ARCH_MOUSE
ID ARCH_MOUSE Reviewed; 168 AA.
AC Q505B7; Q8R0S8; Q9CQ53; Q9D770;
DT 01-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2007, sequence version 2.
DT 03-AUG-2022, entry version 98.
DE RecName: Full=Protein archease;
DE AltName: Full=Protein ZBTB8OS;
GN Name=Zbtb8os; Synonyms=Arch;
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 [MRNA] (ISOFORM 1).
RC STRAIN=C3H/HeJ;
RA Alliel P.M., Goudou D., Bitoun M., Langlois C., Rieger F., Seddiqi N.,
RA Perin J.P.;
RT "Structure, expression and sequence comparison of human and murine
RT archease.";
RL Submitted (DEC-2001) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC STRAIN=C57BL/6J; TISSUE=Pancreas, Placenta, Small intestine, and Tongue;
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 [3]
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=C57BL/6J, and FVB/N; TISSUE=Brain, Kidney, and Thymus;
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 [5]
RP IDENTIFICATION.
RX PubMed=15162483; DOI=10.1002/prot.20141;
RA Canaves J.M.;
RT "Predicted role for the archease protein family based on structural and
RT sequence analysis of TM1083 and MTH1598, two proteins structurally
RT characterized through structural genomics efforts.";
RL Proteins 56:19-27(2004).
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Kidney, Liver, Pancreas, Spleen, and
RC Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
CC -!- FUNCTION: Component of the tRNA-splicing ligase complex required to
CC facilitate the enzymatic turnover of catalytic subunit RTCB. Together
CC with DDX1, acts by facilitating the guanylylation of RTCB, a key
CC intermediate step in tRNA ligation (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Component of the tRNA-splicing ligase complex. {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q505B7-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q505B7-2; Sequence=VSP_024927, VSP_024928;
CC -!- MISCELLANEOUS: [Isoform 2]: May be produced at very low levels due to a
CC premature stop codon in the mRNA, leading to nonsense-mediated mRNA
CC decay. {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the archease family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH26442.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=AAH94629.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AY071852; AAL58522.1; -; mRNA.
DR EMBL; AK007377; BAB24996.1; -; mRNA.
DR EMBL; AK008007; BAB25405.1; -; mRNA.
DR EMBL; AK009527; BAB26341.1; -; mRNA.
DR EMBL; AK132279; BAE21078.1; -; mRNA.
DR EMBL; AL607123; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC026442; AAH26442.1; ALT_INIT; mRNA.
DR EMBL; BC094629; AAH94629.1; ALT_INIT; mRNA.
DR EMBL; BC125606; AAI25607.1; -; mRNA.
DR EMBL; BC125608; AAI25609.1; -; mRNA.
DR RefSeq; NP_080246.1; NM_025970.3.
DR AlphaFoldDB; Q505B7; -.
DR SMR; Q505B7; -.
DR STRING; 10090.ENSMUSP00000120925; -.
DR PhosphoSitePlus; Q505B7; -.
DR EPD; Q505B7; -.
DR jPOST; Q505B7; -.
DR MaxQB; Q505B7; -.
DR PaxDb; Q505B7; -.
DR PeptideAtlas; Q505B7; -.
DR PRIDE; Q505B7; -.
DR ProteomicsDB; 283253; -. [Q505B7-1]
DR ProteomicsDB; 283254; -. [Q505B7-2]
DR Antibodypedia; 54681; 58 antibodies from 15 providers.
DR DNASU; 67106; -.
DR Ensembl; ENSMUST00000146767; ENSMUSP00000114628; ENSMUSG00000057572. [Q505B7-2]
DR GeneID; 67106; -.
DR KEGG; mmu:67106; -.
DR CTD; 339487; -.
DR MGI; MGI:1914356; Zbtb8os.
DR VEuPathDB; HostDB:ENSMUSG00000057572; -.
DR eggNOG; KOG4528; Eukaryota.
DR GeneTree; ENSGT00390000003245; -.
DR InParanoid; Q505B7; -.
DR OrthoDB; 1360804at2759; -.
DR PhylomeDB; Q505B7; -.
DR BioGRID-ORCS; 67106; 28 hits in 72 CRISPR screens.
DR ChiTaRS; Zbtb8os; mouse.
DR PRO; PR:Q505B7; -.
DR Proteomes; UP000000589; Chromosome 4.
DR RNAct; Q505B7; protein.
DR Bgee; ENSMUSG00000057572; Expressed in yolk sac and 77 other tissues.
DR ExpressionAtlas; Q505B7; baseline and differential.
DR Genevisible; Q505B7; MM.
DR GO; GO:0072669; C:tRNA-splicing ligase complex; ISS:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0006388; P:tRNA splicing, via endonucleolytic cleavage and ligation; ISS:UniProtKB.
DR Gene3D; 3.55.10.10; -; 1.
DR InterPro; IPR002804; Archease.
DR InterPro; IPR023572; Archease_dom.
DR InterPro; IPR036820; Archease_dom_sf.
DR PANTHER; PTHR12682; PTHR12682; 1.
DR Pfam; PF01951; Archease; 1.
DR SUPFAM; SSF69819; SSF69819; 1.
PE 1: Evidence at protein level;
KW Acetylation; Alternative splicing; Calcium; Metal-binding;
KW Reference proteome; tRNA processing.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:Q8IWT0"
FT CHAIN 2..168
FT /note="Protein archease"
FT /id="PRO_0000285951"
FT BINDING 39
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 167
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 168
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000250|UniProtKB:Q8IWT0"
FT VAR_SEQ 140..146
FT /note="GTEVKAI -> QSRLLAQ (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_024927"
FT VAR_SEQ 147..168
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_024928"
FT CONFLICT 1
FT /note="M -> S (in Ref. 4; AAH26442)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 168 AA; 19727 MW; 8D9FF80F91C8A66F CRC64;
MAQEEEDVRD YNLTEEQKAT KDKYPPVNRK YEYLDHTADV QLHAWGDTLE EAFEQCAMAM
FGYMTDTGTV EPLRTVEVET QGDDLQSLLF HFLDEWLYKF SADEYFIPRE VKVLNIDQKN
FKLRSIGWGE EFSLSKHPQG TEVKAITYSA MQVYNEEKPE VFFVIIDI
