CD244_MOUSE
ID CD244_MOUSE Reviewed; 397 AA.
AC Q07763; O88654; Q3UV86; Q9JIE0;
DT 24-MAY-2004, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 3.
DT 03-AUG-2022, entry version 153.
DE RecName: Full=Natural killer cell receptor 2B4;
DE AltName: Full=NK cell type I receptor protein 2B4;
DE Short=NKR2B4;
DE AltName: Full=Non-MHC restricted killing associated;
DE AltName: Full=SLAM family member 4;
DE Short=SLAMF4;
DE AltName: Full=Signaling lymphocytic activation molecule 4;
DE AltName: CD_antigen=CD244;
DE Flags: Precursor;
GN Name=Cd244; Synonyms=2b4, Nmrk;
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] (ISOFORM 1).
RC STRAIN=C57BL/6J;
RX PubMed=8228228;
RA Mathew P.A., Garni-Wagner B.A., Land K., Takashima A., Stoneman E.,
RA Bennett M., Kumar V.;
RT "Cloning and characterization of the 2B4 gene encoding a molecule
RT associated with non-MHC-restricted killing mediated by activated natural
RT killer cells and T cells.";
RL J. Immunol. 151:5328-5337(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC STRAIN=A.CA;
RX PubMed=10941850; DOI=10.1007/s002510000198;
RA Kumaresan P.R., Huynh V.T., Mathew P.A.;
RT "Polymorphism in the 2B4 gene of inbred mouse strains.";
RL Immunogenetics 51:758-761(2000).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
RC STRAIN=C57BL/6J;
RA Stepp S.E., Schatzle J.D., Bennett M., Kumar V., Mathew P.A.;
RT "Characterization of genomic structure and alternative splicing of the
RT murine NK cell receptor 2B4.";
RL Submitted (AUG-1998) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=C57BL/6J; TISSUE=Bone;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [5]
RP FUNCTION, AND TISSUE SPECIFICITY.
RX PubMed=8326140;
RA Garni-Wagner B.A., Purohit A., Mathew P.A., Bennett M., Kumar V.;
RT "A novel function-associated molecule related to non-MHC-restricted
RT cytotoxicity mediated by activated natural killer cells and T cells.";
RL J. Immunol. 151:60-70(1993).
RN [6]
RP INTERACTION WITH CD48.
RX PubMed=9841922; DOI=10.1084/jem.188.11.2083;
RA Brown M.H., Boles K., van der Merwe P.A., Kumar V., Mathew P.A.,
RA Barclay A.N.;
RT "2B4, the natural killer and T cell immunoglobulin superfamily surface
RT protein, is a ligand for CD48.";
RL J. Exp. Med. 188:2083-2090(1998).
RN [7]
RP FUNCTION.
RX PubMed=11739483; DOI=10.4049/jimmunol.167.12.6706;
RA Kambayashi T., Assarsson E., Chambers B.J., Ljunggren H.G.;
RT "Regulation of CD8(+) T cell proliferation by 2B4/CD48 interactions.";
RL J. Immunol. 167:6706-6710(2001).
RN [8]
RP FUNCTION.
RX PubMed=12734329; DOI=10.4049/jimmunol.170.10.4881;
RA Lee K.M., Bhawan S., Majima T., Wei H., Nishimura M.I., Yagita H.,
RA Kumar V.;
RT "The NK cell receptor 2B4 augments antigen-specific T cell cytotoxicity
RT through CD48 ligation on neighboring T cells.";
RL J. Immunol. 170:4881-4885(2003).
RN [9]
RP FUNCTION, DOMAIN ITSM MOTIF, PHOSPHORYLATION AT TYR-266; TYR-325; TYR-344
RP AND TYR-369, AND MUTAGENESIS OF TYR-266; TYR-325; TYR-344 AND TYR-369.
RX PubMed=15169881; DOI=10.1128/mcb.24.12.5144-5156.2004;
RA Chen R., Relouzat F., Roncagalli R., Aoukaty A., Tan R., Latour S.,
RA Veillette A.;
RT "Molecular dissection of 2B4 signaling: implications for signal
RT transduction by SLAM-related receptors.";
RL Mol. Cell. Biol. 24:5144-5156(2004).
RN [10]
RP FUNCTION.
