MTX2_MOUSE
ID MTX2_MOUSE Reviewed; 263 AA.
AC O88441; Q3TFR2;
DT 21-FEB-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1998, sequence version 1.
DT 03-AUG-2022, entry version 158.
DE RecName: Full=Metaxin-2;
DE AltName: Full=Mitochondrial outer membrane import complex protein 2;
GN Name=Mtx2; ORFNames=MNCb-0780;
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], INTERACTION WITH MTX1, SUBCELLULAR LOCATION,
RP AND FUNCTION.
RX PubMed=10381257;
RX DOI=10.1002/(sici)1097-4644(19990701)74:1<11::aid-jcb2>3.0.co;2-v;
RA Armstrong L.C., Saenz A.J., Bornstein P.;
RT "Metaxin 1 interacts with metaxin 2, a novel related protein associated
RT with the mammalian mitochondrial outer membrane.";
RL J. Cell. Biochem. 74:11-22(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Brain;
RA Osada N., Kusuda J., Tanuma R., Ito A., Hirata M., Sugano S., Hashimoto K.;
RT "Isolation of full-length cDNA clones from mouse brain cDNA library made by
RT oligo-capping method.";
RL Submitted (APR-2000) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=BALB/cJ, C57BL/6J, and NOD; TISSUE=Kidney, and Thymus;
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=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 [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC Spleen, and 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: Involved in transport of proteins into the mitochondrion.
CC {ECO:0000269|PubMed:10381257}.
CC -!- SUBUNIT: Interacts with MTX1/metaxin-1. Associates with the
CC mitochondrial contact site and cristae organizing system (MICOS)
CC complex, composed of at least MICOS10/MIC10, CHCHD3/MIC19,
CC CHCHD6/MIC25, APOOL/MIC27, IMMT/MIC60, APOO/MIC23/MIC26 and QIL1/MIC13.
CC This complex was also known under the names MINOS or MitOS complex. The
CC MICOS complex associates with mitochondrial outer membrane proteins
CC SAMM50, MTX1 and MTX2 (together described as components of the
CC mitochondrial outer membrane sorting assembly machinery (SAM) complex)
CC and DNAJC11, mitochondrial inner membrane protein TMEM11 and with
CC HSPA9. The MICOS and SAM complexes together with DNAJC11 are part of a
CC large protein complex spanning both membranes termed the mitochondrial
CC intermembrane space bridging (MIB) complex (By similarity).
CC {ECO:0000250|UniProtKB:O75431, ECO:0000269|PubMed:10381257}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion outer membrane
CC {ECO:0000269|PubMed:10381257}. Mitochondrion
CC {ECO:0000250|UniProtKB:O75431}.
CC -!- SIMILARITY: Belongs to the metaxin family. {ECO:0000305}.
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DR EMBL; AF053550; AAC25104.1; -; mRNA.
DR EMBL; AB041562; BAA95046.1; -; mRNA.
DR EMBL; AK087933; BAC40046.1; -; mRNA.
DR EMBL; AK168000; BAE39989.1; -; mRNA.
DR EMBL; AK169048; BAE40836.1; -; mRNA.
DR EMBL; BC006641; AAH06641.1; -; mRNA.
DR CCDS; CCDS16148.1; -.
DR RefSeq; NP_058084.3; NM_016804.4.
DR AlphaFoldDB; O88441; -.
DR SMR; O88441; -.
DR BioGRID; 207298; 24.
DR CORUM; O88441; -.
DR IntAct; O88441; 25.
DR STRING; 10090.ENSMUSP00000028511; -.
DR iPTMnet; O88441; -.
DR PhosphoSitePlus; O88441; -.
DR SwissPalm; O88441; -.
DR EPD; O88441; -.
DR jPOST; O88441; -.
DR MaxQB; O88441; -.
DR PaxDb; O88441; -.
DR PeptideAtlas; O88441; -.
DR PRIDE; O88441; -.
DR ProteomicsDB; 291457; -.
DR TopDownProteomics; O88441; -.
DR Antibodypedia; 33917; 184 antibodies from 26 providers.
DR DNASU; 53375; -.
DR Ensembl; ENSMUST00000028511; ENSMUSP00000028511; ENSMUSG00000027099.
DR GeneID; 53375; -.
DR KEGG; mmu:53375; -.
DR UCSC; uc008kej.2; mouse.
DR CTD; 10651; -.
DR MGI; MGI:1859652; Mtx2.
DR VEuPathDB; HostDB:ENSMUSG00000027099; -.
DR eggNOG; KOG3027; Eukaryota.
DR GeneTree; ENSGT00950000182919; -.
DR HOGENOM; CLU_044137_6_0_1; -.
DR InParanoid; O88441; -.
DR OMA; PWPENAA; -.
DR OrthoDB; 1219712at2759; -.
DR PhylomeDB; O88441; -.
DR TreeFam; TF313422; -.
DR BioGRID-ORCS; 53375; 13 hits in 73 CRISPR screens.
DR ChiTaRS; Mtx2; mouse.
DR PRO; PR:O88441; -.
DR Proteomes; UP000000589; Chromosome 2.
DR RNAct; O88441; protein.
DR Bgee; ENSMUSG00000027099; Expressed in embryonic post-anal tail and 258 other tissues.
DR Genevisible; O88441; MM.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005739; C:mitochondrion; HDA:MGI.
DR GO; GO:0005730; C:nucleolus; ISO:MGI.
DR GO; GO:0001401; C:SAM complex; ISO:MGI.
DR GO; GO:0006839; P:mitochondrial transport; ISS:UniProtKB.
DR GO; GO:0007005; P:mitochondrion organization; IBA:GO_Central.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR InterPro; IPR036282; Glutathione-S-Trfase_C_sf.
DR InterPro; IPR040079; Glutathione_S-Trfase.
DR InterPro; IPR033468; Metaxin_GST.
DR InterPro; IPR019564; Sam37/metaxin_N.
DR Pfam; PF17171; GST_C_6; 1.
DR Pfam; PF10568; Tom37; 1.
DR SFLD; SFLDS00019; Glutathione_Transferase_(cytos; 1.
DR SUPFAM; SSF47616; SSF47616; 1.
PE 1: Evidence at protein level;
KW Acetylation; Membrane; Mitochondrion; Mitochondrion outer membrane;
KW Protein transport; Reference proteome; Transport.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:O75431"
FT CHAIN 2..263
FT /note="Metaxin-2"
FT /id="PRO_0000220996"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0000250|UniProtKB:O75431"
SQ SEQUENCE 263 AA; 29758 MW; D77DE08F05DF7C11 CRC64;
MSLVAEAFVS QIAATEPWPE NATLYQQLRG EQILLSDNAA SLAVQAFLQM CNLPVKVVCR
ANAEYMSPSG KVPFIHVGNQ VVSELGPIVQ FVKAKGHSLS DGLDEVQKAE MKAYMELVNN
MLLTAELYLQ WCDEATVGEI TIARYGSPYP WPLNHILAYQ KQWEVKRKMK AIGWGNKTLD
QVLEDVDQCC QALSQRLGTQ PYFFNKQPTE LDALVFGHLY TILTTQLTSD ELSEKVKNYS
NLLAFCRRIE QHYFEDWGKG RLS
