ARMX3_MOUSE
ID ARMX3_MOUSE Reviewed; 379 AA.
AC Q8BHS6; A2AKS4; Q91VP8; Q9DC32;
DT 20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 138.
DE RecName: Full=Armadillo repeat-containing X-linked protein 3;
GN Name=Armcx3; Synonyms=Alex3;
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 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=FVB/N; 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 [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-61, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT "Large-scale phosphorylation analysis of mouse liver.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN [5]
RP FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH SOX10.
RX PubMed=19304657; DOI=10.1074/jbc.m901177200;
RA Mou Z., Tapper A.R., Gardner P.D.;
RT "The armadillo repeat-containing protein, ARMCX3, physically and
RT functionally interacts with the developmental regulatory factor Sox10.";
RL J. Biol. Chem. 284:13629-13640(2009).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-61; SER-67 AND SER-110, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Kidney, Liver, Lung, Pancreas, 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).
RN [7]
RP FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND INTERACTION WITH
RP MIRO1; MIRO2 AND TRAK2.
RX PubMed=22569362; DOI=10.1038/ncomms1829;
RA Lopez-Domenech G., Serrat R., Mirra S., D'Aniello S., Somorjai I., Abad A.,
RA Vitureira N., Garcia-Arumi E., Alonso M.T., Rodriguez-Prados M.,
RA Burgaya F., Andreu A.L., Garcia-Sancho J., Trullas R., Garcia-Fernandez J.,
RA Soriano E.;
RT "The eutherian Armcx genes regulate mitochondrial trafficking in neurons
RT and interact with Miro and Trak2.";
RL Nat. Commun. 3:814-814(2012).
RN [8]
RP FUNCTION.
RX PubMed=23844091; DOI=10.1371/journal.pone.0067773;
RA Serrat R., Lopez-Domenech G., Mirra S., Quevedo M., Garcia-Fernandez J.,
RA Ulloa F., Burgaya F., Soriano E.;
RT "The non-canonical Wnt/PKC pathway regulates mitochondrial dynamics through
RT degradation of the arm-like domain-containing protein Alex3.";
RL PLoS ONE 8:E67773-E67773(2013).
CC -!- FUNCTION: Regulates mitochondrial aggregation and transport in axons in
CC living neurons (PubMed:22569362, PubMed:23844091). May link
CC mitochondria to the Trak2-kinesin motor complex via its interaction
CC with Miro and Trak2 (PubMed:22569362). Mitochondrial distribution and
CC dynamics is regulated through Armcx3 protein degradation, which is
CC promoted by PCK and negatively regulated by Wnt1 (PubMed:23844091).
CC Enhances the Sox10-mediated transactivation of the neuronal
CC acetylcholine receptor subunit alpha-3 and beta-4 subunit gene
CC promoters (PubMed:19304657). {ECO:0000269|PubMed:19304657,
CC ECO:0000269|PubMed:22569362, ECO:0000269|PubMed:23844091}.
CC -!- SUBUNIT: Interacts (via ARM domain) with MIRO1, MIRO2 and TRAK2. The
CC interaction with Miro is calcium-dependent (PubMed:22569362). Interacts
CC with Sox10 (PubMed:19304657). {ECO:0000269|PubMed:19304657,
CC ECO:0000269|PubMed:22569362}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion outer membrane
CC {ECO:0000269|PubMed:19304657, ECO:0000269|PubMed:22569362}; Single-pass
CC membrane protein {ECO:0000255}. Cytoplasm
CC {ECO:0000269|PubMed:22569362}. Nucleus {ECO:0000269|PubMed:22569362}.
CC -!- TISSUE SPECIFICITY: Highly expressed in the developing neural tissues,
CC neural crest derivatives and hind limbs. Also widely expressed in the
CC adult nervous tissue, especially in the forebrain, including the
CC cerebral cortex, hippocampus and thalamus.
CC {ECO:0000269|PubMed:22569362}.
CC -!- SIMILARITY: Belongs to the eutherian X-chromosome-specific Armcx
CC family. {ECO:0000305}.
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DR EMBL; AK004598; BAB23399.1; -; mRNA.
DR EMBL; AK030729; BAC27102.1; -; mRNA.
DR EMBL; AL772348; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC011101; AAH11101.1; -; mRNA.
DR EMBL; BC051113; AAH51113.1; -; mRNA.
DR CCDS; CCDS30400.1; -.
DR RefSeq; NP_082146.2; NM_027870.3.
DR RefSeq; XP_006528672.1; XM_006528609.2.
DR RefSeq; XP_017174115.1; XM_017318626.1.
DR AlphaFoldDB; Q8BHS6; -.
DR SMR; Q8BHS6; -.
DR BioGRID; 214867; 4.
DR STRING; 10090.ENSMUSP00000080518; -.
DR iPTMnet; Q8BHS6; -.
DR PhosphoSitePlus; Q8BHS6; -.
DR EPD; Q8BHS6; -.
DR jPOST; Q8BHS6; -.
DR MaxQB; Q8BHS6; -.
DR PaxDb; Q8BHS6; -.
DR PeptideAtlas; Q8BHS6; -.
DR PRIDE; Q8BHS6; -.
DR ProteomicsDB; 277306; -.
DR Antibodypedia; 378; 247 antibodies from 29 providers.
DR DNASU; 71703; -.
DR Ensembl; ENSMUST00000081834; ENSMUSP00000080518; ENSMUSG00000049047.