RX PubMed=15998796; DOI=10.1084/jem.20050449;
RA Bloch-Queyrat C., Fondaneche M.C., Chen R., Yin L., Relouzat F.,
RA Veillette A., Fischer A., Latour S.;
RT "Regulation of natural cytotoxicity by the adaptor SAP and the Src-related
RT kinase Fyn.";
RL J. Exp. Med. 202:181-192(2005).
RN [11]
RP FUNCTION, AND INTERACTION WITH SH2D1A; SH2D1B AND SH2D1B2.
RX PubMed=16127454; DOI=10.1038/ni1242;
RA Roncagalli R., Taylor J.E., Zhang S., Shi X., Chen R., Cruz-Munoz M.E.,
RA Yin L., Latour S., Veillette A.;
RT "Negative regulation of natural killer cell function by EAT-2, a SAP-
RT related adaptor.";
RL Nat. Immunol. 6:1002-1010(2005).
RN [12]
RP FUNCTION, AND INTERACTION WITH CD48.
RX PubMed=15905190; DOI=10.1182/blood-2005-01-0185;
RA Lee K.M., Forman J.P., McNerney M.E., Stepp S., Kuppireddi S., Guzior D.,
RA Latchman Y.E., Sayegh M.H., Yagita H., Park C.K., Oh S.B., Wuelfing C.,
RA Schatzle J., Mathew P.A., Sharpe A.H., Kumar V.;
RT "Requirement of homotypic NK-cell interactions through 2B4(CD244)/CD48 in
RT the generation of NK effector functions.";
RL Blood 107:3181-3188(2006).
RN [13]
RP FUNCTION.
RC STRAIN=129/SvJ, and C57BL/6J;
RX PubMed=16425036; DOI=10.1007/s00251-005-0056-3;
RA Calpe S., Erdos E., Liao G., Wang N., Rietdijk S., Simarro M., Scholtz B.,
RA Mooney J., Lee C.H., Shin M.S., Rajnavoelgyi E., Schatzle J.,
RA Morse H.C. III, Terhorst C., Lanyi A.;
RT "Identification and characterization of two related murine genes, Eat2a and
RT Eat2b, encoding single SH2-domain adapters.";
RL Immunogenetics 58:15-25(2006).
RN [14]
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 [15]
RP FUNCTION.
RX PubMed=20962259; DOI=10.4049/jimmunol.1001974;
RA Wang N., Calpe S., Westcott J., Castro W., Ma C., Engel P., Schatzle J.D.,
RA Terhorst C.;
RT "The adapters EAT-2A and -2B are positive regulators of CD244- and CD84-
RT dependent NK cell functions in the C57BL/6 mouse.";
RL J. Immunol. 185:5683-5687(2010).
RN [16]
RP FUNCTION.
RX PubMed=22683124; DOI=10.1016/j.immuni.2012.03.023;
RA Dong Z., Davidson D., Perez-Quintero L.A., Kurosaki T., Swat W.,
RA Veillette A.;
RT "The adaptor SAP controls NK cell activation by regulating the enzymes Vav-
RT 1 and SHIP-1 and by enhancing conjugates with target cells.";
RL Immunity 36:974-985(2012).
RN [17]
RP TISSUE SPECIFICITY, AND FUNCTION.
RX PubMed=25643613; DOI=10.1038/icb.2014.124;
RA Georgoudaki A.M., Khodabandeh S., Puiac S., Persson C.M., Larsson M.K.,
RA Lind M., Hammarfjord O., Nabatti T.H., Wallin R.P., Yrlid U., Rhen M.,
RA Kumar V., Chambers B.J.;
RT "CD244 is expressed on dendritic cells and regulates their functions.";
RL Immunol. Cell Biol. 93:581-590(2015).
RN [18]
RP STRUCTURE BY NMR OF 21-129, AND DISULFIDE BOND.
RX PubMed=15850375; DOI=10.1021/bi050139s;
RA Ames J.B., Vyas V., Lusin J.D., Mariuzza R.;
RT "NMR structure of the natural killer cell receptor 2B4 (CD244):
RT implications for ligand recognition.";
RL Biochemistry 44:6416-6423(2005).
RN [19]
RP X-RAY CRYSTALLOGRAPHY (1.63 ANGSTROMS) OF 19-129 ALONE AND IN COMPLEX WITH
RP CD48, AND DISULFIDE BOND.
