STRN3_RAT
ID STRN3_RAT Reviewed; 794 AA.
AC P58405;
DT 16-NOV-2001, integrated into UniProtKB/Swiss-Prot.
DT 12-JUN-2007, sequence version 2.
DT 03-AUG-2022, entry version 153.
DE RecName: Full=Striatin-3;
DE AltName: Full=Cell cycle autoantigen SG2NA;
DE AltName: Full=S/G2 antigen;
GN Name=Strn3; Synonyms=Gs2na, Sg2na;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Brown Norway;
RX PubMed=15057822; DOI=10.1038/nature02426;
RA Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J.,
RA Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G.,
RA Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G.,
RA Morgan M., Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G.,
RA Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S.,
RA Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T.,
RA Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T., Smith D.,
RA Lee H.-M., Gustafson E., Cahill P., Kana A., Doucette-Stamm L.,
RA Weinstock K., Fechtel K., Weiss R.B., Dunn D.M., Green E.D.,
RA Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K., Zhu B., Marra M.,
RA Schein J., Bosdet I., Fjell C., Jones S., Krzywinski M., Mathewson C.,
RA Siddiqui A., Wye N., McPherson J., Zhao S., Fraser C.M., Shetty J.,
RA Shatsman S., Geer K., Chen Y., Abramzon S., Nierman W.C., Havlak P.H.,
RA Chen R., Durbin K.J., Egan A., Ren Y., Song X.-Z., Li B., Liu Y., Qin X.,
RA Cawley S., Cooney A.J., D'Souza L.M., Martin K., Wu J.Q.,
RA Gonzalez-Garay M.L., Jackson A.R., Kalafus K.J., McLeod M.P.,
RA Milosavljevic A., Virk D., Volkov A., Wheeler D.A., Zhang Z., Bailey J.A.,
RA Eichler E.E., Tuzun E., Birney E., Mongin E., Ureta-Vidal A., Woodwark C.,
RA Zdobnov E., Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J.,
RA Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D., Schmidt J.,
RA Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M., Abril J.F.,
RA Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O., Poliakov A.,
RA Huebner N., Ganten D., Goesele C., Hummel O., Kreitler T., Lee Y.-A.,
RA Monti J., Schulz H., Zimdahl H., Himmelbauer H., Lehrach H., Jacob H.J.,
RA Bromberg S., Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E.,
RA Lazar J., Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M.,
RA Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E., Webber C.,
RA Brandt P., Nyakatura G., Adetobi M., Chiaromonte F., Elnitski L.,
RA Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K., Miller W.,
RA Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S., Zhang Y.,
RA Lindpaintner K., Andrews T.D., Caccamo M., Clamp M., Clarke L., Curwen V.,
RA Durbin R.M., Eyras E., Searle S.M., Cooper G.M., Batzoglou S., Brudno M.,
RA Sidow A., Stone E.A., Payseur B.A., Bourque G., Lopez-Otin C., Puente X.S.,
RA Chakrabarti K., Chatterji S., Dewey C., Pachter L., Bray N., Yap V.B.,
RA Caspi A., Tesler G., Pevzner P.A., Haussler D., Roskin K.M., Baertsch R.,
RA Clawson H., Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J.,
RA Rosenbloom K.R., Trumbower H., Weirauch M., Cooper D.N., Stenson P.D.,
RA Ma B., Brent M., Arumugam M., Shteynberg D., Copley R.R., Taylor M.S.,
RA Riethman H., Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S.,
RA Mockrin S., Collins F.S.;
RT "Genome sequence of the Brown Norway rat yields insights into mammalian
RT evolution.";
RL Nature 428:493-521(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 1-529 (ISOFORM 2).
