ARMX1_HUMAN
ID ARMX1_HUMAN Reviewed; 453 AA.
AC Q9P291; Q53HK2; Q9H2Q0;
DT 20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 150.
DE RecName: Full=Armadillo repeat-containing X-linked protein 1;
DE AltName: Full=ARM protein lost in epithelial cancers on chromosome X 1;
DE Short=Protein ALEX1;
GN Name=ARMCX1; Synonyms=ALEX1; ORFNames=AD032;
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], AND TISSUE SPECIFICITY.
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 [LARGE SCALE MRNA].
RC TISSUE=Adrenal gland;
RA Yang Y., Xu X., Gao G., Xiao H., Chen Z., Han Z.;
RL Submitted (MAR-2000) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Coronary artery;
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 [5]
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 [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Uterus;
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).
CC -!- FUNCTION: Regulates mitochondrial transport during axon regeneration.
CC Increases the proportion of motile mitochondria by recruiting
CC stationary mitochondria into the motile pool. Enhances mitochondria
CC movement and neurite growth in both adult axons and embryonic neurons.
CC Promotes neuronal survival and axon regeneration after nerve injury.
CC May link mitochondria to the Trak1-kinesin motor complex via its
CC interaction with MIRO1. {ECO:0000250|UniProtKB:Q9CX83}.
CC -!- SUBUNIT: Interacts with MIRO1. {ECO:0000250|UniProtKB:Q9CX83}.
CC -!- INTERACTION:
CC Q9P291; Q8NHQ1: CEP70; NbExp=3; IntAct=EBI-2843626, EBI-739624;
CC Q9P291; P38432: COIL; NbExp=3; IntAct=EBI-2843626, EBI-945751;
CC Q9P291; Q92917: GPKOW; NbExp=3; IntAct=EBI-2843626, EBI-746309;
CC Q9P291; Q9NRD5: PICK1; NbExp=3; IntAct=EBI-2843626, EBI-79165;
CC Q9P291; Q9UBB9: TFIP11; NbExp=4; IntAct=EBI-2843626, EBI-1105213;
CC Q9P291; Q96BR9: ZBTB8A; NbExp=6; IntAct=EBI-2843626, EBI-742740;
CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000250|UniProtKB:Q9CX83}.
CC Mitochondrion outer membrane {ECO:0000250|UniProtKB:Q9CX83}; Single-
CC pass membrane protein {ECO:0000255}.
CC -!- TISSUE SPECIFICITY: Expressed at high levels ovary, heart, testis,
CC prostate, brain, spleen and colon. Expressed at very low levels in
CC liver and thymus. Not expressed in peripheral blood leukocytes. Not or
CC reduced expressed in lung, prostate, colon, pancreas and ovarian
CC carcinomas. {ECO:0000269|PubMed:11162520}.
CC -!- SIMILARITY: Belongs to the eutherian X-chromosome-specific Armcx
CC family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAG44561.1; Type=Frameshift; Evidence={ECO:0000305};
CC -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology and
CC Haematology;
CC URL="http://atlasgeneticsoncology.org/Genes/ALEX1Xq22ID477.html";
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; AB039670; BAA94603.1; -; mRNA.
DR EMBL; AF248963; AAG44561.1; ALT_FRAME; mRNA.
DR EMBL; AK074785; BAC11208.1; -; mRNA.
DR EMBL; AK222578; BAD96298.1; -; mRNA.
DR EMBL; Z73913; CAI41999.1; -; Genomic_DNA.
DR EMBL; BC002691; AAH02691.1; -; mRNA.
DR CCDS; CCDS14487.1; -.
DR PIR; JC7582; JC7582.
DR RefSeq; NP_057692.1; NM_016608.1.
DR AlphaFoldDB; Q9P291; -.
DR SMR; Q9P291; -.
DR BioGRID; 119460; 12.
DR IntAct; Q9P291; 8.
DR STRING; 9606.ENSP00000361917; -.
DR iPTMnet; Q9P291; -.
DR PhosphoSitePlus; Q9P291; -.
DR BioMuta; ARMCX1; -.
DR DMDM; 74761871; -.
DR EPD; Q9P291; -.
DR jPOST; Q9P291; -.
DR MassIVE; Q9P291; -.
DR MaxQB; Q9P291; -.
DR PaxDb; Q9P291; -.
DR PeptideAtlas; Q9P291; -.
DR PRIDE; Q9P291; -.
DR ProteomicsDB; 83759; -.
DR Antibodypedia; 28759; 250 antibodies from 29 providers.
DR DNASU; 51309; -.
DR Ensembl; ENST00000372829.8; ENSP00000361917.3; ENSG00000126947.13.
DR GeneID; 51309; -.
DR KEGG; hsa:51309; -.
DR MANE-Select; ENST00000372829.8; ENSP00000361917.3; NM_016608.2; NP_057692.1.
