ID STRN3_HUMAN Reviewed; 797 AA.
AC Q13033; A2RTX7; A6NHZ7; Q9NRA5;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 10-FEB-2009, sequence version 3.
DT 27-MAR-2024, entry version 221.
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 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 ALPHA), AND VARIANT SER-471.
RC TISSUE=Liver;
RX PubMed=7864889; DOI=10.1006/bbrc.1995.1288;
RA Muro Y., Chan E.K., Landberg G., Tan E.M.;
RT "A cell-cycle nuclear autoantigen containing WD-40 motifs expressed mainly
RT in S and G2 phase cells.";
RL Biochem. Biophys. Res. Commun. 207:1029-1037(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM ALPHA).
RC TISSUE=Trachea;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=12508121; DOI=10.1038/nature01348;
RA Heilig R., Eckenberg R., Petit J.-L., Fonknechten N., Da Silva C.,
RA Cattolico L., Levy M., Barbe V., De Berardinis V., Ureta-Vidal A.,
RA Pelletier E., Vico V., Anthouard V., Rowen L., Madan A., Qin S., Sun H.,
RA Du H., Pepin K., Artiguenave F., Robert C., Cruaud C., Bruels T.,
RA Jaillon O., Friedlander L., Samson G., Brottier P., Cure S., Segurens B.,
RA Aniere F., Samain S., Crespeau H., Abbasi N., Aiach N., Boscus D.,
RA Dickhoff R., Dors M., Dubois I., Friedman C., Gouyvenoux M., James R.,
RA Madan A., Mairey-Estrada B., Mangenot S., Martins N., Menard M., Oztas S.,
RA Ratcliffe A., Shaffer T., Trask B., Vacherie B., Bellemere C., Belser C.,
RA Besnard-Gonnet M., Bartol-Mavel D., Boutard M., Briez-Silla S.,
RA Combette S., Dufosse-Laurent V., Ferron C., Lechaplais C., Louesse C.,
RA Muselet D., Magdelenat G., Pateau E., Petit E., Sirvain-Trukniewicz P.,
RA Trybou A., Vega-Czarny N., Bataille E., Bluet E., Bordelais I., Dubois M.,
RA Dumont C., Guerin T., Haffray S., Hammadi R., Muanga J., Pellouin V.,
RA Robert D., Wunderle E., Gauguet G., Roy A., Sainte-Marthe L., Verdier J.,
RA Verdier-Discala C., Hillier L.W., Fulton L., McPherson J., Matsuda F.,
RA Wilson R., Scarpelli C., Gyapay G., Wincker P., Saurin W., Quetier F.,
RA Waterston R., Hood L., Weissenbach J.;
RT "The DNA sequence and analysis of human chromosome 14.";
RL Nature 421:601-607(2003).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM ALPHA).
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 [5]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 120-797 (ISOFORM BETA), AND VARIANT SER-471.
RX PubMed=10748158; DOI=10.1074/jbc.m909782199;
RA Castets F., Rakitina T., Gaillard S., Moqrich A., Mattei M.-G.,
RA Monneron A.;
RT "Zinedin, SG2NA, and striatin are calmodulin-binding, WD repeat proteins
RT principally expressed in the brain.";
RL J. Biol. Chem. 275:19970-19977(2000).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-229, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=16964243; DOI=10.1038/nbt1240;
RA Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.;
RT "A probability-based approach for high-throughput protein phosphorylation
RT analysis and site localization.";
RL Nat. Biotechnol. 24:1285-1292(2006).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-257, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [8]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-229 AND SER-257, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-229, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [11]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-229, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT "System-wide temporal characterization of the proteome and phosphoproteome
RT of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [13]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22223895; DOI=10.1074/mcp.m111.015131;
RA Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T.,
RA Giglione C.;
RT "Comparative large-scale characterisation of plant vs. mammal proteins
RT reveals similar and idiosyncratic N-alpha acetylation features.";
RL Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
RN [14]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN [15]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-214 AND SER-229, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [16]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-257, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [17]
RP INTERACTION WITH STRP1; CDC42BPB AND SIKE1.
