SLAF7_MOUSE
ID SLAF7_MOUSE Reviewed; 333 AA.
AC Q8BHK6; Q8BTL2; Q8CJ63; Q8CJ64; Q8CJ65; Q91XA0;
DT 24-MAY-2005, integrated into UniProtKB/Swiss-Prot.
DT 24-MAY-2005, sequence version 2.
DT 25-MAY-2022, entry version 142.
DE RecName: Full=SLAM family member 7;
DE AltName: Full=Leukocyte cell-surface antigen;
DE AltName: Full=Novel Ly9;
DE AltName: CD_antigen=CD319;
DE Flags: Precursor;
GN Name=Slamf7;
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] (ISOFORMS 2 AND 3), FUNCTION, AND TISSUE
RP SPECIFICITY.
RC STRAIN=BALB/cJ, and C57BL/6J; TISSUE=Thymus;
RX PubMed=12242590; DOI=10.1007/s00251-002-0483-3;
RA Tovar V., Del Valle J., Zapater N., Martin M., Romero X., Pizcueta P.,
RA Bosch J., Terhorst C., Engel P.;
RT "Mouse novel Ly9: a new member of the expanding CD150 (SLAM) family of
RT leukocyte cell-surface receptors.";
RL Immunogenetics 54:394-402(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC STRAIN=C57BL/6J; TISSUE=Aorta, Testis, and Vein;
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4).
RC STRAIN=FVB/N; TISSUE=Salivary gland;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [4]
RP FUNCTION, TISSUE SPECIFICITY, INTERACTION WITH SH2D1B; PTPN6; PTPN11;
RP INPP5D; CSK AND FYN, MUTAGENESIS OF TYR-282; TYR-287 AND TYR-302, DOMAIN
RP ITSM MOTIF, AND PHOSPHORYLATION AT TYR-282 AND TYR-302.
RX PubMed=19151721; DOI=10.1038/ni.1693;
RA Cruz-Munoz M.E., Dong Z., Shi X., Zhang S., Veillette A.;
RT "Influence of CRACC, a SLAM family receptor coupled to the adaptor EAT-2,
RT on natural killer cell function.";
RL Nat. Immunol. 10:297-305(2009).
RN [5]
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 [6]
RP INVOLVEMENT IN FULMINANT HEPATITIS.
RX PubMed=24098802; DOI=10.1371/journal.pone.0076681;
RA Li Y., Cao G., Zheng X., Wang J., Wei H., Tian Z., Sun R.;
RT "CRACC-CRACC interaction between Kupffer and NK cells contributes to poly
RT I:C/D-GalN induced hepatitis.";
RL PLoS ONE 8:E76681-E76681(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). Mediates natural killer (NK) cell activation through
CC a SH2D1A-independent extracellular signal-regulated ERK-mediated
CC pathway (By similarity). Positively regulates NK cell functions by a
CC mechanism dependent on the adapter SH2D1B. In addition to heterotypic
CC NK cells-target cells interactions also homotypic interactions between
CC NK cells may contribute to activation. However, in the absence of
CC SH2D1B, inhibits NK cell function. Acts also inhibitory in T-cells
CC (PubMed:19151721). May play a role in lymphocyte adhesion (By
CC similarity). In LPS-activated monocytes negatively regulates production
CC of pro-inflammatory cytokines (By similarity).
CC {ECO:0000250|UniProtKB:Q9NQ25, ECO:0000269|PubMed:19151721,
CC ECO:0000269|PubMed:19648922}.
CC -!- SUBUNIT: Interacts (via ITSM phosphorylated on Tyr-302) with SH2D1B,
CC PTPN6/SHP-1, PTPN11/SHP-2, INPP5D/SHIP1, CSK and FYN.
CC {ECO:0000269|PubMed:19151721}.
