ID ARMX3_HUMAN Reviewed; 379 AA. AC Q9UH62; Q53HC6; Q7LCF5; Q9NPE4; DT 20-DEC-2005, integrated into UniProtKB/Swiss-Prot. DT 01-MAY-2000, sequence version 1. DT 24-JAN-2024, entry version 168. DE RecName: Full=Armadillo repeat-containing X-linked protein 3; DE AltName: Full=ARM protein lost in epithelial cancers on chromosome X 3; DE Short=Protein ALEX3; GN Name=ARMCX3; Synonyms=ALEX3; ORFNames=BM-017, UNQ2517/PRO6007; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; OC Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RC TISSUE=Testis; RX PubMed=11162520; DOI=10.1006/bbrc.2000.4125; RA Kurochkin I.V., Yonemitsu N., Funahashi S., Nomura H.; RT "ALEX1, a novel human armadillo repeat protein that is expressed RT differentially in normal tissues and carcinomas."; RL Biochem. Biophys. Res. Commun. 280:340-347(2001). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA]. RC TISSUE=Kidney; RA Nicolas G., Galand C., Lecomte M.-C.; RT "Identification of a new protein as a putative binding partner of SH3 RT domain of non-erythroid alpha-spectrin (alpha-fodrin)."; RL Submitted (DEC-1999) to the EMBL/GenBank/DDBJ databases. RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Bone marrow; RX PubMed=11042152; DOI=10.1101/gr.140200; RA Zhang Q.-H., Ye M., Wu X.-Y., Ren S.-X., Zhao M., Zhao C.-J., Fu G., RA Shen Y., Fan H.-Y., Lu G., Zhong M., Xu X.-R., Han Z.-G., Zhang J.-W., RA Tao J., Huang Q.-H., Zhou J., Hu G.-X., Gu J., Chen S.-J., Chen Z.; RT "Cloning and functional analysis of cDNAs with open reading frames for 300 RT previously undefined genes expressed in CD34+ hematopoietic stem/progenitor RT cells."; RL Genome Res. 10:1546-1560(2000). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RX PubMed=12975309; DOI=10.1101/gr.1293003; RA Clark H.F., Gurney A.L., Abaya E., Baker K., Baldwin D.T., Brush J., RA Chen J., Chow B., Chui C., Crowley C., Currell B., Deuel B., Dowd P., RA Eaton D., Foster J.S., Grimaldi C., Gu Q., Hass P.E., Heldens S., Huang A., RA Kim H.S., Klimowski L., Jin Y., Johnson S., Lee J., Lewis L., Liao D., RA Mark M.R., Robbie E., Sanchez C., Schoenfeld J., Seshagiri S., Simmons L., RA Singh J., Smith V., Stinson J., Vagts A., Vandlen R.L., Watanabe C., RA Wieand D., Woods K., Xie M.-H., Yansura D.G., Yi S., Yu G., Yuan J., RA Zhang M., Zhang Z., Goddard A.D., Wood W.I., Godowski P.J., Gray A.M.; RT "The secreted protein discovery initiative (SPDI), a large-scale effort to RT identify novel human secreted and transmembrane proteins: a bioinformatics RT assessment."; RL Genome Res. 13:2265-2270(2003). RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Brain; RA Suzuki Y., Sugano S., Totoki Y., Toyoda A., Takeda T., Sakaki Y., RA Tanaka A., Yokoyama S.; RL Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases. RN [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Retina; RX PubMed=17974005; DOI=10.1186/1471-2164-8-399; RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U., RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D., RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A., RA Wiemann S., Schupp I.; RT "The full-ORF clone resource of the German cDNA consortium."; RL BMC Genomics 8:399-399(2007). RN [7] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=15772651; DOI=10.1038/nature03440; RA Ross M.T., Grafham D.V., Coffey A.J., Scherer S., McLay K., Muzny D., RA Platzer M., Howell G.R., Burrows C., Bird C.P., Frankish A., Lovell F.L., RA Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G., Jones M.C., RA Hurles M.E., Andrews T.D., Scott C.E., Searle S., Ramser J., Whittaker A., RA Deadman R., Carter N.P., Hunt S.E., Chen R., Cree A., Gunaratne P., RA Havlak P., Hodgson A., Metzker M.L., Richards S., Scott G., Steffen D., RA Sodergren E., Wheeler D.A., Worley K.C., Ainscough R., Ambrose K.D., RA Ansari-Lari M.A., Aradhya S., Ashwell R.I., Babbage A.K., Bagguley C.L., RA Ballabio