SCIMP_MOUSE
ID SCIMP_MOUSE Reviewed; 150 AA.
AC Q3UU41; B2RVG2; Q5SX69;
DT 10-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2005, sequence version 1.
DT 03-AUG-2022, entry version 105.
DE RecName: Full=SLP adapter and CSK-interacting membrane protein;
GN Name=Scimp;
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 [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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain;
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 [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-65; SER-77 AND TYR-120, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA Thibault P.;
RT "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL Immunity 30:143-154(2009).
RN [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Spleen;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [6]
RP INTERACTION WITH BLNK AND GRB2, PHOSPHORYLATION, AND TISSUE SPECIFICITY.
RX PubMed=21930792; DOI=10.1128/mcb.05817-11;
RA Draber P., Vonkova I., Stepanek O., Hrdinka M., Kucova M., Skopcova T.,
RA Otahal P., Angelisova P., Horejsi V., Yeung M., Weiss A., Brdicka T.;
RT "SCIMP, a transmembrane adapter protein involved in major
RT histocompatibility complex class II signaling.";
RL Mol. Cell. Biol. 31:4550-4562(2011).
RN [7]
RP FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, INDUCTION,
RP PHOSPHORYLATION, AND DISRUPTION PHENOTYPE.
RX PubMed=27288407; DOI=10.1074/jbc.m116.717157;
RA Kralova J., Fabisik M., Pokorna J., Skopcova T., Malissen B., Brdicka T.;
RT "The Transmembrane Adaptor Protein SCIMP Facilitates Sustained Dectin-1
RT Signaling in Dendritic Cells.";
RL J. Biol. Chem. 291:16530-16540(2016).
RN [8]
RP FUNCTION, INTERACTION WITH CSK; GRB2 AND BLNK, PHOSPHORYLATION AT TYR-58;
RP TYR-96 AND TYR-120, AND MUTAGENESIS OF TYR-58; TYR-96 AND TYR-120.
RX PubMed=28290451; DOI=10.1038/icb.2017.10;
RA Luo L., Tong S.J., Wall A.A., Khromykh T., Sweet M.J., Stow J.L.;
RT "Development of SH2 probes and pull-down assays to detect pathogen-induced,
RT site-specific tyrosine phosphorylation of the TLR adaptor SCIMP.";
RL Immunol. Cell Biol. 95:564-570(2017).
RN [9]
RP FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH LYN; GRB2 AND TLR4, TISSUE
RP SPECIFICITY, PHOSPHORYLATION AT TYR-96, AND MUTAGENESIS OF TYR-58; TRP-95;
RP TYR-96; SER-97; SER-98; VAL-99 AND TYR-120.
RX PubMed=28098138; DOI=10.1038/ncomms14133;
RA Luo L., Bokil N.J., Wall A.A., Kapetanovic R., Lansdaal N.M., Marceline F.,
RA Burgess B.J., Tong S.J., Guo Z., Alexandrov K., Ross I.L., Hibbs M.L.,
RA Stow J.L., Sweet M.J.;
RT "SCIMP is a transmembrane non-TIR TLR adaptor that promotes proinflammatory
RT cytokine production from macrophages.";
RL Nat. Commun. 8:14133-14133(2017).
CC -!- FUNCTION: Lipid tetraspanin-associated transmembrane adapter/mediator
CC that acts as a scaffold for Src-family kinases and other signaling
CC proteins in immune cells (PubMed:27288407, PubMed:28290451,
CC PubMed:28098138). It is involved in major histocompatibility complex
CC class II (MHC-II) signaling transduction in B cells, where it is
CC required in generating the calcium response and enhancing ERK activity
CC upon MHC-II stimulation (By similarity). In dendritic cells, it is
CC involved in sustaining CLEC7A/DECTIN1 signaling after CLEC7A activation
CC by fungal beta-glucans (PubMed:27288407). It also acts as an agonist-
CC inducible signaling adapter for TLR1, TLR2, TLR3, TLR4, and TLR7 by
CC selectively enabling the expression of pro-inflammatory cytokines IL6
CC and IL12B in macrophages and acting as a scaffold for phosphorylation
CC of Toll-like receptors by Src-family kinases (PubMed:28098138).
CC {ECO:0000250|UniProtKB:Q6UWF3, ECO:0000269|PubMed:27288407,
CC ECO:0000269|PubMed:28098138, ECO:0000269|PubMed:28290451}.
CC -!- SUBUNIT: Interacts with CD37, CD53 and CD81 (By similarity). Interacts
CC (via proline-rich region) with LYN (via SH3 domain) (PubMed:28098138).
