ID   ARMC1_BOVIN             Reviewed;         282 AA.
AC   Q3ZBE1; Q5EAC8;
DT   27-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT   27-SEP-2005, sequence version 1.
DT   03-AUG-2022, entry version 93.
DE   RecName: Full=Armadillo repeat-containing protein 1;
GN   Name=ARMC1;
OS   Bos taurus (Bovine).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC   Bovinae; Bos.
OX   NCBI_TaxID=9913;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX   PubMed=16305752; DOI=10.1186/1471-2164-6-166;
RA   Harhay G.P., Sonstegard T.S., Keele J.W., Heaton M.P., Clawson M.L.,
RA   Snelling W.M., Wiedmann R.T., Van Tassell C.P., Smith T.P.L.;
RT   "Characterization of 954 bovine full-CDS cDNA sequences.";
RL   BMC Genomics 6:166-166(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=Crossbred X Angus; TISSUE=Ileum;
RG   NIH - Mammalian Gene Collection (MGC) project;
RL   Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: In association with mitochondrial contact site and cristae
CC       organizing system (MICOS) complex components and mitochondrial outer
CC       membrane sorting assembly machinery (SAM) complex components may
CC       regulate mitochondrial dynamics playing a role in determining
CC       mitochondrial length, distribution and motility.
CC       {ECO:0000250|UniProtKB:Q9NVT9}.
CC   -!- SUBUNIT: Interacts with mitochondrial contact site and cristae
CC       organizing system (MICOS) complex components IMMT/MIC60 and
CC       MICOS10/MIC10 (By similarity). Interacts with mitochondrial outer
CC       membrane sorting assembly machinery (SAM) complex components SAMM50 and
CC       MTX1 (By similarity). {ECO:0000250|UniProtKB:Q9NVT9}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q9NVT9}.
CC       Mitochondrion {ECO:0000250|UniProtKB:Q9NVT9}. Mitochondrion outer
CC       membrane {ECO:0000250|UniProtKB:Q9NVT9}. Note=Associates with the outer
CC       mitochondrion membrane, most likely through its C-terminus (By
CC       similarity). Not integrated into the mitochondrial outer membrane (By
CC       similarity). {ECO:0000250|UniProtKB:Q9NVT9}.
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DR   EMBL; BT020641; AAX08658.1; -; mRNA.
DR   EMBL; BC103407; AAI03408.1; -; mRNA.
DR   RefSeq; NP_001015594.2; NM_001015594.2.
DR   AlphaFoldDB; Q3ZBE1; -.
DR   SMR; Q3ZBE1; -.
DR   STRING; 9913.ENSBTAP00000021138; -.
DR   PaxDb; Q3ZBE1; -.
DR   PRIDE; Q3ZBE1; -.
DR   Ensembl; ENSBTAT00000021138; ENSBTAP00000021138; ENSBTAG00000015901.
DR   GeneID; 514000; -.
DR   KEGG; bta:514000; -.
DR   CTD; 55156; -.
DR   VEuPathDB; HostDB:ENSBTAG00000015901; -.
DR   VGNC; VGNC:26155; ARMC1.
DR   eggNOG; ENOG502QU5Q; Eukaryota.
DR   GeneTree; ENSGT00390000014100; -.
DR   HOGENOM; CLU_077781_0_0_1; -.
DR   InParanoid; Q3ZBE1; -.
DR   OMA; EMNSCRR; -.
DR   OrthoDB; 1490145at2759; -.
DR   TreeFam; TF316742; -.
DR   Proteomes; UP000009136; Chromosome 14.
DR   Bgee; ENSBTAG00000015901; Expressed in oocyte and 105 other tissues.
DR   GO; GO:0005829; C:cytosol; IEA:Ensembl.
DR   GO; GO:0005741; C:mitochondrial outer membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0046872; F:metal ion binding; IEA:InterPro.
DR   GO; GO:0048312; P:intracellular distribution of mitochondria; IEA:Ensembl.
DR   Gene3D; 1.25.10.10; -; 1.
DR   InterPro; IPR011989; ARM-like.
DR   InterPro; IPR016024; ARM-type_fold.
DR   InterPro; IPR000225; Armadillo.
DR   InterPro; IPR036163; HMA_dom_sf.
DR   InterPro; IPR016617; UCP013899_metal-bd.
DR   PANTHER; PTHR28592; PTHR28592; 1.
DR   Pfam; PF00514; Arm; 1.
DR   PIRSF; PIRSF013899; UCP013899; 1.
DR   SUPFAM; SSF48371; SSF48371; 1.
DR   SUPFAM; SSF55008; SSF55008; 1.
PE   2: Evidence at transcript level;
KW   Acetylation; Cytoplasm; Membrane; Mitochondrion;
KW   Mitochondrion outer membrane; Phosphoprotein; Reference proteome.
FT   CHAIN           1..282
FT                   /note="Armadillo repeat-containing protein 1"
FT                   /id="PRO_0000240881"
FT   REPEAT          39..81
FT                   /note="ARM"
FT   REGION          239..261
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        242..257
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         1
FT                   /note="N-acetylmethionine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9NVT9"
FT   MOD_RES         137
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9NVT9"
FT   MOD_RES         189
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9NVT9"
FT   MOD_RES         246
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9D7A8"
FT   MOD_RES         260
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9NVT9"
FT   MOD_RES         267
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9D7A8"
FT   CONFLICT        143
FT                   /note="K -> Q (in Ref. 1; AAX08658)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   282 AA;  31280 MW;  9A00F7D3087777E3 CRC64;
     MNSSSSTMNE EPDALSVVNQ LRDLAADPLN RRAIVQDQGC LPGLILFMDH PNPPVVHSAL
     LALRYLAECR ANREKMKGEL GMMLSLQNVI QKSTTPGETK LLASEIYDIL QSSNMADGDS
     FNEMNSRRRK AQFFLGTTNK RAKTVVLHID GLDDTSRRNL CEEALLKIKG VISFTFQMAV
     QRCVVRIRSD LKAEALASAI ASTKVMKAQQ VVKSESGEEM LVPFQDTPVE VEQNTELPDY
     LPEDESPTKE QDKAVSRVGS HPEGGASWLS TAANFLSRSF YW