TSAP1_RAT
ID TSAP1_RAT Reviewed; 287 AA.
AC Q9QZI7;
DT 02-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 99.
DE RecName: Full=tRNA selenocysteine 1-associated protein 1;
DE AltName: Full=SECp43;
DE AltName: Full=tRNA selenocysteine-associated protein 1;
GN Name=Trnau1ap; Synonyms=Secp43, Trspap1;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], IDENTIFICATION IN A COMPLEX WITH TRNA(SEC),
RP INTERACTION WITH SEPSECS, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RC TISSUE=Cerebellum;
RX PubMed=10606267; DOI=10.1017/s1355838299991598;
RA Ding F., Grabowski P.J.;
RT "Identification of a protein component of a mammalian tRNA(Sec) complex
RT implicated in the decoding of UGA as selenocysteine.";
RL RNA 5:1561-1569(1999).
CC -!- FUNCTION: Involved in the early steps of selenocysteine biosynthesis
CC and tRNA(Sec) charging to the later steps resulting in the
CC cotranslational incorporation of selenocysteine into selenoproteins.
CC Stabilizes the SECISBP2, EEFSEC and tRNA(Sec) complex. May be involved
CC in the methylation of tRNA(Sec). Enhances efficiency of selenoproteins
CC synthesis (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Component of the tRNA(Sec) complex composed at least of
CC EEFSEC, SECISBP2, SEPHS1, SEPSECS, TRNAU1AP and tRNA(Sec). Associates
CC with mRNP and/or polysomes (By similarity). Found in a complex with
CC tRNA(Sec). Interacts with SEPSECS. {ECO:0000250,
CC ECO:0000269|PubMed:10606267}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:10606267}. Cytoplasm
CC {ECO:0000269|PubMed:10606267}. Note=Abundant in the nucleus.
CC -!- TISSUE SPECIFICITY: Ubiquitous. {ECO:0000269|PubMed:10606267}.
CC -!- SIMILARITY: Belongs to the RRM TRSPAP family. {ECO:0000305}.
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DR EMBL; AF181856; AAD54419.1; -; mRNA.
DR RefSeq; NP_075416.1; NM_023027.1.
DR AlphaFoldDB; Q9QZI7; -.
DR SMR; Q9QZI7; -.
DR STRING; 10116.ENSRNOP00000065702; -.
DR PaxDb; Q9QZI7; -.
DR Ensembl; ENSRNOT00000113510; ENSRNOP00000084120; ENSRNOG00000055344.
DR GeneID; 65241; -.
DR KEGG; rno:65241; -.
DR CTD; 54952; -.
DR RGD; 619995; Trnau1ap.
DR eggNOG; KOG0118; Eukaryota.
DR GeneTree; ENSGT00940000156139; -.
DR InParanoid; Q9QZI7; -.
DR OrthoDB; 775799at2759; -.
DR PhylomeDB; Q9QZI7; -.
DR PRO; PR:Q9QZI7; -.
DR Proteomes; UP000002494; Chromosome 5.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; ISS:HGNC-UCL.
DR GO; GO:0000049; F:tRNA binding; IDA:RGD.
DR GO; GO:0001514; P:selenocysteine incorporation; ISS:HGNC-UCL.
DR CDD; cd12612; RRM2_SECp43; 1.
DR Gene3D; 3.30.70.330; -; 2.
DR InterPro; IPR012677; Nucleotide-bd_a/b_plait_sf.
DR InterPro; IPR035979; RBD_domain_sf.
DR InterPro; IPR000504; RRM_dom.
DR InterPro; IPR034510; SECp43_RRM2.
DR InterPro; IPR040434; TSAP1.
DR InterPro; IPR041085; TSAP1_C.
DR PANTHER; PTHR37457; PTHR37457; 1.
DR Pfam; PF00076; RRM_1; 2.
DR Pfam; PF17654; Trnau1ap; 1.
DR SMART; SM00360; RRM; 2.
DR SUPFAM; SSF54928; SSF54928; 1.
DR PROSITE; PS50102; RRM; 2.
PE 1: Evidence at protein level;
KW Cytoplasm; Nucleus; Protein biosynthesis; Reference proteome; Repeat;
KW RNA-binding.
FT CHAIN 1..287
FT /note="tRNA selenocysteine 1-associated protein 1"
FT /id="PRO_0000304920"
FT DOMAIN 3..86
FT /note="RRM 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT DOMAIN 96..175
FT /note="RRM 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
SQ SEQUENCE 287 AA; 32454 MW; 5485AE4CB30E56F5 CRC64;
MAASLWMGDL EPYMDENFIS RAFATMGETV MSVKIIRNRL TGIPAGYCFV EFADLATAEK
CLHKINGKPL PGATPAKRFK LNYATYGKQP DNSPEYSLFV GDLTPDVDDG MLYEFFVKVY
PSCRGGKVVL DQTGVSKGYG FVKFTDELEQ KRALTECQGA VGLGCKPVRL SVAIPKASRV
KPVEYSQMYS YSYNQYYQQY QNYYAQWGYD QNTGSYSYSY PQYGYTQSTM QTYEEVGDDA
LEDPAPQLDV TEANKEFMEQ SEELYDALMD CHWQPLDTVS SEIPAMM