CC -!- INTERACTION:
CC Q8BHK6; O35324: Sh2d1b; NbExp=3; IntAct=EBI-11463802, EBI-8022357;
CC Q8BHK6; P06241: FYN; Xeno; NbExp=2; IntAct=EBI-11463802, EBI-515315;
CC -!- SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane protein.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=1;
CC IsoId=Q8BHK6-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8BHK6-2; Sequence=VSP_013784;
CC Name=3;
CC IsoId=Q8BHK6-3; Sequence=VSP_013783, VSP_013784;
CC Name=4;
CC IsoId=Q8BHK6-4; Sequence=VSP_013783;
CC -!- TISSUE SPECIFICITY: Expressed in spleen, lymph node, bone marrow and
CC testis. Lower levels detected in thymus. Expressed in NK cells, B-
CC cells, natural killer cells and activated T-cells.
CC {ECO:0000269|PubMed:12242590, ECO:0000269|PubMed:19151721}.
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}.
CC -!- MISCELLANEOUS: CRACC:CRACC interaction between NK cells and resident
CC Kupffer cells contribute to Poly I:C/D-GalN-induced fulminant
CC hepatitis. {ECO:0000269|PubMed:24098802}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH11154.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AF467909; AAN63158.1; -; mRNA.
DR EMBL; AF467910; AAN63159.1; -; mRNA.
DR EMBL; AF467911; AAN63160.1; -; mRNA.
DR EMBL; AK030135; BAC26801.1; -; mRNA.
DR EMBL; AK030148; BAC26810.1; -; mRNA.
DR EMBL; AK040678; BAC30665.1; -; mRNA.
DR EMBL; AK089525; BAC40914.1; -; mRNA.
DR EMBL; BC011154; AAH11154.1; ALT_FRAME; mRNA.
DR CCDS; CCDS15500.1; -. [Q8BHK6-1]
DR RefSeq; NP_653122.2; NM_144539.5.
DR RefSeq; XP_011237176.1; XM_011238874.2.
DR RefSeq; XP_011237177.1; XM_011238875.2.
DR RefSeq; XP_011237178.1; XM_011238876.2.
DR AlphaFoldDB; Q8BHK6; -.
DR SMR; Q8BHK6; -.
DR IntAct; Q8BHK6; 6.
DR STRING; 10090.ENSMUSP00000106907; -.
DR GlyGen; Q8BHK6; 5 sites.
DR iPTMnet; Q8BHK6; -.
DR PhosphoSitePlus; Q8BHK6; -.
DR EPD; Q8BHK6; -.
DR MaxQB; Q8BHK6; -.
DR PaxDb; Q8BHK6; -.
DR PRIDE; Q8BHK6; -.
DR ProteomicsDB; 261412; -. [Q8BHK6-1]
DR ProteomicsDB; 261413; -. [Q8BHK6-2]
DR ProteomicsDB; 261414; -. [Q8BHK6-3]
DR ProteomicsDB; 261415; -. [Q8BHK6-4]
DR ABCD; Q8BHK6; 21 sequenced antibodies.
DR DNASU; 75345; -.
DR GeneID; 75345; -.
DR KEGG; mmu:75345; -.
DR UCSC; uc007dov.1; mouse. [Q8BHK6-1]
DR UCSC; uc007doy.1; mouse. [Q8BHK6-2]
DR CTD; 57823; -.
DR MGI; MGI:1922595; Slamf7.
DR eggNOG; ENOG502SRN2; Eukaryota.
DR InParanoid; Q8BHK6; -.
DR OrthoDB; 990343at2759; -.
DR PhylomeDB; Q8BHK6; -.
DR TreeFam; TF334964; -.
DR Reactome; R-MMU-198933; Immunoregulatory interactions between a Lymphoid and a non-Lymphoid cell.
DR BioGRID-ORCS; 75345; 3 hits in 72 CRISPR screens.
DR ChiTaRS; Slamf7; mouse.
DR PRO; PR:Q8BHK6; -.
DR Proteomes; UP000000589; Unplaced.
DR RNAct; Q8BHK6; protein.
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:0005886; C:plasma membrane; IDA:MGI.
DR GO; GO:0042802; F:identical protein binding; ISO:MGI.
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:0032814; P:regulation of natural killer cell activation; IGI:MGI.
DR GO; GO:0042110; P:T cell activation; IBA:GO_Central.
DR Gene3D; 2.60.40.10; -; 2.
DR InterPro; IPR007110; Ig-like_dom.
DR InterPro; IPR036179; Ig-like_dom_sf.
