB RESOURCE: Name=Functional Glycomics Gateway - Glycan Binding;
Note=TIMD-3;
URL="http://www.functionalglycomics.org/glycomics/GBPServlet?&operationType=view&cbpId=cbp_mou_other_382";
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EMBL; AF399831; AAL35776.1; -; mRNA.
EMBL; AL669948; -; NOT_ANNOTATED_CDS; Genomic_DNA.
CCDS; CCDS36135.1; -. [Q8VIM0-1]
RefSeq; NP_599011.2; NM_134250.2. [Q8VIM0-1]
UniGene; Mm.72168; -.
PDB; 3KAA; X-ray; 3.00 A; A/B=29-133.
PDBsum; 3KAA; -.
ProteinModelPortal; Q8VIM0; -.
SMR; Q8VIM0; -.
BioGrid; 228588; 1.
DIP; DIP-61460N; -.
IntAct; Q8VIM0; 8.
STRING; 10090.ENSMUSP00000020668; -.
iPTMnet; Q8VIM0; -.
PhosphoSitePlus; Q8VIM0; -.
PaxDb; Q8VIM0; -.
PRIDE; Q8VIM0; -.
Ensembl; ENSMUST00000020668; ENSMUSP00000020668; ENSMUSG00000020399. [Q8VIM0-1]
GeneID; 171285; -.
KEGG; mmu:171285; -.
UCSC; uc011xtp.1; mouse. [Q8VIM0-1]
CTD; 84868; -.
MGI; MGI:2159682; Havcr2.
eggNOG; ENOG410IJGA; Eukaryota.
eggNOG; ENOG410YSF7; LUCA.
GeneTree; ENSGT00440000039800; -.
HOVERGEN; HBG098563; -.
InParanoid; Q8VIM0; -.
KO; K20414; -.
OMA; GCRFAMP; -.
OrthoDB; EOG091G0MO1; -.
PhylomeDB; Q8VIM0; -.
TreeFam; TF336163; -.
ChiTaRS; Havcr2; mouse.
EvolutionaryTrace; Q8VIM0; -.
PRO; PR:Q8VIM0; -.
Proteomes; UP000000589; Chromosome 11.
Bgee; ENSMUSG00000020399; -.
CleanEx; MM_HAVCR2; -.
ExpressionAtlas; Q8VIM0; baseline and differential.
Genevisible; Q8VIM0; MM.
GO; GO:0030054; C:cell junction; IEA:UniProtKB-SubCell.
GO; GO:0009986; C:cell surface; IDA:UniProtKB.
GO; GO:0005769; C:early endosome; IDA:UniProtKB.
GO; GO:0070062; C:extracellular exosome; ISO:MGI.
GO; GO:0001772; C:immunological synapse; IDA:UniProtKB.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0005886; C:plasma membrane; TAS:Reactome.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0002250; P:adaptive immune response; IEA:UniProtKB-KW.
GO; GO:0071222; P:cellular response to lipopolysaccharide; IDA:UniProtKB.
GO; GO:0050830; P:defense response to Gram-positive bacterium; IMP:UniProtKB.
GO; GO:0006954; P:inflammatory response; IEA:UniProtKB-KW.
GO; GO:0045087; P:innate immune response; IEA:UniProtKB-KW.
GO; GO:0002281; P:macrophage activation involved in immune response; IMP:UniProtKB.
GO; GO:0060135; P:maternal process involved in female pregnancy; IDA:UniProtKB.
GO; GO:0002519; P:natural killer cell tolerance induction; ISO:MGI.
GO; GO:1900425; P:negative regulation of defense response to bacterium; IMP:UniProtKB.
GO; GO:0010629; P:negative regulation of gene expression; ISO:MGI.
GO; GO:0071656; P:negative regulation of granulocyte colony-stimulating factor production; ISO:MGI.
GO; GO:0002838; P:negative regulation of immune response to tumor cell; IMP:UniProtKB.
GO; GO:2000521; P:negative regulation of immunological synapse formation; IMP:UniProtKB.
GO; GO:0045824; P:negative regulation of innate immune response; IMP:UniProtKB.
GO; GO:0032687; P:negative regulation of interferon-alpha production; ISO:MGI.
GO; GO:0032689; P:negative regulation of interferon-gamma production; IMP:UniProtKB.
GO; GO:0032703; P:negative regulation of interleukin-2 production; IMP:UniProtKB.
GO; GO:0032712; P:negative regulation of interleukin-3 production; ISO:MGI.
GO; GO:0032715; P:negative regulation of interleukin-6 production; IMP:UniProtKB.
GO; GO:0030886; P:negative regulation of myeloid dendritic cell activation; ISO:MGI.
