MIEN1_HUMAN
ID MIEN1_HUMAN Reviewed; 115 AA.
AC Q9BRT3;
DT 12-DEC-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 149.
DE RecName: Full=Migration and invasion enhancer 1;
DE AltName: Full=HBV X-transactivated gene 4 protein;
DE AltName: Full=HBV XAg-transactivated protein 4;
DE AltName: Full=Protein C35;
DE Flags: Precursor;
GN Name=MIEN1; Synonyms=C17orf37, RDX12, XTP4;
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], TISSUE SPECIFICITY, SUBCELLULAR LOCATION, AND
RP ISOPRENYLATION.
RX PubMed=17121940; DOI=10.1158/1535-7163.mct-06-0389;
RA Evans E.E., Henn A.D., Jonason A., Paris M.J., Schiffhauer L.M.,
RA Borrello M.A., Smith E.S., Sahasrabudhe D.M., Zauderer M.;
RT "C35 (C17orf37) is a novel tumor biomarker abundantly expressed in breast
RT cancer.";
RL Mol. Cancer Ther. 5:2919-2930(2006).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Liu Y., Cheng J., Lu Y., Wang G., Zhang L., Chen J., Li L.;
RT "Cloning and identification of human gene 4 transactivated by hepatitis B
RT virus X antigen.";
RL Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16625196; DOI=10.1038/nature04689;
RA Zody M.C., Garber M., Adams D.J., Sharpe T., Harrow J., Lupski J.R.,
RA Nicholson C., Searle S.M., Wilming L., Young S.K., Abouelleil A.,
RA Allen N.R., Bi W., Bloom T., Borowsky M.L., Bugalter B.E., Butler J.,
RA Chang J.L., Chen C.-K., Cook A., Corum B., Cuomo C.A., de Jong P.J.,
RA DeCaprio D., Dewar K., FitzGerald M., Gilbert J., Gibson R., Gnerre S.,
RA Goldstein S., Grafham D.V., Grocock R., Hafez N., Hagopian D.S., Hart E.,
RA Norman C.H., Humphray S., Jaffe D.B., Jones M., Kamal M., Khodiyar V.K.,
RA LaButti K., Laird G., Lehoczky J., Liu X., Lokyitsang T., Loveland J.,
RA Lui A., Macdonald P., Major J.E., Matthews L., Mauceli E., McCarroll S.A.,
RA Mihalev A.H., Mudge J., Nguyen C., Nicol R., O'Leary S.B., Osoegawa K.,
RA Schwartz D.C., Shaw-Smith C., Stankiewicz P., Steward C., Swarbreck D.,
RA Venkataraman V., Whittaker C.A., Yang X., Zimmer A.R., Bradley A.,
RA Hubbard T., Birren B.W., Rogers J., Lander E.S., Nusbaum C.;
RT "DNA sequence of human chromosome 17 and analysis of rearrangement in the
RT human lineage.";
RL Nature 440:1045-1049(2006).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain;
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 [5]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [6]
RP FUNCTION, TISSUE SPECIFICITY, SUBCELLULAR LOCATION, AND ISOPRENYLATION AT
RP CYS-112.
RX PubMed=19503095; DOI=10.1038/onc.2009.145;
RA Dasgupta S., Wasson L.M., Rauniyar N., Prokai L., Borejdo J.,
RA Vishwanatha J.K.;
RT "Novel gene C17orf37 in 17q12 amplicon promotes migration and invasion of
RT prostate cancer cells.";
RL Oncogene 28:2860-2872(2009).
RN [7]
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 [8]
RP FUNCTION, SUBCELLULAR LOCATION, ISOPRENYLATION AT CYS-112, AND MUTAGENESIS
RP OF CYS-112 AND 112-CYS--LEU-115.
RX PubMed=21628459; DOI=10.1074/jbc.m111.254599;
RA Dasgupta S., Cushman I., Kpetemey M., Casey P.J., Vishwanatha J.K.;
RT "Prenylated c17orf37 induces filopodia formation to promote cell migration
RT and metastasis.";
RL J. Biol. Chem. 286:25935-25946(2011).
RN [9]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [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 STRUCTURE BY NMR, AND DISULFIDE BOND.
RX PubMed=23284973; DOI=10.1371/journal.pone.0052292;
RA Hsu C.H., Shen T.L., Chang C.F., Chang Y.Y., Huang L.Y.;
RT "Solution structure of the oncogenic MIEN1 protein reveals a thioredoxin-
RT like fold with a redox-active motif.";
RL PLoS ONE 7:E52292-E52292(2012).
CC -!- FUNCTION: Increases cell migration by inducing filopodia formation at
CC the leading edge of migrating cells. Plays a role in regulation of
CC apoptosis, possibly through control of CASP3. May be involved in a
CC redox-related process. {ECO:0000269|PubMed:19503095,
CC ECO:0000269|PubMed:21628459}.
CC -!- SUBUNIT: Interacts with GPX1. {ECO:0000250}.
