TSAP1_PONAB
ID TSAP1_PONAB Reviewed; 287 AA.
AC Q5R462;
DT 02-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT 21-DEC-2004, sequence version 1.
DT 25-MAY-2022, entry version 68.
DE RecName: Full=tRNA selenocysteine 1-associated protein 1;
DE AltName: Full=tRNA selenocysteine-associated protein 1;
GN Name=TRNAU1AP; Synonyms=TRSPAP1;
OS Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Pongo.
OX NCBI_TaxID=9601;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain cortex;
RG The German cDNA consortium;
RL Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
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). Found in a
CC complex with tRNA(Sec). Interacts with SEPSECS. Associates with mRNP
CC and/or polysomes. Found in a complex with EEFSEC, SECISBP2, TRNAU1AP
CC and tRNA(Sec) (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Cytoplasm {ECO:0000250}.
CC Note=Abundant in the nucleus. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the RRM TRSPAP 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; CR861396; CAH93454.1; -; mRNA.
DR RefSeq; NP_001127022.1; NM_001133550.1.
DR AlphaFoldDB; Q5R462; -.
DR SMR; Q5R462; -.
DR GeneID; 100174047; -.
DR KEGG; pon:100174047; -.
DR CTD; 54952; -.
DR InParanoid; Q5R462; -.
DR OrthoDB; 775799at2759; -.
DR Proteomes; UP000001595; Unplaced.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR GO; GO:0006412; P:translation; IEA:UniProtKB-KW.
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 2: Evidence at transcript 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_0000304919"
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; 32527 MW; 0605E23EE1237218 CRC64;
MAASLWMGDL EPYMDENFIS RAFATMGETV MSVKIIRNRL TGIPAGYCFV EFADLATAEK
CLHKINGKPL PGATPAKRFK LNYVTYGKQP DNSPEYSLFV GDLTPDVDDG MLYEFFVKVY
PSCRGGKVVL DQTGVSKGYG FVKFTDELEQ KRALTECQGA VGLGSKPVRL SVAIPKASRV
KPVEYSQMYS YSYNQYYQQY QNYYAQWGYD QNTGSYSYSY PQYGYTQSTM QTYEEVGDDA
LEDPMPQLDV TEANKEFMEQ SEELYDALMD CHWQPLDTVS SEIPAMM