ARMC1_HUMAN
ID ARMC1_HUMAN Reviewed; 282 AA.
AC Q9NVT9; B4E2W7; Q9H018; Q9H820;
DT 27-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 155.
DE RecName: Full=Armadillo repeat-containing protein 1;
GN Name=ARMC1; Synonyms=ARCP;
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 [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Stomach;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16421571; DOI=10.1038/nature04406;
RA Nusbaum C., Mikkelsen T.S., Zody M.C., Asakawa S., Taudien S., Garber M.,
RA Kodira C.D., Schueler M.G., Shimizu A., Whittaker C.A., Chang J.L.,
RA Cuomo C.A., Dewar K., FitzGerald M.G., Yang X., Allen N.R., Anderson S.,
RA Asakawa T., Blechschmidt K., Bloom T., Borowsky M.L., Butler J., Cook A.,
RA Corum B., DeArellano K., DeCaprio D., Dooley K.T., Dorris L. III,
RA Engels R., Gloeckner G., Hafez N., Hagopian D.S., Hall J.L., Ishikawa S.K.,
RA Jaffe D.B., Kamat A., Kudoh J., Lehmann R., Lokitsang T., Macdonald P.,
RA Major J.E., Matthews C.D., Mauceli E., Menzel U., Mihalev A.H.,
RA Minoshima S., Murayama Y., Naylor J.W., Nicol R., Nguyen C., O'Leary S.B.,
RA O'Neill K., Parker S.C.J., Polley A., Raymond C.K., Reichwald K.,
RA Rodriguez J., Sasaki T., Schilhabel M., Siddiqui R., Smith C.L.,
RA Sneddon T.P., Talamas J.A., Tenzin P., Topham K., Venkataraman V., Wen G.,
RA Yamazaki S., Young S.K., Zeng Q., Zimmer A.R., Rosenthal A., Birren B.W.,
RA Platzer M., Shimizu N., Lander E.S.;
RT "DNA sequence and analysis of human chromosome 8.";
RL Nature 439:331-335(2006).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Placenta;
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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 78-282 (ISOFORM 1).
RC TISSUE=Lymph node;
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 [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-260, 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 [7]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [8]
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 [9]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-137; SER-189 AND SER-260, 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).
RN [11]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25944712; DOI=10.1002/pmic.201400617;
RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D.,
RA Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
RT "N-terminome analysis of the human mitochondrial proteome.";
RL Proteomics 15:2519-2524(2015).
RN [12]
RP FUNCTION, INTERACTION WITH IMMT; MICOS10; SAMM50 AND MTX1, AND SUBCELLULAR
RP LOCATION.
RX PubMed=31644573; DOI=10.1371/journal.pone.0218303;
RA Wagner F., Kunz T.C., Chowdhury S.R., Thiede B., Fraunholz M., Eger D.,
RA Kozjak-Pavlovic V.;
RT "Armadillo repeat-containing protein 1 is a dual localization protein
RT associated with mitochondrial intermembrane space bridging complex.";
RL PLoS ONE 14:e0218303-e0218303(2019).
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:0000269|PubMed:31644573}.
CC -!- SUBUNIT: Interacts with mitochondrial contact site and cristae
CC organizing system (MICOS) complex components IMMT/MIC60 and
CC MICOS10/MIC10 (PubMed:31644573). Interacts with mitochondrial outer
CC membrane sorting assembly machinery (SAM) complex components SAMM50 and
CC MTX1 (PubMed:31644573). {ECO:0000269|PubMed:31644573}.
CC -!- INTERACTION:
CC Q9NVT9; Q9H019: MTFR1L; NbExp=7; IntAct=EBI-3506974, EBI-2824497;
CC Q9NVT9; Q9Y225-2: RNF24; NbExp=3; IntAct=EBI-3506974, EBI-13044680;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:31644573}.
CC Mitochondrion {ECO:0000269|PubMed:31644573}. Mitochondrion outer
CC membrane {ECO:0000269|PubMed:31644573}. Note=Associates with the outer
CC mitochondrion membrane, most likely through its C-terminus
CC (PubMed:31644573). Not integrated into the mitochondrial outer membrane
CC (PubMed:31644573). {ECO:0000269|PubMed:31644573}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9NVT9-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9NVT9-2; Sequence=VSP_054645, VSP_054646;
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DR EMBL; AK001373; BAA91656.1; -; mRNA.
DR EMBL; AK024053; BAB14803.1; -; mRNA.
DR EMBL; AK304463; BAG65279.1; -; mRNA.
DR EMBL; AC055822; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC100814; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC011607; AAH11607.1; -; mRNA.
DR EMBL; AL512767; CAC21684.1; -; mRNA.
DR CCDS; CCDS6181.1; -. [Q9NVT9-1]
DR CCDS; CCDS69490.1; -. [Q9NVT9-2]
DR RefSeq; NP_001273631.1; NM_001286702.1. [Q9NVT9-2]
DR RefSeq; NP_060590.1; NM_018120.5. [Q9NVT9-1]
DR RefSeq; XP_016869094.1; XM_017013605.1. [Q9NVT9-1]
DR AlphaFoldDB; Q9NVT9; -.