CC Interacts with CSK (via SH2 domain); this interaction is dependent on
CC phosphorylation of Tyr-96 (PubMed:28290451). Interacts with BLNK (via
CC SH2 domain); this interaction is dependent on phosphorylation of Tyr-
CC 120 (PubMed:21930792, PubMed:28290451). Interacts with GRB2 (via SH2
CC domain); this interaction may be dependent on phosphorylation of Tyr-58
CC (PubMed:21930792, PubMed:28098138). Interacts with TLR4; this
CC interaction occurs upon lipopolysaccharide activation of TLR4 and is
CC enhanced by phosphorylation of Tyr-96 by LYN (PubMed:28098138). This
CC interaction facilitates the phosphorylation of TLR4 by LYN which
CC elicits a selective cytokine response in macrophages (PubMed:28098138).
CC {ECO:0000250|UniProtKB:Q6UWF3, ECO:0000269|PubMed:21930792,
CC ECO:0000269|PubMed:28098138, ECO:0000269|PubMed:28290451}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:28098138};
CC Single-pass membrane protein {ECO:0000255}. Cell membrane
CC {ECO:0000250|UniProtKB:Q6UWF3}; Lipid-anchor
CC {ECO:0000250|UniProtKB:Q6UWF3}. Cytoplasmic vesicle, phagosome
CC {ECO:0000269|PubMed:27288407}. Cell projection, ruffle
CC {ECO:0000269|PubMed:28098138}. Cell projection, filopodium
CC {ECO:0000269|PubMed:28098138}. Note=Together with MHC-II, associates
CC with lipid-enriched microdomains called tetraspanin-enriched
CC microdomains (TEMs) (By similarity). Rapidly translocates into
CC immunological synapse (IS) at cell-cell contacts between antigen-
CC presenting cells (APCs) and T-cells (By similarity). Colocalized with
CC tetraspanins CD37, CD53, and CD81 at the uropod (By similarity).
CC Present at regions of cell-cell contacts but also at the leading edge
CC of migrating cells (By similarity). Localizes to phagosomes in
CC dendritic cells after exposure to particulate beta-glucan
CC (PubMed:27288407). {ECO:0000250|UniProtKB:Q6UWF3,
CC ECO:0000269|PubMed:27288407}.
CC -!- TISSUE SPECIFICITY: Expressed in peripheral blood leukocytes (PBLs) (at
CC protein level) (PubMed:21930792). Expressed in dendritic cells,
CC splenocytes and B cells (at protein level) (PubMed:27288407). Strongly
CC expressed in the spleen and lymph nodes and weakly in other tissues of
CC the immune system, including bone marrow, peripheral blood leukocytes
CC (PBLs) and thymus (PubMed:21930792). Not detected in the majority of
CC nonimmune tissues, with the exception of lung (PubMed:21930792).
CC Expressed in antigen-presenting cells (PubMed:21930792). Expressed in
CC macrophages (PubMed:28098138). {ECO:0000269|PubMed:21930792,
CC ECO:0000269|PubMed:27288407, ECO:0000269|PubMed:28098138}.
CC -!- INDUCTION: Induced in bone marrow-derived macrophages by CSF2 and
CC particulate beta-glucan. {ECO:0000269|PubMed:27288407}.
CC -!- PTM: Phosphorylated by the Src-family protein tyrosine kinases LYN and
CC SRC (PubMed:27288407). Phosphorylation occurs on tyrosine residues upon
CC MHC-II stimulation (PubMed:21930792, PubMed:27288407). Phosphorylation
CC also occurs on tyrosine residues after activation of CLEC7A/DECTIN1 by
CC particulate beta-glucan (PubMed:27288407). Lipopolysaccharide (LPS)
CC induces phosphorylation of Tyr-58, Tyr-96 and Tyr-120 differentially to
CC allow temporal recruitment of effector proteins GRB2, CSK and BLNK
CC (PubMed:28290451). Phosphorylation of Tyr-58 is immediately induced by
CC LPS stimulation and allows GRB2 to bind (PubMed:28290451). Tyr-96 is
CC phosphorylated 5 minutes after LPS stimulation, which then allows CSK
CC to bind, followed by phosphorylation of Tyr-120 10 minutes after LPS
CC induction, which allows BLNK to bind (PubMed:28290451). Phosphorylation
CC at Tyr-96 by LYN occurs after activation of TLR4 by LPS;
CC phosphorylation enhances binding to TLR4 (PubMed:28098138,
CC PubMed:28290451). {ECO:0000269|PubMed:21930792,
CC ECO:0000269|PubMed:27288407, ECO:0000269|PubMed:28098138,
CC ECO:0000269|PubMed:28290451}.
