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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_RAT               Reviewed;         282 AA.
P0C0K5; G3V9I4;
27-SEP-2005, integrated into UniProtKB/Swiss-Prot.
17-FEB-2016, sequence version 2.
12-SEP-2018, entry version 80.
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;
Rattus norvegicus (Rat).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Rattus.
NCBI_TaxID=10116;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=Brown Norway;
Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=Brown Norway;
PubMed=15057822; DOI=10.1038/nature02426;
Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J.,
Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G.,
Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G.,
Morgan M., Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G.,
Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S.,
Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T.,
Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T.,
Smith D., Lee H.-M., Gustafson E., Cahill P., Kana A.,
Doucette-Stamm L., Weinstock K., Fechtel K., Weiss R.B., Dunn D.M.,
Green E.D., Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K.,
Zhu B., Marra M., Schein J., Bosdet I., Fjell C., Jones S.,
Krzywinski M., Mathewson C., Siddiqui A., Wye N., McPherson J.,
Zhao S., Fraser C.M., Shetty J., Shatsman S., Geer K., Chen Y.,
Abramzon S., Nierman W.C., Havlak P.H., Chen R., Durbin K.J., Egan A.,
Ren Y., Song X.-Z., Li B., Liu Y., Qin X., Cawley S., Cooney A.J.,
D'Souza L.M., Martin K., Wu J.Q., Gonzalez-Garay M.L., Jackson A.R.,
Kalafus K.J., McLeod M.P., Milosavljevic A., Virk D., Volkov A.,
Wheeler D.A., Zhang Z., Bailey J.A., Eichler E.E., Tuzun E.,
Birney E., Mongin E., Ureta-Vidal A., Woodwark C., Zdobnov E.,
Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J.,
Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D.,
Schmidt J., Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M.,
Abril J.F., Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O.,
Poliakov A., Huebner N., Ganten D., Goesele C., Hummel O.,
Kreitler T., Lee Y.-A., Monti J., Schulz H., Zimdahl H.,
Himmelbauer H., Lehrach H., Jacob H.J., Bromberg S.,
Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E., Lazar J.,
Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M.,
Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E.,
Webber C., Brandt P., Nyakatura G., Adetobi M., Chiaromonte F.,
Elnitski L., Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K.,
Miller W., Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S.,
Zhang Y., Lindpaintner K., Andrews T.D., Caccamo M., Clamp M.,
Clarke L., Curwen V., Durbin R.M., Eyras E., Searle S.M., Cooper G.M.,
Batzoglou S., Brudno M., Sidow A., Stone E.A., Payseur B.A.,
Bourque G., Lopez-Otin C., Puente X.S., Chakrabarti K., Chatterji S.,
Dewey C., Pachter L., Bray N., Yap V.B., Caspi A., Tesler G.,
Pevzner P.A., Haussler D., Roskin K.M., Baertsch R., Clawson H.,
Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J., Rosenbloom K.R.,
Trumbower H., Weirauch M., Cooper D.N., Stenson P.D., Ma B., Brent M.,
Arumugam M., Shteynberg D., Copley R.R., Taylor M.S., Riethman H.,
Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S., Mockrin S.,
Collins F.S.;
"Genome sequence of the Brown Norway rat yields insights into
mammalian evolution.";
Nature 428:493-521(2004).
[3]
NUCLEOTIDE SEQUENCE [MRNA] OF 22-185.
STRAIN=Lewis.1AV1; TISSUE=Spleen;
PubMed=15020066; DOI=10.1016/j.jneuroim.2003.12.012;
Wefer J., Harris R.A., Lobell A.;
"Protective DNA vaccination against experimental autoimmune
encephalomyelitis is associated with induction of IFNbeta.";
J. Neuroimmunol. 149:66-76(2004).
[4]
TISSUE SPECIFICITY DURING EXPERIMENTAL AUTOIMMUNE ENCEPHALOMYELITIS.
PubMed=15913792; DOI=10.1016/j.jneuroim.2005.04.004;
Gielen A.W., Lobell A., Lidman O., Khademi M., Olsson T., Piehl F.;
"Expression of T cell immunoglobulin- and mucin-domain-containing
molecules-1 and -3 (TIM-1 and -3) in the rat nervous and immune
systems.";
J. Neuroimmunol. 164:93-104(2005).
-!- 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. Regulates macrophage activation. Inhibits T-
helper type 1 lymphocyte (Th1)-mediated auto- and alloimmune
responses and promotes immunological tolerance. 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. In contrast,
shown to activate TCR-induced signaling in T-cells probably
implicating ZAP70, LCP2, LCK and FYN. Expressed on Treg cells can
inhibit Th17 cell responses. 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. 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. 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. Receptor for phosphatidylserine (PtSer); PtSer-
binding is calcium-dependent. May recognize PtSer on apoptotic
cells leading to their phagocytosis. Mediates the engulfment of
apoptotic cells by dendritic cells. Expressed on T-cells, promotes
conjugation but not engulfment of apoptotic cells. Expressed on
dendritic cells (DCs) positively regulates innate immune response
and in synergy with Toll-like receptors promotes secretion of TNF-
alpha. 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. Can enhance mast cell production of Th2 cytokines Il-4,
IL-6 and IL-13. 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.