RX PubMed=25743393; DOI=10.1038/ncomms7449;
RA Lant B., Yu B., Goudreault M., Holmyard D., Knight J.D., Xu P., Zhao L.,
RA Chin K., Wallace E., Zhen M., Gingras A.C., Derry W.B.;
RT "CCM-3/STRIPAK promotes seamless tube extension through endocytic
RT recycling.";
RL Nat. Commun. 6:6449-6449(2015).
CC -!- FUNCTION: Binds calmodulin in a calcium dependent manner. May function
CC as scaffolding or signaling protein.
CC -!- SUBUNIT: Interacts with protein phosphatase 2A (PP2A). Interacts with
CC CDC42BPB (PubMed:25743393). {ECO:0000269|PubMed:25743393, ECO:0000305}.
CC -!- INTERACTION:
CC Q13033; Q9P2B4: CTTNBP2NL; NbExp=8; IntAct=EBI-1053857, EBI-1774273;
CC Q13033; Q9Y3A3-1: MOB4; NbExp=2; IntAct=EBI-1053857, EBI-713946;
CC Q13033; O43815: STRN; NbExp=9; IntAct=EBI-1053857, EBI-1046642;
CC Q13033; Q9Y228: TRAF3IP3; NbExp=2; IntAct=EBI-1053857, EBI-765817;
CC Q13033-2; Q9H0R8: GABARAPL1; NbExp=3; IntAct=EBI-1053876, EBI-746969;
CC Q13033-2; Q5SUL5: HLA-A; NbExp=3; IntAct=EBI-1053876, EBI-8561769;
CC Q13033-2; Q92993: KAT5; NbExp=3; IntAct=EBI-1053876, EBI-399080;
CC Q13033-2; Q8TAP4-4: LMO3; NbExp=3; IntAct=EBI-1053876, EBI-11742507;
CC Q13033-2; Q9Y3A3: MOB4; NbExp=4; IntAct=EBI-1053876, EBI-713935;
CC Q13033-2; P62937-2: PPIA; NbExp=3; IntAct=EBI-1053876, EBI-25884072;
CC Q13033-2; P30153: PPP2R1A; NbExp=9; IntAct=EBI-1053876, EBI-302388;
CC Q13033-2; Q15047-2: SETDB1; NbExp=3; IntAct=EBI-1053876, EBI-9090795;
CC Q13033-2; Q9BRV8: SIKE1; NbExp=4; IntAct=EBI-1053876, EBI-1773646;
CC Q13033-2; Q8N8B7-2: TCEANC; NbExp=3; IntAct=EBI-1053876, EBI-11955057;
CC Q13033-2; P61981: YWHAG; NbExp=3; IntAct=EBI-1053876, EBI-359832;
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 Comment=Additional isoforms seem to exist.;
CC Name=Beta;
CC IsoId=Q13033-1; Sequence=Displayed;
CC Name=Alpha;
CC IsoId=Q13033-2; Sequence=VSP_006786;
CC -!- SIMILARITY: Belongs to the WD repeat striatin family. {ECO:0000305}.
CC -!- CAUTION: Was originally thought to be nuclear.
CC {ECO:0000305|PubMed:7864889}.
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DR EMBL; U17989; AAB81551.1; -; mRNA.
DR EMBL; AK314041; BAG36750.1; -; mRNA.
DR EMBL; AL049830; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC132673; AAI32674.1; -; mRNA.
DR EMBL; AF243424; AAF81201.1; -; mRNA.
DR CCDS; CCDS41938.1; -. [Q13033-1]
DR CCDS; CCDS9641.1; -. [Q13033-2]
DR PIR; JC2522; JC2522.
DR RefSeq; NP_001077362.1; NM_001083893.1. [Q13033-1]
DR RefSeq; NP_055389.3; NM_014574.3. [Q13033-2]
DR PDB; 4N6J; X-ray; 2.00 A; A/B=86-131.
DR PDB; 6AKL; X-ray; 1.75 A; C=165-190.
DR PDB; 6IUR; X-ray; 3.33 A; C/D/G/H=86-131.
DR PDB; 7K36; EM; 3.30 A; B/D/E/F/G=1-797.
DR PDBsum; 4N6J; -.
DR PDBsum; 6AKL; -.
DR PDBsum; 6IUR; -.
DR PDBsum; 7K36; -.
DR AlphaFoldDB; Q13033; -.
