ROMO1_HUMAN
ID ROMO1_HUMAN Reviewed; 79 AA.
AC P60602; A7M872; E1P5R9; E9KL28; Q3MHD5; Q5QP16; Q9CQ98; Q9H1N2;
DT 15-MAR-2004, integrated into UniProtKB/Swiss-Prot.
DT 15-MAR-2004, sequence version 1.
DT 03-AUG-2022, entry version 141.
DE RecName: Full=Reactive oxygen species modulator 1;
DE Short=ROS modulator 1;
DE AltName: Full=Epididymis tissue protein Li 175;
DE AltName: Full=Glyrichin;
DE AltName: Full=Mitochondrial targeting GxxxG motif protein;
DE Short=MTGM;
DE AltName: Full=Protein MGR2 homolog;
GN Name=ROMO1; Synonyms=C20orf52;
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] (ISOFORM 1), FUNCTION, TISSUE SPECIFICITY, AND
RP SUBCELLULAR LOCATION.
RC TISSUE=Brain;
RX PubMed=19535734; DOI=10.1242/jcs.038513;
RA Zhao J., Liu T., Jin S.B., Tomilin N., Castro J., Shupliakov O.,
RA Lendahl U., Nister M.;
RT "The novel conserved mitochondrial inner-membrane protein MTGM regulates
RT mitochondrial morphology and cell proliferation.";
RL J. Cell Sci. 122:2252-2262(2009).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Epididymis;
RX PubMed=20736409; DOI=10.1074/mcp.m110.001719;
RA Li J., Liu F., Wang H., Liu X., Liu J., Li N., Wan F., Wang W., Zhang C.,
RA Jin S., Liu J., Zhu P., Liu Y.;
RT "Systematic mapping and functional analysis of a family of human epididymal
RT secretory sperm-located proteins.";
RL Mol. Cell. Proteomics 9:2517-2528(2010).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=11780052; DOI=10.1038/414865a;
RA Deloukas P., Matthews L.H., Ashurst J.L., Burton J., Gilbert J.G.R.,
RA Jones M., Stavrides G., Almeida J.P., Babbage A.K., Bagguley C.L.,
RA Bailey J., Barlow K.F., Bates K.N., Beard L.M., Beare D.M., Beasley O.P.,
RA Bird C.P., Blakey S.E., Bridgeman A.M., Brown A.J., Buck D., Burrill W.D.,
RA Butler A.P., Carder C., Carter N.P., Chapman J.C., Clamp M., Clark G.,
RA Clark L.N., Clark S.Y., Clee C.M., Clegg S., Cobley V.E., Collier R.E.,
RA Connor R.E., Corby N.R., Coulson A., Coville G.J., Deadman R., Dhami P.D.,
RA Dunn M., Ellington A.G., Frankland J.A., Fraser A., French L., Garner P.,
RA Grafham D.V., Griffiths C., Griffiths M.N.D., Gwilliam R., Hall R.E.,
RA Hammond S., Harley J.L., Heath P.D., Ho S., Holden J.L., Howden P.J.,
RA Huckle E., Hunt A.R., Hunt S.E., Jekosch K., Johnson C.M., Johnson D.,
RA Kay M.P., Kimberley A.M., King A., Knights A., Laird G.K., Lawlor S.,
RA Lehvaeslaiho M.H., Leversha M.A., Lloyd C., Lloyd D.M., Lovell J.D.,
RA Marsh V.L., Martin S.L., McConnachie L.J., McLay K., McMurray A.A.,
RA Milne S.A., Mistry D., Moore M.J.F., Mullikin J.C., Nickerson T.,
RA Oliver K., Parker A., Patel R., Pearce T.A.V., Peck A.I.,
RA Phillimore B.J.C.T., Prathalingam S.R., Plumb R.W., Ramsay H., Rice C.M.,
RA Ross M.T., Scott C.E., Sehra H.K., Shownkeen R., Sims S., Skuce C.D.,
RA Smith M.L., Soderlund C., Steward C.A., Sulston J.E., Swann R.M.,
RA Sycamore N., Taylor R., Tee L., Thomas D.W., Thorpe A., Tracey A.,
RA Tromans A.C., Vaudin M., Wall M., Wallis J.M., Whitehead S.L.,
RA Whittaker P., Willey D.L., Williams L., Williams S.A., Wilming L.,
RA Wray P.W., Hubbard T., Durbin R.M., Bentley D.R., Beck S., Rogers J.;
RT "The DNA sequence and comparative analysis of human chromosome 20.";
RL Nature 414:865-871(2001).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Bone marrow;
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 [6]
RP FUNCTION, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=16842742; DOI=10.1016/j.bbrc.2006.06.140;
RA Chung Y.M., Kim J.S., Yoo Y.D.;
RT "A novel protein, Romo1, induces ROS production in the mitochondria.";
RL Biochem. Biophys. Res. Commun. 347:649-655(2006).
