MIEN1_MOUSE
ID MIEN1_MOUSE Reviewed; 115 AA.
AC Q9CQ86; A2A556;
DT 12-DEC-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 130.
DE RecName: Full=Migration and invasion enhancer 1;
DE Flags: Precursor;
GN Name=Mien1; Synonyms=Rdx12;
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=Aorta, Brain, Pancreas, Tongue, and Vein;
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 GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=FVB/N; TISSUE=Liver;
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 INTERACTION WITH GPX1, SUBCELLULAR LOCATION, TISSUE SPECIFICITY,
RP MUTAGENESIS OF CYS-30 AND CYS-33, AND IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=17503775; DOI=10.1021/bi602462q;
RA Dikiy A., Novoselov S.V., Fomenko D.E., Sengupta A., Carlson B.A.,
RA Cerny R.L., Ginalski K., Grishin N.V., Hatfield D.L., Gladyshev V.N.;
RT "SelT, SelW, SelH, and Rdx12: genomics and molecular insights into the
RT functions of selenoproteins of a novel thioredoxin-like family.";
RL Biochemistry 46:6871-6882(2007).
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Kidney, and Spleen;
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: 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 (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Interacts with GPX1. {ECO:0000269|PubMed:17503775}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000269|PubMed:17503775}.
CC Cell membrane {ECO:0000250}; Lipid-anchor {ECO:0000250}; Cytoplasmic
CC side {ECO:0000250}. Note=Concentrates at the leading edge of migrating
CC cells. Localizes outside membrane raft regions (By similarity).
CC {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Widely expressed with highest levels in kidney
CC followed by brain and testis. {ECO:0000269|PubMed:17503775}.
CC -!- PTM: Isoprenylation facilitates association with the plasma membrane
CC and enhances the migratory phenotype of cells by inducing increased
CC filopodia formation. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the SelWTH family. {ECO:0000305}.
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DR EMBL; AK002959; BAB22480.1; -; mRNA.
DR EMBL; AK007795; BAB25261.1; -; mRNA.
DR EMBL; AK009922; BAB26586.1; -; mRNA.
DR EMBL; AK041314; BAC30901.1; -; mRNA.
DR EMBL; AL591390; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH466556; EDL16143.1; -; Genomic_DNA.
DR EMBL; BC021589; AAH21589.1; -; mRNA.
DR CCDS; CCDS25350.1; -.
DR RefSeq; NP_079835.1; NM_025559.2.
DR AlphaFoldDB; Q9CQ86; -.
DR SMR; Q9CQ86; -.
DR STRING; 10090.ENSMUSP00000002655; -.
DR iPTMnet; Q9CQ86; -.
DR PhosphoSitePlus; Q9CQ86; -.
DR EPD; Q9CQ86; -.
DR MaxQB; Q9CQ86; -.
DR PaxDb; Q9CQ86; -.
DR PeptideAtlas; Q9CQ86; -.
DR PRIDE; Q9CQ86; -.
DR ProteomicsDB; 295666; -.
DR Antibodypedia; 28368; 480 antibodies from 26 providers.
DR DNASU; 103742; -.
DR Ensembl; ENSMUST00000002655; ENSMUSP00000002655; ENSMUSG00000002580.
DR GeneID; 103742; -.
DR KEGG; mmu:103742; -.
DR UCSC; uc007lgj.1; mouse.
DR CTD; 84299; -.
DR MGI; MGI:1913678; Mien1.
DR VEuPathDB; HostDB:ENSMUSG00000002580; -.
DR eggNOG; ENOG502S3GR; Eukaryota.
DR GeneTree; ENSGT00390000010440; -.
DR HOGENOM; CLU_068510_4_1_1; -.
DR InParanoid; Q9CQ86; -.
DR OMA; AAPIKDC; -.
DR OrthoDB; 1615913at2759; -.
DR PhylomeDB; Q9CQ86; -.
DR TreeFam; TF326627; -.
DR BioGRID-ORCS; 103742; 1 hit in 74 CRISPR screens.
DR ChiTaRS; Mien1; mouse.
DR PRO; PR:Q9CQ86; -.
DR Proteomes; UP000000589; Chromosome 11.
DR RNAct; Q9CQ86; protein.
DR Bgee; ENSMUSG00000002580; Expressed in motor neuron and 269 other tissues.
DR Genevisible; Q9CQ86; MM.
DR GO; GO:0034451; C:centriolar satellite; ISO:MGI.
DR GO; GO:0005829; C:cytosol; IDA:UniProtKB.
DR GO; GO:0031235; C:intrinsic component of the cytoplasmic side of the plasma membrane; ISS:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005886; C:plasma membrane; ISO:MGI.
DR GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW.
DR GO; GO:0043066; P:negative regulation of apoptotic process; ISS:UniProtKB.
DR GO; GO:0030335; P:positive regulation of cell migration; ISS:UniProtKB.
DR GO; GO:0051491; P:positive regulation of filopodium assembly; ISS: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 Acetylation; Apoptosis; Cell membrane; Cytoplasm; Disulfide bond;
KW Lipoprotein; Membrane; Prenylation; Redox-active center;
KW Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:Q9BRT3"
FT CHAIN 2..112
FT /note="Migration and invasion enhancer 1"
FT /id="PRO_0000265100"
FT PROPEP 113..115
FT /note="Removed in mature form"
FT /evidence="ECO:0000250"
FT /id="PRO_0000396009"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0000250|UniProtKB:Q9BRT3"
FT LIPID 112
FT /note="S-geranylgeranyl cysteine"
FT /evidence="ECO:0000250"
FT DISULFID 30..33
FT /note="Redox-active"
FT /evidence="ECO:0000250"
FT MUTAGEN 30
FT /note="C->S: No effect on interaction with GPX1."
FT /evidence="ECO:0000269|PubMed:17503775"
FT MUTAGEN 33
FT /note="C->S: No effect on interaction with GPX1."
FT /evidence="ECO:0000269|PubMed:17503775"
SQ SEQUENCE 115 AA; 12295 MW; B36A0340DFBA737A CRC64;
MSGEPAPVSV VPPPGEVEAG SGVHIVVEYC KPCGFEATYL ELASAVKEEY PGIEIESRLG
GTGAFEIEIN GQLVFSKLEN GGFPYEKDLM EAIRRASNGE PVEKITNSRP PCVIL
