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Protein

Signaling lymphocytic activation molecule

Gene

Slamf1

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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.

GO - Molecular functioni

  1. receptor activity Source: InterPro

GO - Biological processi

  1. lymphocyte activation Source: InterPro
  2. regulation of catalytic activity Source: MGI
  3. regulation of vesicle fusion Source: MGI
Complete GO annotation...

Keywords - Molecular functioni

Receptor

Names & Taxonomyi

Protein namesi
Recommended name:
Signaling lymphocytic activation molecule
Alternative name(s):
CD_antigen: CD150
Gene namesi
Name:Slamf1
Synonyms:Slam
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 1

Organism-specific databases

MGIiMGI:1351314. Slamf1.

Subcellular locationi

Cell membrane; Single-pass type I membrane protein
Note: Present on the surface of B-cells and T-cells.

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini25 – 242218ExtracellularSequence AnalysisAdd
BLAST
Transmembranei243 – 26523HelicalSequence AnalysisAdd
BLAST
Topological domaini266 – 34378CytoplasmicSequence AnalysisAdd
BLAST

GO - Cellular componenti

  1. external side of plasma membrane Source: MGI
  2. extracellular vesicular exosome Source: MGI
  3. integral component of membrane Source: UniProtKB-KW
  4. phagocytic vesicle Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2424Sequence AnalysisAdd
BLAST
Chaini25 – 343319Signaling lymphocytic activation moleculePRO_0000014960Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi54 – 541N-linked (GlcNAc...)Sequence Analysis
Glycosylationi58 – 581N-linked (GlcNAc...)Sequence Analysis
Glycosylationi103 – 1031N-linked (GlcNAc...)Sequence Analysis
Glycosylationi126 – 1261N-linked (GlcNAc...)Sequence Analysis
Glycosylationi151 – 1511N-linked (GlcNAc...)Sequence Analysis
Glycosylationi158 – 1581N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi161 ↔ 232PROSITE-ProRule annotation
Disulfide bondi167 ↔ 212PROSITE-ProRule annotation
Glycosylationi192 – 1921N-linked (GlcNAc...)Sequence Analysis
Glycosylationi211 – 2111N-linked (GlcNAc...)Sequence Analysis
Glycosylationi226 – 2261N-linked (GlcNAc...)Sequence Analysis

Post-translational modificationi

Phosphorylated.

Keywords - PTMi

Disulfide bond, Glycoprotein, Phosphoprotein

Proteomic databases

MaxQBiQ9QUM4.
PaxDbiQ9QUM4.
PRIDEiQ9QUM4.

PTM databases

PhosphoSiteiQ9QUM4.

Expressioni

Gene expression databases

BgeeiQ9QUM4.
ExpressionAtlasiQ9QUM4. baseline and differential.
GenevestigatoriQ9QUM4.

Interactioni

Subunit structurei

Interacts with INPP5D/SHIP1 (By similarity). Interacts (via cytoplasmic domain) with SH2D1A and SH2D1B. Interacts (upon tyrosine phosphorylation with) PTPN11, but not with SHP-1.By similarity1 Publication

Binary interactionsi

WithEntry#Exp.IntActNotes
FynP396884EBI-7910086,EBI-524514
Sh2d1aO888902EBI-7910086,EBI-7910438

Protein-protein interaction databases

BioGridi205139. 2 interactions.
IntActiQ9QUM4. 3 interactions.
MINTiMINT-205762.

Structurei

3D structure databases

ProteinModelPortaliQ9QUM4.
SMRiQ9QUM4. Positions 32-141.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini29 – 138110Ig-like V-typeAdd
BLAST
Domaini145 – 22884Ig-like C2-typeAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi286 – 2916SH2-bindingSequence Analysis
Motifi313 – 3186SH2-bindingSequence Analysis
Motifi333 – 3386SH2-bindingSequence Analysis

Domaini

The most membrane-proximal SH2-binding motif interacts with SH2 domain of SH2D1A and does not need to be phosphorylated on tyrosine residues.By similarity

Sequence similaritiesi

Keywords - Domaini

Immunoglobulin domain, Repeat, Signal, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiNOG40451.
GeneTreeiENSGT00510000048858.
HOGENOMiHOG000125310.
HOVERGENiHBG054224.
InParanoidiQ9QUM4.
KOiK06536.
OMAiMNKSIHI.
OrthoDBiEOG7Q8CQJ.
PhylomeDBiQ9QUM4.
TreeFamiTF334964.

Family and domain databases

Gene3Di2.60.40.10. 1 hit.
InterProiIPR007110. Ig-like_dom.
IPR013783. Ig-like_fold.
IPR010407. Sig_lymph_act_molc_N.
IPR015631. SLAM_fam_rcpts.
[Graphical view]
PANTHERiPTHR12080. PTHR12080. 1 hit.
PfamiPF06214. SLAM. 1 hit.
[Graphical view]
ProDomiPD090491. Sig_lymph_act_molc_N. 1 hit.
[Graphical view] [Entries sharing at least one domain]
PROSITEiPS50835. IG_LIKE. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform Long (identifier: Q9QUM4-1) [UniParc]FASTAAdd to basket

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.

