SNTA1_BOVIN
ID SNTA1_BOVIN Reviewed; 505 AA.
AC Q0P5E6;
DT 24-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT 19-SEP-2006, sequence version 1.
DT 03-AUG-2022, entry version 101.
DE RecName: Full=Alpha-1-syntrophin;
GN Name=SNTA1;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Hereford; TISSUE=Fetal medulla;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (AUG-2006) to the EMBL/GenBank/DDBJ databases.
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 extracellular
CC matrix via the dystrophin glycoprotein complex. Plays an important role
CC in synapse formation and in the organization of UTRN and acetylcholine
CC receptors at the neuromuscular synapse. Binds to phosphatidylinositol
CC 4,5-bisphosphate (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Monomer and homodimer. Interacts with the dystrophin related
CC protein DTNA; SGCG of the dystrophin glycoprotein complex; NOS1; GRB2;
CC GA; TGFA; MAPK12 and the sodium channel proteins SCN4A and SCN5A.
CC Interacts with the dystrophin protein DMD in a calmodulin dependent
CC manner and with related protein UTRN; SGCA of the dystrophin
CC glycoprotein complex; F-actin; calmodulin and with the other members of
CC the syntrophin family SNTB1 and SNTB2. Interacts with MYOC; regulates
CC muscle hypertrophy (By similarity). Interacts with DTNB (By
CC similarity). {ECO:0000250, ECO:0000250|UniProtKB:Q61234}.
CC -!- SUBCELLULAR LOCATION: Cell membrane, sarcolemma {ECO:0000250};
CC Peripheral membrane protein {ECO:0000250}; Cytoplasmic side
CC {ECO:0000250}. Cell junction {ECO:0000250}. Cytoplasm, cytoskeleton
CC {ECO:0000250}. Note=In skeletal muscle, it localizes at the cytoplasmic
CC side of the sarcolemmal membrane and at neuromuscular junctions.
CC {ECO:0000250}.
CC -!- DOMAIN: The PH 1 domain mediates the oligomerization in a calcium
CC dependent manner, and the association with the phosphatidylinositol
CC 4,5-bisphosphate. {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 (By similarity). It contains actin-binding sites. {ECO:0000250}.
CC -!- PTM: Phosphorylated by CaM-kinase II. Phosphorylation may inhibit the
CC interaction with DMD (By similarity). {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the syntrophin family. {ECO:0000305}.
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DR EMBL; BC120146; AAI20147.1; -; mRNA.
DR RefSeq; NP_001069366.1; NM_001075898.2.
DR AlphaFoldDB; Q0P5E6; -.
DR BMRB; Q0P5E6; -.
DR SMR; Q0P5E6; -.
DR STRING; 9913.ENSBTAP00000000662; -.
DR PaxDb; Q0P5E6; -.
DR PRIDE; Q0P5E6; -.
DR Ensembl; ENSBTAT00000000662; ENSBTAP00000000662; ENSBTAG00000000512.
DR GeneID; 527488; -.
DR KEGG; bta:527488; -.
DR CTD; 6640; -.
DR VEuPathDB; HostDB:ENSBTAG00000000512; -.
DR VGNC; VGNC:35083; SNTA1.
DR eggNOG; KOG3551; Eukaryota.
DR GeneTree; ENSGT00950000182863; -.
DR HOGENOM; CLU_026406_3_1_1; -.
DR InParanoid; Q0P5E6; -.
DR OMA; DIKHIGW; -.
DR OrthoDB; 1261897at2759; -.
DR TreeFam; TF317932; -.
DR Proteomes; UP000009136; Chromosome 13.
DR Bgee; ENSBTAG00000000512; Expressed in choroid plexus and 99 other tissues.
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:0031594; C:neuromuscular junction; IBA:GO_Central.
DR GO; GO:0045211; C:postsynaptic membrane; IEA:Ensembl.
DR GO; GO:0042383; C:sarcolemma; IBA:GO_Central.
DR GO; GO:0045202; C:synapse; IBA:GO_Central.
