TIM50_DANRE
ID TIM50_DANRE Reviewed; 387 AA.
AC Q6NWD4; Q6PFK0;
DT 06-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT 06-DEC-2005, sequence version 2.
DT 03-AUG-2022, entry version 90.
DE RecName: Full=Mitochondrial import inner membrane translocase subunit TIM50;
DE Flags: Precursor;
GN Name=timm50; Synonyms=tim50; ORFNames=zgc:66357;
OS Danio rerio (Zebrafish) (Brachydanio rerio).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC Danionidae; Danioninae; Danio.
OX NCBI_TaxID=7955;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, DEVELOPMENTAL STAGE, AND DISRUPTION
RP PHENOTYPE.
RX PubMed=15044455; DOI=10.1074/jbc.m402049200;
RA Guo Y., Cheong N., Zhang Z., De Rose R., Deng Y., Farber S.A.,
RA Fernandes-Alnemri T., Alnemri E.S.;
RT "Tim50, a component of the mitochondrial translocator, regulates
RT mitochondrial integrity and cell death.";
RL J. Biol. Chem. 279:24813-24825(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Kidney;
RG NIH - Zebrafish Gene Collection (ZGC) project;
RL Submitted (MAR-2004) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Essential component of the TIM23 complex, a complex that
CC mediates the translocation of transit peptide-containing proteins
CC across the mitochondrial inner membrane. {ECO:0000269|PubMed:15044455}.
CC -!- SUBUNIT: Component of the TIM23 complex at least composed of timm23,
CC timm17 and timm50. {ECO:0000250|UniProtKB:Q3ZCQ8}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane
CC {ECO:0000250|UniProtKB:Q3ZCQ8}; Single-pass membrane protein
CC {ECO:0000250|UniProtKB:Q3ZCQ8}.
CC -!- DEVELOPMENTAL STAGE: At 48 hours post-fertilization (hpf), it is highly
CC expressed in the CNS, particularly in the brain tissues. The pattern is
CC the same at 72 hpf. {ECO:0000269|PubMed:15044455}.
CC -!- DISRUPTION PHENOTYPE: Massive apoptosis in the CNS, probably due to
CC loss of mitochondrial function and increased cytochrome c release.
CC {ECO:0000269|PubMed:15044455}.
CC -!- SIMILARITY: Belongs to the TIM50 family. {ECO:0000305}.
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DR EMBL; AY551343; AAT01210.1; -; mRNA.
DR EMBL; BC057522; AAH57522.1; -; mRNA.
DR EMBL; BC067634; AAH67634.1; -; mRNA.
DR RefSeq; NP_956959.1; NM_200665.2.
DR AlphaFoldDB; Q6NWD4; -.
DR SMR; Q6NWD4; -.
DR STRING; 7955.ENSDARP00000048422; -.
DR PaxDb; Q6NWD4; -.
DR GeneID; 393638; -.
DR KEGG; dre:393638; -.
DR CTD; 92609; -.
DR ZFIN; ZDB-GENE-040426-1618; timm50.
DR eggNOG; KOG2832; Eukaryota.
DR InParanoid; Q6NWD4; -.
DR OrthoDB; 1142452at2759; -.
DR PhylomeDB; Q6NWD4; -.
DR PRO; PR:Q6NWD4; -.
DR Proteomes; UP000000437; Genome assembly.
DR Proteomes; UP000814640; Unplaced.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005743; C:mitochondrial inner membrane; ISS:UniProtKB.
DR GO; GO:0005744; C:TIM23 mitochondrial import inner membrane translocase complex; ISS:UniProtKB.
DR GO; GO:0004722; F:protein serine/threonine phosphatase activity; ISS:UniProtKB.
DR GO; GO:0004725; F:protein tyrosine phosphatase activity; ISS:UniProtKB.
DR GO; GO:0006915; P:apoptotic process; IMP:ZFIN.
DR GO; GO:0007006; P:mitochondrial membrane organization; ISS:UniProtKB.
DR GO; GO:0006470; P:protein dephosphorylation; ISS:UniProtKB.
DR GO; GO:0030150; P:protein import into mitochondrial matrix; IBA:GO_Central.
DR Gene3D; 3.40.50.1000; -; 1.
DR InterPro; IPR004274; FCP1_dom.
DR InterPro; IPR036412; HAD-like_sf.
DR InterPro; IPR023214; HAD_sf.
DR InterPro; IPR027111; Tim50.
DR PANTHER; PTHR12210:SF3; PTHR12210:SF3; 1.
DR Pfam; PF03031; NIF; 1.
DR SMART; SM00577; CPDc; 1.
DR SUPFAM; SSF56784; SSF56784; 1.
DR PROSITE; PS50969; FCP1; 1.
PE 2: Evidence at transcript level;
KW Membrane; Mitochondrion; Mitochondrion inner membrane; Protein transport;
KW Reference proteome; Transit peptide; Translocation; Transmembrane;
KW Transmembrane helix; Transport.
FT TRANSIT 1..26
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN 27..387
FT /note="Mitochondrial import inner membrane translocase
FT subunit TIM50"
FT /id="PRO_0000043118"
FT TOPO_DOM 27..100
FT /note="Mitochondrial matrix"
FT /evidence="ECO:0000255"
FT TRANSMEM 101..121
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 122..387
FT /note="Mitochondrial intermembrane"
FT /evidence="ECO:0000255"
FT DOMAIN 178..321
FT /note="FCP1 homology"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00336"
FT REGION 61..93
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 73..93
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CONFLICT 323
FT /note="T -> I (in Ref. 2; AAH67634)"
FT /evidence="ECO:0000305"
FT CONFLICT 355
FT /note="R -> Q (in Ref. 2; AAH67634)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 387 AA; 43881 MW; 00F49E27F1E1C9D9 CRC64;
MSAVSVYPMC VRASRGLLRL RQGARCSTAP PLLDVVRPLS ADTSSSSATG GLAQAILQER
LQQQQKSQEQ PPPEGEDSGH KQDEQGEDKK QKENTAYAKK MVLRLAGIMG LGGTVGIVYI
FGSNSVDEQG NKIPDEFDND VPVIQQLRRT FKYFKDYRQM IIEPTSPKLL PDPLREPYYQ
PPYTLVLELT DVLLHPEWSL ATGWRFKKRP GIDYLFQQLA PLYEIVIFTS ETGMTAYPLI
DSIDPQGFVM YRLFRDATRY MEGHHVKDVS CLNRDTSKVI VVDCKREAFG LQPFNGLALC
KWDGNSEDRT LYDLAAFLKT IATSGVEDVR SVLENYAHEE DPIEAFKRRQ AQLAREEEQR
ISEMAQQKKQ GFSLGTIAGR FWSRKQQ