CC -!- PTM: Palmitoylated. {ECO:0000250|UniProtKB:Q6UWF3}.
CC -!- DISRUPTION PHENOTYPE: Mice exhibit no difference in leukocyte
CC development and subset representation in lymphoid organs
CC (PubMed:27288407). No effect on B cell mediated activation of antigen-
CC specific T cells and MHCII glycoprotein downstream signaling in B cells
CC (PubMed:27288407). In dendritic cells, mutants show decreased cytokine
CC production beyond 24 hours after stimulation of CLEC7A signaling
CC (PubMed:27288407). {ECO:0000269|PubMed:27288407}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAI25187.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=CAM28154.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AK138818; BAE23788.1; -; mRNA.
DR EMBL; AL596117; CAI25187.1; ALT_INIT; Genomic_DNA.
DR EMBL; CR933735; CAM28154.1; ALT_INIT; Genomic_DNA.
DR EMBL; BC147177; AAI47178.1; -; mRNA.
DR EMBL; BC147178; AAI47179.1; -; mRNA.
DR CCDS; CCDS24967.1; -.
DR RefSeq; NP_001038991.1; NM_001045526.2.
DR AlphaFoldDB; Q3UU41; -.
DR SMR; Q3UU41; -.
DR IntAct; Q3UU41; 2.
DR STRING; 10090.ENSMUSP00000104174; -.
DR iPTMnet; Q3UU41; -.
DR PhosphoSitePlus; Q3UU41; -.
DR SwissPalm; Q3UU41; -.
DR MaxQB; Q3UU41; -.
DR PaxDb; Q3UU41; -.
DR PRIDE; Q3UU41; -.
DR ProteomicsDB; 253410; -.
DR Antibodypedia; 1618; 96 antibodies from 17 providers.
DR Ensembl; ENSMUST00000108534; ENSMUSP00000104174; ENSMUSG00000057135.
DR GeneID; 327957; -.
DR KEGG; mmu:327957; -.
DR UCSC; uc007jwp.1; mouse.
DR CTD; 388325; -.
DR MGI; MGI:3610314; Scimp.
DR VEuPathDB; HostDB:ENSMUSG00000057135; -.
DR eggNOG; ENOG502T3K5; Eukaryota.
DR GeneTree; ENSGT00390000007003; -.
DR HOGENOM; CLU_1781827_0_0_1; -.
DR InParanoid; Q3UU41; -.
DR OMA; NTEKHHF; -.
DR OrthoDB; 1442988at2759; -.
DR PhylomeDB; Q3UU41; -.
DR TreeFam; TF340362; -.
DR BioGRID-ORCS; 327957; 1 hit in 72 CRISPR screens.
DR ChiTaRS; Scimp; mouse.
DR PRO; PR:Q3UU41; -.
DR Proteomes; UP000000589; Chromosome 11.
DR RNAct; Q3UU41; protein.
DR Bgee; ENSMUSG00000057135; Expressed in spleen and 29 other tissues.
DR ExpressionAtlas; Q3UU41; baseline and differential.
DR GO; GO:0030175; C:filopodium; IEA:UniProtKB-SubCell.
DR GO; GO:0001772; C:immunological synapse; ISS:UniProtKB.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0031256; C:leading edge membrane; ISS:UniProtKB.
DR GO; GO:0016020; C:membrane; ISS:UniProtKB.
DR GO; GO:0045335; C:phagocytic vesicle; IMP:UniProtKB.
DR GO; GO:0043235; C:receptor complex; IDA:UniProtKB.
DR GO; GO:0001726; C:ruffle; IEA:UniProtKB-SubCell.
DR GO; GO:0097197; C:tetraspanin-enriched microdomain; ISS:UniProtKB.
DR GO; GO:0031259; C:uropod membrane; ISS:UniProtKB.
DR GO; GO:0060090; F:molecular adaptor activity; IMP:UniProtKB.
DR GO; GO:0071226; P:cellular response to molecule of fungal origin; IMP:UniProtKB.
DR GO; GO:0002720; P:positive regulation of cytokine production involved in immune response; IMP:UniProtKB.
DR GO; GO:0002732; P:positive regulation of dendritic cell cytokine production; IMP:UniProtKB.
DR GO; GO:0070374; P:positive regulation of ERK1 and ERK2 cascade; IMP:UniProtKB.
