STRAP_CHICK
ID STRAP_CHICK Reviewed; 350 AA.
AC Q5ZL33;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 15-JAN-2008, sequence version 2.
DT 03-AUG-2022, entry version 107.
DE RecName: Full=Serine-threonine kinase receptor-associated protein;
GN Name=STRAP; ORFNames=RCJMB04_7p19;
OS Gallus gallus (Chicken).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC Phasianinae; Gallus.
OX NCBI_TaxID=9031;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=CB; TISSUE=Bursa of Fabricius;
RX PubMed=15642098; DOI=10.1186/gb-2004-6-1-r6;
RA Caldwell R.B., Kierzek A.M., Arakawa H., Bezzubov Y., Zaim J., Fiedler P.,
RA Kutter S., Blagodatski A., Kostovska D., Koter M., Plachy J., Carninci P.,
RA Hayashizaki Y., Buerstedde J.-M.;
RT "Full-length cDNAs from chicken bursal lymphocytes to facilitate gene
RT function analysis.";
RL Genome Biol. 6:R6.1-R6.9(2005).
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 (By similarity).
CC {ECO:0000250|UniProtKB:Q9Y3F4}.
CC -!- SUBUNIT: Part of the core SMN complex. {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 -!- SEQUENCE CAUTION:
CC Sequence=CAG31560.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AJ719901; CAG31560.1; ALT_INIT; mRNA.
DR RefSeq; NP_001006247.2; NM_001006247.2.
DR AlphaFoldDB; Q5ZL33; -.
DR SMR; Q5ZL33; -.
DR STRING; 9031.ENSGALP00000021343; -.
DR PaxDb; Q5ZL33; -.
DR Ensembl; ENSGALT00000021374; ENSGALP00000021343; ENSGALG00000013092.
DR GeneID; 418175; -.
DR KEGG; gga:418175; -.
DR CTD; 11171; -.
DR VEuPathDB; HostDB:geneid_418175; -.
DR eggNOG; KOG0278; Eukaryota.
DR GeneTree; ENSGT00940000155197; -.
DR HOGENOM; CLU_000288_57_6_1; -.
DR InParanoid; Q5ZL33; -.
DR OMA; FQHNHIV; -.
DR OrthoDB; 1239790at2759; -.
DR PhylomeDB; Q5ZL33; -.
DR TreeFam; TF323287; -.
DR PRO; PR:Q5ZL33; -.
DR Proteomes; UP000000539; Chromosome 1.
DR Bgee; ENSGALG00000013092; Expressed in spermatid and 14 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; ISS:AgBase.
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; ISS:AgBase.
DR GO; GO:0030512; P:negative regulation of transforming growth factor beta receptor signaling pathway; ISS:AgBase.
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; 6.
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; Reference proteome;
KW Repeat; WD repeat.
FT CHAIN 1..350
FT /note="Serine-threonine kinase receptor-associated protein"
FT /id="PRO_0000313796"
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 311..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"
SQ SEQUENCE 350 AA; 38141 MW; E13C2CF4D1B2B5D0 CRC64;
MAMRQTPLTC SGHTRPVVDL AFSGVTPYGY FLISACKDGK PMLRQGDTGD WIGTFLGHKG
AVWGATLNKD ATKAATAAAD FTAKVWDAVS GDELITLAHK HIVKSVDFTQ DSNYLLTGGQ
DKLLRIYDLS KPEAEPDVVS GHTSGIKKAL WSSDDKQILS ADDKTVRLWD RSTMTEVKAL
NVAMSVSSME YVPEGQILVI TYGKTIAFHS AETLEQIKSF EAPATINSAS LHPEKECLVA
GGEDFKLYKY DYNTGEELES YKGHFGPIHC VRFSPDGELY ASGSEDGTLR LWQTTVGKTY
GLWKCVVPEE ENAEAAKART TLPGTAEEEI EEVASENSDS VYSSTPEVKA