RN [7]
RP FUNCTION, AND INDUCTION.
RX PubMed=17537404; DOI=10.1016/j.bbrc.2007.05.088;
RA Hwang I.T., Chung Y.M., Kim J.J., Chung J.S., Kim B.S., Kim H.J., Kim J.S.,
RA Yoo Y.D.;
RT "Drug resistance to 5-FU linked to reactive oxygen species modulator 1.";
RL Biochem. Biophys. Res. Commun. 359:304-310(2007).
RN [8]
RP FUNCTION.
RX PubMed=18313394; DOI=10.1016/j.bbrc.2008.02.098;
RA Na A.R., Chung Y.M., Lee S.B., Park S.H., Lee M.-S., Yoo Y.D.;
RT "A critical role for Romo1-derived ROS in cell proliferation.";
RL Biochem. Biophys. Res. Commun. 369:672-678(2008).
RN [9]
RP FUNCTION, AND DEVELOPMENTAL STAGE.
RX PubMed=18836179; DOI=10.1074/jbc.m805334200;
RA Chung Y.M., Lee S.B., Kim H.J., Park S.H., Kim J.J., Chung J.S., Yoo Y.D.;
RT "Replicative senescence induced by Romo1-derived reactive oxygen species.";
RL J. Biol. Chem. 283:33763-33771(2008).
RN [10]
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 [11]
RP ANTIBACTERIAL FUNCTION.
RX PubMed=22083756; DOI=10.1002/psc.1421;
RA Sha J., Zhao G., Chen X., Guan W., He Y., Wang Z.;
RT "Antibacterial potential of hGlyrichin encoded by a human gene.";
RL J. Pept. Sci. 18:97-104(2012).
RN [12]
RP IDENTIFICATION BY MASS 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 [13]
RP CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION
RP 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).
CC -!- FUNCTION: Induces production of reactive oxygen species (ROS) which are
CC necessary for cell proliferation. May play a role in inducing oxidative
CC DNA damage and replicative senescence. May play a role in the
CC coordination of mitochondrial morphology and cell proliferation.
CC -!- FUNCTION: Has antibacterial activity against a variety of bacteria
CC including S.aureus, P.aeruginosa and M.tuberculosis. Acts by inducing
CC bacterial membrane breakage.
CC -!- INTERACTION:
CC P60602; Q9UHD4: CIDEB; NbExp=3; IntAct=EBI-11909831, EBI-7062247;
CC P60602; Q6NTF9-3: RHBDD2; NbExp=3; IntAct=EBI-11909831, EBI-17589229;
CC -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane
CC {ECO:0000269|PubMed:16842742, ECO:0000269|PubMed:19535734}; Single-pass
CC membrane protein {ECO:0000269|PubMed:16842742,
CC ECO:0000269|PubMed:19535734}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=P60602-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P60602-2; Sequence=VSP_036486;
CC -!- TISSUE SPECIFICITY: Up-regulated in a number of cancer cell lines when
CC compared to a normal lung fibroblast cell line. Highly expressed in
CC brain tumors. {ECO:0000269|PubMed:16842742,
CC ECO:0000269|PubMed:19535734}.