DR GO; GO:0032735; P:positive regulation of interleukin-12 production; IMP:UniProtKB.
DR GO; GO:0032755; P:positive regulation of interleukin-6 production; IMP:UniProtKB.
DR GO; GO:0031666; P:positive regulation of lipopolysaccharide-mediated signaling pathway; IDA:UniProtKB.
DR GO; GO:0032874; P:positive regulation of stress-activated MAPK cascade; IMP:UniProtKB.
DR GO; GO:0034138; P:toll-like receptor 3 signaling pathway; IMP:UniProtKB.
DR GO; GO:0034142; P:toll-like receptor 4 signaling pathway; IMP:UniProtKB.
DR GO; GO:0034154; P:toll-like receptor 7 signaling pathway; IMP:UniProtKB.
DR GO; GO:0038123; P:toll-like receptor TLR1:TLR2 signaling pathway; IMP:UniProtKB.
DR InterPro; IPR028181; SCIMP.
DR PANTHER; PTHR12044:SF11; PTHR12044:SF11; 1.
DR Pfam; PF15050; SCIMP; 1.
PE 1: Evidence at protein level;
KW Cell membrane; Cell projection; Cytoplasmic vesicle; Lipoprotein; Membrane;
KW Palmitate; Phosphoprotein; Reference proteome; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..150
FT /note="SLP adapter and CSK-interacting membrane protein"
FT /id="PRO_0000295238"
FT TRANSMEM 8..28
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 63..94
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 70..75
FT /note="Proline-rich region necessary for constitutive
FT interaction with LYN"
FT /evidence="ECO:0000269|PubMed:28098138"
FT REGION 93..150
FT /note="Interaction with TLR4"
FT /evidence="ECO:0000269|PubMed:28098138"
FT REGION 110..136
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 58
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000269|PubMed:28290451"
FT MOD_RES 65
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19144319"
FT MOD_RES 77
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19144319"
FT MOD_RES 96
FT /note="Phosphotyrosine; by LYN"
FT /evidence="ECO:0000269|PubMed:28098138,
FT ECO:0000269|PubMed:28290451"
FT MOD_RES 120
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000269|PubMed:28290451,
FT ECO:0007744|PubMed:19144319"
FT LIPID 29
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000250|UniProtKB:Q6UWF3"
FT LIPID 31
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000250|UniProtKB:Q6UWF3"
FT MUTAGEN 58
FT /note="Y->F: Inhibits interaction with BLNK. Slightly
FT inhibits interaction with GRB2. No effect on interactions
FT with TLR4 and CSK."
FT /evidence="ECO:0000269|PubMed:28098138,
FT ECO:0000269|PubMed:28290451"
FT MUTAGEN 95
FT /note="W->A: Inhibits interaction with TLR4. Inhibits IL12B
FT expression after TLR4 activation by lipopolysaccharide. No
FT effect on interaction with LYN."
FT /evidence="ECO:0000269|PubMed:28098138"
FT MUTAGEN 96
FT /note="Y->F: Inhibits interaction with TLR4. Decreases
FT IL12B expression after TLR4 activation by
FT lipopolysaccharide. Inhibits interaction with CSK. No
FT effect on interactions with LYN, GRB2, and BLNK."
FT /evidence="ECO:0000269|PubMed:28098138,
FT ECO:0000269|PubMed:28290451"
FT MUTAGEN 97
FT /note="S->A: No effect on interaction with TLR4."
FT /evidence="ECO:0000269|PubMed:28098138"
FT MUTAGEN 98
FT /note="S->A: No effect on interaction with TLR4."
FT /evidence="ECO:0000269|PubMed:28098138"
FT MUTAGEN 99
FT /note="V->A: No effect on interaction with TLR4."
FT /evidence="ECO:0000269|PubMed:28098138"
FT MUTAGEN 120
FT /note="Y->F: Inhibits interaction with BLNK. No effect on
FT interactions with TLR4, GRB2 and CSK."
FT /evidence="ECO:0000269|PubMed:28098138,
FT ECO:0000269|PubMed:28290451"
SQ SEQUENCE 150 AA; 17140 MW; 0837B592EFC13582 CRC64;
MSWWRDNFWI ILAMSIIFIS LVLGLILYCV CRWQLRQGRN WEIAKPSKQD GRDEEKMYEN
VLNSSPGQLP ALPPRGSPFP GDLAPQEAPR QPSAWYSSVK KVRNKKVFAI SGSTEPENDY
DDVEIPATTE TQHSKTTPFW QAEVGLHSSF
