SLAF8_HUMAN
ID SLAF8_HUMAN Reviewed; 285 AA.
AC Q9P0V8; Q32MC6; Q5VU15;
DT 07-JUN-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 157.
DE RecName: Full=SLAM family member 8;
DE AltName: Full=B-lymphocyte activator macrophage expressed;
DE AltName: Full=BCM-like membrane protein;
DE AltName: CD_antigen=CD353;
DE Flags: Precursor;
GN Name=SLAMF8; Synonyms=BLAME;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, TISSUE SPECIFICITY, AND
RP VARIANT SER-99.
RC TISSUE=Lymphocyte;
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 [MRNA] (ISOFORM 1).
RA Zhang W., Wan T., Cao X.;
RT "Novel human cell membrane protein.";
RL Submitted (APR-1999) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Mammary gland;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16710414; DOI=10.1038/nature04727;
RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A.,
RA Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C.,
RA Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.,
RA Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C.,
RA Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W.,
RA Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J.,
RA Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J.,
RA Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y.,
RA Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J.,
RA Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
RA Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
RA Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
RA Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S.,
RA Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K.,
RA Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R.,
RA Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M.,
RA Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S.,
RA Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J.,
RA Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W.,
RA McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
RA Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
RA Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
RA Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
RA Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S.,
RA Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M.,
RA White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H.,
RA Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E.,
RA Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G.,
RA Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.;
RT "The DNA sequence and biological annotation of human chromosome 1.";
RL Nature 441:315-321(2006).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
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 [6]
RP PROTEIN SEQUENCE OF 23-37.
RX PubMed=15340161; DOI=10.1110/ps.04682504;
RA Zhang Z., Henzel W.J.;
RT "Signal peptide prediction based on analysis of experimentally verified
RT cleavage sites.";
RL Protein Sci. 13:2819-2824(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 -!- INTERACTION:
CC Q9P0V8; P54852: EMP3; NbExp=3; IntAct=EBI-18164173, EBI-3907816;
CC Q9P0V8; Q9NZG7: NINJ2; NbExp=3; IntAct=EBI-18164173, EBI-10317425;
CC -!- SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane protein.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9P0V8-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9P0V8-2; Sequence=VSP_013896;
CC -!- TISSUE SPECIFICITY: Expressed in lymph node, spleen, thymus and bone
CC marrow. {ECO:0000269|PubMed:11313408}.
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DR EMBL; AF146761; AAF67470.1; -; mRNA.
DR EMBL; AK074669; BAC11123.1; -; mRNA.
DR EMBL; AL590560; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC109194; AAI09195.1; -; mRNA.
DR CCDS; CCDS1188.1; -. [Q9P0V8-1]
DR CCDS; CCDS81387.1; -. [Q9P0V8-2]
DR RefSeq; NP_001317670.1; NM_001330741.1. [Q9P0V8-2]
DR RefSeq; NP_064510.1; NM_020125.2. [Q9P0V8-1]
DR AlphaFoldDB; Q9P0V8; -.
DR SMR; Q9P0V8; -.
DR BioGRID; 121206; 18.
DR IntAct; Q9P0V8; 3.
DR STRING; 9606.ENSP00000289707; -.
DR GlyGen; Q9P0V8; 1 site.
DR BioMuta; SLAMF8; -.
DR DMDM; 67461583; -.
DR jPOST; Q9P0V8; -.
DR MassIVE; Q9P0V8; -.
DR PaxDb; Q9P0V8; -.
DR PeptideAtlas; Q9P0V8; -.
DR PRIDE; Q9P0V8; -.
DR ProteomicsDB; 83604; -. [Q9P0V8-1]
DR ProteomicsDB; 83605; -. [Q9P0V8-2]
DR Antibodypedia; 47059; 319 antibodies from 31 providers.
DR CPTC; Q9P0V8; 1 antibody.
DR DNASU; 56833; -.
DR Ensembl; ENST00000289707.10; ENSP00000289707.5; ENSG00000158714.11. [Q9P0V8-1]
DR Ensembl; ENST00000368104.4; ENSP00000357084.4; ENSG00000158714.11. [Q9P0V8-2]
DR GeneID; 56833; -.
DR KEGG; hsa:56833; -.
DR MANE-Select; ENST00000289707.10; ENSP00000289707.5; NM_020125.3; NP_064510.1.
DR UCSC; uc001fue.5; human. [Q9P0V8-1]
DR CTD; 56833; -.
DR DisGeNET; 56833; -.
DR GeneCards; SLAMF8; -.
DR HGNC; HGNC:21391; SLAMF8.
DR HPA; ENSG00000158714; Tissue enhanced (lymphoid).
DR MIM; 606620; gene.
