STRAP_BOVIN
ID STRAP_BOVIN Reviewed; 350 AA.
AC Q5E959;
DT 09-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT 15-MAR-2005, sequence version 1.
DT 03-AUG-2022, entry version 110.
DE RecName: Full=Serine-threonine kinase receptor-associated protein;
GN Name=STRAP;
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].
RX PubMed=16305752; DOI=10.1186/1471-2164-6-166;
RA Harhay G.P., Sonstegard T.S., Keele J.W., Heaton M.P., Clawson M.L.,
RA Snelling W.M., Wiedmann R.T., Van Tassell C.P., Smith T.P.L.;
RT "Characterization of 954 bovine full-CDS cDNA sequences.";
RL BMC Genomics 6:166-166(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Hereford; TISSUE=Fetal muscle;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (AUG-2006) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: The SMN complex catalyzes the assembly of small nuclear
CC ribonucleoproteins (snRNPs), the building blocks of the spliceosome,
CC and thereby plays an important role in the splicing of cellular pre-
CC mRNAs. Most spliceosomal snRNPs contain a common set of Sm proteins
CC SNRPB, SNRPD1, SNRPD2, SNRPD3, SNRPE, SNRPF and SNRPG that assemble in
CC a heptameric protein ring on the Sm site of the small nuclear RNA to
CC form the core snRNP (Sm core). In the cytosol, the Sm proteins SNRPD1,
CC SNRPD2, SNRPE, SNRPF and SNRPG are trapped in an inactive 6S pICln-Sm
CC complex by the chaperone CLNS1A that controls the assembly of the core
CC snRNP. To assemble core snRNPs, the SMN complex accepts the trapped 5Sm
CC proteins from CLNS1A forming an intermediate. Binding of snRNA inside
CC 5Sm triggers eviction of the SMN complex, thereby allowing binding of
CC SNRPD3 and SNRPB to complete assembly of the core snRNP. STRAP plays a
CC role in the cellular distribution of the SMN complex. Negatively
CC regulates TGF-beta signaling but positively regulates the PDPK1 kinase
CC activity by enhancing its autophosphorylation and by significantly
CC reducing the association of PDPK1 with 14-3-3 protein (By similarity).
CC {ECO:0000250|UniProtKB:Q9Y3F4}.
CC -!- SUBUNIT: Part of the core SMN complex that contains SMN1, GEMIN2/SIP1,
CC DDX20/GEMIN3, GEMIN4, GEMIN5, GEMIN6, GEMIN7, GEMIN8 and STRAP/UNRIP.
CC Part of the SMN-Sm complex that contains SMN1, GEMIN2/SIP1,
CC DDX20/GEMIN3, GEMIN4, GEMIN5, GEMIN6, GEMIN7, GEMIN8, STRAP/UNRIP and
CC the Sm proteins SNRPB, SNRPD1, SNRPD2, SNRPD3, SNRPE, SNRPF and SNRPG.
CC Interacts directly with GEMIN6 and GEMIN7. Associates with the SMN
CC complex in the cytoplasm but not in the nucleus. Also interacts with
CC CSDE1/UNR and MAWBP. Interacts with PDPK1. Interacts with TRIM48.
CC {ECO:0000250|UniProtKB:Q9Y3F4}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}.
CC Note=Localized predominantly in the cytoplasm but also found in the
CC nucleus. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the WD repeat STRAP family. {ECO:0000305}.
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DR EMBL; BT021061; AAX09078.1; -; mRNA.
DR EMBL; BC119959; AAI19960.1; -; mRNA.
DR RefSeq; NP_001015567.1; NM_001015567.2.
DR AlphaFoldDB; Q5E959; -.
DR SMR; Q5E959; -.
DR STRING; 9913.ENSBTAP00000018840; -.
DR PaxDb; Q5E959; -.
DR PeptideAtlas; Q5E959; -.
DR PRIDE; Q5E959; -.
DR Ensembl; ENSBTAT00000018840; ENSBTAP00000018840; ENSBTAG00000014175.
DR GeneID; 510201; -.
DR KEGG; bta:510201; -.
DR CTD; 11171; -.
DR VEuPathDB; HostDB:ENSBTAG00000014175; -.
