SNTG1_HUMAN
ID SNTG1_HUMAN Reviewed; 517 AA.
AC Q9NSN8; Q2M3Q0; Q9NY98;
DT 10-OCT-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 171.
DE RecName: Full=Gamma-1-syntrophin;
DE Short=G1SYN;
DE AltName: Full=Syntrophin-4;
DE Short=SYN4;
GN Name=SNTG1;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), TISSUE SPECIFICITY, AND
RP INTERACTION WITH DMD; DTNA AND DTNB.
RC TISSUE=Fetal brain, and Neuron;
RX PubMed=10747910; DOI=10.1074/jbc.m000439200;
RA Piluso G., Mirabella M., Ricci E., Belsito A., Abbondanza C., Servidei S.,
RA Puca A.A., Tonali P., Puca G.A., Nigro V.;
RT "Gamma1- and gamma2-syntrophins, two novel dystrophin-binding proteins
RT localized in neuronal cells.";
RL J. Biol. Chem. 275:15851-15860(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Amygdala;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D.,
RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Brain;
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 [4]
RP INTERACTION WITH DGKZ.
RX PubMed=11352924; DOI=10.1074/jbc.m104156200;
RA Hogan A., Shepherd L., Chabot J., Quenneville S., Prescott S.M.,
RA Topham M.K., Gee S.H.;
RT "Interaction of gamma 1-syntrophin with diacylglycerol kinase-zeta.
RT Regulation of nuclear localization by PDZ interactions.";
RL J. Biol. Chem. 276:26526-26533(2001).
CC -!- FUNCTION: Adapter protein that binds to and probably organizes the
CC subcellular localization of a variety of proteins. May link various
CC receptors to the actin cytoskeleton and the dystrophin glycoprotein
CC complex (By similarity). May participate in regulating the subcellular
CC location of diacylglycerol kinase-zeta to ensure that diacylglycerol is
CC rapidly inactivated following receptor activation. {ECO:0000250}.
CC -!- SUBUNIT: Isoform 1, but not isoform 2, interacts with the dystrophin
CC protein DMD and related proteins DTNA and DTNB. Interacts with DGKZ.
CC {ECO:0000269|PubMed:10747910, ECO:0000269|PubMed:11352924}.
CC -!- INTERACTION:
CC Q9NSN8; Q9HB19: PLEKHA2; NbExp=3; IntAct=EBI-19763427, EBI-4401947;
CC Q9NSN8; P04004: VTN; NbExp=3; IntAct=EBI-19763427, EBI-1036653;
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton. Nucleus. Note=Mainly
CC cytoplasmic and weakly nuclear.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9NSN8-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9NSN8-2; Sequence=VSP_006360;
CC -!- TISSUE SPECIFICITY: Brain specific. In CNS, it is expressed in the
CC perikaryon and proximal portion of the neuronal processes. Strong
CC expression in the hippocampus, neuron-rich dendate granule cells, and
CC pyramidal cell layers. Highly expressed in neurons of the cerebral
CC cortex. Also expressed in the cerebellar cortex, deep cerebellar
CC nuclei, thalamus, and basal ganglia. No expression in muscle cells.
CC {ECO:0000269|PubMed:10747910}.
CC -!- DOMAIN: The PDZ domain binds to the last three or four amino acids of
CC DGKZ. The association with dystrophin or related proteins probably
CC leaves the PDZ domain available to recruit proteins to the membrane.
CC -!- SIMILARITY: Belongs to the syntrophin family. {ECO:0000305}.
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DR EMBL; AJ003030; CAB92968.1; -; mRNA.
DR EMBL; AL161971; CAB82311.1; -; mRNA.
DR EMBL; BC075072; AAH75072.1; -; mRNA.
DR EMBL; BC104829; AAI04830.1; -; mRNA.
DR CCDS; CCDS6147.1; -. [Q9NSN8-1]
DR CCDS; CCDS75737.1; -. [Q9NSN8-2]
DR PIR; T47134; T47134.
DR RefSeq; NP_001274742.1; NM_001287813.2. [Q9NSN8-1]
DR RefSeq; NP_001274743.1; NM_001287814.2. [Q9NSN8-2]
DR RefSeq; NP_001308702.1; NM_001321773.1. [Q9NSN8-1]
DR RefSeq; NP_001308705.1; NM_001321776.1.
DR RefSeq; NP_001308706.1; NM_001321777.1.
DR RefSeq; NP_061840.1; NM_018967.4. [Q9NSN8-1]
DR RefSeq; XP_016869068.1; XM_017013579.1. [Q9NSN8-1]
DR RefSeq; XP_016869069.1; XM_017013580.1. [Q9NSN8-1]
DR AlphaFoldDB; Q9NSN8; -.
DR SMR; Q9NSN8; -.
DR BioGRID; 119928; 31.
DR CORUM; Q9NSN8; -.
DR IntAct; Q9NSN8; 2.
DR STRING; 9606.ENSP00000429842; -.
DR iPTMnet; Q9NSN8; -.
DR PhosphoSitePlus; Q9NSN8; -.
DR BioMuta; SNTG1; -.
DR DMDM; 23822220; -.
DR MassIVE; Q9NSN8; -.
DR PaxDb; Q9NSN8; -.
DR PeptideAtlas; Q9NSN8; -.
DR PRIDE; Q9NSN8; -.
