ARMC1_MOUSE
ID ARMC1_MOUSE Reviewed; 282 AA.
AC Q9D7A8; Q8CBW1;
DT 27-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 141.
DE RecName: Full=Armadillo repeat-containing protein 1;
GN Name=Armc1;
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; TISSUE=Placenta, Tongue, and Urinary bladder;
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 MRNA].
RC STRAIN=C57BL/6J, and FVB/N; TISSUE=Kidney, and 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 [3]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain;
RX PubMed=16452087; DOI=10.1074/mcp.t500041-mcp200;
RA Trinidad J.C., Specht C.G., Thalhammer A., Schoepfer R., Burlingame A.L.;
RT "Comprehensive identification of phosphorylation sites in postsynaptic
RT density preparations.";
RL Mol. Cell. Proteomics 5:914-922(2006).
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-246 AND SER-267, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC Spleen, and 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).
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; AK009402; BAB26266.1; -; mRNA.
DR EMBL; AK034483; BAC28724.1; -; mRNA.
DR EMBL; AK079299; BAC37600.1; -; mRNA.
DR EMBL; AK082783; BAC38617.1; -; mRNA.
DR EMBL; AK144184; BAE25753.1; -; mRNA.
DR EMBL; AK145993; BAE26814.1; -; mRNA.
DR EMBL; AK167233; BAE39357.1; -; mRNA.
DR EMBL; BC021451; AAH21451.1; -; mRNA.
DR EMBL; BC051067; AAH51067.1; -; mRNA.
DR CCDS; CCDS17255.1; -.
DR RefSeq; NP_083116.1; NM_028840.2.
DR AlphaFoldDB; Q9D7A8; -.
DR SMR; Q9D7A8; -.
DR BioGRID; 216608; 1.
DR STRING; 10090.ENSMUSP00000029125; -.
DR iPTMnet; Q9D7A8; -.
DR PhosphoSitePlus; Q9D7A8; -.
DR SwissPalm; Q9D7A8; -.
DR EPD; Q9D7A8; -.
DR jPOST; Q9D7A8; -.
DR MaxQB; Q9D7A8; -.
DR PaxDb; Q9D7A8; -.
DR PeptideAtlas; Q9D7A8; -.
DR PRIDE; Q9D7A8; -.
DR ProteomicsDB; 277291; -.
DR Antibodypedia; 11918; 211 antibodies from 19 providers.
DR Ensembl; ENSMUST00000029125; ENSMUSP00000029125; ENSMUSG00000027599.
DR GeneID; 74252; -.
DR KEGG; mmu:74252; -.
DR UCSC; uc008oro.1; mouse.
DR CTD; 55156; -.
DR MGI; MGI:1921502; Armc1.
DR VEuPathDB; HostDB:ENSMUSG00000027599; -.
DR eggNOG; ENOG502QU5Q; Eukaryota.
DR GeneTree; ENSGT00390000014100; -.
DR HOGENOM; CLU_077781_0_0_1; -.
DR InParanoid; Q9D7A8; -.
DR OMA; EMNSCRR; -.
DR OrthoDB; 1490145at2759; -.
DR PhylomeDB; Q9D7A8; -.
DR TreeFam; TF316742; -.
DR BioGRID-ORCS; 74252; 2 hits in 56 CRISPR screens.
DR ChiTaRS; Armc1; mouse.
DR PRO; PR:Q9D7A8; -.
DR Proteomes; UP000000589; Chromosome 3.
DR RNAct; Q9D7A8; protein.
DR Bgee; ENSMUSG00000027599; Expressed in lateral septal nucleus and 256 other tissues.
DR Genevisible; Q9D7A8; MM.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0005741; C:mitochondrial outer membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005739; C:mitochondrion; HDA:MGI.
DR GO; GO:0046872; F:metal ion binding; IEA:InterPro.
DR GO; GO:0048312; P:intracellular distribution of mitochondria; ISO:MGI.
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 1: Evidence at protein 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_0000240883"
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:0007744|PubMed:21183079"
FT MOD_RES 260
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9NVT9"
FT MOD_RES 267
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT CONFLICT 135
FT /note="L -> W (in Ref. 1; BAC28724)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 282 AA; 31247 MW; F92D73386FA531BF CRC64;
MNSSSSTMNE EPDALSVVNQ LRDLAADPLN RRAIVQDQGC LPGLILFMDH PNPPVVHSAL
LALRYLAECR ANREKMKGEL GMMLSLQNVI QKTTTPGETK LLASEIYDIL QSSNLADGDS
FNEMNSRRRK AQFFLGTTNK RAKTVVLHID GLDDTSRRNL CEEALLKIKG VISFTFQMAV
QRCVVRIRSD LKAEALASAI ASTKVMKAQQ VVKSESGEEM LVPFQDAPVE VEENTELPDY
LPEDESPTKE QDKAVSRVGS HPEGGASWLS TAANFLSRSF YW
