Q13291 (SLAF1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Signaling lymphocytic activation molecule

Alternative name(s):
CDw150
IPO-3
CD_antigen=CD150

Gene names

Name:	SLAMF1
Synonyms:	SLAM

Organism

Homo sapiens (Human)

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	335 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	High-affinity self-ligand important in bidirectional T-cell to B-cell stimulation. SLAM-induced signal-transduction events in T-lymphocytes are different from those in B-cells. Two modes of SLAM signaling are likely to exist: one in which the inhibitor SH2D1A acts as a negative regulator and another in which protein-tyrosine phosphatase 2C (PTPN11)-dependent signal transduction operates.
Subunit structure	Interacts (via cytoplasmic domain) with SH2D1A, and with PTPN11. Interacts with INPP5D/SHIP1. Binds to Measles virus H protein and acts as a receptor for this virus. Ref.5 Ref.6
Subcellular location	Cell membrane; Single-pass type I membrane protein. Note: Present on the surface of B-cells and T-cells.
Tissue specificity	Constitutively expressed on peripheral blood memory T-cells, T-cell clones, immature thymocytes and a proportion of B-cells, and is rapidly induced on naive T-cells after activation.
Domain	The most membrane-proximal SH2-binding motif interacts with SH2 domain of SH2D1A and does not need to be phosphorylated on tyrosine residues.
Post-translational modification	Phosphorylated by FYN. Ref.7
Sequence similarities	Contains 1 Ig-like C2-type (immunoglobulin-like) domain. Contains 1 Ig-like V-type (immunoglobulin-like) domain.

Ontologies

Keywords
Biological process	Host-virus interaction
Cellular component	Cell membrane Membrane
Coding sequence diversity	Alternative splicing Polymorphism
Domain	Immunoglobulin domain Repeat Signal Transmembrane Transmembrane helix
Molecular function	Receptor
PTM	Disulfide bond Glycoprotein Phosphoprotein
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	interspecies interaction between organisms Inferred from electronic annotation. Source: UniProtKB-KW lymphocyte activation Inferred from electronic annotation. Source: InterPro positive regulation of cell proliferation Traceable author statement. Source: ProtInc
Cellular component	integral to membrane Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	antigen binding Traceable author statement. Source: ProtInc transmembrane signaling receptor activity Traceable author statement. Source: ProtInc
Complete GO annotation...

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: Q13291-1)

Also known as: Long;

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

Isoform 2 (identifier: Q13291-2)

Also known as: Short;

The sequence of this isoform differs from the canonical sequence as follows:
     289-298: PLQKKLDSFP → DTHHQTSDLF
     299-335: Missing.

Isoform 3 (identifier: Q13291-3)

Also known as: Secreted;

The sequence of this isoform differs from the canonical sequence as follows:
     234-263: Missing.

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Signal peptide

1 – 20

20

Potential

Chain

21 – 335

315

Signaling lymphocytic activation molecule

PRO_0000014959

Regions

Topological domain

21 – 237

217

Extracellular Potential

Transmembrane

238 – 258

21

Helical; Potential

Topological domain

259 – 335

77

Cytoplasmic Potential

Domain

144 – 223

80

Ig-like C2-type

Domain

? – 152

Ig-like V-type

Motif

281 – 286

6

SH2-binding Potential

Motif

307 – 312

6

SH2-binding Potential

Motif

327 – 332

6

SH2-binding Potential

Amino acid modifications

Modified residue

281

1

Phosphotyrosine Ref.7

Glycosylation

53

1

N-linked (GlcNAc...) Potential

Glycosylation

57

1

N-linked (GlcNAc...) Potential

Glycosylation

102

1

N-linked (GlcNAc...) Potential

Glycosylation

125

1

N-linked (GlcNAc...) Potential

Glycosylation

150

1

N-linked (GlcNAc...) Potential

Glycosylation

155

1

N-linked (GlcNAc...) Potential

Glycosylation

189

1

N-linked (GlcNAc...) Potential

Glycosylation

217

1

N-linked (GlcNAc...) Potential

Disulfide bond

158 ↔ 228

By similarity

Disulfide bond

164 ↔ 209

By similarity

Natural variations

Alternative sequence

234 – 263

30

Missing in isoform 3.

VSP_002567

Alternative sequence

289 – 298

10

PLQKKLDSFP → DTHHQTSDLF in isoform 2.

VSP_002568

Alternative sequence

299 – 335

37

Missing in isoform 2.

VSP_002569

Natural variant

11

1

F → L.
Corresponds to variant rs2295612 [ dbSNP | Ensembl ].

VAR_021924

Natural variant

81

1

L → F in a breast cancer sample; somatic mutation. Ref.11

VAR_035524

Natural variant

333

1

P → T.
Corresponds to variant rs3796504 [ dbSNP | Ensembl ].

VAR_021925

Secondary structure

1

.

.

.

335

Helix Strand Turn

Details...