GO; GO:0032815; P:negative regulation of natural killer cell activation; IMP:UniProtKB.
GO; GO:0002859; P:negative regulation of natural killer cell mediated cytotoxicity directed against tumor cell target; IMP:UniProtKB.
GO; GO:0032088; P:negative regulation of NF-kappaB transcription factor activity; ISO:MGI.
GO; GO:2001189; P:negative regulation of T cell activation via T cell receptor contact with antigen bound to MHC molecule on antigen presenting cell; ISO:MGI.
GO; GO:0042130; P:negative regulation of T cell proliferation; IMP:UniProtKB.
GO; GO:0002826; P:negative regulation of T-helper 1 type immune response; IMP:UniProtKB.
GO; GO:0032720; P:negative regulation of tumor necrosis factor production; ISO:MGI.
GO; GO:0032480; P:negative regulation of type I interferon production; IMP:UniProtKB.
GO; GO:0032722; P:positive regulation of chemokine production; IMP:UniProtKB.
GO; GO:0001819; P:positive regulation of cytokine production; IMP:UniProtKB.
GO; GO:1900426; P:positive regulation of defense response to bacterium; IMP:UniProtKB.
GO; GO:0070374; P:positive regulation of ERK1 and ERK2 cascade; IDA:UniProtKB.
GO; GO:0045089; P:positive regulation of innate immune response; IMP:UniProtKB.
GO; GO:0032729; P:positive regulation of interferon-gamma production; IMP:UniProtKB.
GO; GO:0032732; P:positive regulation of interleukin-1 production; IMP:UniProtKB.
GO; GO:0032753; P:positive regulation of interleukin-4 production; ISO:MGI.
GO; GO:0043032; P:positive regulation of macrophage activation; IMP:UniProtKB.
GO; GO:1901224; P:positive regulation of NIK/NF-kappaB signaling; IDA:UniProtKB.
GO; GO:0042102; P:positive regulation of T cell proliferation; IMP:UniProtKB.
GO; GO:1904469; P:positive regulation of tumor necrosis factor secretion; IMP:UniProtKB.
GO; GO:0002652; P:regulation of tolerance induction dependent upon immune response; IMP:UniProtKB.
GO; GO:0034138; P:toll-like receptor 3 signaling pathway; IMP:UniProtKB.
GO; GO:0034154; P:toll-like receptor 7 signaling pathway; IMP:UniProtKB.
GO; GO:0034162; P:toll-like receptor 9 signaling pathway; IMP:UniProtKB.
Gene3D; 2.60.40.10; -; 1.
InterPro; IPR007110; Ig-like_dom.
InterPro; IPR036179; Ig-like_dom_sf.
InterPro; IPR013783; Ig-like_fold.
InterPro; IPR003599; Ig_sub.
InterPro; IPR013106; Ig_V-set.
Pfam; PF07686; V-set; 1.
SMART; SM00409; IG; 1.
SUPFAM; SSF48726; SSF48726; 1.
PROSITE; PS50835; IG_LIKE; 1.
1: Evidence at protein level;
3D-structure; Adaptive immunity; Alternative splicing; Cell junction;
Complete proteome; Disulfide bond; Glycoprotein; Immunity;
Immunoglobulin domain; Inflammatory response; Innate immunity;
Membrane; Metal-binding; Phosphoprotein; Reference proteome; Secreted;
Signal; Transmembrane; Transmembrane helix.
SIGNAL 1 19 {ECO:0000255}.
CHAIN 20 281 Hepatitis A virus cellular receptor 2
homolog.
/FTId=PRO_0000042102.
TOPO_DOM 20 193 Extracellular. {ECO:0000255}.
TRANSMEM 194 214 Helical. {ECO:0000255}.
TOPO_DOM 215 281 Cytoplasmic. {ECO:0000255}.
DOMAIN 20 125 Ig-like V-type.
REGION 252 270 Interaction with BAG6.
{ECO:0000269|PubMed:22863785}.
COMPBIAS 221 224 Poly-Lys.
METAL 115 115 Calcium; via carbonyl oxygen.
{ECO:0000244|PDB:3KAA,
ECO:0000269|PubMed:20083673}.
METAL 117 117 Calcium; via carbonyl oxygen.
{ECO:0000244|PDB:3KAA,
ECO:0000269|PubMed:20083673}.
METAL 120 120 Calcium. {ECO:0000244|PDB:3KAA,
ECO:0000269|PubMed:20083673}.
BINDING 61 61 Phosphatidylserine.
{ECO:0000244|PDB:3KAA,
ECO:0000269|PubMed:20083673}.
BINDING 62 62 Phosphatidylserine; via amide nitrogen.
{ECO:0000244|PDB:3KAA,
ECO:0000269|PubMed:20083673}.