RX PubMed=17950006; DOI=10.1016/j.immuni.2007.08.019;
RA Velikovsky C.A., Deng L., Chlewicki L.K., Fernandez M.M., Kumar V.,
RA Mariuzza R.A.;
RT "Structure of natural killer receptor 2B4 bound to CD48 reveals basis for
RT heterophilic recognition in signaling lymphocyte activation molecule
RT family.";
RL Immunity 27:572-584(2007).
CC -!- FUNCTION: Heterophilic receptor of the signaling lymphocytic activation
CC molecule (SLAM) family; its ligand is CD48. SLAM receptors triggered by
CC homo- or heterotypic cell-cell interactions are modulating the
CC activation and differentiation of a wide variety of immune cells and
CC thus are involved in the regulation and interconnection of both innate
CC and adaptive immune response. Activities are controlled by presence or
CC absence of small cytoplasmic adapter proteins, SH2D1A/SAP and/or
CC SH2D1B/EAT-2. Acts as activating natural killer (NK) cell receptor
CC (PubMed:8326140, PubMed:12734329, PubMed:19648922, PubMed:20962259).
CC Activating function implicates association with SH2D1A and FYN.
CC Downstreaming signaling involves predominantly VAV1, and, to a lesser
CC degree, INPP5D/SHIP1 and CBL. Signal attenuation in the absence of
CC SH2D1A is proposed to be dependent on INPP5D and to a lesser extent
CC PTPN6/SHP-1 and PTPN11/SHP-2. Stimulates NK cell cytotoxicity,
CC production of IFN-gamma and granule exocytosis (PubMed:8326140,
CC PubMed:15169881, PubMed:15998796, PubMed:22683124). Optimal expansion
CC and activation of NK cells seems to be dependent on the engagement of
CC CD244 with CD48 expressed on neighboring NK cells (PubMed:15905190).
CC Regulation of NK cell activity by adapters Sh2d1b and Sh2d1b2 is
CC reported conflictingly (PubMed:16127454, PubMed:16425036). Acts as
CC costimulator in NK activation by enhancing signals by other NK
CC receptors such as NCR3 and NCR1. At early stages of NK cell
CC differentiation may function as an inhibitory receptor possibly
CC ensuring the self-tolerance of developing NK cells (By similarity).
CC Involved in the regulation of CD8(+) T-cell proliferation; expression
CC on activated T-cells and binding to CD488 provides costimulatory-like
CC function for neighboring T-cells (PubMed:11739483). Inhibits
CC inflammatory responses in dendritic cells (DCs) (PubMed:25643613).
CC {ECO:0000250|UniProtKB:Q9BZW8, ECO:0000269|PubMed:11739483,
CC ECO:0000269|PubMed:12734329, ECO:0000269|PubMed:15169881,
CC ECO:0000269|PubMed:15998796, ECO:0000269|PubMed:19648922,
CC ECO:0000269|PubMed:20962259, ECO:0000269|PubMed:22683124,
CC ECO:0000269|PubMed:8326140, ECO:0000305|PubMed:16127454,
CC ECO:0000305|PubMed:16425036}.
CC -!- SUBUNIT: Interacts with CD48 (PubMed:9841922, PubMed:15905190).
CC Interacts (via phosphorylated ITSM 1-4) with SH2D1A/SAP (via SH2
CC domain); SH2D1A probably mediates association with FYN. Interacts (via
CC phosphorylated ITSM 3) with PTPN11/SHP-2, INPP5D/SHIP1, PTPN6/SHP-1 and
CC CSK; binding of SH2D1A prevents association with PTPN11, PTPN6 and CSK.
CC Interacts weakly (via phosphorylated ITSM 2) with PTPN11 and CSK.
CC Interacts with SH2D1B and SH2D1B2. Interacts with MHC class I proteins;
CC the interaction is proposed to prevent self-killing of NK cells (By
CC similarity). {ECO:0000250|UniProtKB:Q9BZW8,
CC ECO:0000269|PubMed:15905190, ECO:0000269|PubMed:16127454,
CC ECO:0000269|PubMed:9841922}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass type I
CC membrane protein {ECO:0000305}. Cell membrane {ECO:0000305}.
