SNTG2_HUMAN
ID SNTG2_HUMAN Reviewed; 539 AA.
AC Q9NY99; Q05AH5;
DT 10-OCT-2002, integrated into UniProtKB/Swiss-Prot.
DT 18-MAY-2010, sequence version 2.
DT 03-AUG-2022, entry version 157.
DE RecName: Full=Gamma-2-syntrophin;
DE Short=G2SYN;
DE AltName: Full=Syntrophin-5;
DE Short=SYN5;
GN Name=SNTG2;
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] (ISOFORM 1), TISSUE SPECIFICITY, AND INTERACTION
RP 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 GENOMIC DNA].
RX PubMed=15815621; DOI=10.1038/nature03466;
RA Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P.,
RA Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C.,
RA Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L.,
RA Du H., Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A.,
RA Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J.,
RA Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M.,
RA Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T.,
RA Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S.,
RA Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K.,
RA McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C.,
RA Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S.,
RA Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C.,
RA Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M.,
RA Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C.,
RA Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J.,
RA Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E.,
RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X.,
RA Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M.,
RA Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C.,
RA Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S.,
RA Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H.,
RA Wilson R.K.;
RT "Generation and annotation of the DNA sequences of human chromosomes 2 and
RT 4.";
RL Nature 434:724-731(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
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).
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). {ECO:0000250}.
CC -!- SUBUNIT: Interacts with the dystrophin protein DMD and related proteins
CC DTNA and DTNB. {ECO:0000269|PubMed:10747910}.
CC -!- INTERACTION:
CC Q9NY99-2; O60941-5: DTNB; NbExp=3; IntAct=EBI-18173613, EBI-11984733;
CC Q9NY99-2; Q8TD10: MIPOL1; NbExp=3; IntAct=EBI-18173613, EBI-2548751;
CC Q9NY99-2; Q8N3R9: PALS1; NbExp=3; IntAct=EBI-18173613, EBI-2513978;
CC -!- SUBCELLULAR LOCATION: Cell membrane, sarcolemma; Peripheral membrane
CC protein; Cytoplasmic side. Cytoplasm, cytoskeleton. Note=In skeletal
CC muscle, it localizes at the cytoplasmic side of the sarcolemmal
CC membrane.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9NY99-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9NY99-2; Sequence=VSP_039175;
CC -!- TISSUE SPECIFICITY: Widely expressed. Strong expression in brain and
CC testis. In CNS, it is expressed in the perikaryon and proximal portion
CC of the neuronal processes. Strong expression in the hippocampus,
CC neuron-rich dendate granule cells, and pyramidal cell layers. Highly
CC expressed in neurons of the cerebral cortex. Also expressed in the
CC cerebellar cortex, deep cerebellar nuclei, thalamus, and basal ganglia.
CC {ECO:0000269|PubMed:10747910}.
CC -!- DOMAIN: The association with dystrophin or related proteins probably
CC leaves the PDZ domain available to recruit proteins to the membrane.
CC {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the syntrophin family. {ECO:0000305}.
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DR EMBL; AJ003029; CAB92969.1; -; mRNA.
DR EMBL; AC108462; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC114808; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC116614; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC140476; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC144444; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC144527; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC225604; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC125251; AAI25252.1; -; mRNA.
DR CCDS; CCDS46220.1; -. [Q9NY99-1]
DR RefSeq; NP_061841.2; NM_018968.3. [Q9NY99-1]
DR AlphaFoldDB; Q9NY99; -.
DR SMR; Q9NY99; -.
DR BioGRID; 119929; 25.
DR IntAct; Q9NY99; 13.
DR MINT; Q9NY99; -.
DR STRING; 9606.ENSP00000311837; -.
DR GlyGen; Q9NY99; 1 site, 2 O-linked glycans (1 site).
DR iPTMnet; Q9NY99; -.
DR PhosphoSitePlus; Q9NY99; -.
DR BioMuta; SNTG2; -.
DR DMDM; 296452909; -.
DR MassIVE; Q9NY99; -.
DR PaxDb; Q9NY99; -.
DR PeptideAtlas; Q9NY99; -.
DR PRIDE; Q9NY99; -.
DR ProteomicsDB; 83200; -. [Q9NY99-1]
DR ProteomicsDB; 83201; -. [Q9NY99-2]
DR Antibodypedia; 26199; 80 antibodies from 21 providers.
DR DNASU; 54221; -.
DR Ensembl; ENST00000308624.10; ENSP00000311837.5; ENSG00000172554.12. [Q9NY99-1]
DR Ensembl; ENST00000407292.1; ENSP00000385020.1; ENSG00000172554.12. [Q9NY99-2]
DR GeneID; 54221; -.
DR KEGG; hsa:54221; -.
DR MANE-Select; ENST00000308624.10; ENSP00000311837.5; NM_018968.4; NP_061841.2.
DR UCSC; uc002qwq.4; human. [Q9NY99-1]
DR CTD; 54221; -.
DR DisGeNET; 54221; -.
DR GeneCards; SNTG2; -.
DR HGNC; HGNC:13741; SNTG2.
