ID   TIM50_PONAB             Reviewed;         353 AA.
AC   Q5RAJ8;
DT   06-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT   21-DEC-2004, sequence version 1.
DT   25-MAY-2022, entry version 68.
DE   RecName: Full=Mitochondrial import inner membrane translocase subunit TIM50;
DE   Flags: Precursor;
GN   Name=TIMM50; Synonyms=TIM50;
OS   Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Pongo.
OX   NCBI_TaxID=9601;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Kidney;
RG   The German cDNA consortium;
RL   Submitted (NOV-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. Has some phosphatase activity
CC       in vitro; however such activity may not be relevant in vivo.
CC       {ECO:0000250|UniProtKB:Q3ZCQ8}.
CC   -!- SUBUNIT: Component of the TIM23 complex at least composed of TIMM23,
CC       TIMM17 (TIMM17A or TIMM17B) and TIMM50; within this complex, directly
CC       interacts with TIMM23. The complex interacts with the TIMM44 component
CC       of the PAM complex and with DNAJC15. {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   -!- SIMILARITY: Belongs to the TIM50 family. {ECO:0000305}.
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DR   EMBL; CR859017; CAH91212.1; -; mRNA.
DR   RefSeq; NP_001125713.1; NM_001132241.1.
DR   AlphaFoldDB; Q5RAJ8; -.
DR   SMR; Q5RAJ8; -.
DR   STRING; 9601.ENSPPYP00000011161; -.
DR   GeneID; 100172637; -.
DR   KEGG; pon:100172637; -.
DR   CTD; 92609; -.
DR   eggNOG; KOG2832; Eukaryota.
DR   InParanoid; Q5RAJ8; -.
DR   OrthoDB; 1142452at2759; -.
DR   Proteomes; UP000001595; 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:0007006; P:mitochondrial membrane organization; ISS:UniProtKB.
DR   GO; GO:0006470; P:protein dephosphorylation; ISS:UniProtKB.
DR   GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
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; Phosphoprotein;
KW   Protein transport; Reference proteome; Transit peptide; Translocation;
KW   Transmembrane; Transmembrane helix; Transport.
FT   TRANSIT         1..44
FT                   /note="Mitochondrion"
FT                   /evidence="ECO:0000255"
FT   CHAIN           45..353
FT                   /note="Mitochondrial import inner membrane translocase
FT                   subunit TIM50"
FT                   /id="PRO_0000043117"
FT   TOPO_DOM        45..65
FT                   /note="Mitochondrial matrix"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        66..86
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        87..353
FT                   /note="Mitochondrial intermembrane"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          143..286
FT                   /note="FCP1 homology"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00336"
FT   REGION          22..60
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        42..59
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         45
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q3ZCQ8"
FT   MOD_RES         341
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q3ZCQ8"
SQ   SEQUENCE   353 AA;  39603 MW;  3B93CFA52A63FE45 CRC64;
     MAASAAVFSR LRSGLRLGSR GLCTRLATPP PRAPDQAAEI GSRGSTKAQG PQQQPGSEGP
     SYAKKVALWL AGLLGAGGTV SVVYIFGNNP VDENGAKIPD EFDNDPILVQ QLRRTYKYFK
     DYRQMIIEPT SPCLLPDPLQ EPYYQPPYTL VLELTGVLLH LEWSLATGWR FKKRPGIETL
     FQQLAPLYEI VIFTSETGMT AFPLIDSVDP HGFISYRLFR DATRYMDGHH VKDISCLNRD
     PARVVVVDCK KEAFRLQPYN GVALRPWDGN SDDRVLLDLS AFLKTIALNG VEDVRTVLEH
     YALEDDPLAA FKQRQSRLEQ EEQQRLAELS KSNKQNLFLG SLTSRLWPRS KQP