DR SMR; Q9NVT9; -.
DR BioGRID; 120458; 57.
DR IntAct; Q9NVT9; 30.
DR MINT; Q9NVT9; -.
DR STRING; 9606.ENSP00000276569; -.
DR GlyGen; Q9NVT9; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q9NVT9; -.
DR PhosphoSitePlus; Q9NVT9; -.
DR SwissPalm; Q9NVT9; -.
DR BioMuta; ARMC1; -.
DR DMDM; 74734555; -.
DR EPD; Q9NVT9; -.
DR jPOST; Q9NVT9; -.
DR MassIVE; Q9NVT9; -.
DR MaxQB; Q9NVT9; -.
DR PaxDb; Q9NVT9; -.
DR PeptideAtlas; Q9NVT9; -.
DR PRIDE; Q9NVT9; -.
DR ProteomicsDB; 5860; -.
DR ProteomicsDB; 82856; -. [Q9NVT9-1]
DR Antibodypedia; 11918; 211 antibodies from 19 providers.
DR DNASU; 55156; -.
DR Ensembl; ENST00000276569.8; ENSP00000276569.3; ENSG00000104442.10. [Q9NVT9-1]
DR Ensembl; ENST00000458464.3; ENSP00000388572.2; ENSG00000104442.10. [Q9NVT9-2]
DR GeneID; 55156; -.
DR KEGG; hsa:55156; -.
DR MANE-Select; ENST00000276569.8; ENSP00000276569.3; NM_018120.6; NP_060590.1.
DR UCSC; uc003xvl.4; human. [Q9NVT9-1]
DR CTD; 55156; -.
DR GeneCards; ARMC1; -.
DR HGNC; HGNC:17684; ARMC1.
DR HPA; ENSG00000104442; Low tissue specificity.
DR neXtProt; NX_Q9NVT9; -.
DR OpenTargets; ENSG00000104442; -.
DR PharmGKB; PA134882659; -.
DR VEuPathDB; HostDB:ENSG00000104442; -.
DR eggNOG; ENOG502QU5Q; Eukaryota.
DR GeneTree; ENSGT00390000014100; -.
DR HOGENOM; CLU_077781_0_0_1; -.
DR InParanoid; Q9NVT9; -.
DR OMA; EMNSCRR; -.
DR OrthoDB; 1490145at2759; -.
DR PhylomeDB; Q9NVT9; -.
DR TreeFam; TF316742; -.
DR PathwayCommons; Q9NVT9; -.
DR SignaLink; Q9NVT9; -.
DR BioGRID-ORCS; 55156; 18 hits in 1074 CRISPR screens.
DR ChiTaRS; ARMC1; human.
DR GenomeRNAi; 55156; -.
DR Pharos; Q9NVT9; Tbio.
DR PRO; PR:Q9NVT9; -.
DR Proteomes; UP000005640; Chromosome 8.
DR RNAct; Q9NVT9; protein.
DR Bgee; ENSG00000104442; Expressed in secondary oocyte and 210 other tissues.
DR ExpressionAtlas; Q9NVT9; baseline and differential.
DR Genevisible; Q9NVT9; HS.
DR GO; GO:0005829; C:cytosol; IDA:UniProtKB.
DR GO; GO:0005741; C:mitochondrial outer membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005739; C:mitochondrion; IDA:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; IEA:InterPro.
DR GO; GO:0048312; P:intracellular distribution of mitochondria; IMP:UniProtKB.
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; Alternative splicing; Cytoplasm; Membrane; Mitochondrion;
KW Mitochondrion outer membrane; Phosphoprotein; Reference proteome.
FT CHAIN 1..282
FT /note="Armadillo repeat-containing protein 1"
FT /id="PRO_0000240882"
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:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:22814378"
FT MOD_RES 137
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 189
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 246
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9D7A8"
FT MOD_RES 260
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19690332,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 267
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9D7A8"
FT VAR_SEQ 1..53
FT /note="MNSSTSTMSEEPDALSVVNQLRDLAADPLNRRAIVQDQGCLPGLILFMDHPN
FT P -> MSAWPYFIYGPSQPSSRPLRFACSSILGRMPCKQRKDERRTGYDVELTKCYTE
FT (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_054645"
FT VAR_SEQ 54..155
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_054646"
SQ SEQUENCE 282 AA; 31281 MW; 9CDF2DCFEC6C3A08 CRC64;
MNSSTSTMSE EPDALSVVNQ LRDLAADPLN RRAIVQDQGC LPGLILFMDH PNPPVVHSAL
LALRYLAECR ANREKMKGEL GMMLSLQNVI QKTTTPGETK LLASEIYDIL QSSNMADGDS
FNEMNSRRRK AQFFLGTTNK RAKTVVLHID GLDDTSRRNL CEEALLKIKG VISFTFQMAV
QRCVVRIRSD LKAEALASAI ASTKVMKAQQ VVKSESGEEM LVPFQDTPVE VEQNTELPDY
LPEDESPTKE QDKAVSRVGS HPEGGASWLS TAANFLSRSF YW
