SNT1_CAEEL
ID SNT1_CAEEL Reviewed; 440 AA.
AC Q93646; Q9XVP8;
DT 09-NOV-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1997, sequence version 1.
DT 03-AUG-2022, entry version 149.
DE RecName: Full=Syntrophin-1;
GN Name=stn-1 {ECO:0000303|PubMed:14499607}; ORFNames=F30A10.8;
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239;
RN [1] {ECO:0000305}
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORMS A AND B), FUNCTION, TISSUE
RP SPECIFICITY, DEVELOPMENTAL STAGE, AND INTERACTION WITH DYB-1.
RC STRAIN=Bristol N2 {ECO:0000269|PubMed:14499607};
RX PubMed=14499607; DOI=10.1016/j.jmb.2003.08.021;
RA Grisoni K., Gieseler K., Mariol M.-C., Martin E., Carre-Pierrat M.,
RA Moulder G., Barstead R., Segalat L.;
RT "The stn-1 syntrophin gene of C.elegans is functionally related to
RT dystrophin and dystrobrevin.";
RL J. Mol. Biol. 332:1037-1046(2003).
RN [2] {ECO:0000312|EMBL:CAB03025.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2 {ECO:0000312|EMBL:CAB03025.1};
RX PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG The C. elegans sequencing consortium;
RT "Genome sequence of the nematode C. elegans: a platform for investigating
RT biology.";
RL Science 282:2012-2018(1998).
RN [3] {ECO:0000305}
RP FUNCTION.
RX PubMed=12234669; DOI=10.1016/s0378-1119(02)00762-x;
RA Grisoni K., Martin E., Gieseler K., Mariol M.-C., Segalat L.;
RT "Genetic evidence for a dystrophin-glycoprotein complex (DGC) in
RT Caenorhabditis elegans.";
RL Gene 294:77-86(2002).
RN [4] {ECO:0000305}
RP INTERACTION WITH DYB-1 AND DYS-1.
RX PubMed=10561496; DOI=10.1016/s0014-5793(99)01421-0;
RA Gieseler K., Abdel-Dayem M., Segalat L.;
RT "In vitro interactions of Caenorhabditis elegans dystrophin with
RT dystrobrevin and syntrophin.";
RL FEBS Lett. 461:59-62(1999).
RN [5] {ECO:0000305}
RP INTERACTION WITH SNF-6.
RX PubMed=15318222; DOI=10.1038/nature02798;
RA Kim H., Rogers M.J., Richmond J.E., McIntire S.L.;
RT "SNF-6 is an acetylcholine transporter interacting with the dystrophin
RT complex in Caenorhabditis elegans.";
RL Nature 430:891-896(2004).
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 (DGC). May also act by slowing calcium channel
CC activity via a direct or indirect mechanism potentially involving other
CC second messengers. Plays an early role in the formation of the
CC neuromuscular junction and is necessary for muscle maintenance.
CC {ECO:0000269|PubMed:12234669, ECO:0000269|PubMed:14499607}.
CC -!- SUBUNIT: Component of the dystrophin glycoprotein complex (DGC).
CC Interacts with dyb-1, dys-1 and snf-6 to form the DGC.
CC {ECO:0000269|PubMed:10561496, ECO:0000269|PubMed:14499607,
CC ECO:0000269|PubMed:15318222}.
CC -!- INTERACTION:
CC Q93646; O76689: snf-6; NbExp=2; IntAct=EBI-447079, EBI-447522;
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000250}; Peripheral membrane
CC protein {ECO:0000250}. Cytoplasm, cytoskeleton {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=a {ECO:0000269|PubMed:14499607}; Synonyms=Alpha;
CC IsoId=Q93646-1; Sequence=Displayed;
CC Name=b {ECO:0000269|PubMed:14499607}; Synonyms=Beta;
CC IsoId=Q93646-2; Sequence=VSP_051613;
CC -!- TISSUE SPECIFICITY: Expressed in neurons and muscles; particularly
CC strong expression in the body wall, head and vulval muscles, and in
CC ventral nerve cord (at protein level). {ECO:0000269|PubMed:14499607}.
CC -!- DEVELOPMENTAL STAGE: Expressed both maternally and zygotically.
CC {ECO:0000269|PubMed:14499607}.
CC -!- SIMILARITY: Belongs to the syntrophin family.
CC {ECO:0000269|PubMed:14499607}.
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DR EMBL; Z81072; CAB03025.1; -; Genomic_DNA.
DR EMBL; Z81072; CAB03028.1; -; Genomic_DNA.
DR PIR; T21568; T21568.
DR PIR; T21570; T21570.
DR RefSeq; NP_492521.1; NM_060120.4. [Q93646-1]
DR AlphaFoldDB; Q93646; -.
DR SMR; Q93646; -.
DR BioGRID; 57332; 4.