DR ProteomicsDB; 82570; -. [Q9NSN8-1]
DR ProteomicsDB; 82571; -. [Q9NSN8-2]
DR Antibodypedia; 24371; 117 antibodies from 23 providers.
DR DNASU; 54212; -.
DR Ensembl; ENST00000517473.5; ENSP00000431123.1; ENSG00000147481.17. [Q9NSN8-2]
DR Ensembl; ENST00000518864.5; ENSP00000429276.1; ENSG00000147481.17. [Q9NSN8-1]
DR Ensembl; ENST00000642720.2; ENSP00000493900.1; ENSG00000147481.17. [Q9NSN8-1]
DR GeneID; 54212; -.
DR KEGG; hsa:54212; -.
DR MANE-Select; ENST00000642720.2; ENSP00000493900.1; NM_018967.5; NP_061840.1.
DR UCSC; uc003xqs.3; human. [Q9NSN8-1]
DR CTD; 54212; -.
DR DisGeNET; 54212; -.
DR GeneCards; SNTG1; -.
DR HGNC; HGNC:13740; SNTG1.
DR HPA; ENSG00000147481; Tissue enhanced (brain, lymphoid tissue).
DR MIM; 608714; gene.
DR neXtProt; NX_Q9NSN8; -.
DR OpenTargets; ENSG00000147481; -.
DR PharmGKB; PA37806; -.
DR VEuPathDB; HostDB:ENSG00000147481; -.
DR eggNOG; KOG3549; Eukaryota.
DR GeneTree; ENSGT00950000182863; -.
DR HOGENOM; CLU_039445_0_0_1; -.
DR InParanoid; Q9NSN8; -.
DR OMA; HNKVDAN; -.
DR PhylomeDB; Q9NSN8; -.
DR TreeFam; TF317932; -.
DR PathwayCommons; Q9NSN8; -.
DR SignaLink; Q9NSN8; -.
DR SIGNOR; Q9NSN8; -.
DR BioGRID-ORCS; 54212; 6 hits in 1073 CRISPR screens.
DR ChiTaRS; SNTG1; human.
DR GeneWiki; SNTG1; -.
DR GenomeRNAi; 54212; -.
DR Pharos; Q9NSN8; Tbio.
DR PRO; PR:Q9NSN8; -.
DR Proteomes; UP000005640; Chromosome 8.
DR RNAct; Q9NSN8; protein.
DR Bgee; ENSG00000147481; Expressed in Brodmann (1909) area 23 and 105 other tissues.
DR ExpressionAtlas; Q9NSN8; baseline and differential.
DR Genevisible; Q9NSN8; HS.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005856; C:cytoskeleton; IDA:LIFEdb.
DR GO; GO:0016010; C:dystrophin-associated glycoprotein complex; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0032587; C:ruffle membrane; IDA:UniProtKB.
DR GO; GO:0016013; C:syntrophin complex; TAS:ProtInc.
DR GO; GO:0003779; F:actin binding; IEA:UniProtKB-KW.
DR GO; GO:0008022; F:protein C-terminus binding; IPI:UniProtKB.
DR GO; GO:0005198; F:structural molecule activity; IEA:InterPro.
DR GO; GO:0007154; P:cell communication; TAS:ProtInc.
DR Gene3D; 2.30.42.10; -; 1.
DR InterPro; IPR001478; PDZ.
DR InterPro; IPR036034; PDZ_sf.
DR InterPro; IPR001849; PH_domain.
DR InterPro; IPR015482; Syntrophin.
DR InterPro; IPR015483; Syntrophin_gamma.
DR PANTHER; PTHR10554; PTHR10554; 1.
DR PANTHER; PTHR10554:SF2; PTHR10554:SF2; 1.
DR Pfam; PF00595; PDZ; 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; Alternative splicing; Cytoplasm; Cytoskeleton; Nucleus;
KW Reference proteome.
FT CHAIN 1..517
FT /note="Gamma-1-syntrophin"
FT /id="PRO_0000184013"
FT DOMAIN 57..140
FT /note="PDZ"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00143"
FT DOMAIN 283..390
FT /note="PH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00145"
FT VAR_SEQ 428..464
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:10747910"
FT /id="VSP_006360"
SQ SEQUENCE 517 AA; 57969 MW; FB0C87AB18CB5D79 CRC64;
MDFRTACEET KTGICLLQDG NQEPFKVRLH LAKDILMIQE QDVICVSGEP FYSGERTVTI
RRQTVGGFGL SIKGGAEHNI PVVVSKISKE QRAELSGLLF IGDAILQING INVRKCRHEE
VVQVLRNAGE EVTLTVSFLK RAPAFLKLPL NEDCACAPSD QSSGTSSPLC DSGLHLNYHP
NNTDTLSCSS WPTSPGLRWE KRWCDLRLIP LLHSRFSQYV PGTDLSRQNA FQVIAVDGVC
TGIIQCLSAE DCVDWLQAIA TNISNLTKHN IKKINRNFPV NQQIVYMGWC EAREQDPLQD
RVYSPTFLAL RGSCLYKFLA PPVTTWDWTR AEKTFSVYEI MCKILKDSDL LDRRKQCFTV
QSESGEDLYF SVELESDLAQ WERAFQTATF LEVERIQCKT YACVLESHLM GLTIDFSTGF
ICFDAATKAV LWRYKFSQLK GSSDDGKSKI KFLFQNPDTK QIEAKELEFS NLFAVLHCIH
SFFAAKVACL DPLFLGNQAT ASTAASSATT SKAKYTT