Beta strand

278 – 281

4

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 (Long) [UniParc]. Last modified November 1, 1996. Version 1. Checksum: BFB0F27EA31D8C04	FASTA	335	37,231
	10 20 30 40 50 60 MDPKGLLSLT FVLFLSLAFG ASYGTGGRMM NCPKILRQLG SKVLLPLTYE RINKSMNKSI 70 80 90 100 110 120 HIVVTMAKSL ENSVENKIVS LDPSEAGPPR YLGDRYKFYL ENLTLGIRES RKEDEGWYLM 130 140 150 160 170 180 TLEKNVSVQR FCLQLRLYEQ VSTPEIKVLN KTQENGTCTL ILGCTVEKGD HVAYSWSEKA 190 200 210 220 230 240 GTHPLNPANS SHLLSLTLGP QHADNIYICT VSNPISNNSQ TFSPWPGCRT DPSETKPWAV 250 260 270 280 290 300 YAGLLGGVIM ILIMVVILQL RRRGKTNHYQ TTVEKKSLTI YAQVQKPGPL QKKLDSFPAQ 310 320 330 DPCTTIYVAA TEPVPESVQE TNSITVYASV TLPES
	Isoform 2 (Short) [UniParc]. Checksum: DCE97AC03ACDC045	FASTA	298	33,365
	10 20 30 40 50 60 MDPKGLLSLT FVLFLSLAFG ASYGTGGRMM NCPKILRQLG SKVLLPLTYE RINKSMNKSI 70 80 90 100 110 120 HIVVTMAKSL ENSVENKIVS LDPSEAGPPR YLGDRYKFYL ENLTLGIRES RKEDEGWYLM 130 140 150 160 170 180 TLEKNVSVQR FCLQLRLYEQ VSTPEIKVLN KTQENGTCTL ILGCTVEKGD HVAYSWSEKA 190 200 210 220 230 240 GTHPLNPANS SHLLSLTLGP QHADNIYICT VSNPISNNSQ TFSPWPGCRT DPSETKPWAV 250 260 270 280 290 YAGLLGGVIM ILIMVVILQL RRRGKTNHYQ TTVEKKSLTI YAQVQKPGDT HHQTSDLF
	Isoform 3 (Secreted) [UniParc]. Checksum: F5CBDC25B2E19967	FASTA	305	33,839
	10 20 30 40 50 60 MDPKGLLSLT FVLFLSLAFG ASYGTGGRMM NCPKILRQLG SKVLLPLTYE RINKSMNKSI 70 80 90 100 110 120 HIVVTMAKSL ENSVENKIVS LDPSEAGPPR YLGDRYKFYL ENLTLGIRES RKEDEGWYLM 130 140 150 160 170 180 TLEKNVSVQR FCLQLRLYEQ VSTPEIKVLN KTQENGTCTL ILGCTVEKGD HVAYSWSEKA 190 200 210 220 230 240 GTHPLNPANS SHLLSLTLGP QHADNIYICT VSNPISNNSQ TFSPWPGCRT DPSGKTNHYQ 250 260 270 280 290 300 TTVEKKSLTI YAQVQKPGPL QKKLDSFPAQ DPCTTIYVAA TEPVPESVQE TNSITVYASV TLPES

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"A novel receptor involved in T-cell activation." Cocks B.G., Chang C.-C.J., Carballido J.M., Yssel H., de Vries J.E., Aversa G. Nature 376:260-263(1995) [PubMed: 7617038] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 2 AND 3). Tissue: T-cell.
[2]	"The DNA sequence and biological annotation of human chromosome 1." Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K. , Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R. Nature 441:315-321(2006) [PubMed: 16710414] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[3]	Mural R.J., Istrail S., Sutton G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C. Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[4]	"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). Tissue: Testis.
[5]	"CDw150 associates with src-homology 2-containing inositol phosphatase and modulates CD95-mediated apoptosis." Mikhalap S.V., Shlapatska L.M., Berdova A.G., Law C.L., Clark E.A., Sidorenko S.P. J. Immunol. 162:5719-5727(1999) [PubMed: 10229804] [Abstract] Cited for: INTERACTION WITH INPP5D.
[6]	"SLAM (CDw150) is a cellular receptor for measles virus." Tatsuo H., Ono N., Tanaka K., Yanagi Y. Nature 406:893-897(2000) [PubMed: 10972291] [Abstract] Cited for: INTERACTION WITH MEASLES VIRUS HN PROTEIN.
[7]	"Global survey of phosphotyrosine signaling identifies oncogenic kinases in lung cancer." Rikova K., Guo A., Zeng Q., Possemato A., Yu J., Haack H., Nardone J., Lee K., Reeves C., Li Y., Hu Y., Tan Z., Stokes M., Sullivan L., Mitchell J., Wetzel R., Macneill J., Ren J.M. , Yuan J., Bakalarski C.E., Villen J., Kornhauser J.M., Smith B., Li D., Zhou X., Gygi S.P., Gu T.-L., Polakiewicz R.D., Rush J., Comb M.J. Cell 131:1190-1203(2007) [PubMed: 18083107] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-281, MASS SPECTROMETRY. Tissue: Lung carcinoma.
[8]	"The X-linked lymphoproliferative-disease gene product SAP regulates signals induced through the co-receptor SLAM." Sayos J., Wu C., Morra M., Wang N., Zhang X., Allen D., van Schaik S., Notarangelo L., Geha R., Roncarolo M.G., Oettgen H., de Vries J.E., Aversa G., Terhorst C. Nature 395:462-469(1998) [PubMed: 9774102] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.1 ANGSTROMS) OF 276-286 IN COMPLEX WITH SH2D1A.
[9]	"A 'three-pronged' binding mechanism for the SAP/SH2D1A SH2 domain: structural basis and relevance to the XLP syndrome." Hwang P.M., Li C., Morra M., Lillywhite J., Muhandiram D.R., Gertler F., Terhorst C., Kay L.E., Pawson T., Forman-Kay J.D., Li S.-C. EMBO J. 21:314-323(2002) [PubMed: 11823424] [Abstract] Cited for: STRUCTURE BY NMR OF 276-282 IN COMPLEX WITH SH2D1A.
[10]	"SAP couples Fyn to SLAM immune receptors." Chan B., Lanyi A., Song H.K., Griesbach J., Simarro-Grande M., Poy F., Howie D., Sumegi J., Terhorst C., Eck M.J. Nat. Cell Biol. 5:155-160(2003) [PubMed: 12545174] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 276-286 IN COMPLEX WITH SH2D1A AND FYN.
[11]	"The consensus coding sequences of human breast and colorectal cancers." Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D., Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P., Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V. , Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H., Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W., Velculescu V.E. Science 314:268-274(2006) [PubMed: 16959974] [Abstract] Cited for: VARIANT [LARGE SCALE ANALYSIS] PHE-81.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