RC STRAIN=Sprague-Dawley;
RA Long X., Bigsby R.M., Nephew K.P.;
RT "Rat SG2NA gene partial sequence.";
RL Submitted (JAN-2001) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-149; SER-227; SER-255 AND
RP SER-332, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
CC -!- FUNCTION: Binds calmodulin in a calcium dependent manner. May function
CC as scaffolding or signaling protein (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Interacts with protein phosphatase 2A (PP2A). Interacts with
CC CDC42BPB. {ECO:0000250|UniProtKB:Q13033}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Membrane {ECO:0000250};
CC Peripheral membrane protein {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=P58405-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P58405-2; Sequence=VSP_026164, VSP_026165;
CC -!- SIMILARITY: Belongs to the WD repeat striatin family. {ECO:0000305}.
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DR EMBL; AABR03048613; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AY026526; AAK07683.1; -; mRNA.
DR RefSeq; NP_001025068.1; NM_001029897.3. [P58405-1]
DR AlphaFoldDB; P58405; -.
DR SMR; P58405; -.
DR BioGRID; 250366; 1.
DR CORUM; P58405; -.
DR IntAct; P58405; 1.
DR STRING; 10116.ENSRNOP00000007509; -.
DR iPTMnet; P58405; -.
DR PhosphoSitePlus; P58405; -.
DR jPOST; P58405; -.
DR PaxDb; P58405; -.
DR PRIDE; P58405; -.
DR Ensembl; ENSRNOT00000077578; ENSRNOP00000074395; ENSRNOG00000060335. [P58405-1]
DR GeneID; 114520; -.
DR KEGG; rno:114520; -.
DR UCSC; RGD:621827; rat. [P58405-1]
DR CTD; 29966; -.
DR RGD; 621827; Strn3.
DR eggNOG; KOG0642; Eukaryota.
DR GeneTree; ENSGT00950000183095; -.
DR InParanoid; P58405; -.
DR OMA; TSHRLMR; -.
DR OrthoDB; 334070at2759; -.
DR PhylomeDB; P58405; -.
DR TreeFam; TF313387; -.
DR PRO; PR:P58405; -.
DR Proteomes; UP000002494; Chromosome 6.
DR Bgee; ENSRNOG00000060335; Expressed in quadriceps femoris and 20 other tissues.
DR ExpressionAtlas; P58405; baseline and differential.
DR Genevisible; P58405; RN.
DR GO; GO:0005737; C:cytoplasm; IDA:RGD.
DR GO; GO:0030425; C:dendrite; IDA:RGD.
DR GO; GO:0090443; C:FAR/SIN/STRIPAK complex; ISO:RGD.
DR GO; GO:0005794; C:Golgi apparatus; ISO:RGD.
DR GO; GO:0043025; C:neuronal cell body; IDA:RGD.
DR GO; GO:0005654; C:nucleoplasm; ISO:RGD.
DR GO; GO:0005886; C:plasma membrane; ISO:RGD.
DR GO; GO:0032991; C:protein-containing complex; IDA:RGD.
DR GO; GO:0070016; F:armadillo repeat domain binding; ISO:RGD.
DR GO; GO:0005516; F:calmodulin binding; IBA:GO_Central.
DR GO; GO:0019901; F:protein kinase binding; ISO:RGD.
DR GO; GO:0051721; F:protein phosphatase 2A binding; ISO:RGD.
DR GO; GO:0044877; F:protein-containing complex binding; IDA:RGD.
DR GO; GO:0031267; F:small GTPase binding; ISO:RGD.
DR GO; GO:0033147; P:negative regulation of intracellular estrogen receptor signaling pathway; IMP:RGD.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IMP:RGD.
DR GO; GO:0032355; P:response to estradiol; IDA:RGD.
DR Gene3D; 2.130.10.10; -; 3.
DR InterPro; IPR020472; G-protein_beta_WD-40_rep.
DR InterPro; IPR013258; Striatin_N.
DR InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR InterPro; IPR001680; WD40_repeat.
DR InterPro; IPR019775; WD40_repeat_CS.
DR InterPro; IPR036322; WD40_repeat_dom_sf.
DR Pfam; PF08232; Striatin; 1.
DR Pfam; PF00400; WD40; 5.
