SNTB1_MOUSE
ID SNTB1_MOUSE Reviewed; 537 AA.
AC Q99L88; O35925;
DT 10-OCT-2002, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 4.
DT 03-AUG-2022, entry version 172.
DE RecName: Full=Beta-1-syntrophin;
DE AltName: Full=59 kDa dystrophin-associated protein A1 basic component 1;
DE Short=DAPA1B;
DE AltName: Full=Syntrophin-2;
GN Name=Sntb1; Synonyms=Snt2b1;
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] (ISOFORM 1), SUBCELLULAR LOCATION, AND
RP INTERACTION WITH DMD; DTNA AND 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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Mammary tumor;
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 [3]
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 [4]
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 [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-86; THR-213 AND SER-218, AND
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 [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-86; SER-204; THR-213;
RP SER-218; SER-225; SER-235 AND SER-388, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC and 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).
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.
CC -!- SUBUNIT: Monomer and homodimer (Probable). Interacts with the viral
CC HTLV-1 TAX protein and other members of the syntrophin family: SNTA1
CC and SNTB2 (By similarity). Interacts with the dystrophin protein DMD
CC and related proteins DTNA and UTRN and with the sodium channel proteins
CC SCN4A and SCN5A. Interacts with DTNB (PubMed:10893187). {ECO:0000250,
CC ECO:0000269|PubMed:10893187, ECO:0000269|PubMed:9214383,
CC ECO:0000269|PubMed:9412493, ECO:0000305}.
CC -!- INTERACTION:
CC Q99L88; P25100: ADRA1D; Xeno; NbExp=2; IntAct=EBI-295943, EBI-489993;
CC -!- SUBCELLULAR LOCATION: Cell membrane, sarcolemma
CC {ECO:0000269|PubMed:9214383}; Peripheral membrane protein
CC {ECO:0000269|PubMed:9214383}; Cytoplasmic side
CC {ECO:0000269|PubMed:9214383}. Cell junction
CC {ECO:0000269|PubMed:9214383}. Cytoplasm, cytoskeleton
CC {ECO:0000269|PubMed:9214383}. Note=In skeletal muscle, it localizes at
CC the cytoplasmic side of the sarcolemmal membrane and at neuromuscular
CC junctions.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q99L88-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q99L88-2; Sequence=VSP_006356, VSP_006357;
CC -!- TISSUE SPECIFICITY: Ubiquitous. Expressed at high levels in the liver.
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 by CaM-kinase II. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the syntrophin family. {ECO:0000305}.
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DR EMBL; U89997; AAB66697.1; -; mRNA.
DR EMBL; BC003748; AAH03748.1; -; mRNA.
DR CCDS; CCDS27479.1; -. [Q99L88-1]
DR RefSeq; NP_057876.1; NM_016667.3. [Q99L88-1]
DR RefSeq; XP_006520734.1; XM_006520671.3. [Q99L88-1]
DR AlphaFoldDB; Q99L88; -.
DR SMR; Q99L88; -.
DR BioGRID; 203383; 8.
DR CORUM; Q99L88; -.
DR IntAct; Q99L88; 13.
DR MINT; Q99L88; -.
DR STRING; 10090.ENSMUSP00000041294; -.
DR iPTMnet; Q99L88; -.
DR PhosphoSitePlus; Q99L88; -.
DR EPD; Q99L88; -.
DR jPOST; Q99L88; -.
DR MaxQB; Q99L88; -.
DR PaxDb; Q99L88; -.
DR PeptideAtlas; Q99L88; -.
DR PRIDE; Q99L88; -.
DR ProteomicsDB; 257541; -. [Q99L88-1]
DR ProteomicsDB; 257542; -. [Q99L88-2]
DR Antibodypedia; 13755; 162 antibodies from 25 providers.
DR DNASU; 20649; -.
DR Ensembl; ENSMUST00000039769; ENSMUSP00000041294; ENSMUSG00000060429. [Q99L88-1]
DR Ensembl; ENSMUST00000110200; ENSMUSP00000105829; ENSMUSG00000060429. [Q99L88-2]
DR GeneID; 20649; -.
DR KEGG; mmu:20649; -.
DR UCSC; uc007vsk.1; mouse. [Q99L88-1]
DR CTD; 6641; -.
DR MGI; MGI:101781; Sntb1.
DR VEuPathDB; HostDB:ENSMUSG00000060429; -.
DR eggNOG; KOG3551; Eukaryota.
