Scimp
entrez
327957
canonical
uniprot
Q3UU41
canonical
ensembl
ENSMUSG00000057135
resolver
ensp
ENSMUSP00000104174
resolver
enst
ENSMUST00000108534
resolver
genesymbol
Scimp
resolver
uniprot
B2RVG2
resolver
uniprot
Q5SX69
resolver
uniprot_entry
SCIMP_MOUSE
resolver
uniprot_sec
B2RVG2
resolver
uniprot_sec
Q5SX69
resolver
amino_acid_sequence
MSWWRDNFWIILAMSIIFISLVLGLILYCVCRWQLRQGRNWEIAKPSKQDGRDEEKMYENVLNSSPGQLPALPPRGSPFPGDLAPQEAPRQPSAWYSSVKKVRNKKVFAISGSTEPENDYDDVEIPATTETQHSKTTPFWQAEVGLHSSF
uniprot
proteins
function
FUNCTION: Lipid tetraspanin-associated transmembrane adapter/mediator that acts as a scaffold for Src-family kinases and other signaling proteins in immune cells (PubMed:27288407, PubMed:28098138, PubMed:28290451). It is involved in major histocompatibility complex class II (MHC-II) signaling transduction in B cells, where it is required in generating the calcium response and enhancing ERK activity upon MHC-II stimulation (By similarity). In dendritic cells, it is involved in sustaining CLEC7A/DECTIN1 signaling after CLEC7A activation by fungal beta-glucans (PubMed:27288407). It also acts as an agonist-inducible signaling adapter for TLR1, TLR2, TLR3, TLR4, and TLR7 by selectively enabling the expression of pro-inflammatory cytokines IL6 and IL12B in macrophages and acting as a scaffold for phosphorylation of Toll-like receptors by Src-family kinases (PubMed:28098138). {ECO:0000250|UniProtKB:Q6UWF3, ECO:0000269|PubMed:27288407, ECO:0000269|PubMed:28098138, ECO:0000269|PubMed:28290451}.
uniprot
proteins
mass_dalton
17140
uniprot
proteins
mutagenesis
MUTAGEN 58; /note="Y->F: Inhibits interaction with BLNK. Slightly inhibits interaction with GRB2. No effect on interactions with TLR4 and CSK."; /evidence="ECO:0000269|PubMed:28098138, ECO:0000269|PubMed:28290451"; MUTAGEN 95; /note="W->A: Inhibits interaction with TLR4. Inhibits IL12B expression after TLR4 activation by lipopolysaccharide. No effect on interaction with LYN."; /evidence="ECO:0000269|PubMed:28098138"; MUTAGEN 96; /note="Y->F: Inhibits interaction with TLR4. Decreases IL12B expression after TLR4 activation by lipopolysaccharide. Inhibits interaction with CSK. No effect on interactions with LYN, GRB2, and BLNK."; /evidence="ECO:0000269|PubMed:28098138, ECO:0000269|PubMed:28290451"; MUTAGEN 97; /note="S->A: No effect on interaction with TLR4."; /evidence="ECO:0000269|PubMed:28098138"; MUTAGEN 98; /note="S->A: No effect on interaction with TLR4."; /evidence="ECO:0000269|PubMed:28098138"; MUTAGEN 99; /note="V->A: No effect on interaction with TLR4."; /evidence="ECO:0000269|PubMed:28098138"; MUTAGEN 120; /note="Y->F: Inhibits interaction with BLNK. No effect on interactions with TLR4, GRB2 and CSK."; /evidence="ECO:0000269|PubMed:28098138, ECO:0000269|PubMed:28290451
uniprot
proteins
post_translational_modification
PTM: Phosphorylated by the Src-family protein tyrosine kinases LYN and SRC (PubMed:27288407). Phosphorylation occurs on tyrosine residues upon MHC-II stimulation (PubMed:21930792, PubMed:27288407). Phosphorylation also occurs on tyrosine residues after activation of CLEC7A/DECTIN1 by particulate beta-glucan (PubMed:27288407). Lipopolysaccharide (LPS) induces phosphorylation of Tyr-58, Tyr-96 and Tyr-120 differentially to allow temporal recruitment of effector proteins GRB2, CSK and BLNK (PubMed:28290451). Phosphorylation of Tyr-58 is immediately induced by LPS stimulation and allows GRB2 to bind (PubMed:28290451). Tyr-96 is phosphorylated 5 minutes after LPS stimulation, which then allows CSK to bind, followed by phosphorylation of Tyr-120 10 minutes after LPS induction, which allows BLNK to bind (PubMed:28290451). Phosphorylation at Tyr-96 by LYN occurs after activation of TLR4 by LPS; phosphorylation enhances binding to TLR4 (PubMed:28098138, PubMed:28290451). {ECO:0000269|PubMed:21930792, ECO:0000269|PubMed:27288407, ECO:0000269|PubMed:28098138, ECO:0000269|PubMed:28290451}.; PTM: Palmitoylated. {ECO:0000250|UniProtKB:Q6UWF3}.
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
16141072
uniprot
proteins
pubmed
19144319
uniprot
proteins
pubmed
19468303
uniprot
proteins
pubmed
21183079
uniprot
proteins
pubmed
21930792
uniprot
proteins
pubmed
27288407
uniprot
proteins
pubmed
28098138
uniprot
proteins
pubmed
28290451
uniprot
proteins
sequence_length
150
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:28098138}; Single-pass membrane protein {ECO:0000255}. Cell membrane {ECO:0000250|UniProtKB:Q6UWF3}; Lipid-anchor {ECO:0000250|UniProtKB:Q6UWF3}. Cytoplasmic vesicle, phagosome {ECO:0000269|PubMed:27288407}. Cell projection, ruffle {ECO:0000269|PubMed:28098138}. Cell projection, filopodium {ECO:0000269|PubMed:28098138}. Note=Together with MHC-II, associates with lipid-enriched microdomains called tetraspanin-enriched microdomains (TEMs) (By similarity). Rapidly translocates into immunological synapse (IS) at cell-cell contacts between antigen-presenting cells (APCs) and T-cells (By similarity). Colocalized with tetraspanins CD37, CD53, and CD81 at the uropod (By similarity). Present at regions of cell-cell contacts but also at the leading edge of migrating cells (By similarity). Localizes to phagosomes in dendritic cells after exposure to particulate beta-glucan (PubMed:27288407). {ECO:0000250|UniProtKB:Q6UWF3, ECO:0000269|PubMed:27288407}.
uniprot
proteins
transmembrane_region
TRANSMEM 8..28; /note="Helical"; /evidence="ECO:0000255
uniprot
proteins