ATP23_MOUSE
ID ATP23_MOUSE Reviewed; 201 AA.
AC Q9CWQ3;
DT 29-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 122.
DE RecName: Full=Mitochondrial inner membrane protease ATP23 homolog;
DE EC=3.4.24.-;
DE AltName: Full=XRCC6-binding protein 1;
GN Name=Atp23; Synonyms=Xrcc6bp1;
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;
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 MRNA].
RC STRAIN=C57BL/6J; TISSUE=Mammary gland;
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 [3]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Heart, and Kidney;
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 -!- SUBUNIT: Interacts with XRCC6. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the peptidase M76 family. {ECO:0000305}.
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DR EMBL; AK010471; BAB26964.1; -; mRNA.
DR EMBL; BC030630; AAH30630.1; -; mRNA.
DR CCDS; CCDS24220.1; -.
DR RefSeq; NP_081134.2; NM_026858.3.
DR AlphaFoldDB; Q9CWQ3; -.
DR STRING; 10090.ENSMUSP00000128382; -.
DR MEROPS; M76.001; -.
DR PhosphoSitePlus; Q9CWQ3; -.
DR MaxQB; Q9CWQ3; -.
DR PaxDb; Q9CWQ3; -.
DR PeptideAtlas; Q9CWQ3; -.
DR PRIDE; Q9CWQ3; -.
DR ProteomicsDB; 277073; -.
DR Antibodypedia; 28994; 98 antibodies from 17 providers.
DR Ensembl; ENSMUST00000026504; ENSMUSP00000026504; ENSMUSG00000025436.
DR GeneID; 68876; -.
DR KEGG; mmu:68876; -.
DR UCSC; uc007hhf.2; mouse.
DR CTD; 91419; -.
DR MGI; MGI:1916984; Atp23.
DR VEuPathDB; HostDB:ENSMUSG00000025436; -.
DR eggNOG; KOG3314; Eukaryota.
DR GeneTree; ENSGT00390000010948; -.
DR InParanoid; Q9CWQ3; -.
DR OrthoDB; 1288109at2759; -.
DR PhylomeDB; Q9CWQ3; -.
DR BioGRID-ORCS; 68876; 1 hit in 73 CRISPR screens.
DR ChiTaRS; Xrcc6bp1; mouse.
DR PRO; PR:Q9CWQ3; -.
DR Proteomes; UP000000589; Chromosome 10.
DR RNAct; Q9CWQ3; protein.
DR Bgee; ENSMUSG00000025436; Expressed in yolk sac and 157 other tissues.
DR ExpressionAtlas; Q9CWQ3; baseline and differential.
DR Genevisible; Q9CWQ3; MM.
DR GO; GO:0030054; C:cell junction; ISO:MGI.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0031314; C:extrinsic component of mitochondrial inner membrane; IBA:GO_Central.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; ISO:MGI.
DR GO; GO:0005886; C:plasma membrane; ISO:MGI.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro.
DR GO; GO:0034982; P:mitochondrial protein processing; IBA:GO_Central.
DR GO; GO:0033615; P:mitochondrial proton-transporting ATP synthase complex assembly; IBA:GO_Central.
DR InterPro; IPR019165; Peptidase_M76_ATP23.
DR PANTHER; PTHR21711; PTHR21711; 1.
DR Pfam; PF09768; Peptidase_M76; 1.
DR PROSITE; PS00142; ZINC_PROTEASE; 1.
PE 1: Evidence at protein level;
KW Hydrolase; Metal-binding; Metalloprotease; Protease; Reference proteome.
FT CHAIN 1..201
FT /note="Mitochondrial inner membrane protease ATP23 homolog"
FT /id="PRO_0000330345"
FT REGION 1..40
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 126
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT BINDING 125
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 129
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
SQ SEQUENCE 201 AA; 21710 MW; C751144473BFF7D3 CRC64;
MAGAPGGGEL GPAAGEPLLQ RPDSGQGSPE PPAHGKPQQG FLSSLFTRDQ SCPLMLQKTL
DTNPYVKLLL DAMKHSGCAV NRGRHFSCEV CDGNVSGGFD ASTSQIVLCE NNIRNQAHMG
RVVTHELIHA FDHCRAHVHW FTNIRHLACS EIRAASLSGD CSLVNELFRL RFGLKQHHQI
ETSCVSRPAM NSQSCLGLVS A
