SNTB2_MOUSE
ID SNTB2_MOUSE Reviewed; 520 AA.
AC Q61235;
DT 10-OCT-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1997, sequence version 2.
DT 03-AUG-2022, entry version 181.
DE RecName: Full=Beta-2-syntrophin;
DE AltName: Full=59 kDa dystrophin-associated protein A1 basic component 2;
DE AltName: Full=Syntrophin-3;
DE Short=SNT3;
DE AltName: Full=Syntrophin-like;
DE Short=SNTL;
GN Name=Sntb2; Synonyms=Snt2b2;
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 [MRNA].
RC TISSUE=Diaphragm;
RX PubMed=7592771; DOI=10.1074/jbc.270.43.25859;
RA Adams M.E., Dwyer T.M., Dowler L.L., White R.A., Froehner S.C.;
RT "Mouse alpha 1- and beta 2-syntrophin gene structure, chromosome
RT localization, and homology with a discs large domain.";
RL J. Biol. Chem. 270:25859-25865(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 91-520.
RC TISSUE=Diaphragm;
RX PubMed=7691103; DOI=10.1016/0896-6273(93)90157-m;
RA Adams M.E., Butler M.H., Dwyer T.M., Peters M.F., Murnane A.A.,
RA Froehner S.C.;
RT "Two forms of mouse syntrophin, a 58 kDa dystrophin-associated protein,
RT differ in primary structure and tissue distribution.";
RL Neuron 11:531-540(1993).
RN [3]
RP SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND INTERACTION WITH UTRN.
RX PubMed=9214383; DOI=10.1083/jcb.138.1.81;
RA Peters M.F., Adams M.E., Froehner S.C.;
RT "Differential association of syntrophin pairs with the dystrophin
RT complex.";
RL J. Cell Biol. 138:81-93(1997).
RN [4]
RP INTERACTION WITH SCN4A AND SCN5A.
RX PubMed=9412493; DOI=10.1523/jneurosci.18-01-00128.1998;
RA Gee S.H., Madhavan R., Levinson S.R., Caldwell J.H., Sealock R.,
RA Froehner S.C.;
RT "Interaction of muscle and brain sodium channels with multiple members of
RT the syntrophin family of dystrophin-associated proteins.";
RL J. Neurosci. 18:128-137(1998).
RN [5]
RP INTERACTION WITH SAST; MAST205; MICROTUBULES AND MICROTUBULE-ASSOCIATED
RP PROTEINS.
RX PubMed=10404183; DOI=10.1038/10165;
RA Lumeng C., Phelps S., Crawford G.E., Walden P.D., Barald K.,
RA Chamberlain J.S.;
RT "Interactions between beta 2-syntrophin and a family of microtubule-
RT associated serine/threonine kinases.";
RL Nat. Neurosci. 2:611-617(1999).
RN [6]
RP INTERACTION WITH DTNB.
RX PubMed=10893187; DOI=10.1242/jcs.113.15.2715;
RA Loh N.Y., Newey S.E., Davies K.E., Blake D.J.;
RT "Assembly of multiple dystrobrevin-containing complexes in the kidney.";
RL J. Cell Sci. 113:2715-2724(2000).
RN [7]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain cortex;
RX PubMed=17114649; DOI=10.1074/mcp.m600046-mcp200;
RA Munton R.P., Tweedie-Cullen R., Livingstone-Zatchej M., Weinandy F.,
RA Waidelich M., Longo D., Gehrig P., Potthast F., Rutishauser D., Gerrits B.,
RA Panse C., Schlapbach R., Mansuy I.M.;
RT "Qualitative and quantitative analyses of protein phosphorylation in naive
RT and stimulated mouse synaptosomal preparations.";
RL Mol. Cell. Proteomics 6:283-293(2007).
RN [8]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT "Large-scale phosphorylation analysis of mouse liver.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-75 AND SER-90, 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 [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-90, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic fibroblast;
RX PubMed=19131326; DOI=10.1074/mcp.m800451-mcp200;
RA Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.;
RT "Large scale localization of protein phosphorylation by use of electron
RT capture dissociation mass spectrometry.";
RL Mol. Cell. Proteomics 8:904-912(2009).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-202; SER-213; SER-373 AND
RP SER-375, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Lung, Spleen, and
RC Testis;
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).