DR EMDB; EMD-22650; -.
DR SMR; Q13033; -.
DR BioGRID; 118999; 152.
DR CORUM; Q13033; -.
DR IntAct; Q13033; 94.
DR MINT; Q13033; -.
DR STRING; 9606.ENSP00000350071; -.
DR GlyGen; Q13033; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q13033; -.
DR PhosphoSitePlus; Q13033; -.
DR BioMuta; STRN3; -.
DR DMDM; 223634717; -.
DR EPD; Q13033; -.
DR jPOST; Q13033; -.
DR MassIVE; Q13033; -.
DR MaxQB; Q13033; -.
DR PaxDb; 9606-ENSP00000350071; -.
DR PeptideAtlas; Q13033; -.
DR ProteomicsDB; 59114; -. [Q13033-1]
DR ProteomicsDB; 59115; -. [Q13033-2]
DR Pumba; Q13033; -.
DR Antibodypedia; 176; 147 antibodies from 23 providers.
DR DNASU; 29966; -.
DR Ensembl; ENST00000355683.9; ENSP00000347909.5; ENSG00000196792.12. [Q13033-2]
DR Ensembl; ENST00000357479.10; ENSP00000350071.5; ENSG00000196792.12. [Q13033-1]
DR GeneID; 29966; -.
DR KEGG; hsa:29966; -.
DR MANE-Select; ENST00000357479.10; ENSP00000350071.5; NM_001083893.2; NP_001077362.1.
DR UCSC; uc001wqu.3; human. [Q13033-1]
DR AGR; HGNC:15720; -.
DR CTD; 29966; -.
DR DisGeNET; 29966; -.
DR GeneCards; STRN3; -.
DR HGNC; HGNC:15720; STRN3.
DR HPA; ENSG00000196792; Low tissue specificity.
DR MIM; 614766; gene.
DR neXtProt; NX_Q13033; -.
DR OpenTargets; ENSG00000196792; -.
DR PharmGKB; PA38394; -.
DR VEuPathDB; HostDB:ENSG00000196792; -.
DR eggNOG; KOG0642; Eukaryota.
DR GeneTree; ENSGT00950000183095; -.
DR HOGENOM; CLU_009108_2_0_1; -.
DR InParanoid; Q13033; -.
DR OMA; SKCSQEV; -.
DR OrthoDB; 5481146at2759; -.
DR PhylomeDB; Q13033; -.
DR TreeFam; TF313387; -.
DR PathwayCommons; Q13033; -.
DR SignaLink; Q13033; -.
DR BioGRID-ORCS; 29966; 17 hits in 1156 CRISPR screens.
DR ChiTaRS; STRN3; human.
DR GeneWiki; STRN3; -.
DR GenomeRNAi; 29966; -.
DR Pharos; Q13033; Tbio.
DR PRO; PR:Q13033; -.
DR Proteomes; UP000005640; Chromosome 14.
DR RNAct; Q13033; Protein.
DR Bgee; ENSG00000196792; Expressed in calcaneal tendon and 209 other cell types or tissues.
DR ExpressionAtlas; Q13033; baseline and differential.
DR Genevisible; Q13033; HS.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0030425; C:dendrite; ISS:UniProtKB.
DR GO; GO:0090443; C:FAR/SIN/STRIPAK complex; IDA:UniProtKB.
DR GO; GO:0005794; C:Golgi apparatus; IDA:UniProtKB.
DR GO; GO:0043025; C:neuronal cell body; ISS:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; IDA:UniProtKB.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR GO; GO:0032991; C:protein-containing complex; ISS:UniProtKB.
DR GO; GO:0070016; F:armadillo repeat domain binding; IPI:UniProtKB.
DR GO; GO:0005516; F:calmodulin binding; IBA:GO_Central.
DR GO; GO:0051721; F:protein phosphatase 2A binding; IDA:UniProtKB.
DR GO; GO:0044877; F:protein-containing complex binding; IDA:UniProtKB.
DR GO; GO:0031267; F:small GTPase binding; IPI:UniProtKB.
DR GO; GO:0045892; P:negative regulation of DNA-templated transcription; IDA:UniProtKB.
