ID   MIEN1_BOVIN             Reviewed;         115 AA.
AC   Q148C8;
DT   12-DEC-2006, integrated into UniProtKB/Swiss-Prot.
DT   22-AUG-2006, sequence version 1.
DT   03-AUG-2022, entry version 89.
DE   RecName: Full=Migration and invasion enhancer 1;
DE   Flags: Precursor;
GN   Name=MIEN1; Synonyms=RDX12;
OS   Bos taurus (Bovine).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC   Bovinae; Bos.
OX   NCBI_TaxID=9913;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=Hereford; TISSUE=Fetal pons;
RG   NIH - Mammalian Gene Collection (MGC) project;
RL   Submitted (JUN-2006) to the EMBL/GenBank/DDBJ databases.
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:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000250}. Cell membrane
CC       {ECO:0000250}; Lipid-anchor {ECO:0000250}; Cytoplasmic side
CC       {ECO:0000250}. Note=Concentrates at the leading edge of migrating
CC       cells. Localizes outside membrane raft regions (By similarity).
CC       {ECO:0000250}.
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; BC118463; AAI18464.1; -; mRNA.
DR   RefSeq; NP_001068689.1; NM_001075221.2.
DR   AlphaFoldDB; Q148C8; -.
DR   SMR; Q148C8; -.
DR   STRING; 9913.ENSBTAP00000029060; -.
DR   PaxDb; Q148C8; -.
DR   PRIDE; Q148C8; -.
DR   Ensembl; ENSBTAT00000029060; ENSBTAP00000029060; ENSBTAG00000021802.
DR   GeneID; 505710; -.
DR   KEGG; bta:505710; -.
DR   CTD; 84299; -.
DR   VEuPathDB; HostDB:ENSBTAG00000021802; -.
DR   VGNC; VGNC:31468; MIEN1.
DR   eggNOG; ENOG502S3GR; Eukaryota.
DR   GeneTree; ENSGT00390000010440; -.
DR   HOGENOM; CLU_068510_4_0_1; -.
DR   InParanoid; Q148C8; -.
DR   OMA; AAPIKDC; -.
DR   OrthoDB; 1615913at2759; -.
DR   TreeFam; TF326627; -.
DR   Proteomes; UP000009136; Chromosome 19.
DR   Bgee; ENSBTAG00000021802; Expressed in pons and 109 other tissues.
DR   GO; GO:0034451; C:centriolar satellite; IEA:Ensembl.
DR   GO; GO:0005829; C:cytosol; ISS:UniProtKB.
DR   GO; GO:0031235; C:intrinsic component of the cytoplasmic side of the plasma membrane; ISS:UniProtKB.
DR   GO; GO:0005654; C:nucleoplasm; IEA:Ensembl.
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   3: Inferred from homology;
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_0000265098"
FT   PROPEP          113..115
FT                   /note="Removed in mature form"
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000396007"
FT   REGION          1..22
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
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"
SQ   SEQUENCE   115 AA;  12342 MW;  6580D3266BA6086E CRC64;
     MSGDTGTTSV APPPGETEPG HGVRIVVEYC EPCGFEATYL ELASAVKEQY PGIEIESRLG
     GTGAFEIEIN GQLVFSKLEN GGFPYEKDLI EAIRRASNGE PLEKITNSRP PCVIL