SLAF8_MOUSE
ID SLAF8_MOUSE Reviewed; 278 AA.
AC Q9D3G2; Q8R3T7;
DT 07-JUN-2005, integrated into UniProtKB/Swiss-Prot.
DT 07-JUN-2005, sequence version 2.
DT 25-MAY-2022, entry version 120.
DE RecName: Full=SLAM family member 8;
DE AltName: Full=B-lymphocyte activator macrophage expressed;
DE AltName: CD_antigen=CD353;
DE Flags: Precursor;
GN Name=Slamf8; Synonyms=Blame;
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], AND FUNCTION.
RX PubMed=11313408; DOI=10.4049/jimmunol.166.9.5675;
RA Kingsbury G.A., Feeney L.A., Nong Y., Calandra S.A., Murphy C.J.,
RA Corcoran J.M., Wang Y., Prabhu Das M.R., Busfield S.J., Fraser C.C.,
RA Villeval J.-L.;
RT "Cloning, expression, and function of BLAME, a novel member of the CD2
RT family.";
RL J. Immunol. 166:5675-5680(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Thymus;
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].
RC STRAIN=Czech II; TISSUE=Mammary tumor;
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).
CC -!- FUNCTION: May play a role in B-lineage commitment and/or modulation of
CC signaling through the B-cell receptor. {ECO:0000269|PubMed:11313408}.
CC -!- SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane protein.
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DR EMBL; AK017911; BAB30999.1; -; mRNA.
DR EMBL; BC024587; AAH24587.1; -; mRNA.
DR CCDS; CCDS15517.1; -.
DR RefSeq; NP_083360.2; NM_029084.3.
DR AlphaFoldDB; Q9D3G2; -.
DR SMR; Q9D3G2; -.
DR STRING; 10090.ENSMUSP00000067527; -.
DR GlyGen; Q9D3G2; 2 sites.
DR PaxDb; Q9D3G2; -.
DR PRIDE; Q9D3G2; -.
DR DNASU; 74748; -.
DR GeneID; 74748; -.
DR KEGG; mmu:74748; -.
DR CTD; 56833; -.
DR MGI; MGI:1921998; Slamf8.
DR eggNOG; ENOG502S183; Eukaryota.
DR InParanoid; Q9D3G2; -.
DR OrthoDB; 1532935at2759; -.
DR PhylomeDB; Q9D3G2; -.
DR BioGRID-ORCS; 74748; 3 hits in 74 CRISPR screens.
DR PRO; PR:Q9D3G2; -.
DR Proteomes; UP000000589; Unplaced.
DR RNAct; Q9D3G2; protein.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0042802; F:identical protein binding; IDA:MGI.
DR GO; GO:0038023; F:signaling receptor activity; IDA:MGI.
DR GO; GO:0002336; P:B-1 B cell lineage commitment; IDA:UniProtKB.
DR GO; GO:0071466; P:cellular response to xenobiotic stimulus; IMP:MGI.
DR GO; GO:0042742; P:defense response to bacterium; IMP:MGI.
DR GO; GO:0002232; P:leukocyte chemotaxis involved in inflammatory response; IMP:MGI.
DR GO; GO:2000509; P:negative regulation of dendritic cell chemotaxis; IMP:MGI.
DR GO; GO:0010760; P:negative regulation of macrophage chemotaxis; IMP:MGI.
DR GO; GO:0090027; P:negative regulation of monocyte chemotaxis; IMP:MGI.
DR GO; GO:1902623; P:negative regulation of neutrophil migration; IMP:MGI.
DR GO; GO:0060266; P:negative regulation of respiratory burst involved in inflammatory response; IMP:MGI.
DR GO; GO:0090383; P:phagosome acidification; IMP:MGI.
DR GO; GO:0045577; P:regulation of B cell differentiation; IDA:UniProtKB.
DR GO; GO:0043549; P:regulation of kinase activity; IMP:MGI.
DR GO; GO:0033860; P:regulation of NAD(P)H oxidase activity; IMP:MGI.
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; 2.
DR PROSITE; PS50835; IG_LIKE; 1.
PE 2: Evidence at transcript level;
KW Disulfide bond; Glycoprotein; Immunoglobulin domain; Membrane;
KW Reference proteome; Signal; Transmembrane; Transmembrane helix.
FT SIGNAL 1..20
FT /evidence="ECO:0000250"
FT CHAIN 21..278
FT /note="SLAM family member 8"
FT /id="PRO_0000014966"
FT TOPO_DOM 21..231
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 232..252
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 253..278
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 126..213
FT /note="Ig-like C2-type"
FT CARBOHYD 83
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 154
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 150..199
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT CONFLICT 107
FT /note="G -> R (in Ref. 2; BAB30999)"
FT /evidence="ECO:0000305"
FT CONFLICT 164
FT /note="W -> R (in Ref. 2; BAB30999)"
FT /evidence="ECO:0000305"
FT CONFLICT 175
FT /note="R -> H (in Ref. 2; BAB30999)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 278 AA; 30646 MW; 7E33B1D9E010EB0A CRC64;
MWSLWSLLLF EALLPVVVVS VQVLSKVGDS ELLVAECPPG FQVREAIWRS LWPSEELLAT
FFRGSLETLY HSRFLGRVQL YDNLSLELGP LKPGDSGNFS VLMVDTGGQT WTQTLYLKVY
DAVPKPEVQV FTAAAEETQP LNTCQVFLSC WAPNISDITY SWRWEGTVDF NGEVRSHFSN
GQVLSVSLGL GDKDVAFTCI ASNPVSWDMT TVTPWESCHH EAASGKASYK DVLLVVVPIT
LFLILAGLFG AWHHGLCSGK KKDACTDGVL PETENALV