A., Banerjee R., Barker G.E., Barlow K.F., Barrett I.P., RA Bates K.N., Beare D.M., Beasley H., Beasley O., Beck A., Bethel G., RA Blechschmidt K., Brady N., Bray-Allen S., Bridgeman A.M., Brown A.J., RA Brown M.J., Bonnin D., Bruford E.A., Buhay C., Burch P., Burford D., RA Burgess J., Burrill W., Burton J., Bye J.M., Carder C., Carrel L., RA Chako J., Chapman J.C., Chavez D., Chen E., Chen G., Chen Y., Chen Z., RA Chinault C., Ciccodicola A., Clark S.Y., Clarke G., Clee C.M., Clegg S., RA Clerc-Blankenburg K., Clifford K., Cobley V., Cole C.G., Conquer J.S., RA Corby N., Connor R.E., David R., Davies J., Davis C., Davis J., Delgado O., RA Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S., Draper H., RA Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I., Eades T., RA Ellwood M., Emery-Cohen A., Errington H., Evans K.L., Faulkner L., RA Francis F., Frankland J., Fraser A.E., Galgoczy P., Gilbert J., Gill R., RA Gloeckner G., Gregory S.G., Gribble S., Griffiths C., Grocock R., Gu Y., RA Gwilliam R., Hamilton C., Hart E.A., Hawes A., Heath P.D., Heitmann K., RA Hennig S., Hernandez J., Hinzmann B., Ho S., Hoffs M., Howden P.J., RA Huckle E.J., Hume J., Hunt P.J., Hunt A.R., Isherwood J., Jacob L., RA Johnson D., Jones S., de Jong P.J., Joseph S.S., Keenan S., Kelly S., RA Kershaw J.K., Khan Z., Kioschis P., Klages S., Knights A.J., Kosiura A., RA Kovar-Smith C., Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L., RA Liu W., Lloyd C., Lloyd D.M., Loulseged H., Loveland J.E., Lovell J.D., RA Lozado R., Lu J., Lyne R., Ma J., Maheshwari M., Matthews L.H., RA McDowall J., McLaren S., McMurray A., Meidl P., Meitinger T., Milne S., RA Miner G., Mistry S.L., Morgan M., Morris S., Mueller I., Mullikin J.C., RA Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N., Okwuonu G., Palmer S., RA Pandian R., Parker D., Parrish J., Pasternak S., Patel D., Pearce A.V., RA Pearson D.M., Pelan S.E., Perez L., Porter K.M., Ramsey Y., Reichwald K., RA Rhodes S., Ridler K.A., Schlessinger D., Schueler M.G., Sehra H.K., RA Shaw-Smith C., Shen H., Sheridan E.M., Shownkeen R., Skuce C.D., RA Smith M.L., Sotheran E.C., Steingruber H.E., Steward C.A., Storey R., RA Swann R.M., Swarbreck D., Tabor P.E., Taudien S., Taylor T., Teague B., RA Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S., Tromans A.C., RA d'Urso M., Verduzco D., Villasana D., Waldron L., Wall M., Wang Q., RA Warren J., Warry G.L., Wei X., West A., Whitehead S.L., Whiteley M.N., RA Wilkinson J.E., Willey D.L., Williams G., Williams L., Williamson A., RA Williamson H., Wilming L., Woodmansey R.L., Wray P.W., Yen J., Zhang J., RA Zhou J., Zoghbi H., Zorilla S., Buck D., Reinhardt R., Poustka A., RA Rosenthal A., Lehrach H., Meindl A., Minx P.J., Hillier L.W., Willard H.F., RA Wilson R.K., Waterston R.H., Rice C.M., Vaudin M., Coulson A., Nelson D.L., RA Weinstock G., Sulston J.E., Durbin R.M., Hubbard T., Gibbs R.A., Beck S., RA Rogers J., Bentley D.R.; RT "The DNA sequence of the human X chromosome."; RL Nature 434:325-337(2005). RN [8] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Skin; 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 [9] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-61 AND SER-67, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026; RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.; RT "Global, in vivo, and site-specific phosphorylation dynamics in signaling RT networks."; RL Cell 127:635-648(2006). RN [10] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-61, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Liver; RX PubMed=18318008; DOI=10.1002/pmic.200700884; RA Han G., Ye M., Zhou H., Jiang X., Feng S., Jiang X., Tian R., Wan D., RA Zou H., Gu J.; RT "Large-scale phosphoproteome analysis of human liver tissue by enrichment RT and fractionation of phosphopeptides with strong anion exchange RT chromatography."; RL Proteomics 8:1346-1361(2008). RN [11] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-61, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Leukemic T-cell; RX PubMed=19690332; DOI=10.1126/scisignal.2000007; RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., RA Rodionov V., Han D.K.; RT "Quantitative phosphoproteomic analysis of T cell receptor signaling RT reveals system-wide modulation of protein-protein interactions."; RL Sci. Signal. 