DR Ensembl; ENSMUST00000086880; ENSMUSP00000084093; ENSMUSG00000049047.
DR Ensembl; ENSMUST00000086884; ENSMUSP00000084097; ENSMUSG00000049047.
DR GeneID; 71703; -.
DR KEGG; mmu:71703; -.
DR UCSC; uc009ugo.2; mouse.
DR CTD; 51566; -.
DR MGI; MGI:1918953; Armcx3.
DR VEuPathDB; HostDB:ENSMUSG00000049047; -.
DR eggNOG; ENOG502TCDI; Eukaryota.
DR GeneTree; ENSGT00940000162753; -.
DR HOGENOM; CLU_037187_0_0_1; -.
DR InParanoid; Q8BHS6; -.
DR OMA; DSKSIVW; -.
DR OrthoDB; 860703at2759; -.
DR PhylomeDB; Q8BHS6; -.
DR TreeFam; TF335652; -.
DR Reactome; R-MMU-9013404; RAC2 GTPase cycle.
DR BioGRID-ORCS; 71703; 2 hits in 74 CRISPR screens.
DR ChiTaRS; Armcx3; mouse.
DR PRO; PR:Q8BHS6; -.
DR Proteomes; UP000000589; Chromosome X.
DR RNAct; Q8BHS6; protein.
DR Bgee; ENSMUSG00000049047; Expressed in dentate gyrus of hippocampal formation granule cell and 68 other tissues.
DR Genevisible; Q8BHS6; MM.
DR GO; GO:1904115; C:axon cytoplasm; IEA:GOC.
DR GO; GO:0005829; C:cytosol; IDA:MGI.
DR GO; GO:0031307; C:integral component of mitochondrial outer membrane; IDA:MGI.
DR GO; GO:0005739; C:mitochondrion; IDA:MGI.
DR GO; GO:0005634; C:nucleus; IDA:MGI.
DR GO; GO:0019896; P:axonal transport of mitochondrion; IDA:MGI.
DR GO; GO:0007005; P:mitochondrion organization; IDA:MGI.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IGI:MGI.
DR GO; GO:0008104; P:protein localization; IDA:MGI.
DR Gene3D; 1.25.10.10; -; 2.
DR InterPro; IPR011989; ARM-like.
DR InterPro; IPR006911; ARM-rpt_dom.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR000225; Armadillo.
DR Pfam; PF04826; Arm_2; 1.
DR SUPFAM; SSF48371; SSF48371; 1.
DR PROSITE; PS50176; ARM_REPEAT; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; Membrane; Mitochondrion; Mitochondrion outer membrane; Nucleus;
KW Phosphoprotein; Reference proteome; Repeat; Signal-anchor; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..379
FT /note="Armadillo repeat-containing X-linked protein 3"
FT /id="PRO_0000191368"
FT TOPO_DOM 1..6
FT /note="Mitochondrial intermembrane"
FT /evidence="ECO:0000305|PubMed:19304657"
FT TRANSMEM 7..29
FT /note="Helical; Signal-anchor"
FT /evidence="ECO:0000255"
FT TOPO_DOM 30..379
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:19304657"
FT REPEAT 111..151
FT /note="ARM 1"
FT /evidence="ECO:0000255"
FT REPEAT 153..192
FT /note="ARM 2"
FT /evidence="ECO:0000255"
FT REPEAT 233..272
FT /note="ARM 3"
FT /evidence="ECO:0000255"
FT REGION 1..6
FT /note="Mitochondrion outer membrane (MOM)-targeting
FT sequence"
FT /evidence="ECO:0000305|PubMed:22569362"
FT REGION 26..37
FT /note="Mitochondrion outer membrane (MOM)-targeting
FT sequence"
FT /evidence="ECO:0000305|PubMed:22569362"
FT REGION 89..98
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000305|PubMed:23844091"
FT REGION 95..116
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 61
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 67
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 72
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9UH62"
FT MOD_RES 110
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT CONFLICT 4
FT /note="A -> T (in Ref. 3; AAH11101)"
FT /evidence="ECO:0000305"
FT CONFLICT 53
FT /note="S -> P (in Ref. 1; BAB23399)"
FT /evidence="ECO:0000305"
FT CONFLICT 68
FT /note="N -> Y (in Ref. 1; BAB23399)"
FT /evidence="ECO:0000305"
FT CONFLICT 333
FT /note="L -> P (in Ref. 1; BAB23399)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 379 AA; 42620 MW; 6EA7B87544652055 CRC64;
MGYARKVGWV TAGLVIGAGA CYCIYRLTRG RKQNKEKMAE GGSGDVDDAG DCSGARYNDW
SDDDDDSNES KSIVWYPPWA RIGTEAGTRA RARARARATR ARRAVQKRAS PNSDDTVLSP
QELQKVLCLV EMSEKPYILE AALIALGNNA AYAFNRDIIR DLGGLPIVAK ILNTRDPIVK
EKALIVLNNL SVNAENQRRL KVYMNQVCDD TVTSRLNSSV QLAGLRLLTN MTVTNEYQHI
LANSISDFFR LFSAGNEETK LQVLKLLLNL AENPAMTREL LRAQVPSSLG SLFNKKEYKE
VILKLLIIFE NINDNFKWEE NEPAQNHFSE GSLFFFLKEF QVCADKVLGI ESRHDFQVRV
KVGKFVAKLT ERMFPKSQE
