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   27-MAR-2024, entry version 146.
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.ENSMUSP00000084097; -.
DR   iPTMnet; Q8BHS6; -.
DR   PhosphoSitePlus; Q8BHS6; -.
DR   EPD; Q8BHS6; -.
DR   jPOST; Q8BHS6; -.
DR   MaxQB; Q8BHS6; -.
DR   PaxDb; 10090-ENSMUSP00000080518; -.
DR   PeptideAtlas; Q8BHS6; -.
DR   ProteomicsDB; 277306; -.
DR   Pumba; Q8BHS6; -.
DR   Antibodypedia; 378; 264 antibodies from 29 providers.
DR   DNASU; 71703; -.
DR   Ensembl; ENSMUST00000081834.10; ENSMUSP00000080518.4; ENSMUSG00000049047.12.
DR   Ensembl; ENSMUST00000086880.11; ENSMUSP00000084093.5; ENSMUSG00000049047.12.
DR   Ensembl; ENSMUST00000086884.5; ENSMUSP00000084097.5; ENSMUSG00000049047.12.
DR   GeneID; 71703; -.
DR   KEGG; mmu:71703; -.
DR   UCSC; uc009ugo.2; mouse.
DR   AGR; MGI:1918953; -.
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; 2912889at2759; -.
DR   PhylomeDB; Q8BHS6; -.
DR   TreeFam; TF335652; -.
DR   Reactome; R-MMU-9013404; RAC2 GTPase cycle.
DR   BioGRID-ORCS; 71703; 2 hits in 79 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 70 other cell types or tissues.
DR   GO; GO:1904115; C:axon cytoplasm; IEA:GOC.
DR   GO; GO:0005829; C:cytosol; IDA:MGI.
DR   GO; GO:0005741; C: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; Leucine-rich Repeat Variant; 2.
DR   InterPro; IPR011989; ARM-like.
DR   InterPro; IPR006911; ARM-rpt_dom.
DR   InterPro; IPR016024; ARM-type_fold.
DR   InterPro; IPR000225; Armadillo.
DR   PANTHER; PTHR15712; ARMADILLO REPEAT CONTAINING PROTEIN; 1.
DR   PANTHER; PTHR15712:SF8; ARMADILLO REPEAT-CONTAINING X-LINKED PROTEIN 3; 1.
DR   Pfam; PF04826; Arm_2; 1.
DR   SUPFAM; SSF48371; ARM repeat; 1.
DR   PROSITE; PS50176; ARM_REPEAT; 1.
DR   Genevisible; Q8BHS6; MM.
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
//