DR InterPro; IPR013783; Ig-like_fold.
DR SUPFAM; SSF48726; SSF48726; 1.
DR PROSITE; PS50835; IG_LIKE; 1.
PE 1: Evidence at protein level;
KW Adaptive immunity; Alternative splicing; Disulfide bond; Glycoprotein;
KW Immunity; Immunoglobulin domain; Innate immunity; Membrane; Phosphoprotein;
KW Receptor; Reference proteome; Signal; Transmembrane; Transmembrane helix.
FT SIGNAL 1..22
FT /evidence="ECO:0000250"
FT CHAIN 23..333
FT /note="SLAM family member 7"
FT /id="PRO_0000014964"
FT TOPO_DOM 23..224
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 225..245
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 246..333
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 27..112
FT /note="Ig-like V-type"
FT DOMAIN 128..203
FT /note="Ig-like C2-type"
FT REGION 276..294
FT /note="Interaction with FYN when phosphorylated at Tyr-282"
FT MOTIF 300..305
FT /note="ITSM"
FT /evidence="ECO:0000250|UniProtKB:Q13291,
FT ECO:0000305|PubMed:19151721"
FT MOD_RES 282
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000305|PubMed:19151721"
FT MOD_RES 302
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000305|PubMed:19151721"
FT CARBOHYD 42
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 95
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 139
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 156
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 142..212
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 148..192
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT VAR_SEQ 255..289
FT /note="Missing (in isoform 3 and isoform 4)"
FT /evidence="ECO:0000303|PubMed:12242590,
FT ECO:0000303|PubMed:15489334"
FT /id="VSP_013783"
FT VAR_SEQ 312..333
FT /note="KSPSSLPAKPLVPRSLSFENVI -> RSCPAEHHLTCQPLSLDHARAQ (in
FT isoform 2 and isoform 3)"
FT /evidence="ECO:0000303|PubMed:12242590,
FT ECO:0000303|PubMed:16141072"
FT /id="VSP_013784"
FT MUTAGEN 282
FT /note="Y->F: No effect on interaction with SH2D1B,
FT increases NK cell activation in presence of SH2D1B,
FT abolishes NK cell inhibition in absence of SH2D1B."
FT /evidence="ECO:0000269|PubMed:19151721"
FT MUTAGEN 287
FT /note="Y->F: No effect on interaction with SH2D1, no effect
FT on NK cell activation in presence of SH2D1B, no effect on
FT NK cell inhibition in absence of SH2D1B."
FT /evidence="ECO:0000269|PubMed:19151721"
FT MUTAGEN 302
FT /note="Y->F: Disrupts interaction with SH2D1B, abolishes NK
FT cell activation in presence of SH2D1B, no effect on NK cell
FT inhibition in absence of SH2D1B."
FT /evidence="ECO:0000269|PubMed:19151721"
FT CONFLICT 118
FT /note="V -> A (in Ref. 1; AAN63158)"
FT /evidence="ECO:0000305"
FT CONFLICT 248
FT /note="T -> M (in Ref. 1; AAN63158 and 2; BAC26801/
FT BAC26810/BAC30665/BAC40914)"
FT /evidence="ECO:0000305"
FT CONFLICT 253
FT /note="G -> R (in Ref. 1; AAN63159 and 3)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 333 AA; 37187 MW; 8D40B823FEBE7129 CRC64;
MARFSTYIIF TSVLCQLTVT AASGTLKKVA GALDGSVTFT LNITEIKVDY VVWTFNTFFL
AMVKKDGVTS QSSNKERIVF PDGLYSMKLS QLKKNDSGAY RAEIYSTSSQ ASLIQEYVLH
VYKHLSRPKV TIDRQSNKNG TCVINLTCST DQDGENVTYS WKAVGQGDNQ FHDGATLSIA
WRSGEKDQAL TCMARNPVSN SFSTPVFPQK LCEDAATDLT SLRGILYILC FSAVLILFAV
LLTIFHTTWI KKGKGCEEDK KRVDRHQEMP DLCPHLEENA DYDTIPYTEK RRPEEDAPNT
FYSTVQIPKV VKSPSSLPAK PLVPRSLSFE NVI