CC -!- DEVELOPMENTAL STAGE: Expression increases in senescent cells.
CC {ECO:0000269|PubMed:18836179}.
CC -!- INDUCTION: By the anticancer drug fluorouracil (5FU).
CC {ECO:0000269|PubMed:17537404}.
CC -!- MISCELLANEOUS: Enforced expression in IMR-90 cells leads to increased
CC levels of ROS and induces premature cell senescence and nuclear DNA
CC damage.
CC -!- SIMILARITY: Belongs to the MGR2 family. {ECO:0000305}.
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DR EMBL; AM397244; CAL37002.1; -; mRNA.
DR EMBL; AM397245; CAL37003.1; -; mRNA.
DR EMBL; AM397246; CAL37004.1; -; mRNA.
DR EMBL; GU727625; ADU87627.1; -; mRNA.
DR EMBL; AL357374; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471077; EAW76168.1; -; Genomic_DNA.
DR EMBL; CH471077; EAW76169.1; -; Genomic_DNA.
DR EMBL; BC008488; AAH08488.1; -; mRNA.
DR EMBL; BC105281; AAI05282.1; -; mRNA.
DR CCDS; CCDS13264.1; -. [P60602-1]
DR RefSeq; NP_542786.1; NM_080748.2. [P60602-1]
DR RefSeq; XP_016883167.1; XM_017027678.1. [P60602-1]
DR AlphaFoldDB; P60602; -.
DR BioGRID; 126718; 27.
DR ComplexPortal; CPX-6129; TIM23 mitochondrial inner membrane pre-sequence translocase complex, TIM17A variant.
DR ComplexPortal; CPX-6130; TIM23 mitochondrial inner membrane pre-sequence translocase complex, TIM17B variant.
DR IntAct; P60602; 6.
DR MINT; P60602; -.
DR STRING; 9606.ENSP00000363191; -.
DR TCDB; 1.A.111.1.1; the reactive oxygen species modulator 1 (romo1) family.
DR GlyGen; P60602; 1 site, 1 O-linked glycan (1 site).
DR PhosphoSitePlus; P60602; -.
DR SwissPalm; P60602; -.
DR BioMuta; ROMO1; -.
DR DMDM; 45593159; -.
DR EPD; P60602; -.
DR jPOST; P60602; -.
DR MassIVE; P60602; -.
DR MaxQB; P60602; -.
DR PaxDb; P60602; -.
DR PeptideAtlas; P60602; -.
DR PRIDE; P60602; -.
DR ProteomicsDB; 57216; -. [P60602-1]
DR ProteomicsDB; 57217; -. [P60602-2]
DR TopDownProteomics; P60602-1; -. [P60602-1]
DR Antibodypedia; 2412; 155 antibodies from 17 providers.
DR DNASU; 140823; -.
DR Ensembl; ENST00000336695.4; ENSP00000338293.4; ENSG00000125995.16. [P60602-1]
DR Ensembl; ENST00000374072.5; ENSP00000363185.1; ENSG00000125995.16. [P60602-2]
DR Ensembl; ENST00000374077.8; ENSP00000363190.3; ENSG00000125995.16. [P60602-1]
DR Ensembl; ENST00000374078.5; ENSP00000363191.1; ENSG00000125995.16. [P60602-1]
DR Ensembl; ENST00000397416.1; ENSP00000380561.1; ENSG00000125995.16. [P60602-1]
DR GeneID; 140823; -.
DR KEGG; hsa:140823; -.
DR MANE-Select; ENST00000374077.8; ENSP00000363190.3; NM_080748.3; NP_542786.1.
DR UCSC; uc002xdy.4; human. [P60602-1]
DR CTD; 140823; -.
DR DisGeNET; 140823; -.
DR GeneCards; ROMO1; -.
DR HGNC; HGNC:16185; ROMO1.
DR HPA; ENSG00000125995; Low tissue specificity.
DR MIM; 618894; gene.
DR neXtProt; NX_P60602; -.