DR IntAct; Q93646; 15.
DR STRING; 6239.F30A10.8a; -.
DR EPD; Q93646; -.
DR PaxDb; Q93646; -.
DR EnsemblMetazoa; F30A10.8.1; F30A10.8.1; WBGene00006062. [Q93646-1]
DR EnsemblMetazoa; F30A10.8.2; F30A10.8.2; WBGene00006062. [Q93646-1]
DR EnsemblMetazoa; F30A10.8.3; F30A10.8.3; WBGene00006062. [Q93646-1]
DR GeneID; 266844; -.
DR KEGG; cel:CELE_F30A10.8; -.
DR UCSC; F30A10.8b; c. elegans. [Q93646-1]
DR CTD; 266844; -.
DR WormBase; F30A10.8; CE09809; WBGene00006062; stn-1. [Q93646-1]
DR eggNOG; KOG3551; Eukaryota.
DR GeneTree; ENSGT00950000182863; -.
DR HOGENOM; CLU_026406_1_0_1; -.
DR InParanoid; Q93646; -.
DR OMA; QYPFETI; -.
DR OrthoDB; 1261897at2759; -.
DR PhylomeDB; Q93646; -.
DR SignaLink; Q93646; -.
DR PRO; PR:Q93646; -.
DR Proteomes; UP000001940; Chromosome I.
DR Bgee; WBGene00006062; Expressed in pharyngeal muscle cell (C elegans) and 3 other tissues.
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; IMP:UniProtKB.
DR GO; GO:0005277; F:acetylcholine transmembrane transporter activity; IMP:UniProtKB.
DR GO; GO:0005246; F:calcium channel regulator activity; IMP:UniProtKB.
DR GO; GO:0005198; F:structural molecule activity; IEA:InterPro.
DR GO; GO:0015870; P:acetylcholine transport; IMP:UniProtKB.
DR GO; GO:0046716; P:muscle cell cellular homeostasis; IMP:UniProtKB.
DR GO; GO:0032413; P:negative regulation of ion transmembrane transporter activity; IGI:WormBase.
DR GO; GO:0040013; P:negative regulation of locomotion; IMP:WormBase.
DR GO; GO:0007528; P:neuromuscular junction development; TAS:UniProtKB.
DR GO; GO:0040017; P:positive regulation of locomotion; IMP:UniProtKB.
DR GO; GO:0043058; P:regulation of backward locomotion; IMP:WormBase.
DR GO; GO:0043059; P:regulation of forward locomotion; IMP:WormBase.
DR GO; GO:0046662; P:regulation of oviposition; IMP:WormBase.
DR GO; GO:0045214; P:sarcomere organization; IGI:WormBase.
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; IPR015482; Syntrophin.
DR InterPro; IPR031072; Syntrophin-1.
DR PANTHER; PTHR10554; PTHR10554; 1.
DR PANTHER; PTHR10554:SF12; PTHR10554:SF12; 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; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Cytoplasm; Cytoskeleton; Membrane;
KW Reference proteome; Repeat.
FT CHAIN 1..440
FT /note="Syntrophin-1"
FT /id="PRO_0000184017"
FT DOMAIN 2..208
FT /note="PH 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00145"
FT DOMAIN 45..128
FT /note="PDZ"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00143"
FT DOMAIN 227..340
FT /note="PH 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00145"
FT DOMAIN 384..440
FT /note="SU"
FT /evidence="ECO:0000255"
FT VAR_SEQ 411..440
FT /note="ELDLLNSAKPVVFILHSFLATKVYRLGLYA -> VKMDFILTLISYL (in
FT isoform b)"
FT /evidence="ECO:0000303|PubMed:14499607"
FT /id="VSP_051613"
SQ SEQUENCE 440 AA; 49005 MW; 7FCE5ACC6CE124B6 CRC64;
MAAVRSGLVD IFVQGQWHRV LATLDPTAIT LQTMEQNEAE AEKRTVRVVK YDGNGLGISI
KGGRDNNMPI VISKIFKGMA ADQAGELFLD DVIISVNGEN LLDASHEEAV RALKRAGRVV
DLQVQYRRED MMHRENIVEN VEWDDDIRER VRTIGLKLAY VARAGIDADA EGRILEMRSP
SGRYSLAMRC SSSEEADGWF EALHACTTCL LTQALAQVNI MLGNNPQVRH MGWIAEQVSE
NGISMWKPKF MTLTNSEILF YEAVPQLKAE WAEPRLVRPL VATRVVQTSS RTAPVIKGLT
DVISFRMRTG TQQGVRTHTI RVETHAELAR WVRAVVIGGY EACLSTSQVS APCLWRGESC
ELIVNLDNGI SLLSSTGEVL WQHSFETIRA TGDDGGRFLW VDFGPPHGEQ ELDLLNSAKP
VVFILHSFLA TKVYRLGLYA
