ID   ARMX3_RAT               Reviewed;         379 AA.
AC   Q5XID7;
DT   20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT   23-NOV-2004, sequence version 1.
DT   27-MAR-2024, entry version 112.
DE   RecName: Full=Armadillo repeat-containing X-linked protein 3;
GN   Name=Armcx3;
OS   Rattus norvegicus (Rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Rattus.
OX   NCBI_TaxID=10116;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Heart;
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   [2]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-61 AND SER-67, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=22673903; DOI=10.1038/ncomms1871;
RA   Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA   Olsen J.V.;
RT   "Quantitative maps of protein phosphorylation sites across 14 different rat
RT   organs and tissues.";
RL   Nat. Commun. 3:876-876(2012).
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   -!- 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}.
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DR   EMBL; BC083747; AAH83747.1; -; mRNA.
DR   RefSeq; NP_001014295.1; NM_001014273.1.
DR   AlphaFoldDB; Q5XID7; -.
DR   SMR; Q5XID7; -.
DR   BioGRID; 266720; 1.
DR   STRING; 10116.ENSRNOP00000075527; -.
DR   iPTMnet; Q5XID7; -.
DR   PhosphoSitePlus; Q5XID7; -.
DR   PaxDb; 10116-ENSRNOP00000033859; -.
DR   Ensembl; ENSRNOT00000029664.6; ENSRNOP00000033859.4; ENSRNOG00000025730.7.
DR   Ensembl; ENSRNOT00000088760.2; ENSRNOP00000075527.2; ENSRNOG00000025730.7.
DR   Ensembl; ENSRNOT00000114177.1; ENSRNOP00000086605.1; ENSRNOG00000025730.7.
DR   Ensembl; ENSRNOT00000114255.1; ENSRNOP00000086584.1; ENSRNOG00000025730.7.
DR   Ensembl; ENSRNOT00055024822; ENSRNOP00055020286; ENSRNOG00055014461.
DR   Ensembl; ENSRNOT00055024832; ENSRNOP00055020290; ENSRNOG00055014461.
DR   Ensembl; ENSRNOT00060037691; ENSRNOP00060031083; ENSRNOG00060021764.
DR   Ensembl; ENSRNOT00060037710; ENSRNOP00060031102; ENSRNOG00060021764.
DR   Ensembl; ENSRNOT00065009085; ENSRNOP00065006474; ENSRNOG00065006014.
DR   Ensembl; ENSRNOT00065009088; ENSRNOP00065006477; ENSRNOG00065006014.
DR   GeneID; 367902; -.
DR   KEGG; rno:367902; -.
DR   UCSC; RGD:1549739; rat.
DR   AGR; RGD:1549739; -.
DR   CTD; 51566; -.
DR   RGD; 1549739; Armcx3.
DR   eggNOG; ENOG502TCDI; Eukaryota.
DR   GeneTree; ENSGT00940000162753; -.
DR   HOGENOM; CLU_037187_0_0_1; -.
DR   InParanoid; Q5XID7; -.
DR   OMA; DSKSIVW; -.
DR   OrthoDB; 2912889at2759; -.
DR   PhylomeDB; Q5XID7; -.
DR   TreeFam; TF335652; -.
DR   Reactome; R-RNO-9013404; RAC2 GTPase cycle.
DR   PRO; PR:Q5XID7; -.
DR   Proteomes; UP000002494; Chromosome X.
DR   Bgee; ENSRNOG00000025730; Expressed in cerebellum and 20 other cell types or tissues.
DR   ExpressionAtlas; Q5XID7; baseline and differential.
DR   GO; GO:1904115; C:axon cytoplasm; IEA:GOC.
DR   GO; GO:0005829; C:cytosol; ISO:RGD.
DR   GO; GO:0005741; C:mitochondrial outer membrane; ISO:RGD.
DR   GO; GO:0005739; C:mitochondrion; ISO:RGD.
DR   GO; GO:0005634; C:nucleus; ISO:RGD.
DR   GO; GO:0019896; P:axonal transport of mitochondrion; ISO:RGD.
DR   GO; GO:0007005; P:mitochondrion organization; ISO:RGD.
DR   GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; ISO:RGD.
DR   GO; GO:0008104; P:protein localization; ISO:RGD.
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; Q5XID7; RN.
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_0000191369"
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          34..69
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          89..98
FT                   /note="Nuclear localization signal"
FT                   /evidence="ECO:0000250|UniProtKB:Q8BHS6"
FT   MOD_RES         61
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:22673903"
FT   MOD_RES         67
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:22673903"
FT   MOD_RES         72
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9UH62"
FT   MOD_RES         110
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9UH62"
SQ   SEQUENCE   379 AA;  42553 MW;  E4EA20CAAF376842 CRC64;
     MGYARKVGWV TAGLVIGAGA CYCIYRLTRG RKQNKEKMAE GGPGDVEDAG DCSGARYNDW
     SDDDDDSNES KSIVWYPPWA RIGTEAGTRA RARARARATR ARRAVQKRAS PNSDDTVLSP
     QELQKVLCLV EMSEKPYILE AALIALGNNA AYAFNRDIIR DLGGLPIVAK ILNTRDPIVK
     EKALIVLNNL SVNAENQRRL KIYMNQVCDD TVTSRLNSSV QLAGLRLLTN MTVTNEYQHI
     LANSISDFFR LFSAGNEETK LQVLKLLLNL AENPAMTREL LGAHVPSSLG SLFNKKEYKE
     VILKLLSIFE NINDNFKWEE NEPAQNHFSE GSLFFFLKEF QVCADKVLGI ESHHDFQVRV
     KVGKFVTKLT ERMFPKSQE
//