CC -!- FUNCTION: Adapter protein that binds to and probably organizes the
CC subcellular localization of a variety of membrane proteins. May link
CC various receptors to the actin cytoskeleton and the dystrophin
CC glycoprotein complex. May play a role in the regulation of secretory
CC granules via its interaction with PTPRN (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Monomer and homodimer (Probable). Interacts with the
CC dystrophin protein DMD and related protein DTNA; and with the other
CC members of the syntrophin family: SNTA1 and SNTB1. Interacts with the
CC neuroregulin receptor ERBB4. Interacts with PTPRN when phosphorylated,
CC protecting PTPRN from protein cleavage by CAPN1. Dephosphorylation upon
CC insulin stimulation disrupts the interaction with PTPRN and results in
CC the cleavage of PTPRN (By similarity). Interacts with the sodium
CC channel proteins SCN4A and SCN5A. Interacts with SAST, MAST205,
CC microtubules and microtubule-associated proteins. Interacts with the
CC dystrophin related protein UTRN. Interacts with DTNB (PubMed:10893187).
CC {ECO:0000250, ECO:0000269|PubMed:10404183, ECO:0000269|PubMed:10893187,
CC ECO:0000269|PubMed:9214383, ECO:0000269|PubMed:9412493, ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000269|PubMed:9214383}.
CC Cytoplasmic vesicle, secretory vesicle membrane
CC {ECO:0000269|PubMed:9214383}; Peripheral membrane protein
CC {ECO:0000269|PubMed:9214383}. Cell junction {ECO:0000250}. Cytoplasm,
CC cytoskeleton {ECO:0000269|PubMed:9214383}. Note=Membrane-associated. In
CC insulinoma cell line, it is enriched in secretory granules (By
CC similarity). In muscle, it is exclusively localized at the
CC neuromuscular junction. {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Ubiquitous. Expressed at high levels in the testis.
CC {ECO:0000269|PubMed:9214383}.
CC -!- DOMAIN: The PH 1 domain mediates the oligomerization in a calcium
CC dependent manner. {ECO:0000250}.
CC -!- DOMAIN: The PDZ domain binds to the last three or four amino acids of
CC ion channels and receptor proteins. The association with dystrophin or
CC related proteins probably leaves the PDZ domain available to recruit
CC proteins to the membrane (By similarity). {ECO:0000250}.
CC -!- DOMAIN: The SU domain binds calmodulin in a calcium-dependent manner.
CC {ECO:0000250}.
CC -!- PTM: Phosphorylated. Partially dephosphorylated upon insulin
CC stimulation (By similarity). {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the syntrophin family. {ECO:0000305}.
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DR EMBL; U00678; AAC53060.1; -; mRNA.
DR CCDS; CCDS22642.1; -.
DR RefSeq; NP_033255.1; NM_009229.4.
DR AlphaFoldDB; Q61235; -.
DR SMR; Q61235; -.
DR BioGRID; 203384; 6.
DR CORUM; Q61235; -.
DR IntAct; Q61235; 10.
DR MINT; Q61235; -.
DR STRING; 10090.ENSMUSP00000037324; -.
DR iPTMnet; Q61235; -.
DR PhosphoSitePlus; Q61235; -.
DR EPD; Q61235; -.
DR jPOST; Q61235; -.
DR MaxQB; Q61235; -.
DR PaxDb; Q61235; -.
DR PRIDE; Q61235; -.
DR ProteomicsDB; 261536; -.
DR Antibodypedia; 656; 155 antibodies from 20 providers.
DR DNASU; 20650; -.
DR Ensembl; ENSMUST00000212524; ENSMUSP00000148684; ENSMUSG00000041308.
DR GeneID; 20650; -.
DR KEGG; mmu:20650; -.
DR UCSC; uc009ngt.1; mouse.
DR CTD; 6645; -.
DR MGI; MGI:101771; Sntb2.
DR VEuPathDB; HostDB:ENSMUSG00000041308; -.
DR eggNOG; KOG3551; Eukaryota.
DR GeneTree; ENSGT00950000182863; -.
DR HOGENOM; CLU_026406_3_1_1; -.
DR InParanoid; Q61235; -.
DR OMA; AHSWFMA; -.
DR OrthoDB; 1261897at2759; -.
DR PhylomeDB; Q61235; -.
DR TreeFam; TF317932; -.
DR BioGRID-ORCS; 20650; 1 hit in 72 CRISPR screens.
DR ChiTaRS; Sntb2; mouse.
DR PRO; PR:Q61235; -.
DR Proteomes; UP000000589; Chromosome 8.
DR RNAct; Q61235; protein.
DR Bgee; ENSMUSG00000041308; Expressed in lumbar dorsal root ganglion and 221 other tissues.
