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}.
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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