DR GO; GO:0003779; F:actin binding; IEA:UniProtKB-KW.
DR GO; GO:0051117; F:ATPase binding; IEA:Ensembl.
DR GO; GO:0005516; F:calmodulin binding; IEA:UniProtKB-KW.
DR GO; GO:0050998; F:nitric-oxide synthase binding; IEA:Ensembl.
DR GO; GO:0017080; F:sodium channel regulator activity; IEA:Ensembl.
DR GO; GO:0005198; F:structural molecule activity; IEA:InterPro.
DR GO; GO:0044325; F:transmembrane transporter binding; IEA:Ensembl.
DR GO; GO:1902083; P:negative regulation of peptidyl-cysteine S-nitrosylation; IEA:Ensembl.
DR GO; GO:0007528; P:neuromuscular junction development; IEA:Ensembl.
DR GO; GO:0002027; P:regulation of heart rate; IEA:Ensembl.
DR GO; GO:1902305; P:regulation of sodium ion transmembrane transport; IEA:Ensembl.
DR GO; GO:0003117; P:regulation of vasoconstriction by circulating norepinephrine; IEA:Ensembl.
DR GO; GO:0060307; P:regulation of ventricular cardiac muscle cell membrane repolarization; IEA:Ensembl.
DR GO; GO:0086005; P:ventricular cardiac muscle cell action potential; IEA:Ensembl.
DR CDD; cd01258; PHsplit_syntrophin; 1.
DR Gene3D; 2.30.29.30; -; 2.
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; IPR028552; SNTA1.
DR InterPro; IPR015482; Syntrophin.
DR PANTHER; PTHR10554; PTHR10554; 1.
DR PANTHER; PTHR10554:SF6; PTHR10554:SF6; 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 2: Evidence at transcript level;
KW Actin-binding; Calcium; Calmodulin-binding; Cell junction; Cell membrane;
KW Cytoplasm; Cytoskeleton; Membrane; Phosphoprotein; Reference proteome;
KW Repeat.
FT CHAIN 1..505
FT /note="Alpha-1-syntrophin"
FT /id="PRO_0000295662"
FT DOMAIN 6..269
FT /note="PH 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00145"
FT DOMAIN 87..170
FT /note="PDZ"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00143"
FT DOMAIN 293..401
FT /note="PH 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00145"
FT DOMAIN 449..505
FT /note="SU"
FT REGION 1..77
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 180..211
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 483..505
FT /note="Calmodulin-binding"
FT /evidence="ECO:0000250"
FT COMPBIAS 180..194
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 101
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q61234"
FT MOD_RES 184
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q13424"
FT MOD_RES 189
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q13424"
FT MOD_RES 193
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q13424"
FT MOD_RES 200
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q61234"
SQ SEQUENCE 505 AA; 53873 MW; 32262C6284D5D7A5 CRC64;
MASGRRAPRT GLLELRAGAG SGAGGERWQR AVLSLEEDAL TVSPADGEPG PEPGAQREPE
PAQLNGAAEP GAASPPLPEA LLLQPRRVTV RKADAGGLGI SIKGGRENKM PILISKIFKG
LAADQTEALF VGDAILSVNG EDLSSATHDE AVQVLKKTGK EVVLEVKYMK EVSPYFKNSA
SGTSVGWDSP PASPLQRQPS SPGPPPRDLR DAKHMSLKMA YVSRRCTPTD PETRYLEICS
ADGRDTLFLR AKDEASAKSW AAAIQAQVNT LTPRVKDELQ ALLSATSTAG SQDIKRIGWL
TEQLPSGGTA PTLALLTEKE LLLYSCLPQT REALSRPART APLITTRLVH SGPSKGSVPY
DAELSFALRT GTRHGVDTHL FSVESPQELA AWTRQLVDGC HRAAEGVQEV STACTWNGRA
CSLSVHIDNG FTLWAAEPGA ARAVLLRQPF EKLQMSSDDG ASLLFLDFGG AEGEIQLDLH
SCPKTMVFII HSFLSAKVTR LGLLA