DR GO; GO:0033147; P:negative regulation of intracellular estrogen receptor signaling pathway; ISS:UniProtKB.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IDA:UniProtKB.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IDA:UniProtKB.
DR GO; GO:0032355; P:response to estradiol; ISS:UniProtKB.
DR CDD; cd00200; WD40; 1.
DR Gene3D; 1.20.5.300; -; 1.
DR Gene3D; 2.130.10.10; YVTN repeat-like/Quinoprotein amine dehydrogenase; 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; IPR019775; WD40_repeat_CS.
DR InterPro; IPR036322; WD40_repeat_dom_sf.
DR InterPro; IPR001680; WD40_rpt.
DR PANTHER; PTHR15653; STRIATIN; 1.
DR PANTHER; PTHR15653:SF3; STRIATIN-3; 1.
DR Pfam; PF08232; Striatin; 1.
DR Pfam; PF00400; WD40; 5.
DR PRINTS; PR00320; GPROTEINBRPT.
DR SMART; SM00320; WD40; 7.
DR SUPFAM; SSF50978; WD40 repeat-like; 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 3D-structure; Acetylation; Alternative splicing; Calmodulin-binding;
KW Coiled coil; Cytoplasm; Membrane; Phosphoprotein; Reference proteome;
KW Repeat; WD repeat.
FT CHAIN 1..797
FT /note="Striatin-3"
FT /id="PRO_0000051236"
FT REPEAT 478..517
FT /note="WD 1"
FT REPEAT 531..570
FT /note="WD 2"
FT REPEAT 584..623
FT /note="WD 3"
FT REPEAT 679..718
FT /note="WD 4"
FT REPEAT 721..760
FT /note="WD 5"
FT REPEAT 767..796
FT /note="WD 6"
FT REGION 1..60
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 71..79
FT /note="Caveolin-binding"
FT /evidence="ECO:0000255"
FT REGION 166..183
FT /note="Calmodulin-binding"
FT /evidence="ECO:0000255"
FT REGION 224..278
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 313..338
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 77..136
FT /evidence="ECO:0000255"
FT COMPBIAS 252..267
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 324..338
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0007744|PubMed:22223895,
FT ECO:0007744|PubMed:22814378"
FT MOD_RES 150
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P58405"
FT MOD_RES 202
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9ERG2"
FT MOD_RES 214
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 229
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:16964243,
FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163"
FT MOD_RES 257
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:24275569"
FT MOD_RES 335
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9ERG2"
FT VAR_SEQ 330..413
FT /note="Missing (in isoform Alpha)"
FT /evidence="ECO:0000303|PubMed:14702039,
FT ECO:0000303|PubMed:15489334, ECO:0000303|PubMed:7864889"
FT /id="VSP_006786"
FT VARIANT 471
FT /note="N -> S (in dbSNP:rs2273171)"
FT /evidence="ECO:0000269|PubMed:10748158,
FT ECO:0000269|PubMed:7864889"
FT /id="VAR_054337"
FT CONFLICT 63
FT /note="Y -> N (in Ref. 1; AAB81551)"
FT /evidence="ECO:0000305"
FT HELIX 86..129
FT /evidence="ECO:0007829|PDB:4N6J"
FT HELIX 175..185
FT /evidence="ECO:0007829|PDB:6AKL"