DR PRINTS; PR00320; GPROTEINBRPT.
DR SMART; SM00320; WD40; 7.
DR SUPFAM; SSF50978; SSF50978; 1.
DR PROSITE; PS00678; WD_REPEATS_1; 2.
DR PROSITE; PS50082; WD_REPEATS_2; 4.
DR PROSITE; PS50294; WD_REPEATS_REGION; 1.
PE 1: Evidence at protein level;
KW Acetylation; Alternative splicing; Calmodulin-binding; Coiled coil;
KW Cytoplasm; Membrane; Phosphoprotein; Reference proteome; Repeat; WD repeat.
FT CHAIN 1..794
FT /note="Striatin-3"
FT /id="PRO_0000051238"
FT REPEAT 475..514
FT /note="WD 1"
FT REPEAT 528..567
FT /note="WD 2"
FT REPEAT 581..620
FT /note="WD 3"
FT REPEAT 676..715
FT /note="WD 4"
FT REPEAT 718..757
FT /note="WD 5"
FT REPEAT 764..794
FT /note="WD 6"
FT REGION 1..59
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 70..78
FT /note="Caveolin-binding"
FT /evidence="ECO:0000255"
FT REGION 164..181
FT /note="Calmodulin-binding"
FT /evidence="ECO:0000255"
FT REGION 309..339
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 76..135
FT /evidence="ECO:0000255"
FT COMPBIAS 321..335
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0000250|UniProtKB:Q13033"
FT MOD_RES 149
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 200
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9ERG2"
FT MOD_RES 212
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q13033"
FT MOD_RES 227
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 255
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 332
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT VAR_SEQ 9
FT /note="G -> GGQGMAVPPRPQQGRGG (in isoform 2)"
FT /evidence="ECO:0000303|Ref.2"
FT /id="VSP_026164"
FT VAR_SEQ 327..410
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|Ref.2"
FT /id="VSP_026165"
SQ SEQUENCE 794 AA; 87111 MW; 78B43BE6B92EF3C8 CRC64;
MDELAGGGGG QGMAVPPRPQ QGPGGNLSLP PGANGAPGGG GPPAAETAGP PAGPELSRPQ
QYTIPGILHY IQHEWARFEM ERAHWEVERA ELQARIAFLQ GERKGQENLK KDLVRRIKML
EYALKQERAK YHKLKYGTEL NQGDLKMPTF ESEETKDAEA PPAQNSQLTW KQGRQLLRQY
LQEVGYTDTI LDVRSQRVRS LLGLSNSEPN GSIEAKNLEQ ILNGGESPKQ KGQEIKRPSG
DVLETFNFLE NADDSDEEEN DMIEGIPEGK DKLRIHKHKI GNEGLAADLT DDPDTEEALK
EFDFLVTAED GEGAGEARSS GDGTEWDKDD LSPTAEVWDV DQGLMSKLKE QYKKERKGKR
GAKRVNRTNL CDMITDLGDD ELPHIPSGII NQSRSASTRM TDHEGSRAEE AEPITFPSGG
GKSFIMGSDD VLLSVLGLGD LADLTVTNDA DYSYDLPANK DALRKTWNPK YTLRSHFDGV
RALAFHPVEP VLVTASEDHT LKLWNLQKTV PAKKSASLDV EPIYTFRAHI GPVLSLAISS
NGEQCFSGGI DATIQWWNMP SPNVDPYDTY ESHVLAGTLV AHTDAVWGLA YSGIKNQLLS
CSADGTIRLW NPQEKLPCIC TYNGDKEHGI PTSVDFIGCD PAHMVTSFNT GSAIIYDLET
SQSLVMLSSQ VDSGLQSSNH INRVVSHPTL PVTITAHEDR HIKFFDNKTG KMIHSMVAHL
DAVTSLAVDP NGIYLMSGSH DCSIRLWNLD SKTCVQEITA HRKKLDESIY DVAFHPSKAY
IASAGADALA KVFV
