SNTA1_RABIT
ID SNTA1_RABIT Reviewed; 505 AA.
AC Q28626;
DT 10-OCT-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 143.
DE RecName: Full=Alpha-1-syntrophin;
DE AltName: Full=59 kDa dystrophin-associated protein A1 acidic component 1;
DE AltName: Full=59-1 DAP;
DE AltName: Full=Syntrophin-1;
GN Name=SNTA1; Synonyms=SNT1;
OS Oryctolagus cuniculus (Rabbit).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Lagomorpha; Leporidae; Oryctolagus.
OX NCBI_TaxID=9986;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 31-52; 58-63; 65-66;
RP 92-103; 110-116; 178-196; 235-238; 242-244; 246-249; 258-281; 296-319;
RP 356-369 AND 374-393, AND INTERACTION WITH THE DYSTROPHIN-ASSOCIATED
RP COMPLEX.
RC TISSUE=Skeletal muscle;
RX PubMed=8119949; DOI=10.1016/s0021-9258(17)37566-x;
RA Yang B., Ibraghimov-Beskrovnaya O., Moomaw C.R., Slaughter C.A.,
RA Campbell K.P.;
RT "Heterogeneity of the 59-kDa dystrophin-associated protein revealed by cDNA
RT cloning and expression.";
RL J. Biol. Chem. 269:6040-6044(1994).
RN [2]
RP INTERACTION WITH DMD; UTRN; SGCA; SNTB1 AND SNTB2.
RX PubMed=7890602; DOI=10.1074/jbc.270.10.4975;
RA Yang B., Jung D., Rafael J.A., Chamberlain J.S., Campbell K.P.;
RT "Identification of alpha-syntrophin binding to syntrophin triplet,
RT dystrophin, and utrophin.";
RL J. Biol. Chem. 270:4975-4978(1995).
RN [3]
RP INTERACTION WITH F-ACTIN AND CALMODULIN.
RX PubMed=9512352; DOI=10.1016/s0014-5793(98)00085-4;
RA Iwata Y., Pan Y., Yoshida T., Hanada H., Shigekawa M.;
RT "Alpha1-syntrophin has distinct binding sites for actin and calmodulin.";
RL FEBS Lett. 423:173-177(1998).
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 dystrophin glycoprotein complex. Plays an important role in
CC 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 (By
CC similarity). Interacts with the dystrophin protein DMD in a calmodulin
CC dependent 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 -!- INTERACTION:
CC Q28626; G1SR27: GRB2; NbExp=2; IntAct=EBI-8680114, EBI-9693910;
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 -!- TISSUE SPECIFICITY: Highly expressed in skeletal and cardiac muscle and
CC is also detected in brain.
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; U01243; AAA68937.1; -; mRNA.
DR PIR; A53214; A53214.
DR RefSeq; NP_001075802.1; NM_001082333.1.
DR AlphaFoldDB; Q28626; -.
DR BMRB; Q28626; -.
DR SMR; Q28626; -.
DR CORUM; Q28626; -.
DR IntAct; Q28626; 2.
DR MINT; Q28626; -.
DR STRING; 9986.ENSOCUP00000010241; -.
DR PRIDE; Q28626; -.
DR GeneID; 100009179; -.
DR KEGG; ocu:100009179; -.
DR CTD; 6640; -.
DR eggNOG; KOG3551; Eukaryota.
DR InParanoid; Q28626; -.
DR OrthoDB; 1261897at2759; -.
DR Proteomes; UP000001811; Unplaced.
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:0042383; C:sarcolemma; 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 GO; GO:0035556; P:intracellular signal transduction; IDA:CACAO.
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 1: Evidence at protein level;
KW Actin-binding; Calcium; Calmodulin-binding; Cell junction; Cell membrane;
KW Cytoplasm; Cytoskeleton; Direct protein sequencing; Membrane;
KW Phosphoprotein; Reference proteome; Repeat.
FT CHAIN 1..505
FT /note="Alpha-1-syntrophin"
FT /id="PRO_0000184008"
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..24
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 39..75
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 183..212
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 483..505
FT /note="Calmodulin-binding"
FT /evidence="ECO:0000250"
FT COMPBIAS 183..208
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; 53760 MW; 5E4151266C0DD1AB CRC64;
MASGRRAPRT GLLELRAGTG AGAGGERWQR VLVSLAEDAL TVSPADGEPG PEPGAVREPE
PAQINGAAEP GAAPPQLPEA LLLQRRRVTV RKADAGGLGI SIKGGRENKM PILISKIFKG
LAADQTEALF VGDAILSVNG EDLSSATHDE AVQALKKTGK EVVLEVKYMK EVSPYFKNSA
GGTSVGWDSP PASPLQRQPS SPGPQTRNLS EAKHVPLKMA YVSRRCTPSD PEHRYLEICS
ADGQDTIFLR AKDEASARSW AGAIQAQINA LLPWVKDELQ ALLAASSPAG SQDIKQIGWL
TEQLPSGGTA PTLALLTEKE LLLYGGLPQT REALSRPART APLIATRLVH SGPSKGSVPY
DAELSFALRT GTRHGVDTHL FSVESPQELA AWTRQLVDGC HRAAEGVQEV STACTWNGRP
CNLSVHIDKG FTLWAAEPGA ARAVLLRQPF EKLQMSSDDG ASLLFLDFGG AEGEIQLDLH
SCPKTMVFII HSFLSAKVTR LGLLA