CC Note=Receptor engagement results in a recruitment to lipid drafts
CC essential for the subsequent tyrosine phosphorylation of the ITSMs.
CC {ECO:0000250|UniProtKB:Q9BZW8}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1; Synonyms=m2B4L;
CC IsoId=Q07763-1; Sequence=Displayed;
CC Name=2; Synonyms=m2B4S;
CC IsoId=Q07763-2; Sequence=VSP_010401, VSP_010402;
CC -!- TISSUE SPECIFICITY: Expressed in natural killer (NK) cells, T cells and
CC dendritic cells. {ECO:0000269|PubMed:25643613,
CC ECO:0000269|PubMed:8326140}.
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, ECO:0000305|PubMed:15169881}.
CC -!- PTM: N-linked glycosylation is essential for the binding to its ligand
CC CD48. Also O-glycosylated, in contrast, O-linked sialylation has a
CC negative impact on ligand binding (By similarity). {ECO:0000250}.
CC -!- PTM: Phosphorylated by FYN and CSK at tyrosine residues following
CC activation. Coligation with inhibitory receptors such as KIR2DL1
CC inhibits phosphorylation upon contact of NK cells with sensitive target
CC cells. {ECO:0000250|UniProtKB:Q9BZW8}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; L19057; AAA16353.1; -; mRNA.
DR EMBL; AF234831; AAF91290.1; -; mRNA.
DR EMBL; AF082803; AAC34859.1; -; mRNA.
DR EMBL; AK137505; BAE23386.1; -; mRNA.
DR CCDS; CCDS35778.1; -. [Q07763-1]
DR PIR; I49443; I49443.
DR RefSeq; NP_061199.2; NM_018729.2. [Q07763-1]
DR PDB; 1Z2K; NMR; -; A=21-129.
DR PDB; 2PTT; X-ray; 1.63 A; B=19-129.
DR PDB; 2PTU; X-ray; 2.38 A; A/B/C/D=19-129.
DR PDBsum; 1Z2K; -.
DR PDBsum; 2PTT; -.
DR PDBsum; 2PTU; -.
DR AlphaFoldDB; Q07763; -.
DR SMR; Q07763; -.
DR BioGRID; 201792; 2.
DR STRING; 10090.ENSMUSP00000004829; -.
DR GlyGen; Q07763; 7 sites.
DR iPTMnet; Q07763; -.
DR PhosphoSitePlus; Q07763; -.
DR EPD; Q07763; -.
DR PaxDb; Q07763; -.
DR PRIDE; Q07763; -.
DR ProteomicsDB; 283743; -. [Q07763-1]
DR ProteomicsDB; 283744; -. [Q07763-2]
DR Antibodypedia; 2392; 831 antibodies from 42 providers.
DR DNASU; 18106; -.
DR Ensembl; ENSMUST00000004829; ENSMUSP00000004829; ENSMUSG00000004709. [Q07763-1]
DR GeneID; 18106; -.
DR KEGG; mmu:18106; -.
DR UCSC; uc007dor.1; mouse. [Q07763-2]
DR UCSC; uc007dos.1; mouse. [Q07763-1]
DR CTD; 18106; -.
DR MGI; MGI:109294; Cd244.
DR VEuPathDB; HostDB:ENSMUSG00000004709; -.
DR eggNOG; ENOG502S7N7; Eukaryota.
DR GeneTree; ENSGT01030000234540; -.
DR HOGENOM; CLU_065827_0_0_1; -.
DR InParanoid; Q07763; -.
DR OMA; TCFCVWR; -.
DR OrthoDB; 1532935at2759; -.
DR PhylomeDB; Q07763; -.
DR TreeFam; TF334964; -.
DR Reactome; R-MMU-202733; Cell surface interactions at the vascular wall.
DR BioGRID-ORCS; 18106; 4 hits in 72 CRISPR screens.
DR EvolutionaryTrace; Q07763; -.
DR PRO; PR:Q07763; -.
DR Proteomes; UP000000589; Chromosome 1.
DR RNAct; Q07763; protein.
DR Bgee; ENSMUSG00000004709; Expressed in granulocyte and 49 other tissues.
DR ExpressionAtlas; Q07763; baseline and differential.
DR Genevisible; Q07763; MM.
DR GO; GO:0009897; C:external side of plasma membrane; IDA:MGI.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0042288; F:MHC class I protein binding; ISO:MGI.