DR HPA; ENSG00000172554; Low tissue specificity.
DR MIM; 608715; gene.
DR neXtProt; NX_Q9NY99; -.
DR OpenTargets; ENSG00000172554; -.
DR PharmGKB; PA37807; -.
DR VEuPathDB; HostDB:ENSG00000172554; -.
DR eggNOG; KOG3549; Eukaryota.
DR GeneTree; ENSGT00950000182863; -.
DR HOGENOM; CLU_039445_0_0_1; -.
DR InParanoid; Q9NY99; -.
DR OMA; NKYCSSD; -.
DR OrthoDB; 1103724at2759; -.
DR PhylomeDB; Q9NY99; -.
DR TreeFam; TF317932; -.
DR PathwayCommons; Q9NY99; -.
DR SignaLink; Q9NY99; -.
DR SIGNOR; Q9NY99; -.
DR BioGRID-ORCS; 54221; 13 hits in 1065 CRISPR screens.
DR ChiTaRS; SNTG2; human.
DR GenomeRNAi; 54221; -.
DR Pharos; Q9NY99; Tbio.
DR PRO; PR:Q9NY99; -.
DR Proteomes; UP000005640; Chromosome 2.
DR RNAct; Q9NY99; protein.
DR Bgee; ENSG00000172554; Expressed in sural nerve and 96 other tissues.
DR ExpressionAtlas; Q9NY99; baseline and differential.
DR Genevisible; Q9NY99; HS.
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:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005886; C:plasma membrane; IDA:HPA.
DR GO; GO:0042383; C:sarcolemma; IEA:UniProtKB-SubCell.
DR GO; GO:0016013; C:syntrophin complex; TAS:ProtInc.
DR GO; GO:0003779; F:actin binding; IEA:UniProtKB-KW.
DR GO; GO:0097109; F:neuroligin family protein binding; IPI:BHF-UCL.
DR GO; GO:0030165; F:PDZ domain binding; IPI:UniProtKB.
DR GO; GO:0005198; F:structural molecule activity; IEA:InterPro.
DR GO; GO:0007417; P:central nervous system development; TAS:ProtInc.
DR Gene3D; 2.30.42.10; -; 1.
DR InterPro; IPR001478; PDZ.
DR InterPro; IPR036034; PDZ_sf.
DR InterPro; IPR015482; Syntrophin.
DR PANTHER; PTHR10554; PTHR10554; 1.
DR Pfam; PF00595; PDZ; 1.
DR SMART; SM00228; PDZ; 1.
DR SUPFAM; SSF50156; SSF50156; 1.
DR PROSITE; PS50106; PDZ; 1.
PE 1: Evidence at protein level;
KW Actin-binding; Alternative splicing; Cell membrane; Cytoplasm;
KW Cytoskeleton; Membrane; Reference proteome.
FT CHAIN 1..539
FT /note="Gamma-2-syntrophin"
FT /id="PRO_0000184015"
FT DOMAIN 73..156
FT /note="PDZ"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00143"
FT DOMAIN 296..421
FT /note="PH"
FT REGION 168..209
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 170..204
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VAR_SEQ 71..197
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_039175"
FT VARIANT 168
FT /note="S -> Y (in dbSNP:rs28505970)"
FT /id="VAR_034501"
FT VARIANT 200
FT /note="S -> L (in dbSNP:rs6751090)"
FT /id="VAR_034502"
FT VARIANT 391
FT /note="I -> V (in dbSNP:rs13023962)"
FT /id="VAR_034503"
FT CONFLICT 495
FT /note="T -> M (in Ref. 1; CAB92969 and 3; AAI25252)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 539 AA; 60217 MW; 0D3B1E24CC05D365 CRC64;
MGTEGPPPPA ASRGRQGCLL VPARTKTTIA LLYDEESENA YDIRLKLTKE VLTIQKQDVV
CVGGSHQGRN RRTVTLRRQP VGGLGLSIKG GSEHNVPVVI SKIFEDQAAD QTGMLFVGDA
VLQVNGIHVE NATHEEVVHL LRNAGDEVTI TVEYLREAPA FLKLPLGSPG PSSDHSSGAS
SPLFDSGLHL NGNSSTTAPS SPSSPIAKDP RYEKRWLDTL SVPLSMARIS RYKAGTEKLR
WNAFEVLALD GVSSGILRFY TAQDGTDWLR AVSANIRELT LQNMKMANKC CSPSDQVVHM
GWVNEKLQGA DSSQTFRPKF LALKGPSFYV FSTPPVSTFD WVRAERTYHL CEVLFKVHKF
WLTEDCWLQA NLYLGLQDFD FEDQRPYCFS IVAGHGKSHV FNVELGSELA MWEKSFQRAT
FMEVQRTGSR TYMCSWQGEM LCFTVDFALG FTCFESKTKN VLWRFKFSQL KGSSDDGKTR
VKLLFQNLDT KQIETKELEF QDLRAVLHCI HSFIAAKVAS VDPGFMDSQS LARKYMYSS
