STRN3_BOVIN
ID STRN3_BOVIN Reviewed; 797 AA.
AC A5D7H2;
DT 28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 12-JUN-2007, sequence version 1.
DT 03-AUG-2022, entry version 94.
DE RecName: Full=Striatin-3;
GN Name=STRN3;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Hereford; TISSUE=Basal ganglia;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (APR-2007) to the EMBL/GenBank/DDBJ databases.
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 -!- SIMILARITY: Belongs to the WD repeat striatin family. {ECO:0000305}.
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DR EMBL; BC140553; AAI40554.1; -; mRNA.
DR RefSeq; NP_001091511.1; NM_001098042.1.
DR AlphaFoldDB; A5D7H2; -.
DR SMR; A5D7H2; -.
DR STRING; 9913.ENSBTAP00000029119; -.
DR PaxDb; A5D7H2; -.
DR PRIDE; A5D7H2; -.
DR Ensembl; ENSBTAT00000029119; ENSBTAP00000029119; ENSBTAG00000021845.
DR GeneID; 516375; -.
DR KEGG; bta:516375; -.
DR CTD; 29966; -.
DR VEuPathDB; HostDB:ENSBTAG00000021845; -.
DR VGNC; VGNC:35425; STRN3.
DR eggNOG; KOG0642; Eukaryota.
DR GeneTree; ENSGT00950000183095; -.
DR HOGENOM; CLU_009108_2_0_1; -.
DR InParanoid; A5D7H2; -.
DR OMA; TSHRLMR; -.
DR OrthoDB; 334070at2759; -.
DR TreeFam; TF313387; -.
DR Proteomes; UP000009136; Chromosome 21.
DR Bgee; ENSBTAG00000021845; Expressed in longissimus thoracis muscle and 105 other tissues.
DR ExpressionAtlas; A5D7H2; baseline and differential.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0030425; C:dendrite; IBA:GO_Central.
DR GO; GO:0090443; C:FAR/SIN/STRIPAK complex; IEA:Ensembl.
DR GO; GO:0005794; C:Golgi apparatus; IEA:Ensembl.
DR GO; GO:0005654; C:nucleoplasm; ISS:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; IEA:Ensembl.
DR GO; GO:0070016; F:armadillo repeat domain binding; IBA:GO_Central.
DR GO; GO:0005516; F:calmodulin binding; IBA:GO_Central.
DR GO; GO:0051721; F:protein phosphatase 2A binding; IBA:GO_Central.
DR GO; GO:0044877; F:protein-containing complex binding; IBA:GO_Central.
DR GO; GO:0031267; F:small GTPase binding; IEA:Ensembl.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; ISS:UniProtKB.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; ISS:UniProtKB.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; ISS:UniProtKB.
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 2: Evidence at transcript level;
KW Acetylation; Calmodulin-binding; Coiled coil; Cytoplasm; Membrane;
KW Phosphoprotein; Reference proteome; Repeat; WD repeat.
FT CHAIN 1..797
FT /note="Striatin-3"
FT /id="PRO_0000379881"
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 313..336
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 77..136
FT /evidence="ECO:0000255"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0000250|UniProtKB:Q13033"
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:0000250|UniProtKB:Q13033"
FT MOD_RES 229
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q13033"
FT MOD_RES 257
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q13033"
FT MOD_RES 335
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9ERG2"
SQ SEQUENCE 797 AA; 87423 MW; 4A8E5DB70B883ED9 CRC64;
MDELAGGGGG GPAMASPPRQ QQGPGGNMSL SPGGNGAAGG GGPPATEGAG PAAGPELSRP
QQYTIPGILH YIQHEWARFE MERAHWEVER AELQARIAFL QGERKGQENL KKDLVRRIKM
LEYALKQERA KYHKLKYGTE LNQGDLKMPT FESEETKDTE APTAPQNSQL TWKQGRQLLR
QYLQEVGYTD TILDVRSQRV RSLLGLSNSE PNGSVETKNL EQILNGGESP KQKGQEIKRT
SGDVLETFNF LENADDSDEE EENDMIEGIP EGKDKHRINK HKIGNEGLAA DLTDDPDTEE
ALKEFDFLVT AEDGEGAGEA RSSGDGTEWD KDDLSPTTEV WDVDQGLISK LKEQYKKERK
GKKGVKRVNR TKLYDTIADL GDDELPLIPS GIINQSRSAS TRMTDHEGAR AEEAEPITFP
SGGGKSFIMG SDDVLLSVLG LGDLADLTVT NDADYSYDLP ANKDAFRKTW NPKYTLRSHF
DGVRALAFHP VEPVLVTASE DHTLKLWNLQ KTVPAKKSAS LDVEPIYTFR AHIGPVLSLA
ISSNGEQCFS GGTDATIQWW NMPSPNVDPY DTYEPNVLAG TLIAHTDAVW GLAYSGIKNQ
LLSCSADGTV RLWNPQEKLP CICTYNGDKE HGIPTSVDFI GCDPAHMVTS FNTGSTVIYD
LETSQSLVML SSQMDSGLQS SNHINRVVSH PTLPVTITAH EDRHIKFFDN KTGKMIHSMV
AHLDAVTSLA VDPNGIYLMS GSHDCSIRLW NLDSKTCVQE ITAHRKKLDE SIYDVAFHPS
KAYIASAGAD ALAKVFV