DR GO; GO:0038023; F:signaling receptor activity; IEA:InterPro.
DR GO; GO:0002250; P:adaptive immune response; IEA:UniProtKB-KW.
DR GO; GO:0045087; P:innate immune response; IEA:UniProtKB-KW.
DR GO; GO:0001773; P:myeloid dendritic cell activation; IMP:UniProtKB.
DR GO; GO:0002323; P:natural killer cell activation involved in immune response; IMP:UniProtKB.
DR GO; GO:2000566; P:positive regulation of CD8-positive, alpha-beta T cell proliferation; IMP:UniProtKB.
DR GO; GO:0071663; P:positive regulation of granzyme B production; ISO:MGI.
DR GO; GO:0060732; P:positive regulation of inositol phosphate biosynthetic process; ISO:MGI.
DR GO; GO:0032729; P:positive regulation of interferon-gamma production; ISO:MGI.
DR GO; GO:0032757; P:positive regulation of interleukin-8 production; ISO:MGI.
DR GO; GO:0032819; P:positive regulation of natural killer cell proliferation; IMP:UniProtKB.
DR Gene3D; 2.60.40.10; -; 2.
DR InterPro; IPR036179; Ig-like_dom_sf.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR024304; NK_rcpt_2B4.
DR InterPro; IPR024303; NK_rcpt_2B4_Ig_dom.
DR PANTHER; PTHR12080:SF56; PTHR12080:SF56; 1.
DR Pfam; PF11465; Receptor_2B4; 1.
DR SUPFAM; SSF48726; SSF48726; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Adaptive immunity; Alternative splicing; Cell membrane;
KW Disulfide bond; Glycoprotein; Immunity; Immunoglobulin domain;
KW Innate immunity; Membrane; Phosphoprotein; Receptor; Reference proteome;
KW Repeat; Signal; Transmembrane; Transmembrane helix.
FT SIGNAL 1..19
FT /evidence="ECO:0000255"
FT CHAIN 20..397
FT /note="Natural killer cell receptor 2B4"
FT /id="PRO_0000014669"
FT TOPO_DOM 20..226
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 227..247
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 248..397
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 22..129
FT /note="Ig-like 1"
FT DOMAIN 131..215
FT /note="Ig-like 2"
FT REGION 277..300
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 264..269
FT /note="ITSM 1"
FT /evidence="ECO:0000250|UniProtKB:Q13291"
FT MOTIF 323..328
FT /note="ITSM 2"
FT /evidence="ECO:0000250|UniProtKB:Q13291"
FT MOTIF 342..347
FT /note="ITSM 3"
FT /evidence="ECO:0000250|UniProtKB:Q13291"
FT MOTIF 367..372
FT /note="ITSM 4"
FT /evidence="ECO:0000250|UniProtKB:Q13291"
FT COMPBIAS 278..292
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 266
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000305|PubMed:15169881"
FT MOD_RES 325
FT /note="Phosphotyrosine; by FYN"
FT /evidence="ECO:0000305|PubMed:15169881"
FT MOD_RES 344
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000305|PubMed:15169881"
FT MOD_RES 369
FT /note="Phosphotyrosine; by FYN"
FT /evidence="ECO:0000305|PubMed:15169881"
FT CARBOHYD 78
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 145
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 161
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 178
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 197
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 206
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 210
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 22..119
FT /evidence="ECO:0000269|PubMed:15850375,
FT ECO:0000269|PubMed:17950006"
FT DISULFID 154..196
FT /evidence="ECO:0000250"
FT VAR_SEQ 309..340
FT /note="LEQLPQQTFPGDRGTMYSMIQCKPSDSTSQEK -> MFSSLLAFLLHQFPGS
FT TQRGKEKRERAEKNGK (in isoform 2)"
FT /evidence="ECO:0000303|Ref.3"
FT /id="VSP_010401"
FT VAR_SEQ 341..397
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|Ref.3"
FT /id="VSP_010402"
FT MUTAGEN 266
FT /note="Y->F: Abolishes downstream phosphorylation of CBL
FT and VAV1; when associated with F-325, F-344 and F-369."
FT /evidence="ECO:0000269|PubMed:15169881"
FT MUTAGEN 266
FT /note="Y->F: Decreases downstream phosphorylation of CBL
FT and VAV1."