DR ExpressionAtlas; Q61235; baseline and differential.
DR Genevisible; Q61235; MM.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-SubCell.
DR GO; GO:0005737; C:cytoplasm; ISO:MGI.
DR GO; GO:0016010; C:dystrophin-associated glycoprotein complex; IBA:GO_Central.
DR GO; GO:0005794; C:Golgi apparatus; ISO:MGI.
DR GO; GO:0005874; C:microtubule; IEA:UniProtKB-KW.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005886; C:plasma membrane; ISO:MGI.
DR GO; GO:0032991; C:protein-containing complex; ISO:MGI.
DR GO; GO:0045202; C:synapse; IDA:MGI.
DR GO; GO:0030658; C:transport vesicle membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0003779; F:actin binding; IEA:UniProtKB-KW.
DR GO; GO:0005516; F:calmodulin binding; IEA:UniProtKB-KW.
DR GO; GO:0005198; F:structural molecule activity; IEA:InterPro.
DR CDD; cd01258; PHsplit_syntrophin; 1.
DR Gene3D; 2.30.29.30; -; 1.
DR Gene3D; 2.30.42.10; -; 1.
DR InterPro; IPR001478; PDZ.
DR InterPro; IPR036034; PDZ_sf.
DR InterPro; IPR011993; PH-like_dom_sf.
DR InterPro; IPR001849; PH_domain.
DR InterPro; IPR041428; PHsplit_syntrophin.
DR InterPro; IPR028550; SNTB2.
DR InterPro; IPR015482; Syntrophin.
DR PANTHER; PTHR10554; PTHR10554; 1.
DR PANTHER; PTHR10554:SF8; PTHR10554:SF8; 1.
DR Pfam; PF00595; PDZ; 1.
DR Pfam; PF18012; PH_17; 1.
DR SMART; SM00228; PDZ; 1.
DR SMART; SM00233; PH; 2.
DR SUPFAM; SSF50156; SSF50156; 1.
DR PROSITE; PS50106; PDZ; 1.
DR PROSITE; PS50003; PH_DOMAIN; 1.
PE 1: Evidence at protein level;
KW Actin-binding; Calcium; Calmodulin-binding; Cell junction; Cytoplasm;
KW Cytoplasmic vesicle; Cytoskeleton; Membrane; Microtubule; Phosphoprotein;
KW Reference proteome; Repeat.
FT CHAIN 1..520
FT /note="Beta-2-syntrophin"
FT /id="PRO_0000184012"
FT DOMAIN 95..178
FT /note="PDZ"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00143"
FT DOMAIN 143..280
FT /note="PH 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00145"
FT DOMAIN 305..417
FT /note="PH 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00145"
FT DOMAIN 464..520
FT /note="SU"
FT REGION 45..95
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 195..220
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 498..520
FT /note="Calmodulin-binding"
FT /evidence="ECO:0000250"
FT COMPBIAS 69..86
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 195..214
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 75
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19144319"
FT MOD_RES 90
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19131326,
FT ECO:0007744|PubMed:19144319"
FT MOD_RES 109
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q13425"
FT MOD_RES 191
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q13425"
FT MOD_RES 202
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 213
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 373
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 375
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
SQ SEQUENCE 520 AA; 56382 MW; 9F6886837C1CDB20 CRC64;
MAVWTRATKA GLVELLLRER WVRVVAELSG ESLSLTGDAA AVEPEPPAAA FNGLPNGGGG
ESLPGSPNRG LGPPSPPAPP RGPAGEASAS PPVRRVRVVK QEAGGLGISI KGGRENRMPI
LISKIFPGLA ADQSRALRLG DAILSVNGTD LRQATHDQAV QALKRAGKEV LLEVKFIREV
TPYIKKPSLV SDLPWEGASP QSPSFSGSED SGSPKHQNTT KDRKVIPLKM CFAARNLSMP
DLENRLIELH SPDSRNTLIL RCKDTATAHS WFVAIHTNIM ALLPQVLAEL NAMLGATSTA
GGSKEVKHIA WLAEQAKLDG GRQQWRPVLM AVTEKDLLLY DCMPWTRDAW ASPCHSYPLV
ATRLVHSGSG CRSPSLGSDL TFATRTGSRQ GIEMHLFRVE THRDLSTWTR ILVQGCHAAA
ELIKEVSLGC TLSGQEVRFT VHYEHGFTIT RDNGGASSIL YRYPFERLKM SADDGIRNLY
LDFGGPEGEL TMDLHSCPKP IVFVLHTFLS AKVTRMGLLV