CC -!- INTERACTION:
CC Q9BRT3; Q03989: ARID5A; NbExp=3; IntAct=EBI-6137472, EBI-948603;
CC Q9BRT3; Q96D03: DDIT4L; NbExp=3; IntAct=EBI-6137472, EBI-742054;
CC Q9BRT3; Q9H8Y8: GORASP2; NbExp=3; IntAct=EBI-6137472, EBI-739467;
CC Q9BRT3; Q8WUI4-6: HDAC7; NbExp=5; IntAct=EBI-6137472, EBI-12094670;
CC Q9BRT3; Q14774: HLX; NbExp=3; IntAct=EBI-6137472, EBI-6678255;
CC Q9BRT3; P26583: HMGB2; NbExp=6; IntAct=EBI-6137472, EBI-1057009;
CC Q9BRT3; P78424: POU6F2; NbExp=3; IntAct=EBI-6137472, EBI-12029004;
CC Q9BRT3; Q04864: REL; NbExp=3; IntAct=EBI-6137472, EBI-307352;
CC Q9BRT3; Q04864-2: REL; NbExp=3; IntAct=EBI-6137472, EBI-10829018;
CC Q9BRT3; Q15654: TRIP6; NbExp=3; IntAct=EBI-6137472, EBI-742327;
CC Q9BRT3; O95231: VENTX; NbExp=3; IntAct=EBI-6137472, EBI-10191303;
CC Q9BRT3; A0A0C4DGF1: ZBTB32; NbExp=5; IntAct=EBI-6137472, EBI-10188476;
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol. Cell membrane; Lipid-anchor;
CC Cytoplasmic side. Note=Concentrates at the leading edge of migrating
CC cells. Localizes outside membrane raft regions.
CC -!- TISSUE SPECIFICITY: Among normal tissues, present only in Leydig cells.
CC Strongly up-regulated in breast cancers and in brain cancer distant
CC metastasis (at protein level). Up-regulated in prostate cancer cells
CC and in the higher grades of prostate adenocarcinoma (at protein level).
CC {ECO:0000269|PubMed:17121940, ECO:0000269|PubMed:19503095}.
CC -!- PTM: Isoprenylation facilitates association with the plasma membrane
CC and enhances the migratory phenotype of cells by inducing increased
CC filopodia formation. {ECO:0000269|PubMed:17121940,
CC ECO:0000269|PubMed:19503095, ECO:0000269|PubMed:21628459}.
CC -!- SIMILARITY: Belongs to the SelWTH family. {ECO:0000305}.
CC -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology and
CC Haematology;
CC URL="http://atlasgeneticsoncology.org/Genes/MIEN1ID52476ch17q12.html";
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DR EMBL; AY508814; AAR92035.1; -; mRNA.
DR EMBL; AF490253; AAO85461.1; -; mRNA.
DR EMBL; AC079199; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC006006; AAH06006.1; -; mRNA.
DR CCDS; CCDS11344.1; -.
DR RefSeq; NP_001317135.1; NM_001330206.1.
DR RefSeq; NP_115715.3; NM_032339.4.
DR PDB; 2LJK; NMR; -; A=1-115.
DR PDBsum; 2LJK; -.
DR AlphaFoldDB; Q9BRT3; -.
DR BMRB; Q9BRT3; -.
DR SMR; Q9BRT3; -.
DR BioGRID; 124025; 19.
DR IntAct; Q9BRT3; 13.
DR STRING; 9606.ENSP00000377778; -.
DR iPTMnet; Q9BRT3; -.
DR PhosphoSitePlus; Q9BRT3; -.
DR BioMuta; MIEN1; -.
DR DMDM; 74732925; -.
DR EPD; Q9BRT3; -.
DR jPOST; Q9BRT3; -.
DR MassIVE; Q9BRT3; -.
DR MaxQB; Q9BRT3; -.
DR PaxDb; Q9BRT3; -.
DR PeptideAtlas; Q9BRT3; -.
DR PRIDE; Q9BRT3; -.
DR ProteomicsDB; 78828; -.
DR Antibodypedia; 28368; 480 antibodies from 26 providers.
DR DNASU; 84299; -.
DR Ensembl; ENST00000394231.8; ENSP00000377778.3; ENSG00000141741.12.
DR GeneID; 84299; -.
DR KEGG; hsa:84299; -.
DR MANE-Select; ENST00000394231.8; ENSP00000377778.3; NM_032339.5; NP_115715.3.
DR UCSC; uc002hsq.4; human.
DR CTD; 84299; -.
DR DisGeNET; 84299; -.
DR GeneCards; MIEN1; -.
DR HGNC; HGNC:28230; MIEN1.
DR HPA; ENSG00000141741; Low tissue specificity.
DR MIM; 611802; gene.
DR neXtProt; NX_Q9BRT3; -.
DR OpenTargets; ENSG00000141741; -.
DR PharmGKB; PA134947080; -.
DR VEuPathDB; HostDB:ENSG00000141741; -.