FT /evidence="ECO:0000269|PubMed:15169881"
FT MUTAGEN 325
FT /note="Y->F: Abolishes downstream phosphorylation of CBL
FT and VAV1; when associated with F-266, F-344 and F-369."
FT /evidence="ECO:0000269|PubMed:15169881"
FT MUTAGEN 325
FT /note="Y->F: Weakly decreases downstream phosphorylation of
FT CBL and VAV1; when associated with F-344 and F-369."
FT /evidence="ECO:0000269|PubMed:15169881"
FT MUTAGEN 344
FT /note="Y->F: Abolishes downstream phosphorylation of CBL
FT and VAV1; when associated with F-266, F-325 and F-369."
FT /evidence="ECO:0000269|PubMed:15169881"
FT MUTAGEN 344
FT /note="Y->F: Weakly decreases downstream phosphorylation of
FT CBL and VAV1; when associated with F-325 and F-369."
FT /evidence="ECO:0000269|PubMed:15169881"
FT MUTAGEN 369
FT /note="Y->F: Abolishes downstream phosphorylation of CBL
FT and VAV1; when associated with F-266, F-325 and F-344."
FT /evidence="ECO:0000269|PubMed:15169881"
FT MUTAGEN 369
FT /note="Y->F: Weakly decreases downstream phosphorylation of
FT CBL and VAV1; when associated with F-325 and F-344."
FT /evidence="ECO:0000269|PubMed:15169881"
FT CONFLICT 38
FT /note="Q -> P (in Ref. 2; AAF91290)"
FT /evidence="ECO:0000305"
FT CONFLICT 156
FT /note="V -> A (in Ref. 2; AAF91290)"
FT /evidence="ECO:0000305"
FT CONFLICT 166
FT /note="L -> FW (in Ref. 1; AAA16353)"
FT /evidence="ECO:0000305"
FT CONFLICT 362
FT /note="S -> Y (in Ref. 1; AAA16353)"
FT /evidence="ECO:0000305"
FT STRAND 25..31
FT /evidence="ECO:0007829|PDB:2PTT"
FT STRAND 37..39
FT /evidence="ECO:0007829|PDB:2PTT"
FT STRAND 50..56
FT /evidence="ECO:0007829|PDB:2PTT"
FT STRAND 60..62
FT /evidence="ECO:0007829|PDB:2PTU"
FT STRAND 63..73
FT /evidence="ECO:0007829|PDB:2PTT"
FT STRAND 76..78
FT /evidence="ECO:0007829|PDB:2PTT"
FT HELIX 79..83
FT /evidence="ECO:0007829|PDB:2PTT"
FT STRAND 85..87
FT /evidence="ECO:0007829|PDB:2PTT"
FT TURN 89..91
FT /evidence="ECO:0007829|PDB:2PTT"
FT STRAND 94..98
FT /evidence="ECO:0007829|PDB:2PTT"
FT HELIX 101..103
FT /evidence="ECO:0007829|PDB:2PTT"
FT STRAND 105..112
FT /evidence="ECO:0007829|PDB:2PTT"
FT STRAND 117..127
FT /evidence="ECO:0007829|PDB:2PTT"
SQ SEQUENCE 397 AA; 44836 MW; 0E2F0D946F7B63A7 CRC64;
MLGQAVLFTT FLLLRAHQGQ DCPDSSEEVV GVSGKPVQLR PSNIQTKDVS VQWKKTEQGS
HRKIEILNWY NDGPSWSNVS FSDIYGFDYG DFALSIKSAK LQDSGHYLLE ITNTGGKVCN
KNFQLLILDH VETPNLKAQW KPWTNGTCQL FLSCLVTKDD NVSYALYRGS TLISNQRNST
HWENQIDASS LHTYTCNVSN RASWANHTLN FTHGCQSVPS NFRFLPFGVI IVILVTLFLG
AIICFCVWTK KRKQLQFSPK EPLTIYEYVK DSRASRDQQG CSRASGSPSA VQEDGRGQRE
LDRRVSEVLE QLPQQTFPGD RGTMYSMIQC KPSDSTSQEK CTVYSVVQPS RKSGSKKRNQ
NSSLSCTVYE EVGNPWLKAH NPARLSRREL ENFDVYS