DR VGNC; VGNC:35420; STRAP.
DR eggNOG; KOG0278; Eukaryota.
DR GeneTree; ENSGT00940000155197; -.
DR HOGENOM; CLU_000288_57_6_1; -.
DR InParanoid; Q5E959; -.
DR OMA; FQHNHIV; -.
DR OrthoDB; 1239790at2759; -.
DR TreeFam; TF323287; -.
DR Proteomes; UP000009136; Chromosome 5.
DR Bgee; ENSBTAG00000014175; Expressed in tongue muscle and 105 other tissues.
DR GO; GO:0005829; C:cytosol; ISS:UniProtKB.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0032797; C:SMN complex; ISS:UniProtKB.
DR GO; GO:0034719; C:SMN-Sm protein complex; ISS:UniProtKB.
DR GO; GO:0003729; F:mRNA binding; IEA:Ensembl.
DR GO; GO:0005102; F:signaling receptor binding; IEA:Ensembl.
DR GO; GO:1990447; F:U2 snRNP binding; IEA:Ensembl.
DR GO; GO:0000380; P:alternative mRNA splicing, via spliceosome; IEA:Ensembl.
DR GO; GO:0030277; P:maintenance of gastrointestinal epithelium; IEA:Ensembl.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IEA:Ensembl.
DR GO; GO:0030512; P:negative regulation of transforming growth factor beta receptor signaling pathway; IEA:Ensembl.
DR GO; GO:0030182; P:neuron differentiation; IEA:Ensembl.
DR GO; GO:0000387; P:spliceosomal snRNP assembly; ISS:UniProtKB.
DR Gene3D; 2.130.10.10; -; 1.
DR InterPro; IPR020472; G-protein_beta_WD-40_rep.
DR InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR InterPro; IPR001680; WD40_repeat.
DR InterPro; IPR036322; WD40_repeat_dom_sf.
DR Pfam; PF00400; WD40; 4.
DR PRINTS; PR00320; GPROTEINBRPT.
DR SMART; SM00320; WD40; 7.
DR SUPFAM; SSF50978; SSF50978; 1.
DR PROSITE; PS00678; WD_REPEATS_1; 1.
DR PROSITE; PS50082; WD_REPEATS_2; 4.
DR PROSITE; PS50294; WD_REPEATS_REGION; 1.
PE 2: Evidence at transcript level;
KW Cytoplasm; mRNA processing; mRNA splicing; Nucleus; Phosphoprotein;
KW Reference proteome; Repeat; WD repeat.
FT CHAIN 1..350
FT /note="Serine-threonine kinase receptor-associated protein"
FT /id="PRO_0000271399"
FT REPEAT 12..56
FT /note="WD 1"
FT REPEAT 57..96
FT /note="WD 2"
FT REPEAT 98..137
FT /note="WD 3"
FT REPEAT 141..179
FT /note="WD 4"
FT REPEAT 180..212
FT /note="WD 5"
FT REPEAT 221..262
FT /note="WD 6"
FT REPEAT 263..302
FT /note="WD 7"
FT REGION 327..350
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 336..350
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 312
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9Y3F4"
FT MOD_RES 335
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9Y3F4"
FT MOD_RES 338
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9Y3F4"
FT MOD_RES 342
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:Q9Z1Z2"
SQ SEQUENCE 350 AA; 38485 MW; 27FE6834FF1AD765 CRC64;
MAMRQTPLTC SGHTRPVVDL AFSGITPYGY FLISACKDGK PMLRQGDTGD WIGTFLGHKG
AVWGATLNKD ATKAATAAAD FTAKVWDAVS GDELMTLAHK HIVKTVDFTQ DSNYLLTGGQ
DKLLRIYDLN KPEAEPKEIS GHTSGIKKAL WCSEDKQILS ADDKTVRLWD HATMTEVKSL
NFNMSVSSME YIPEGEILVI TYGRSIAFHS AVSLDPIKSF EAPATINSAS LHPEKEFVVA
GGEDFKLYKY DYNSGEELES YKGHFGPIHC VRFSPDGELY ASGSEDGTLR LWQTVVGKTY
GLWKCVLPEE DSGELAKPKI NFPETAEEEL EEIASENSDS IYSSTPEVKA