2:RA46-RA46(2009). RN [12] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=21269460; DOI=10.1186/1752-0509-5-17; RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., RA Bennett K.L., Superti-Furga G., Colinge J.; RT "Initial characterization of the human central proteome."; RL BMC Syst. Biol. 5:17-17(2011). RN [13] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-61, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=21406692; DOI=10.1126/scisignal.2001570; RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.; RT "System-wide temporal characterization of the proteome and phosphoproteome RT of human embryonic stem cell differentiation."; RL Sci. Signal. 4:RS3-RS3(2011). RN [14] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-61; SER-72 AND SER-110, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma, and Erythroleukemia; RX PubMed=23186163; DOI=10.1021/pr300630k; RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J., RA Mohammed S.; RT "Toward a comprehensive characterization of a human cancer cell RT phosphoproteome."; RL J. Proteome Res. 12:260-271(2013). CC -!- FUNCTION: Regulates mitochondrial aggregation and transport in axons in CC living neurons. May link mitochondria to the TRAK2-kinesin motor CC complex via its interaction with Miro and TRAK2. Mitochondrial CC distribution and dynamics is regulated through ARMCX3 protein CC degradation, which is promoted by PCK and negatively regulated by WNT1. CC Enhances the SOX10-mediated transactivation of the neuronal CC acetylcholine receptor subunit alpha-3 and beta-4 subunit gene CC promoters. {ECO:0000250|UniProtKB:Q8BHS6}. CC -!- SUBUNIT: Interacts (via ARM domain) with MIRO1, MIRO2 and TRAK2. The CC interaction with Miro is calcium-dependent. Interacts with SOX10. CC {ECO:0000250|UniProtKB:Q8BHS6}. CC -!- INTERACTION: CC Q9UH62; Q08426: EHHADH; NbExp=3; IntAct=EBI-717832, EBI-2339219; CC Q9UH62; B3EWG5: FAM25C; NbExp=3; IntAct=EBI-717832, EBI-14240149; CC Q9UH62; Q9H063: MAF1; NbExp=3; IntAct=EBI-717832, EBI-720354; CC -!- SUBCELLULAR LOCATION: Mitochondrion outer membrane CC {ECO:0000250|UniProtKB:Q8BHS6}; Single-pass membrane protein CC {ECO:0000255}. Cytoplasm {ECO:0000250|UniProtKB:Q8BHS6}. Nucleus CC {ECO:0000250|UniProtKB:Q8BHS6}. CC -!- SIMILARITY: Belongs to the eutherian X-chromosome-specific Armcx CC family. {ECO:0000305}. CC -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology and CC Haematology; CC URL="https://atlasgeneticsoncology.org/gene/479/ALEX3Xq22"; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AB039669; BAA94602.1; -; mRNA. DR EMBL; AF211175; AAF24487.1; -; mRNA. DR EMBL; AF208859; AAF64273.1; -; mRNA. DR EMBL; AY359079; AAQ89438.1; -; mRNA. DR EMBL; AK222655; BAD96375.1; -; mRNA. DR EMBL; CR933656; CAI45955.1; -; mRNA. DR EMBL; AL121883; CAI42939.1; -; Genomic_DNA. DR EMBL; BC005194; AAH05194.1; -; mRNA. DR CCDS; CCDS14489.1; -. DR RefSeq; NP_057691.1; NM_016607.3. DR RefSeq; NP_808816.1; NM_177947.2. DR RefSeq; NP_808817.1; NM_177948.2. DR RefSeq; XP_005262198.1; XM_005262141.2. DR AlphaFoldDB; Q9UH62; -. DR SMR; Q9UH62; -. DR BioGRID; 119614; 132. DR IntAct; Q9UH62; 29. DR MINT; Q9UH62; -. DR STRING; 9606.ENSP00000340672; -. DR iPTMnet; Q9UH62; -. DR MetOSite; Q9UH62; -. DR PhosphoSitePlus; Q9UH62; -. DR SwissPalm; Q9UH62; -. DR BioMuta; ARMCX3; -. DR DMDM; 74753322; -. DR EPD; Q9UH62; -. DR jPOST; Q9UH62; -. DR MassIVE; Q9UH62; -. DR MaxQB; Q9UH62; -. DR PaxDb; 9606-ENSP00000340672; -. DR