TSAP1_MOUSE
ID TSAP1_MOUSE Reviewed; 287 AA.
AC Q80VC6; Q05DN9; Q4FZE9; Q7TMM7;
DT 02-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2005, sequence version 2.
DT 03-AUG-2022, entry version 140.
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 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 [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Bone marrow;
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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J, Czech II, FVB/N, and FVB/N-3;
RC TISSUE=Brain, and Mammary tumor;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [4]
RP FUNCTION, IDENTIFICATION IN A COMPLEX WITH SEPSECS AND TRNA(SEC),
RP INTERACTION WITH SEPSECS, AND SUBCELLULAR LOCATION.
RX PubMed=16230358; DOI=10.1074/jbc.m506696200;
RA Xu X.-M., Mix H., Carlson B.A., Grabowski P.J., Gladyshev V.N., Berry M.J.,
RA Hatfield D.L.;
RT "Evidence for direct roles of two additional factors, SECp43 and soluble
RT liver antigen, in the selenoprotein synthesis machinery.";
RL J. Biol. Chem. 280:41568-41575(2005).
RN [5]
RP FUNCTION, IDENTIFICATION IN A COMPLEX WITH EEFSEC; SECISBP2; SEPHS1;
RP SEPSECS AND TRNA(SEC), ASSOCIATION WITH MRNP, ASSOCIATION WITH POLYSOMES,
RP AND SUBCELLULAR LOCATION.
RX PubMed=16508009; DOI=10.1128/mcb.26.6.2337-2346.2006;
RA Small-Howard A., Morozova N., Stoytcheva Z., Forry E.P., Mansell J.B.,
RA Harney J.W., Carlson B.A., Xu X.M., Hatfield D.L., Berry M.J.;
RT "Supramolecular complexes mediate selenocysteine incorporation in vivo.";
RL Mol. Cell. Biol. 26:2337-2346(2006).
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. {ECO:0000269|PubMed:16230358, ECO:0000269|PubMed:16508009}.
CC -!- SUBUNIT: Found in a complex with tRNA(Sec) (By similarity). Interacts
CC with SEPSECS (By similarity). Component of the tRNA(Sec) complex
CC composed at least of EEFSEC, SECISBP2, SEPHS1, SEPSECS, TRNAU1AP and
CC tRNA(Sec). Associates with mRNP and/or polysomes. {ECO:0000250,
CC ECO:0000269|PubMed:16230358, ECO:0000269|PubMed:16508009}.
CC -!- SUBCELLULAR LOCATION: Nucleus. Cytoplasm. Note=Abundant in the nucleus.
CC {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; AK152986; BAE31634.1; -; mRNA.
DR EMBL; CR752656; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC005795; AAH05795.1; -; mRNA.
DR EMBL; BC048840; AAH48840.2; -; mRNA.
DR EMBL; BC055454; AAH55454.1; -; mRNA.
DR EMBL; BC099594; AAH99594.1; -; mRNA.
DR CCDS; CCDS18722.1; -.
DR RefSeq; NP_082201.2; NM_027925.3.
DR AlphaFoldDB; Q80VC6; -.
DR SMR; Q80VC6; -.
DR CORUM; Q80VC6; -.
DR STRING; 10090.ENSMUSP00000030730; -.
DR iPTMnet; Q80VC6; -.
DR PhosphoSitePlus; Q80VC6; -.
DR EPD; Q80VC6; -.
DR MaxQB; Q80VC6; -.
DR PaxDb; Q80VC6; -.
DR PeptideAtlas; Q80VC6; -.
DR PRIDE; Q80VC6; -.
DR ProteomicsDB; 297659; -.
DR Antibodypedia; 30961; 151 antibodies from 23 providers.
DR DNASU; 71787; -.
DR Ensembl; ENSMUST00000030730; ENSMUSP00000030730; ENSMUSG00000028898.
DR GeneID; 71787; -.
DR KEGG; mmu:71787; -.
DR UCSC; uc008vbb.1; mouse.
DR CTD; 54952; -.
DR MGI; MGI:1919037; Trnau1ap.
DR VEuPathDB; HostDB:ENSMUSG00000028898; -.
DR eggNOG; KOG0118; Eukaryota.
DR GeneTree; ENSGT00940000156139; -.
DR HOGENOM; CLU_016304_3_0_1; -.
DR InParanoid; Q80VC6; -.
DR OMA; LKICNAV; -.
DR OrthoDB; 775799at2759; -.
DR PhylomeDB; Q80VC6; -.
DR TreeFam; TF313275; -.
DR BioGRID-ORCS; 71787; 5 hits in 74 CRISPR screens.
DR ChiTaRS; Trnau1ap; mouse.
DR PRO; PR:Q80VC6; -.
DR Proteomes; UP000000589; Chromosome 4.
DR RNAct; Q80VC6; protein.
DR Bgee; ENSMUSG00000028898; Expressed in manus and 237 other tissues.
DR ExpressionAtlas; Q80VC6; baseline and differential.
DR Genevisible; Q80VC6; MM.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IDA:HGNC-UCL.
DR GO; GO:0000049; F:tRNA binding; ISO:MGI.
DR GO; GO:0001514; P:selenocysteine incorporation; IDA: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_0000304918"
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"
FT CONFLICT 31
FT /note="M -> L (in Ref. 2; AAH05795)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 287 AA; 32423 MW; 54840556B804F6E4 CRC64;
MAASLWMGDL EPYMDENFIS RAFATMGETV MSVKIIRNRL TGIPAGYCFV EFADLATAEK
CLHKINGKPL PGATPAKRFK LNYATYGKQP DNSPEYSLFV GDLTPDVDDG MLYEFFVKVY
PSCRGGKVVL DPTGVSKGYG FVKFTDELEQ KRALTECQGA VGLGCKPVRL SVAIPKASRV
KPVEYSQMYS YSYNQYYQQY QNYYAQWGYD QNTGSYSYSY PQYGYTQSTM QTYEEVGDDA
LEDPAPQLDV TEANKEFMEQ SEELYDALMD CHWQPLDTVS SEIPAMM