DR GeneTree; ENSGT00950000182863; -.
DR HOGENOM; CLU_026406_3_1_1; -.
DR InParanoid; Q99L88; -.
DR OMA; RAETCKD; -.
DR OrthoDB; 1261897at2759; -.
DR PhylomeDB; Q99L88; -.
DR TreeFam; TF317932; -.
DR BioGRID-ORCS; 20649; 2 hits in 73 CRISPR screens.
DR ChiTaRS; Sntb1; mouse.
DR PRO; PR:Q99L88; -.
DR Proteomes; UP000000589; Chromosome 15.
DR RNAct; Q99L88; protein.
DR Bgee; ENSMUSG00000060429; Expressed in parotid gland and 201 other tissues.
DR Genevisible; Q99L88; MM.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-SubCell.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
DR GO; GO:0016010; C:dystrophin-associated glycoprotein complex; IBA:GO_Central.
DR GO; GO:0032991; C:protein-containing complex; ISO:MGI.
DR GO; GO:0042383; C:sarcolemma; IEA:UniProtKB-SubCell.
DR GO; GO:0045202; C:synapse; IDA:MGI.
DR GO; GO:0003779; F:actin binding; IEA:UniProtKB-KW.
DR GO; GO:0005516; F:calmodulin binding; IEA:UniProtKB-KW.
DR GO; GO:0030165; F:PDZ domain binding; ISO:MGI.
DR GO; GO:0005198; F:structural molecule activity; IEA:InterPro.
DR CDD; cd01258; PHsplit_syntrophin; 1.
DR Gene3D; 2.30.29.30; -; 3.
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; IPR015482; Syntrophin.
DR PANTHER; PTHR10554; PTHR10554; 1.
DR Pfam; PF00595; PDZ; 1.
DR Pfam; PF00169; PH; 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; 2.
PE 1: Evidence at protein level;
KW Acetylation; Actin-binding; Alternative splicing; Calcium;
KW Calmodulin-binding; Cell junction; Cell membrane; Cytoplasm; Cytoskeleton;
KW Membrane; Phosphoprotein; Reference proteome; Repeat.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:Q13884"
FT CHAIN 2..537
FT /note="Beta-1-syntrophin"
FT /id="PRO_0000184010"
FT DOMAIN 18..297
FT /note="PH 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00145"
FT DOMAIN 111..194
FT /note="PDZ"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00143"
FT DOMAIN 321..432
FT /note="PH 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00145"
FT DOMAIN 481..537
FT /note="SU"
FT REGION 204..233
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 517..537
FT /note="Calmodulin-binding"
FT /evidence="ECO:0000250"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000250|UniProtKB:Q13884"
FT MOD_RES 86
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 125
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q13884"
FT MOD_RES 204
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 213
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 218
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 225
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 231
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q13884"
FT MOD_RES 235
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 388
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT VAR_SEQ 262..276
FT /note="RQLEIHSPDAKHTVI -> STHPSDLIPIQGWAA (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_006356"
FT VAR_SEQ 277..537
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_006357"
SQ SEQUENCE 537 AA; 58081 MW; 91A5E4DD0A97A665 CRC64;
MAVAAAAVAA PAGGGGARAQ RSGLLEVLVR DRWHKVLVNL SEDALVLSCE EGAAAYNGIG
AATNGSFCRG SGTGHPVPGV AQAPDSPAGV RTAFTDLPEQ VPESISNQKR GVKVLKQELG
GLGISIKGGK ENKMPILISK IFKGLAADQT QALYVGDAIL SVNGADLRDA THDEAVQALK
RAGKEVLLEV KYMREATPYV KKGSPVSEIG WETPPPESPR LGGGSAEPLS SQSFSFHRDR
KSIPLKMCYV TRNMTLADPE NRQLEIHSPD AKHTVILRSK DSATAQAWFS AIHSNAGDLL
TRVVADIREQ LGKTGIAGSR EIRHLGWLAE KVPGESEKQW KPALVVLTEK DLLIYDSMPR
RKEAWFSPVH SYPLLATRLV HSGPGKGSPQ AGMDLSFATR TGTKQGIETH LFRAEISRDL
SHWTRSIVQG CHNSAELTAE ITTACTYRNQ ECRLTIHYDN GFSISTEPQD GAFPKTIIQS
PYEKLKMSSD DGIRMLYLDF GGKEGEIQLD LHSCPKPIVF IIHSFLSAKI TRLGLVA