U33017 mRNA. Translation: AAA75380.1.
AL121985, AL138930 Genomic DNA. Translation: CAH73505.1.
AL138930, AL121985 Genomic DNA. Translation: CAI15154.1.
CH471121 Genomic DNA. Translation: EAW52706.1.
BC132792 mRNA. Translation: AAI32793.1.

IPI

IPI00012469.
IPI00220229.
IPI00374060.

PIR

S58892.

RefSeq

NP_003028.1. NM_003037.2.

UniGene

Hs.523660.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1D4T	X-ray	1.10	B	276-286	[»]
1D4W	X-ray	1.80	C/D	276-286	[»]
1KA6	NMR	-	B	276-282	[»]
1KA7	NMR	-	B	276-286	[»]
1M27	X-ray	2.50	B	276-286	[»]
2DZF	model	-	@	1-335	[»]
2IE9	model	-	@	1-335	[»]
2IFL	model	-	@	3-335	[»]
2IG5	model	-	@	1-335	[»]

ProteinModelPortal

Q13291.

SMR

Q13291. Positions 30-229.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-40767N.

IntAct

Q13291. 1 interaction.

MINT

MINT-113752.

STRING

Q13291.

PTM databases

PhosphoSite

Q13291.

Polymorphism databases

DMDM

9297047.

Proteomic databases

PRIDE

Q13291.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000302035; ENSP00000306190; ENSG00000117090.

GeneID

6504.

KEGG

hsa:6504.

UCSC

uc001fwl.2. human.

Organism-specific databases

CTD

6504.

GeneCards

GC01M160577.

H-InvDB

HIX0001221.

HGNC

HGNC:10903. SLAMF1.

HPA

CAB002438.

MIM

603492. gene.

neXtProt

NX_Q13291.

PharmGKB

PA35803.

GenAtlas

Search...

Phylogenomic databases

eggNOG

prNOG08642.

HOGENOM

HBG125873.

HOVERGEN

HBG054224.

InParanoid

Q13291.

OMA

DHVAYSW.

OrthoDB

EOG4CJVHV.

PhylomeDB

Q13291.

Gene expression databases

ArrayExpress

Q13291.

Bgee

Q13291.

CleanEx

HS_SLAMF1.

Genevestigator

Q13291.

GermOnline

ENSG00000117090. Homo sapiens.

Family and domain databases

InterPro

IPR007110. Ig-like.
IPR010407. Sig_lymph_act_molc_N.
IPR015631. SLAM_fam_rcpts.
[Graphical view]

KO

K06536.

PANTHER

PTHR12080. SLAM_related. 1 hit.

Pfam

PF06214. SLAM. 1 hit.
[Graphical view]

ProDom

PD090491. Sig_lymph_act_molc_N. 1 hit.
[Graphical view] [Entries sharing at least one domain]

PROSITE

PS50835. IG_LIKE. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

NextBio

25289.

SOURCE

Search...

Entry information

Entry name

SLAF1_HUMAN

Accession

Primary (citable) accession number: Q13291
Secondary accession number(s): Q5W172

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 1, 2000
Last sequence update:	November 1, 1996
Last modified:	January 25, 2012
This is version 113 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.