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   27-MAR-2024, entry version 180.
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   PDB; 7PC7; X-ray; 2.10 A; A/B=54-143.
DR   PDB; 7PC8; X-ray; 2.50 A; A/B=54-143.
DR   PDB; 7QQN; X-ray; 2.45 A; A/C=54-143.
DR   PDBsum; 7PC7; -.
DR   PDBsum; 7PC8; -.
DR   PDBsum; 7QQN; -.
DR   AlphaFoldDB; Q9NSN8; -.
DR   SMR; Q9NSN8; -.
DR   BioGRID; 119928; 31.
DR   ComplexPortal; CPX-2453; Dystrophin glycoprotein complex, CNS variant.
DR   CORUM; Q9NSN8; -.
DR   IntAct; Q9NSN8; 2.
DR   STRING; 9606.ENSP00000493900; -.
DR   iPTMnet; Q9NSN8; -.
DR   PhosphoSitePlus; Q9NSN8; -.
DR   BioMuta; SNTG1; -.
DR   DMDM; 23822220; -.
DR   MassIVE; Q9NSN8; -.
DR   PaxDb; 9606-ENSP00000429842; -.
DR   PeptideAtlas; Q9NSN8; -.
DR   ProteomicsDB; 82570; -. [Q9NSN8-1]
DR   ProteomicsDB; 82571; -. [Q9NSN8-2]
DR   Antibodypedia; 24371; 124 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   AGR; HGNC:13740; -.
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; DEYATEW; -.
DR   OrthoDB; 2906429at2759; -.
DR   PhylomeDB; Q9NSN8; -.
DR   TreeFam; TF317932; -.
DR   PathwayCommons; Q9NSN8; -.
DR   SignaLink; Q9NSN8; -.
DR   SIGNOR; Q9NSN8; -.
DR   BioGRID-ORCS; 54212; 7 hits in 1151 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 107 other cell types or tissues.
DR   ExpressionAtlas; Q9NSN8; baseline and differential.
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:0005198; F:structural molecule activity; IEA:InterPro.
DR   GO; GO:0007154; P:cell communication; TAS:ProtInc.
DR   CDD; cd00992; PDZ_signaling; 1.
DR   CDD; cd00821; PH; 1.
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   PANTHER; PTHR10554:SF2; GAMMA-1-SYNTROPHIN; 1.
DR   PANTHER; PTHR10554; SYNTROPHIN; 1.
DR   Pfam; PF00595; PDZ; 1.
DR   SMART; SM00228; PDZ; 1.
DR   SMART; SM00233; PH; 2.
DR   SUPFAM; SSF50156; PDZ domain-like; 1.
DR   SUPFAM; SSF50729; PH domain-like; 2.
DR   PROSITE; PS50106; PDZ; 1.
DR   PROSITE; PS50003; PH_DOMAIN; 1.
DR   Genevisible; Q9NSN8; HS.
PE   1: Evidence at protein level;
KW   3D-structure; Actin-binding; Alternative splicing; Cytoplasm; Cytoskeleton;
KW   Nucleus; 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"
FT   STRAND          56..61
FT                   /evidence="ECO:0007829|PDB:7PC7"
FT   STRAND          64..66
FT                   /evidence="ECO:0007829|PDB:7PC7"
FT   STRAND          69..73
FT                   /evidence="ECO:0007829|PDB:7PC7"
FT   HELIX           76..78
FT                   /evidence="ECO:0007829|PDB:7PC7"
FT   STRAND          83..87
FT                   /evidence="ECO:0007829|PDB:7PC7"
FT   HELIX           89..94
FT                   /evidence="ECO:0007829|PDB:7PC7"
FT   TURN            95..98
FT                   /evidence="ECO:0007829|PDB:7QQN"
FT   STRAND          103..108
FT                   /evidence="ECO:0007829|PDB:7PC7"
FT   HELIX           118..126
FT                   /evidence="ECO:0007829|PDB:7PC7"
FT   STRAND          130..138
FT                   /evidence="ECO:0007829|PDB:7PC7"
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
//