SNTG1_MOUSE
ID SNTG1_MOUSE Reviewed; 517 AA.
AC Q925E1; Q9D3Z5;
DT 10-OCT-2002, integrated into UniProtKB/Swiss-Prot.
DT 10-OCT-2002, sequence version 2.
DT 25-MAY-2022, entry version 138.
DE RecName: Full=Gamma-1-syntrophin;
DE Short=G1SYN;
DE AltName: Full=Syntrophin-4;
DE Short=SYN4;
GN Name=Sntg1;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC STRAIN=C57BL/6J;
RA Alessi A., Adams M.E., Froehner S.C.;
RT "Cloning and characterization of mouse gamma syntrophins.";
RL Submitted (APR-2001) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC STRAIN=C57BL/6J; TISSUE=Testis;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
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. May participate in regulating the subcellular location of
CC diacylglycerol kinase-zeta to ensure that diacylglycerol is rapidly
CC inactivated following receptor activation (By similarity).
CC {ECO:0000250}.
CC -!- SUBUNIT: Interacts with the dystrophin protein DMD and related proteins
CC DTNA and DTNB. Interacts with DGKZ (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000250}. Nucleus
CC {ECO:0000250}. Note=Mainly cytoplasmic and weakly nuclear.
CC {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q925E1-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q925E1-2; Sequence=VSP_006361, VSP_006362;
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 (By
CC similarity). {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the syntrophin family. {ECO:0000305}.
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DR EMBL; AF367759; AAK53399.1; -; mRNA.
DR EMBL; AK016927; BAB30501.1; -; mRNA.
DR CCDS; CCDS35509.1; -. [Q925E1-1]
DR RefSeq; NP_001277322.1; NM_001290393.1.
DR AlphaFoldDB; Q925E1; -.
DR BioGRID; 214473; 6.
DR STRING; 10090.ENSMUSP00000118101; -.
DR iPTMnet; Q925E1; -.
DR PhosphoSitePlus; Q925E1; -.
DR PaxDb; Q925E1; -.
DR PRIDE; Q925E1; -.
DR ProteomicsDB; 261093; -. [Q925E1-1]
DR ProteomicsDB; 261094; -. [Q925E1-2]
DR DNASU; 71096; -.
DR GeneID; 71096; -.
DR KEGG; mmu:71096; -.
DR UCSC; uc007agg.2; mouse. [Q925E1-2]
DR UCSC; uc011whz.2; mouse. [Q925E1-1]
DR CTD; 54212; -.
DR MGI; MGI:1918346; Sntg1.
DR eggNOG; KOG3549; Eukaryota.
DR InParanoid; Q925E1; -.
DR PhylomeDB; Q925E1; -.
DR BioGRID-ORCS; 71096; 2 hits in 73 CRISPR screens.
DR ChiTaRS; Sntg1; mouse.
DR PRO; PR:Q925E1; -.
DR Proteomes; UP000000589; Unplaced.
DR RNAct; Q925E1; protein.
DR GO; GO:0005737; C:cytoplasm; ISO:MGI.
DR GO; GO:0005856; C:cytoskeleton; ISO:MGI.
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; ISO:MGI.
DR GO; GO:0003779; F:actin binding; IEA:UniProtKB-KW.
DR GO; GO:0008022; F:protein C-terminus binding; ISO:MGI.
DR GO; GO:0005198; F:structural molecule activity; IEA:InterPro.
DR Gene3D; 2.30.29.30; -; 1.
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; 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 SUPFAM; SSF50156; SSF50156; 1.
DR PROSITE; PS50106; PDZ; 1.
DR PROSITE; PS50003; PH_DOMAIN; 1.
PE 2: Evidence at transcript level;
KW Actin-binding; Alternative splicing; Cytoplasm; Cytoskeleton; Nucleus;
KW Reference proteome.
FT CHAIN 1..517
FT /note="Gamma-1-syntrophin"
FT /id="PRO_0000184014"
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 1..275
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_006361"
FT VAR_SEQ 276..283
FT /note="RNFPVNQQ -> MIKHLPSY (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_006362"
SQ SEQUENCE 517 AA; 57982 MW; 20133EFD3ED9EF6D CRC64;
MDFRTTCEET KTGVCLLQDG NQEPFKVRLH LARDLLMLQE QDVLCVSGEP FYSGERTVTI
RRQTVGGFGL SIKGGAEHNI PVVISKISKE QRAELSGLLF IGDAILQING INVRKCRHEE
VVQVLRNAGE EVTLTVSFLK RAPAFLKLPV NEDCACAPSD QSSGTSSPLC DSGLHLNYHP
NNTDTLSCSS WPTSPGLRWE KRWCDLRLIP LLHARFSQYV PGTDLSRQNE SQVVAVDGVC
SGILQCLSAE DCMDWLQAIA SNISNLTKHN IKKINRNFPV NQQIVYMGWC EAREQESLQD
RVYTPVFLAL RGSCLYRFLS PPVTTWDWTR AEKTFSVCEI MCKVLKDSDL LDRRKHCFTM
QSECGEDLYF SVELESDLAQ WERAFQTATF LEVERIQCKT YACVLESHLM GLTIDFSTGF
ICFDAATKAV LWRYKFSQLK GSSDDGKSKI KFLFQNPDTK QIEAKELEFS NLFAVLHCIH
SFFAAKVACL DPLFLGNQAA TTAAVSSAST SKAKHLA