Negatively regulates NK cell function in LPS-induced endotoxic
shock. {ECO:0000250|UniProtKB:Q8TDQ0,
ECO:0000250|UniProtKB:Q8VIM0}.
-!- SUBUNIT: Interacts with HMGB1; impairs HMGB1 binding to B-DNA and
likely HMGB1-mediated innate immume response. Interacts with BAG6.
Interacts (phosphorylated) with PIK3R1 and PIK3R2. Interacts (not
dependent on its phosphorylation status) with FYN. 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. {ECO:0000250|UniProtKB:Q8TDQ0,
ECO:0000250|UniProtKB:Q8VIM0}.
-!- SUBCELLULAR LOCATION: 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}.
-!- MISCELLANEOUS: Expression is up-regulated in the spinal cord
during experimental autoimmune encephalomyelitis (EAE) and
following antigen restimulation of the encephalitogenic TCRBV8S2+
population. Expression was also detected by in situ hybridization
in resident cells of the nervous system.
-!- SIMILARITY: Belongs to the immunoglobulin superfamily. TIM family.
{ECO:0000305}.
-----------------------------------------------------------------------
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-----------------------------------------------------------------------
EMBL; CH473948; EDM04175.1; -; Genomic_DNA.
EMBL; AABR07029515; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AJ549521; CAD79372.1; -; mRNA.
RefSeq; NP_001094232.1; NM_001100762.1.
UniGene; Rn.219486; -.
ProteinModelPortal; P0C0K5; -.
SMR; P0C0K5; -.
STRING; 10116.ENSRNOP00000048351; -.
PaxDb; P0C0K5; -.
PRIDE; P0C0K5; -.
Ensembl; ENSRNOT00000048485; ENSRNOP00000048351; ENSRNOG00000031443.
GeneID; 363578; -.
KEGG; rno:363578; -.
UCSC; RGD:1305233; rat.
CTD; 84868; -.
RGD; 1305233; Havcr2.
eggNOG; ENOG410IJGA; Eukaryota.
eggNOG; ENOG410YSF7; LUCA.
GeneTree; ENSGT00440000039800; -.
HOGENOM; HOG000010109; -.
HOVERGEN; HBG098563; -.
InParanoid; P0C0K5; -.
KO; K20414; -.
OMA; GCRFAMP; -.
OrthoDB; EOG091G0MO1; -.
TreeFam; TF336163; -.
PRO; PR:P0C0K5; -.
Proteomes; UP000002494; Chromosome 10.
Bgee; ENSRNOG00000031443; Expressed in 8 organ(s), highest expression level in spleen.
GO; GO:0030054; C:cell junction; IEA:UniProtKB-SubCell.
GO; GO:0009986; C:cell surface; IDA:RGD.
GO; GO:0005769; C:early endosome; IEA:Ensembl.
GO; GO:0001772; C:immunological synapse; IEA:Ensembl.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
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; IEA:Ensembl.
GO; GO:0050830; P:defense response to Gram-positive bacterium; IEA:Ensembl.
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; IEA:Ensembl.
GO; GO:0060135; P:maternal process involved in female pregnancy; IEA:Ensembl.
GO; GO:0002519; P:natural killer cell tolerance induction; IEA:Ensembl.
GO; GO:1900425; P:negative regulation of defense response to bacterium; IEA:Ensembl.
GO; GO:0010629; P:negative regulation of gene expression; IEA:Ensembl.
GO; GO:0071656; P:negative regulation of granulocyte colony-stimulating factor production; IEA:Ensembl.
GO; GO:2000521; P:negative regulation of immunological synapse formation; IEA:Ensembl.
GO; GO:0032687; P:negative regulation of interferon-alpha production; IEA:Ensembl.
GO; GO:0032689; P:negative regulation of interferon-gamma production; IEA:Ensembl.
GO; GO:0032703; P:negative regulation of interleukin-2 production; IEA:Ensembl.
GO; GO:0032712; P:negative regulation of interleukin-3 production; IEA:Ensembl.
GO; GO:0032715; P:negative regulation of interleukin-6 production; IEA:Ensembl.
GO; GO:0030886; P:negative regulation of myeloid dendritic cell activation; IEA:Ensembl.
GO; GO:0032815; P:negative regulation of natural killer cell activation; IEA:Ensembl.
GO; GO:0002859; P:negative regulation of natural killer cell mediated cytotoxicity directed against tumor cell target; IEA:Ensembl.
GO; GO:0032088; P:negative regulation of NF-kappaB transcription factor activity; IEA:Ensembl.