DR OpenTargets; ENSG00000125995; -.
DR PharmGKB; PA164725540; -.
DR VEuPathDB; HostDB:ENSG00000125995; -.
DR eggNOG; KOG4096; Eukaryota.
DR GeneTree; ENSGT00390000005315; -.
DR HOGENOM; CLU_142435_2_0_1; -.
DR InParanoid; P60602; -.
DR OMA; FMIGFCV; -.
DR OrthoDB; 1635599at2759; -.
DR PhylomeDB; P60602; -.
DR TreeFam; TF300273; -.
DR PathwayCommons; P60602; -.
DR SignaLink; P60602; -.
DR SIGNOR; P60602; -.
DR BioGRID-ORCS; 140823; 481 hits in 1090 CRISPR screens.
DR ChiTaRS; ROMO1; human.
DR GenomeRNAi; 140823; -.
DR Pharos; P60602; Tbio.
DR PRO; PR:P60602; -.
DR Proteomes; UP000005640; Chromosome 20.
DR RNAct; P60602; protein.
DR Bgee; ENSG00000125995; Expressed in apex of heart and 181 other tissues.
DR Genevisible; P60602; HS.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005743; C:mitochondrial inner membrane; IC:ComplexPortal.
DR GO; GO:0005739; C:mitochondrion; IDA:UniProtKB.
DR GO; GO:0005744; C:TIM23 mitochondrial import inner membrane translocase complex; IBA:GO_Central.
DR GO; GO:0061844; P:antimicrobial humoral immune response mediated by antimicrobial peptide; IMP:UniProtKB.
DR GO; GO:0034614; P:cellular response to reactive oxygen species; IMP:UniProtKB.
DR GO; GO:0051838; P:cytolysis by host of symbiont cells; IDA:UniProtKB.
DR GO; GO:0042742; P:defense response to bacterium; IDA:UniProtKB.
DR GO; GO:0050829; P:defense response to Gram-negative bacterium; IDA:UniProtKB.
DR GO; GO:0050830; P:defense response to Gram-positive bacterium; IDA:UniProtKB.
DR GO; GO:0006886; P:intracellular protein transport; IC:ComplexPortal.
DR GO; GO:0031640; P:killing of cells of another organism; IDA:UniProtKB.
DR GO; GO:0008284; P:positive regulation of cell population proliferation; IDA:UniProtKB.
DR GO; GO:2000379; P:positive regulation of reactive oxygen species metabolic process; IDA:UniProtKB.
DR GO; GO:0030150; P:protein import into mitochondrial matrix; IBA:GO_Central.
DR GO; GO:0045039; P:protein insertion into mitochondrial inner membrane; IBA:GO_Central.
DR GO; GO:0090399; P:replicative senescence; IMP:GO_Central.
DR InterPro; IPR018450; Romo1/Mgr2.
DR PANTHER; PTHR28525; PTHR28525; 1.
DR Pfam; PF10247; Romo1; 1.
DR SMART; SM01378; Romo1; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Antibiotic; Antimicrobial; Membrane; Mitochondrion;
KW Mitochondrion inner membrane; Reference proteome; Transmembrane;
KW Transmembrane helix.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:25944712"
FT CHAIN 2..79
FT /note="Reactive oxygen species modulator 1"
FT /id="PRO_0000079433"
FT TRANSMEM 22..44
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 42..60
FT /note="Sufficient for antibacterial activity"
FT VAR_SEQ 44..79
FT /note="RIGMRGRELMGGIGKTMMQSGGTFGTFMAIGMGIRC -> SSILVSSSGSEC
FT GVES (in isoform 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_036486"
FT VARIANT 28
FT /note="A -> P (in dbSNP:rs1044521)"
FT /id="VAR_014127"
SQ SEQUENCE 79 AA; 8183 MW; AD959C88C89EF80A CRC64;
MPVAVGPYGQ SQPSCFDRVK MGFVMGCAVG MAAGALFGTF SCLRIGMRGR ELMGGIGKTM
MQSGGTFGTF MAIGMGIRC