DR UCSC; uc004ehv.4; human.
DR CTD; 51309; -.
DR DisGeNET; 51309; -.
DR GeneCards; ARMCX1; -.
DR HGNC; HGNC:18073; ARMCX1.
DR HPA; ENSG00000126947; Low tissue specificity.
DR MIM; 300362; gene.
DR neXtProt; NX_Q9P291; -.
DR OpenTargets; ENSG00000126947; -.
DR PharmGKB; PA128394658; -.
DR VEuPathDB; HostDB:ENSG00000126947; -.
DR eggNOG; ENOG502QYZW; Eukaryota.
DR GeneTree; ENSGT00940000162561; -.
DR HOGENOM; CLU_037187_0_0_1; -.
DR InParanoid; Q9P291; -.
DR OMA; DVKAEAH; -.
DR OrthoDB; 860703at2759; -.
DR PhylomeDB; Q9P291; -.
DR TreeFam; TF335652; -.
DR PathwayCommons; Q9P291; -.
DR SignaLink; Q9P291; -.
DR BioGRID-ORCS; 51309; 14 hits in 694 CRISPR screens.
DR GeneWiki; ARMCX1; -.
DR GenomeRNAi; 51309; -.
DR Pharos; Q9P291; Tbio.
DR PRO; PR:Q9P291; -.
DR Proteomes; UP000005640; Chromosome X.
DR RNAct; Q9P291; protein.
DR Bgee; ENSG00000126947; Expressed in germinal epithelium of ovary and 204 other tissues.
DR ExpressionAtlas; Q9P291; baseline and differential.
DR Genevisible; Q9P291; HS.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005741; C:mitochondrial outer membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005739; C:mitochondrion; IBA:GO_Central.
DR GO; GO:0061484; P:hematopoietic stem cell homeostasis; IEA:Ensembl.
DR Gene3D; 1.25.10.10; -; 1.
DR InterPro; IPR011989; ARM-like.
DR InterPro; IPR006911; ARM-rpt_dom.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR000225; Armadillo.
DR Pfam; PF04826; Arm_2; 1.
DR SMART; SM00185; ARM; 2.
DR SUPFAM; SSF48371; SSF48371; 1.
DR PROSITE; PS50176; ARM_REPEAT; 1.
PE 1: Evidence at protein level;
KW Membrane; Mitochondrion; Mitochondrion outer membrane; Reference proteome;
KW Repeat; Signal-anchor; Transmembrane; Transmembrane helix.
FT CHAIN 1..453
FT /note="Armadillo repeat-containing X-linked protein 1"
FT /id="PRO_0000191360"
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..453
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:Q8BHS6"
FT REPEAT 195..235
FT /note="ARM 1"
FT /evidence="ECO:0000255"
FT REPEAT 237..276
FT /note="ARM 2"
FT /evidence="ECO:0000255"
FT REPEAT 358..398
FT /note="ARM 3"
FT /evidence="ECO:0000255"
FT REPEAT 415..453
FT /note="ARM 4"
FT /evidence="ECO:0000255"
FT REGION 1..6
FT /note="Mitochondrion outer membrane (MOM)-targeting
FT sequence"
FT /evidence="ECO:0000305"
FT REGION 26..36
FT /note="Mitochondrion outer membrane (MOM)-targeting
FT sequence"
FT /evidence="ECO:0000305"
FT REGION 58..77
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 132..182
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CONFLICT 21
FT /note="C -> R (in Ref. 4; BAD96298)"
FT /evidence="ECO:0000305"
FT CONFLICT 357
FT /note="N -> Y (in Ref. 4; BAD96298)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 453 AA; 49180 MW; 01BED98EC3F64672 CRC64;
MGRTREAGCV AAGVVIGAGA CYCVYRLAWG RDENEKIWDE DEESTDTSEI GVETVKGAKT
NAGAGSGAKL QGDSEVKPEV SLGLEDCPGV KEKAHSGSHS GGGLEAKAKA LFNTLKEQAS
AKAGKGARVG TISGNRTLAP SLPCPGGRGG GCHPTRSGSR AGGRASGKSK GKARSKSTRA
PATTWPVRRG KFNFPYKIDD ILSAPDLQKV LNILERTNDP FIQEVALVTL GNNAAYSFNQ
NAIRELGGVP IIAKLIKTKD PIIREKTYNA LNNLSVNAEN QGKIKTYISQ VCDDTMVCRL
DSAVQMAGLR LLTNMTVTNH YQHLLSYSFP DFFALLFLGN HFTKIQIMKL IINFTENPAM
TRELVSCKVP SELISLFNKE WDREILLNIL TLFENINDNI KNEGLASSRK EFSRSSLFFL
FKESGVCVKK IKALANHNDL VVKVKVLKVL TKL
