MIA40_ARATH
ID MIA40_ARATH Reviewed; 162 AA.
AC Q8GYJ4;
DT 02-NOV-2016, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 114.
DE RecName: Full=Mitochondrial intermembrane space import and assembly protein 40 homolog {ECO:0000305};
DE Short=AtMIA40 {ECO:0000303|PubMed:20829360};
GN Name=MIA40 {ECO:0000303|PubMed:20829360};
GN OrderedLocusNames=At5g23395 {ECO:0000312|Araport:AT5G23395};
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=9501997; DOI=10.1093/dnares/4.6.401;
RA Nakamura Y., Sato S., Kaneko T., Kotani H., Asamizu E., Miyajima N.,
RA Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. III. Sequence
RT features of the regions of 1,191,918 bp covered by seventeen physically
RT assigned P1 clones.";
RL DNA Res. 4:401-414(1997).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
RX PubMed=27862469; DOI=10.1111/tpj.13415;
RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA Town C.D.;
RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT genome.";
RL Plant J. 89:789-804(2017).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=11910074; DOI=10.1126/science.1071006;
RA Seki M., Narusaka M., Kamiya A., Ishida J., Satou M., Sakurai T.,
RA Nakajima M., Enju A., Akiyama K., Oono Y., Muramatsu M., Hayashizaki Y.,
RA Kawai J., Carninci P., Itoh M., Ishii Y., Arakawa T., Shibata K.,
RA Shinagawa A., Shinozaki K.;
RT "Functional annotation of a full-length Arabidopsis cDNA collection.";
RL Science 296:141-145(2002).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=14593172; DOI=10.1126/science.1088305;
RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA Ecker J.R.;
RT "Empirical analysis of transcriptional activity in the Arabidopsis
RT genome.";
RL Science 302:842-846(2003).
RN [5]
RP FUNCTION, SUBCELLULAR LOCATION, AND DISRUPTION PHENOTYPE.
RX PubMed=20829360; DOI=10.1074/jbc.m110.121202;
RA Carrie C., Giraud E., Duncan O., Xu L., Wang Y., Huang S., Clifton R.,
RA Murcha M., Filipovska A., Rackham O., Vrielink A., Whelan J.;
RT "Conserved and novel functions for Arabidopsis thaliana MIA40 in assembly
RT of proteins in mitochondria and peroxisomes.";
RL J. Biol. Chem. 285:36138-36148(2010).
CC -!- FUNCTION: Required for the import and folding of small cysteine-
CC containing proteins in the mitochondrial intermembrane space
CC (Probable). Involved in the mitochondrial oxidative folding of the
CC copper-zinc superoxide dismutase CSD1, the copper chaperone for
CC superoxide dismutase CCS, and subunits of the mitochondrial membrane
CC respiratory chain NADH dehydrogenase (Complex I). Involved in the
CC peroxisomal oxidative folding of the copper-zinc superoxide dismutase
CC CSD3, and the fatty acid beta-oxidation multifunctional protein AIM1
CC (PubMed:20829360). {ECO:0000269|PubMed:20829360, ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion intermembrane space
CC {ECO:0000269|PubMed:20829360}. Peroxisome matrix
CC {ECO:0000269|PubMed:20829360}.
CC -!- DISRUPTION PHENOTYPE: No visible phenotype under normal growth
CC conditions. {ECO:0000269|PubMed:20829360}.
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DR EMBL; AB007648; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CP002688; AED93159.1; -; Genomic_DNA.
DR EMBL; BT005086; AAO50619.1; -; mRNA.
DR EMBL; AK117582; BAC42240.1; -; mRNA.
DR RefSeq; NP_680211.1; NM_147906.5.
DR AlphaFoldDB; Q8GYJ4; -.
DR SMR; Q8GYJ4; -.
DR STRING; 3702.AT5G23395.1; -.
DR PaxDb; Q8GYJ4; -.
DR PRIDE; Q8GYJ4; -.
DR ProteomicsDB; 238366; -.
DR EnsemblPlants; AT5G23395.1; AT5G23395.1; AT5G23395.
DR GeneID; 832404; -.
DR Gramene; AT5G23395.1; AT5G23395.1; AT5G23395.
DR KEGG; ath:AT5G23395; -.
DR Araport; AT5G23395; -.
DR TAIR; locus:504956369; AT5G23395.
DR eggNOG; KOG4149; Eukaryota.
DR HOGENOM; CLU_120204_0_0_1; -.
DR InParanoid; Q8GYJ4; -.
DR OMA; KCVKANP; -.
DR OrthoDB; 1594252at2759; -.
DR PhylomeDB; Q8GYJ4; -.
DR PRO; PR:Q8GYJ4; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q8GYJ4; baseline and differential.
DR GO; GO:0005758; C:mitochondrial intermembrane space; IBA:GO_Central.
DR GO; GO:0005739; C:mitochondrion; IDA:TAIR.
DR GO; GO:0005782; C:peroxisomal matrix; IEA:UniProtKB-SubCell.
DR GO; GO:0005777; C:peroxisome; IDA:TAIR.
DR GO; GO:0015035; F:protein-disulfide reductase activity; IBA:GO_Central.
DR GO; GO:0045041; P:protein import into mitochondrial intermembrane space; IBA:GO_Central.
DR GO; GO:0022417; P:protein maturation by protein folding; IBA:GO_Central.
DR GO; GO:0006626; P:protein targeting to mitochondrion; IMP:TAIR.
DR GO; GO:0006625; P:protein targeting to peroxisome; IMP:TAIR.
DR InterPro; IPR010625; CHCH.
DR InterPro; IPR039289; CHCHD4.
DR PANTHER; PTHR21622; PTHR21622; 1.
DR Pfam; PF06747; CHCH; 1.
PE 2: Evidence at transcript level;
KW Disulfide bond; Mitochondrion; Oxidoreductase; Peroxisome;
KW Protein transport; Redox-active center; Reference proteome; Translocation;
KW Transport.
FT CHAIN 1..162
FT /note="Mitochondrial intermembrane space import and
FT assembly protein 40 homolog"
FT /id="PRO_0000437984"
FT DOMAIN 76..120
FT /note="CHCH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01150"
FT REGION 1..61
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 119..162
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 79..89
FT /note="Cx9C motif 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01150"
FT MOTIF 102..112
FT /note="Cx9C motif 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01150"
FT COMPBIAS 1..40
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 123..141
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT DISULFID 68..70
FT /note="Redox-active"
FT /evidence="ECO:0000250|UniProtKB:Q8N4Q1"
FT DISULFID 79..112
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01150"
FT DISULFID 89..102
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01150"
SQ SEQUENCE 162 AA; 17367 MW; D2F2339CD867E8C3 CRC64;
MGQAQSDENS IPTTTTTNTP PPSANSPRDS EDTSSPSMDS LLAEAAAYGE DDNENESLEA
KAQRALDCPC IADLRNGSCG SQFSEAFLCF LKSTAEEKGS DCVNPFVALQ SCINANPDAF
SKSVTGDEKE TEKKEEQPPV QDHRIIPPLW AKDPPRSGNS KL