PeptideAtlas; Q9UH62; -. DR ProteomicsDB; 84277; -. DR Pumba; Q9UH62; -. DR Antibodypedia; 378; 264 antibodies from 29 providers. DR DNASU; 51566; -. DR Ensembl; ENST00000341189.8; ENSP00000340672.4; ENSG00000102401.20. DR Ensembl; ENST00000471229.7; ENSP00000454483.1; ENSG00000102401.20. DR Ensembl; ENST00000537169.1; ENSP00000439032.1; ENSG00000102401.20. DR GeneID; 51566; -. DR KEGG; hsa:51566; -. DR MANE-Select; ENST00000471229.7; ENSP00000454483.1; NM_177947.3; NP_808816.1. DR UCSC; uc004ehz.2; human. DR AGR; HGNC:24065; -. DR CTD; 51566; -. DR DisGeNET; 51566; -. DR GeneCards; ARMCX3; -. DR HGNC; HGNC:24065; ARMCX3. DR HPA; ENSG00000102401; Low tissue specificity. DR MIM; 300364; gene. DR neXtProt; NX_Q9UH62; -. DR OpenTargets; ENSG00000102401; -. DR PharmGKB; PA134977725; -. DR VEuPathDB; HostDB:ENSG00000102401; -. DR eggNOG; ENOG502TCDI; Eukaryota. DR GeneTree; ENSGT00940000162753; -. DR HOGENOM; CLU_037187_0_0_1; -. DR InParanoid; Q9UH62; -. DR OMA; DSKSIVW; -. DR OrthoDB; 2912889at2759; -. DR PhylomeDB; Q9UH62; -. DR TreeFam; TF335652; -. DR PathwayCommons; Q9UH62; -. DR Reactome; R-HSA-9013404; RAC2 GTPase cycle. DR SignaLink; Q9UH62; -. DR BioGRID-ORCS; 51566; 11 hits in 775 CRISPR screens. DR ChiTaRS; ARMCX3; human. DR GeneWiki; ARMCX3; -. DR GenomeRNAi; 51566; -. DR Pharos; Q9UH62; Tbio. DR PRO; PR:Q9UH62; -. DR Proteomes; UP000005640; Chromosome X. DR RNAct; Q9UH62; Protein. DR Bgee; ENSG00000102401; Expressed in lateral nuclear group of thalamus and 206 other cell types or tissues. DR ExpressionAtlas; Q9UH62; baseline and differential. DR Genevisible; Q9UH62; HS. DR GO; GO:1904115; C:axon cytoplasm; IEA:GOC. DR GO; GO:0005829; C:cytosol; IEA:Ensembl. DR GO; GO:0005741; C:mitochondrial outer membrane; IEA:UniProtKB-SubCell. DR GO; GO:0005739; C:mitochondrion; IBA:GO_Central. DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell. DR GO; GO:0019896; P:axonal transport of mitochondrion; IEA:Ensembl. DR GO; GO:0007005; P:mitochondrion organization; IEA:Ensembl. DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IEA:Ensembl. DR GO; GO:0008104; P:protein localization; IEA:Ensembl. 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:SF23; ARM_2 DOMAIN-CONTAINING PROTEIN; 1. DR PANTHER; PTHR15712; ARMADILLO REPEAT CONTAINING PROTEIN; 1. DR Pfam; PF04826; Arm_2; 1. DR SUPFAM; SSF48371; ARM repeat; 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_0000191366" FT TOPO_DOM 1..6 FT /note="Mitochondrial intermembrane" FT /evidence="ECO:0000250|UniProtKB:Q8BHS6" FT TRANSMEM 7..29 FT /note="Helical; Signal-anchor" FT /evidence="ECO:0000255" FT TOPO_DOM 30..379 FT /note="Cytoplasmic" FT /evidence="ECO:0000250|UniProtKB:Q8BHS6" 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" FT REGION 26..37 FT /note="Mitochondrion outer membrane (MOM)-targeting FT sequence" FT /evidence="ECO:0000305" FT REGION 89..98 FT /note="Nuclear localization signal" FT /evidence="ECO:0000250|UniProtKB:Q8BHS6" 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:17081983, FT ECO:0007744|PubMed:18318008, ECO:0007744|PubMed:19690332, FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163" FT MOD_RES 67 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:17081983" FT MOD_RES 72 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 110 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT CONFLICT 310 FT /note="E -> V (in Ref. 5; BAD96375)" FT /evidence="ECO:0000305" SQ SEQUENCE 379 AA; 42501 MW; B715D7F83DF4DFB0 CRC64; MGYARKVGWV TAGLVIGAGA CYCIYRLTRG RKQNKEKMAE GGSGDVDDAG DCSGARYNDW SDDDDDSNES KSIVWYPPWA RIGTEAGTRA RARARARATR ARRAVQKRAS PNSDDTVLSP QELQKVLCLV EMSEKPYILE AALIALGNNA AYAFNRDIIR DLGGLPIVAK ILNTRDPIVK EKALIVLNNL SVNAENQRRL KVYMNQVCDD TITSRLNSSV QLAGLRLLTN MTVTNEYQHM LANSISDFFR LFSAGNEETK LQVLKLLLNL AENPAMTREL LRAQVPSSLG SLFNKKENKE VILKLLVIFE NINDNFKWEE NEPTQNQFGE GSLFFFLKEF QVCADKVLGI ESHHDFLVKV KVGKFMAKLA EHMFPKSQE //