DR eggNOG; ENOG502S3GR; Eukaryota.
DR GeneTree; ENSGT00390000010440; -.
DR HOGENOM; CLU_068510_4_0_1; -.
DR InParanoid; Q9BRT3; -.
DR OMA; AAPIKDC; -.
DR OrthoDB; 1615913at2759; -.
DR PhylomeDB; Q9BRT3; -.
DR TreeFam; TF326627; -.
DR PathwayCommons; Q9BRT3; -.
DR SignaLink; Q9BRT3; -.
DR BioGRID-ORCS; 84299; 44 hits in 1075 CRISPR screens.
DR ChiTaRS; MIEN1; human.
DR GenomeRNAi; 84299; -.
DR Pharos; Q9BRT3; Tbio.
DR PRO; PR:Q9BRT3; -.
DR Proteomes; UP000005640; Chromosome 17.
DR RNAct; Q9BRT3; protein.
DR Bgee; ENSG00000141741; Expressed in mucosa of transverse colon and 182 other tissues.
DR ExpressionAtlas; Q9BRT3; baseline and differential.
DR Genevisible; Q9BRT3; HS.
DR GO; GO:0034451; C:centriolar satellite; IDA:HPA.
DR GO; GO:0005829; C:cytosol; IDA:UniProtKB.
DR GO; GO:0031235; C:intrinsic component of the cytoplasmic side of the plasma membrane; IDA:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005886; C:plasma membrane; IDA:HPA.
DR GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW.
DR GO; GO:0043066; P:negative regulation of apoptotic process; IDA:UniProtKB.
DR GO; GO:0030335; P:positive regulation of cell migration; IDA:UniProtKB.
DR GO; GO:0051491; P:positive regulation of filopodium assembly; IDA:UniProtKB.
DR GO; GO:0010269; P:response to selenium ion; IBA:GO_Central.
DR InterPro; IPR011893; Selenoprotein_Rdx-typ.
DR InterPro; IPR036249; Thioredoxin-like_sf.
DR Pfam; PF10262; Rdx; 1.
DR SUPFAM; SSF52833; SSF52833; 1.
DR TIGRFAMs; TIGR02174; CXXU_selWTH; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Apoptosis; Cell membrane; Cytoplasm;
KW Disulfide bond; Lipoprotein; Membrane; Prenylation; Redox-active center;
KW Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:19413330,
FT ECO:0007744|PubMed:22814378"
FT CHAIN 2..112
FT /note="Migration and invasion enhancer 1"
FT /id="PRO_0000265099"
FT PROPEP 113..115
FT /note="Removed in mature form"
FT /evidence="ECO:0000305"
FT /id="PRO_0000396008"
FT REGION 1..21
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0007744|PubMed:19413330,
FT ECO:0007744|PubMed:22814378"
FT LIPID 112
FT /note="S-geranylgeranyl cysteine"
FT /evidence="ECO:0000269|PubMed:19503095,
FT ECO:0000269|PubMed:21628459"
FT DISULFID 30..33
FT /note="Redox-active"
FT /evidence="ECO:0000269|PubMed:23284973"
FT MUTAGEN 112..115
FT /note="Missing: No effect on subcellular location. Low
FT protein abundance, suggesting that stability is affected."
FT /evidence="ECO:0000269|PubMed:21628459"
FT MUTAGEN 112
FT /note="C->S: Abolishes prenylation. Predominantly cysolic
FT with little plasma membrane-associated expression. Reduces
FT cell migration by affecting filopodia formation."
FT /evidence="ECO:0000269|PubMed:21628459"
FT STRAND 26..29
FT /evidence="ECO:0007829|PDB:2LJK"
FT TURN 31..34
FT /evidence="ECO:0007829|PDB:2LJK"
FT HELIX 36..46
FT /evidence="ECO:0007829|PDB:2LJK"
FT TURN 47..49
FT /evidence="ECO:0007829|PDB:2LJK"
FT STRAND 51..53
FT /evidence="ECO:0007829|PDB:2LJK"
FT STRAND 56..59
FT /evidence="ECO:0007829|PDB:2LJK"
FT STRAND 61..63
FT /evidence="ECO:0007829|PDB:2LJK"
FT STRAND 65..68
FT /evidence="ECO:0007829|PDB:2LJK"
FT HELIX 77..80
FT /evidence="ECO:0007829|PDB:2LJK"
FT TURN 86..90
FT /evidence="ECO:0007829|PDB:2LJK"
FT HELIX 91..96
FT /evidence="ECO:0007829|PDB:2LJK"
FT TURN 97..99
FT /evidence="ECO:0007829|PDB:2LJK"
SQ SEQUENCE 115 AA; 12403 MW; 5D8B911C0F23DDC1 CRC64;
MSGEPGQTSV APPPEEVEPG SGVRIVVEYC EPCGFEATYL ELASAVKEQY PGIEIESRLG
GTGAFEIEIN GQLVFSKLEN GGFPYEKDLI EAIRRASNGE TLEKITNSRP PCVIL