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; IEA:Ensembl.
GO; GO:0042130; P:negative regulation of T cell proliferation; IEA:Ensembl.
GO; GO:0002826; P:negative regulation of T-helper 1 type immune response; IEA:Ensembl.
GO; GO:0032720; P:negative regulation of tumor necrosis factor production; IEA:Ensembl.
GO; GO:0032722; P:positive regulation of chemokine production; IEA:Ensembl.
GO; GO:1900426; P:positive regulation of defense response to bacterium; IEA:Ensembl.
GO; GO:0070374; P:positive regulation of ERK1 and ERK2 cascade; IEA:Ensembl.
GO; GO:0032729; P:positive regulation of interferon-gamma production; IEA:Ensembl.
GO; GO:0032732; P:positive regulation of interleukin-1 production; IEA:Ensembl.
GO; GO:0032753; P:positive regulation of interleukin-4 production; IEA:Ensembl.
GO; GO:0043032; P:positive regulation of macrophage activation; IEA:Ensembl.
GO; GO:1901224; P:positive regulation of NIK/NF-kappaB signaling; IEA:Ensembl.
GO; GO:0042102; P:positive regulation of T cell proliferation; IEA:Ensembl.
GO; GO:1904469; P:positive regulation of tumor necrosis factor secretion; IEA:Ensembl.
GO; GO:0002652; P:regulation of tolerance induction dependent upon immune response; IEA:Ensembl.
GO; GO:0034138; P:toll-like receptor 3 signaling pathway; IEA:Ensembl.
GO; GO:0034154; P:toll-like receptor 7 signaling pathway; IEA:Ensembl.
GO; GO:0034162; P:toll-like receptor 9 signaling pathway; IEA:Ensembl.
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.
2: Evidence at transcript level;
Adaptive immunity; Cell junction; Complete proteome; Disulfide bond;
Glycoprotein; Immunity; Immunoglobulin domain; Inflammatory response;
Innate immunity; Membrane; Metal-binding; Phosphoprotein;
Reference proteome; Signal; Transmembrane; Transmembrane helix.
SIGNAL 1 21 {ECO:0000255}.
CHAIN 22 282 Hepatitis A virus cellular receptor 2
homolog.
/FTId=PRO_0000072703.
TOPO_DOM 22 194 Extracellular. {ECO:0000255}.
TRANSMEM 195 215 Helical. {ECO:0000255}.
TOPO_DOM 216 282 Cytoplasmic. {ECO:0000255}.
DOMAIN 22 131 Ig-like V-type. {ECO:0000255|PROSITE-
ProRule:PRU00114}.
REGION 253 271 Interaction with BAG6.
{ECO:0000250|UniProtKB:Q8VIM0}.
METAL 115 115 Calcium; via carbonyl oxygen.
{ECO:0000250|UniProtKB:Q8VIM0}.
METAL 117 117 Calcium; via carbonyl oxygen.
{ECO:0000250|UniProtKB:Q8VIM0}.
METAL 120 120 Calcium. {ECO:0000250|UniProtKB:Q8VIM0}.
BINDING 62 62 Phosphatidylserine; via amide nitrogen.
{ECO:0000250|UniProtKB:Q8VIM0}.
BINDING 112 112 Phosphatidylserine.
{ECO:0000250|UniProtKB:Q8VIM0}.
BINDING 119 119 Phosphatidylserine; via amide nitrogen.
{ECO:0000250|UniProtKB:Q8VIM0}.
MOD_RES 257 257 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 147 147 O-linked (GalNAc...) threonine.
{ECO:0000250|UniProtKB:Q8TDQ0}.
CARBOHYD 173 173 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 38 111 {ECO:0000250|UniProtKB:Q8VIM0,
ECO:0000255|PROSITE-ProRule:PRU00114}.
DISULFID 52 63 {ECO:0000250|UniProtKB:Q8VIM0,
ECO:0000255|PROSITE-ProRule:PRU00114}.
DISULFID 58 110 {ECO:0000250|UniProtKB:Q8VIM0,
ECO:0000255|PROSITE-ProRule:PRU00114}.
SEQUENCE 282 AA; 30641 MW; 41A5D7F6B0DE96A8 CRC64;
MFSWLPFSCA LLLLQPLPAR SLENAYTAEV GKNAYLPCSY TVPAPGTLVP ICWGKGSCPL
LQCASVVLRT DETNVTYRKS RRYQLKGNFY KGDMSLTIKN VTLADSGTYC CRIQFPGPMN
DEKLELKLSI TEPAKVIPAG TAHGDSTTAS PRTLTTEGSG SETQTLVTLH DNNGTKISTW
ADEIKDSGET IRTAVHIGVG VSAGLALALI LGVLILKWYS SKKKKLQDLS LITLANSPPG
GLVNAGAGRI RSEENIYTIE ENIYEMENSN EYYCYVSSQQ PS


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