BINDING 112 112 Phosphatidylserine.
{ECO:0000244|PDB:3KAA,
ECO:0000269|PubMed:20083673}.
BINDING 119 119 Phosphatidylserine; via amide nitrogen.
{ECO:0000244|PDB:3KAA,
ECO:0000269|PubMed:20083673}.
MOD_RES 256 256 Phosphotyrosine; by ITK.
{ECO:0000250|UniProtKB:Q8TDQ0}.
CARBOHYD 74 74 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 100 100 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 146 146 O-linked (GalNAc...) threonine.
{ECO:0000250|UniProtKB:Q8TDQ0}.
CARBOHYD 172 172 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 38 111 {ECO:0000244|PDB:3KAA,
ECO:0000255|PROSITE-ProRule:PRU00114,
ECO:0000269|PubMed:20083673}.
DISULFID 52 63 {ECO:0000244|PDB:3KAA,
ECO:0000255|PROSITE-ProRule:PRU00114,
ECO:0000269|PubMed:20083673}.
DISULFID 58 110 {ECO:0000244|PDB:3KAA,
ECO:0000255|PROSITE-ProRule:PRU00114,
ECO:0000269|PubMed:20083673}.
VAR_SEQ 133 217 AKVTPAQTAHGDSTTASPRTLTTERNGSETQTLVTLHNNNG
TKISTWADEIKDSGETIRTAIHIGVGVSAGLTLALIIGVLI
LKW -> G (in isoform 2).
{ECO:0000269|PubMed:14556006}.
/FTId=VSP_058116.
MUTAGEN 53 53 W->A: Greatly decreases
phosphatidylserine binding.
{ECO:0000269|PubMed:20083673}.
MUTAGEN 60 62 WSQ->VFE: Decreases phosphatidylserine
binding. {ECO:0000269|PubMed:20083673}.
MUTAGEN 62 62 Q->A: No effect on phagocytic activity.
{ECO:0000269|PubMed:19224762}.
MUTAGEN 112 112 R->A: Abolishes phagocytic activity.
{ECO:0000269|PubMed:19224762}.
MUTAGEN 118 119 LM->AA: Decreases phosphatidylserine
binding. {ECO:0000269|PubMed:20083673}.
MUTAGEN 120 121 ND->AA: Decreases phosphatidylserine
binding, abolishes phagocytic activity.
{ECO:0000269|PubMed:19224762,
ECO:0000269|PubMed:20083673}.
MUTAGEN 256 256 Y->F: Abolishes phosphorylation, disrupts
interaction with PIK3R1 and PIK3R2, no
LGALS9-mediated disruption of interaction
with BAG6; when associated with F-263.
{ECO:0000269|PubMed:21807895,
ECO:0000269|PubMed:22863785}.
MUTAGEN 263 263 Y->F: Abolishes phosphorylation, disrupts
interaction with PIK3R1 and PIK3R2, no
LGALS9-mediated disruption of interaction
with BAG6; when associated with F-256.
{ECO:0000269|PubMed:21807895,
ECO:0000269|PubMed:22863785}.
STRAND 34 36 {ECO:0000244|PDB:3KAA}.
STRAND 51 57 {ECO:0000244|PDB:3KAA}.
STRAND 60 62 {ECO:0000244|PDB:3KAA}.
STRAND 66 70 {ECO:0000244|PDB:3KAA}.
STRAND 72 77 {ECO:0000244|PDB:3KAA}.
STRAND 81 85 {ECO:0000244|PDB:3KAA}.
HELIX 89 91 {ECO:0000244|PDB:3KAA}.
STRAND 96 100 {ECO:0000244|PDB:3KAA}.
HELIX 103 105 {ECO:0000244|PDB:3KAA}.
STRAND 107 113 {ECO:0000244|PDB:3KAA}.
STRAND 116 119 {ECO:0000244|PDB:3KAA}.
STRAND 125 130 {ECO:0000244|PDB:3KAA}.
SEQUENCE 281 AA; 30934 MW; C0349E4BD0E5761D CRC64;
MFSGLTLNCV LLLLQLLLAR SLENAYVFEV GKNAYLPCSY TLSTPGALVP MCWGKGFCPW
SQCTNELLRT DERNVTYQKS SRYQLKGDLN KGDVSLIIKN VTLDDHGTYC CRIQFPGLMN
DKKLELKLDI KAAKVTPAQT AHGDSTTASP RTLTTERNGS ETQTLVTLHN NNGTKISTWA
DEIKDSGETI RTAIHIGVGV SAGLTLALII GVLILKWYSC KKKKLSSLSL ITLANLPPGG
LANAGAVRIR SEENIYTIEE NVYEVENSNE YYCYVNSQQP S


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