« Hide

        10         20         30         40         50
MDPKGSLSWR ILLFLSLAFE LSYGTGGGVM DCPVILQKLG QDTWLPLTNE
60 70 80 90 100
HQINKSVNKS VRILVTMATS PGSKSNKKIV SFDLSKGSYP DHLEDGYHFQ
110 120 130 140 150
SKNLSLKILG NRRESEGWYL VSVEENVSVQ QFCKQLKLYE QVSPPEIKVL
160 170 180 190 200
NKTQENENGT CSLLLACTVK KGDHVTYSWS DEAGTHLLSR ANRSHLLHIT
210 220 230 240 250
LSNQHQDSIY NCTASNPVSS ISRTFNLSSQ ACKQESSSES SPWMQYTLVP
260 270 280 290 300
LGVVIIFILV FTAIIMMKRQ GKSNHCQPPV EEKSLTIYAQ VQKSGPQEKK
310 320 330 340
LHDALTDQDP CTTIYVAATE PAPESVQEPN PTTVYASVTL PES
Length:343
Mass (Da):38,094
Last modified:May 1, 2000 - v1
Checksum:i7980470157E834C4
GO
Isoform Short (identifier: Q9QUM4-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     296-343: PQEKKLHDAL...VYASVTLPES → VRSMPHLAGVSVIFRTGFLIAALHTTMVLQGLLE

Show »
Length:329
Mass (Da):36,590
Checksum:i3F43476A7CD3686F
GO

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei296 – 34348PQEKK…TLPES → VRSMPHLAGVSVIFRTGFLI AALHTTMVLQGLLE in isoform Short. 1 PublicationVSP_002570Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF149791 mRNA. Translation: AAF22231.1.
AF149792 mRNA. Translation: AAF22232.1.
AF164523
, AF164519, AF164520, AF164521, AF164522 Genomic DNA. Translation: AAF13818.1.
AF160990 mRNA. Translation: AAF14535.1.
CCDSiCCDS15502.1. [Q9QUM4-1]
RefSeqiNP_038758.2. NM_013730.4. [Q9QUM4-1]
UniGeneiMm.103648.

Genome annotation databases

EnsembliENSMUST00000015460; ENSMUSP00000015460; ENSMUSG00000015316. [Q9QUM4-1]
GeneIDi27218.
KEGGimmu:27218.
UCSCiuc007dpc.1. mouse. [Q9QUM4-1]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF149791 mRNA. Translation: AAF22231.1.
AF149792 mRNA. Translation: AAF22232.1.
AF164523
, AF164519, AF164520, AF164521, AF164522 Genomic DNA. Translation: AAF13818.1.
AF160990 mRNA. Translation: AAF14535.1.
CCDSiCCDS15502.1. [Q9QUM4-1]
RefSeqiNP_038758.2. NM_013730.4. [Q9QUM4-1]
UniGeneiMm.103648.

3D structure databases

ProteinModelPortaliQ9QUM4.
SMRiQ9QUM4. Positions 32-141.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi205139. 2 interactions.
IntActiQ9QUM4. 3 interactions.
MINTiMINT-205762.

PTM databases

PhosphoSiteiQ9QUM4.

Proteomic databases

MaxQBiQ9QUM4.
PaxDbiQ9QUM4.
PRIDEiQ9QUM4.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000015460; ENSMUSP00000015460; ENSMUSG00000015316. [Q9QUM4-1]
GeneIDi27218.
KEGGimmu:27218.
UCSCiuc007dpc.1. mouse. [Q9QUM4-1]

Organism-specific databases

CTDi6504.
MGIiMGI:1351314. Slamf1.

Phylogenomic databases

eggNOGiNOG40451.
GeneTreeiENSGT00510000048858.
HOGENOMiHOG000125310.
HOVERGENiHBG054224.
InParanoidiQ9QUM4.
KOiK06536.
OMAiMNKSIHI.
OrthoDBiEOG7Q8CQJ.
PhylomeDBiQ9QUM4.
TreeFamiTF334964.

Miscellaneous databases

NextBioi305116.
PROiQ9QUM4.
SOURCEiSearch...

Gene expression databases

BgeeiQ9QUM4.
ExpressionAtlasiQ9QUM4. baseline and differential.
GenevestigatoriQ9QUM4.

Family and domain databases

Gene3Di2.60.40.10. 1 hit.
InterProiIPR007110. Ig-like_dom.
IPR013783. Ig-like_fold.
IPR010407. Sig_lymph_act_molc_N.
IPR015631. SLAM_fam_rcpts.
[Graphical view]
PANTHERiPTHR12080. PTHR12080. 1 hit.
PfamiPF06214. SLAM. 1 hit.
[Graphical view]
ProDomiPD090491. Sig_lymph_act_molc_N. 1 hit.
[Graphical view] [Entries sharing at least one domain]
PROSITEiPS50835. IG_LIKE. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. "Molecular and functional characterization of mouse signaling lymphocytic activation molecule (SLAM): differential expression and responsiveness in Th1 and Th2 cells."
    Castro A.G., Hauser T.M., Cocks B.G., Abrams J., Zurawski S., Churakova T., Zonin F., Robinson D., Tangye S.G., Aversa G., Nichols K.E., de Vries J.E., Lanier L.L., O'Garra A.
    J. Immunol. 163:5860-5870(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS LONG AND SHORT).
    Strain: BALB/c.
  2. Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM LONG).
  3. "Genomic organization of murine Slam."
    Wu C., Wang N., Sayos J., Terhorst C.
    Submitted (JUN-1999) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM LONG).
  4. "Structural basis for the interaction of the free SH2 domain EAT-2 with SLAM receptors in hematopoietic cells."
    Morra M., Lu J., Poy F., Martin M., Sayos J., Calpe S., Gullo C., Howie D., Rietdijk S., Thompson A., Coyle A.J., Denny C., Yaffe M.B., Engel P., Eck M.J., Terhorst C.
    EMBO J. 20:5840-5852(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH SH2D1B.

Entry informationi

Entry nameiSLAF1_MOUSE
AccessioniPrimary (citable) accession number: Q9QUM4
Secondary accession number(s): Q9QXZ3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 1, 2000
Last sequence update: May 1, 2000
Last modified: March 4, 2015
This is version 118 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.