FT STRAND 471..476
FT /evidence="ECO:0007829|PDB:7K36"
FT STRAND 485..488
FT /evidence="ECO:0007829|PDB:7K36"
FT STRAND 490..498
FT /evidence="ECO:0007829|PDB:7K36"
FT STRAND 500..502
FT /evidence="ECO:0007829|PDB:7K36"
FT STRAND 504..508
FT /evidence="ECO:0007829|PDB:7K36"
FT STRAND 526..528
FT /evidence="ECO:0007829|PDB:7K36"
FT STRAND 538..541
FT /evidence="ECO:0007829|PDB:7K36"
FT STRAND 545..551
FT /evidence="ECO:0007829|PDB:7K36"
FT STRAND 555..561
FT /evidence="ECO:0007829|PDB:7K36"
FT STRAND 569..571
FT /evidence="ECO:0007829|PDB:7K36"
FT HELIX 575..577
FT /evidence="ECO:0007829|PDB:7K36"
FT STRAND 578..583
FT /evidence="ECO:0007829|PDB:7K36"
FT STRAND 589..594
FT /evidence="ECO:0007829|PDB:7K36"
FT STRAND 601..605
FT /evidence="ECO:0007829|PDB:7K36"
FT STRAND 610..613
FT /evidence="ECO:0007829|PDB:7K36"
FT STRAND 623..625
FT /evidence="ECO:0007829|PDB:7K36"
FT STRAND 637..639
FT /evidence="ECO:0007829|PDB:7K36"
FT STRAND 647..650
FT /evidence="ECO:0007829|PDB:7K36"
FT STRAND 652..654
FT /evidence="ECO:0007829|PDB:7K36"
FT STRAND 656..659
FT /evidence="ECO:0007829|PDB:7K36"
FT STRAND 661..663
FT /evidence="ECO:0007829|PDB:7K36"
FT STRAND 668..670
FT /evidence="ECO:0007829|PDB:7K36"
FT STRAND 684..689
FT /evidence="ECO:0007829|PDB:7K36"
FT STRAND 691..700
FT /evidence="ECO:0007829|PDB:7K36"
FT STRAND 703..709
FT /evidence="ECO:0007829|PDB:7K36"
FT TURN 710..712
FT /evidence="ECO:0007829|PDB:7K36"
FT STRAND 717..720
FT /evidence="ECO:0007829|PDB:7K36"
FT STRAND 726..731
FT /evidence="ECO:0007829|PDB:7K36"
FT STRAND 735..742
FT /evidence="ECO:0007829|PDB:7K36"
FT TURN 743..745
FT /evidence="ECO:0007829|PDB:7K36"
FT STRAND 747..753
FT /evidence="ECO:0007829|PDB:7K36"
FT STRAND 758..761
FT /evidence="ECO:0007829|PDB:7K36"
FT STRAND 774..777
FT /evidence="ECO:0007829|PDB:7K36"
FT STRAND 779..781
FT /evidence="ECO:0007829|PDB:7K36"
FT STRAND 784..787
FT /evidence="ECO:0007829|PDB:7K36"
FT STRAND 793..797
FT /evidence="ECO:0007829|PDB:7K36"
SQ SEQUENCE 797 AA; 87209 MW; 2179BD257186DFB0 CRC64;
MDELAGGGGG GPGMAAPPRQ QQGPGGNLGL SPGGNGAAGG GGPPASEGAG PAAGPELSRP
QQYTIPGILH YIQHEWARFE MERAHWEVER AELQARIAFL QGERKGQENL KKDLVRRIKM
LEYALKQERA KYHKLKYGTE LNQGDLKMPT FESEETKDTE APTAPQNSQL TWKQGRQLLR
QYLQEVGYTD TILDVRSQRV RSLLGLSNSE PNGSVETKNL EQILNGGESP KQKGQEIKRS
SGDVLETFNF LENADDSDED EENDMIEGIP EGKDKHRMNK HKIGNEGLAA DLTDDPDTEE
ALKEFDFLVT AEDGEGAGEA RSSGDGTEWD KDDLSPTAEV WDVDQGLISK LKEQYKKERK
GKKGVKRANR TKLYDMIADL GDDELPHIPS GIINQSRSAS TRMTDHEGAR AEEAEPITFP
SGGGKSFIMG SDDVLLSVLG LGDLADLTVT NDADYSYDLP ANKDAFRKTW NPKYTLRSHF
DGVRALAFHP VEPVLVTASE DHTLKLWNLQ KTVPAKKSAS LDVEPIYTFR AHIGPVLSLA
ISSNGEQCFS GGIDATIQWW NMPSPSVDPY DTYEPNVLAG TLVGHTDAVW GLAYSGIKNQ
LLSCSADGTV RLWNPQEKLP CICTYNGDKK HGIPTSVDFI GCDPAHMVTS FNTGSAVIYD
LETSQSLVIL SSQVDSGLQS NNHINRVVSH PTLPVTITAH EDRHIKFFDN KTGKMIHSMV
AHLDAVTSLA VDPNGIYLMS GSHDCSIRLW NLDSKTCVQE ITAHRKKLDE SIYDVAFHSS
KAYIASAGAD ALAKVFV
//
