STRAP_MOUSE
ID STRAP_MOUSE Reviewed; 350 AA.
AC Q9Z1Z2; Q8BP89; Q8C6F6;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 15-JAN-2008, sequence version 2.
DT 03-AUG-2022, entry version 166.
DE RecName: Full=Serine-threonine kinase receptor-associated protein;
DE AltName: Full=UNR-interacting protein;
GN Name=Strap; Synonyms=Unrip;
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].
RX PubMed=9856985; DOI=10.1074/jbc.273.52.34671;
RA Datta P.K., Chytil A., Gorska A.E., Moses H.L.;
RT "Identification of STRAP, a novel WD domain protein in transforming growth
RT factor-beta signaling.";
RL J. Biol. Chem. 273:34671-34674(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Bone marrow, Embryo, Pancreas, and Placenta;
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).
RN [3]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-342, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Mast cell;
RX PubMed=17947660; DOI=10.4049/jimmunol.179.9.5864;
RA Cao L., Yu K., Banh C., Nguyen V., Ritz A., Raphael B.J., Kawakami Y.,
RA Kawakami T., Salomon A.R.;
RT "Quantitative time-resolved phosphoproteomic analysis of mast cell
RT signaling.";
RL J. Immunol. 179:5864-5876(2007).
RN [4]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AF096285; AAC98300.1; -; mRNA.
DR EMBL; AK075804; BAC35972.1; -; mRNA.
DR EMBL; AK077504; BAC36834.1; -; mRNA.
DR EMBL; AK145971; BAE26796.1; -; mRNA.
DR EMBL; AK152283; BAE31097.1; -; mRNA.
DR CCDS; CCDS51945.1; -.
DR RefSeq; NP_035629.2; NM_011499.3.
DR AlphaFoldDB; Q9Z1Z2; -.
DR SMR; Q9Z1Z2; -.
DR BioGRID; 203557; 24.
DR CORUM; Q9Z1Z2; -.
DR IntAct; Q9Z1Z2; 2.
DR STRING; 10090.ENSMUSP00000068267; -.
DR iPTMnet; Q9Z1Z2; -.
DR PhosphoSitePlus; Q9Z1Z2; -.
DR SwissPalm; Q9Z1Z2; -.
DR REPRODUCTION-2DPAGE; IPI00130670; -.
DR REPRODUCTION-2DPAGE; Q9Z1Z2; -.
DR EPD; Q9Z1Z2; -.
DR jPOST; Q9Z1Z2; -.
DR MaxQB; Q9Z1Z2; -.
DR PaxDb; Q9Z1Z2; -.
DR PRIDE; Q9Z1Z2; -.
DR ProteomicsDB; 258666; -.
DR Antibodypedia; 12145; 224 antibodies from 32 providers.
DR DNASU; 20901; -.
DR Ensembl; ENSMUST00000064910; ENSMUSP00000068267; ENSMUSG00000030224.
DR GeneID; 20901; -.
DR KEGG; mmu:20901; -.
DR UCSC; uc012euz.1; mouse.
DR CTD; 11171; -.
DR MGI; MGI:1329037; Strap.
DR VEuPathDB; HostDB:ENSMUSG00000030224; -.
DR eggNOG; KOG0278; Eukaryota.
DR GeneTree; ENSGT00940000155197; -.
DR HOGENOM; CLU_000288_57_6_1; -.
DR InParanoid; Q9Z1Z2; -.
DR OMA; FQHNHIV; -.
DR OrthoDB; 1239790at2759; -.
DR PhylomeDB; Q9Z1Z2; -.
DR TreeFam; TF323287; -.
DR Reactome; R-MMU-2173788; Downregulation of TGF-beta receptor signaling.
DR BioGRID-ORCS; 20901; 25 hits in 77 CRISPR screens.
DR ChiTaRS; Strap; mouse.
DR PRO; PR:Q9Z1Z2; -.
DR Proteomes; UP000000589; Chromosome 6.
DR RNAct; Q9Z1Z2; protein.
DR Bgee; ENSMUSG00000030224; Expressed in mandibular prominence and 286 other tissues.
DR ExpressionAtlas; Q9Z1Z2; baseline and differential.
DR Genevisible; Q9Z1Z2; MM.
DR GO; GO:0005737; C:cytoplasm; ISO:MGI.
DR GO; GO:0005829; C:cytosol; ISS:UniProtKB.
DR GO; GO:0005634; C:nucleus; IDA:MGI.
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; IDA:MGI.
DR GO; GO:0003723; F:RNA binding; IBA:GO_Central.
DR GO; GO:0005102; F:signaling receptor binding; IDA:MGI.
DR GO; GO:1990447; F:U2 snRNP binding; IDA:MGI.
DR GO; GO:0000380; P:alternative mRNA splicing, via spliceosome; IMP:MGI.
DR GO; GO:0048856; P:anatomical structure development; IMP:MGI.
DR GO; GO:0030277; P:maintenance of gastrointestinal epithelium; ISO:MGI.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IDA:MGI.
DR GO; GO:0030512; P:negative regulation of transforming growth factor beta receptor signaling pathway; IDA:MGI.
DR GO; GO:0030182; P:neuron differentiation; IMP:MGI.
DR GO; GO:0022618; P:ribonucleoprotein complex assembly; IMP:MGI.
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 1: Evidence at protein 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_0000051231"
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 326..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:0007744|PubMed:17947660"
FT CONFLICT 288
FT /note="T -> P (in Ref. 2; BAC36834)"
FT /evidence="ECO:0000305"
FT CONFLICT 330
FT /note="L -> LA (in Ref. 1; AAC98300)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 350 AA; 38442 MW; 99A71583618B1514 CRC64;
MAMRQTPLTC SGHTRPVVDL AFSGITPYGY FLISACKDGK PMLRQGDTGD WIGTFLGHKG
AVWGATLNKD ATKAATAAAD FTAKVWDAVS GDELMTLAHK HIVKTVDFTQ DSNYLLTGGQ
DKLLRIYDLN KPEAEPKEIS GHTSGIKKAL WCSDDKQILS ADDKTVRLWD HATMTEVKSL
NFNMSVSSME YIPEGEILVI TYGRSIAFHS AVSLEPIKSF EAPATINSAS LHPEKEFLVA
GGEDFKLYKY DYNSGEELES YKGHFGPIHC VRFSPDGELY ASGSEDGTLR LWQTVVGKTY
GLWKCVLPEE DSGELAKPKI GFPETAEEEL EEIASENSDS IYSSTPEVKA