DR neXtProt; NX_Q9P0V8; -.
DR OpenTargets; ENSG00000158714; -.
DR PharmGKB; PA134983606; -.
DR VEuPathDB; HostDB:ENSG00000158714; -.
DR eggNOG; ENOG502S183; Eukaryota.
DR GeneTree; ENSGT01030000234540; -.
DR HOGENOM; CLU_083521_1_0_1; -.
DR InParanoid; Q9P0V8; -.
DR OMA; PNTCQVF; -.
DR OrthoDB; 1532935at2759; -.
DR PhylomeDB; Q9P0V8; -.
DR TreeFam; TF334964; -.
DR PathwayCommons; Q9P0V8; -.
DR SignaLink; Q9P0V8; -.
DR BioGRID-ORCS; 56833; 5 hits in 1062 CRISPR screens.
DR GeneWiki; SLAMF8; -.
DR GenomeRNAi; 56833; -.
DR Pharos; Q9P0V8; Tbio.
DR PRO; PR:Q9P0V8; -.
DR Proteomes; UP000005640; Chromosome 1.
DR RNAct; Q9P0V8; protein.
DR Bgee; ENSG00000158714; Expressed in vermiform appendix and 152 other tissues.
DR Genevisible; Q9P0V8; HS.
DR GO; GO:0009986; C:cell surface; NAS:UniProtKB.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0042802; F:identical protein binding; ISS:UniProtKB.
DR GO; GO:0038023; F:signaling receptor activity; ISS:UniProtKB.
DR GO; GO:0002336; P:B-1 B cell lineage commitment; ISS:UniProtKB.
DR GO; GO:0042742; P:defense response to bacterium; ISS:UniProtKB.
DR GO; GO:0002232; P:leukocyte chemotaxis involved in inflammatory response; ISS:UniProtKB.
DR GO; GO:2000509; P:negative regulation of dendritic cell chemotaxis; ISS:UniProtKB.
DR GO; GO:0010760; P:negative regulation of macrophage chemotaxis; ISS:UniProtKB.
DR GO; GO:0090027; P:negative regulation of monocyte chemotaxis; ISS:UniProtKB.
DR GO; GO:1902623; P:negative regulation of neutrophil migration; ISS:UniProtKB.
DR GO; GO:0060266; P:negative regulation of respiratory burst involved in inflammatory response; ISS:UniProtKB.
DR GO; GO:0090383; P:phagosome acidification; ISS:UniProtKB.
DR GO; GO:0045577; P:regulation of B cell differentiation; ISS:UniProtKB.
DR GO; GO:0043549; P:regulation of kinase activity; ISS:UniProtKB.
DR GO; GO:0033860; P:regulation of NAD(P)H oxidase activity; ISS:UniProtKB.
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 1: Evidence at protein level;
KW Alternative splicing; Direct protein sequencing; Disulfide bond;
KW Glycoprotein; Immunoglobulin domain; Membrane; Reference proteome; Signal;
KW Transmembrane; Transmembrane helix.
FT SIGNAL 1..22
FT /evidence="ECO:0000269|PubMed:15340161"
FT CHAIN 23..285
FT /note="SLAM family member 8"
FT /id="PRO_0000014965"
FT TOPO_DOM 23..233
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 234..254
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 255..285
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 128..215
FT /note="Ig-like C2-type"
FT REGION 262..285
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 85
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 152..201
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT VAR_SEQ 14..122
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_013896"
FT VARIANT 5
FT /note="P -> T (in dbSNP:rs2494514)"
FT /id="VAR_049940"
FT VARIANT 99
FT /note="G -> S (in dbSNP:rs34687326)"
FT /evidence="ECO:0000269|PubMed:11313408"
FT /id="VAR_049941"
FT VARIANT 129
FT /note="V -> M (in dbSNP:rs3795331)"
FT /id="VAR_049942"
SQ SEQUENCE 285 AA; 31670 MW; 1BA63F4F90739AB2 CRC64;
MVMRPLWSLL LWEALLPITV TGAQVLSKVG GSVLLVAARP PGFQVREAIW RSLWPSEELL
ATFFRGSLET LYHSRFLGRA QLHSNLSLEL GPLESGDSGN FSVLMVDTRG QPWTQTLQLK
VYDAVPRPVV QVFIAVERDA QPSKTCQVFL SCWAPNISEI TYSWRRETTM DFGMEPHSLF
TDGQVLSISL GPGDRDVAYS CIVSNPVSWD LATVTPWDSC HHEAAPGKAS YKDVLLVVVP
VSLLLMLVTL FSAWHWCPCS GKKKKDVHAD RVGPETENPL VQDLP
