ID   MTX3_XENLA              Reviewed;         309 AA.
AC   Q3KPT9; Q6QIT1;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   20-MAY-2008, sequence version 2.
DT   03-AUG-2022, entry version 61.
DE   RecName: Full=Metaxin-3;
DE            Short=xMTX3;
GN   Name=mtx3;
OS   Xenopus laevis (African clawed frog).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC   Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX   NCBI_TaxID=8355;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Embryo;
RX   PubMed=16147884; DOI=10.1080/10425170500129660;
RA   Adolph K.W.;
RT   "Characterization of the cDNA and amino acid sequences of Xenopus metaxin
RT   3, and relationship to Xenopus metaxins 1 and 2.";
RL   DNA Seq. 16:252-259(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Testis;
RG   NIH - Xenopus Gene Collection (XGC) project;
RL   Submitted (OCT-2005) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Could function in transport of proteins into the
CC       mitochondrion. {ECO:0000250}.
CC   -!- SUBUNIT: Part of a large protein complex spanning both mitochondrial
CC       membranes termed the mitochondrial intermembrane space bridging (MIB)
CC       complex. {ECO:0000250|UniProtKB:Q5HYI7}.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000250|UniProtKB:Q5HYI7}.
CC       Mitochondrion outer membrane {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the metaxin family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAI06560.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; AY538738; AAT02187.1; -; mRNA.
DR   EMBL; BC106559; AAI06560.1; ALT_INIT; mRNA.
DR   RefSeq; NP_001084474.1; NM_001091005.1.
DR   AlphaFoldDB; Q3KPT9; -.
DR   SMR; Q3KPT9; -.
DR   DNASU; 407751; -.
DR   GeneID; 407751; -.
DR   KEGG; xla:407751; -.
DR   CTD; 407751; -.
DR   Xenbase; XB-GENE-994130; mtx3.L.
DR   OrthoDB; 1472286at2759; -.
DR   Proteomes; UP000186698; Chromosome 1L.
DR   Bgee; 407751; Expressed in testis and 19 other tissues.
DR   GO; GO:0001401; C:SAM complex; IEA:InterPro.
DR   GO; GO:0007005; P:mitochondrion organization; IEA:InterPro.
DR   GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR   InterPro; IPR036282; Glutathione-S-Trfase_C_sf.
DR   InterPro; IPR040079; Glutathione_S-Trfase.
DR   InterPro; IPR017410; Metaxin1/3.
DR   InterPro; IPR033468; Metaxin_GST.
DR   InterPro; IPR019564; Sam37/metaxin_N.
DR   Pfam; PF17171; GST_C_6; 1.
DR   Pfam; PF10568; Tom37; 1.
DR   PIRSF; PIRSF038150; Metaxin; 1.
DR   SFLD; SFLDS00019; Glutathione_Transferase_(cytos; 1.
DR   SUPFAM; SSF47616; SSF47616; 1.
PE   2: Evidence at transcript level;
KW   Membrane; Mitochondrion; Mitochondrion outer membrane; Protein transport;
KW   Reference proteome; Transport.
FT   CHAIN           1..309
FT                   /note="Metaxin-3"
FT                   /id="PRO_0000337102"
FT   REGION          274..309
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        283..309
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CONFLICT        147
FT                   /note="I -> N (in Ref. 1; AAT02187)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   309 AA;  34644 MW;  72DDF7D702361120 CRC64;
     MMELRCWGSD WGLPSVHPEC LVVLAYARFA GAPLKVTPVD YTWASPKGTV PFLTSAGEDT
     HQPANILNFF RKQKYNADYV LSAKEGSDTL AYIALLEEKL LPAVLHTFWV DTENYCNVTR
     PWYASHTPFP LNYYLPGKMS RDALDRILVT RGQPPLYSLS EVEAQIYKDA KECLNLFSNR
     LGTAQYFFGS TPTSLDAFVF GFLAPLYKAH LHKVNLQQHL KQLSNLCHFC DHILSAYFVS
     DDAGTSAAGQ EAIDANLQKL TQLVNKESNL IEKMDDNLRR SPQNRPQKLS TLKPVGGAEN
     SHSSDLLSH