TIM50_KLULA
ID TIM50_KLULA Reviewed; 480 AA.
AC Q6CM45;
DT 06-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT 16-AUG-2004, sequence version 1.
DT 25-MAY-2022, entry version 94.
DE RecName: Full=Mitochondrial import inner membrane translocase subunit TIM50;
DE Flags: Precursor;
GN Name=TIM50; OrderedLocusNames=KLLA0E23188g;
OS Kluyveromyces lactis (strain ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 /
OS NRRL Y-1140 / WM37) (Yeast) (Candida sphaerica).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Kluyveromyces.
OX NCBI_TaxID=284590;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 / NRRL Y-1140 / WM37;
RX PubMed=15229592; DOI=10.1038/nature02579;
RA Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S., Lafontaine I.,
RA de Montigny J., Marck C., Neuveglise C., Talla E., Goffard N., Frangeul L.,
RA Aigle M., Anthouard V., Babour A., Barbe V., Barnay S., Blanchin S.,
RA Beckerich J.-M., Beyne E., Bleykasten C., Boisrame A., Boyer J.,
RA Cattolico L., Confanioleri F., de Daruvar A., Despons L., Fabre E.,
RA Fairhead C., Ferry-Dumazet H., Groppi A., Hantraye F., Hennequin C.,
RA Jauniaux N., Joyet P., Kachouri R., Kerrest A., Koszul R., Lemaire M.,
RA Lesur I., Ma L., Muller H., Nicaud J.-M., Nikolski M., Oztas S.,
RA Ozier-Kalogeropoulos O., Pellenz S., Potier S., Richard G.-F.,
RA Straub M.-L., Suleau A., Swennen D., Tekaia F., Wesolowski-Louvel M.,
RA Westhof E., Wirth B., Zeniou-Meyer M., Zivanovic Y., Bolotin-Fukuhara M.,
RA Thierry A., Bouchier C., Caudron B., Scarpelli C., Gaillardin C.,
RA Weissenbach J., Wincker P., Souciet J.-L.;
RT "Genome evolution in yeasts.";
RL Nature 430:35-44(2004).
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. Required to direct preproteins
CC in transit and direct them to the channel protein TIM23, and possibly
CC facilitates transfer of the translocating proteins from the TOM complex
CC to the TIM23 complex (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Component of the TIM23 complex, at least composed of TIM23,
CC TIM17, TIM50 and TIM21. Interacts with preproteins in transit (By
CC similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane {ECO:0000250};
CC Single-pass membrane protein {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the TIM50 family. {ECO:0000305}.
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DR EMBL; CR382125; CAH00081.1; -; Genomic_DNA.
DR RefSeq; XP_454994.1; XM_454994.1.
DR AlphaFoldDB; Q6CM45; -.
DR SMR; Q6CM45; -.
DR STRING; 28985.XP_454994.1; -.
DR EnsemblFungi; CAH00081; CAH00081; KLLA0_E23101g.
DR GeneID; 2894383; -.
DR KEGG; kla:KLLA0_E23101g; -.
DR eggNOG; KOG2832; Eukaryota.
DR HOGENOM; CLU_023309_1_2_1; -.
DR InParanoid; Q6CM45; -.
DR OMA; LGRNWDT; -.
DR Proteomes; UP000000598; Chromosome E.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005744; C:TIM23 mitochondrial import inner membrane translocase complex; IEA:EnsemblFungi.
DR GO; GO:0042802; F:identical protein binding; IEA:EnsemblFungi.
DR GO; GO:0030943; F:mitochondrion targeting sequence binding; IEA:EnsemblFungi.
DR GO; GO:0008320; F:protein transmembrane transporter activity; IEA:EnsemblFungi.
DR GO; GO:0030150; P:protein import into mitochondrial matrix; IEA:EnsemblFungi.
DR GO; GO:0046902; P:regulation of mitochondrial membrane permeability; IEA:EnsemblFungi.
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 3: Inferred from homology;
KW Membrane; Mitochondrion; Mitochondrion inner membrane; Protein transport;
KW Reference proteome; Transit peptide; Translocation; Transmembrane;
KW Transmembrane helix; Transport.
FT TRANSIT 1..39
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN 40..480
FT /note="Mitochondrial import inner membrane translocase
FT subunit TIM50"
FT /id="PRO_0000043133"
FT TOPO_DOM 40..118
FT /note="Mitochondrial matrix"
FT /evidence="ECO:0000255"
FT TRANSMEM 119..135
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 136..480
FT /note="Mitochondrial intermembrane"
FT /evidence="ECO:0000255"
FT DOMAIN 190..333
FT /note="FCP1 homology"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00336"
FT REGION 63..107
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 63..97
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 480 AA; 55467 MW; 7E94C86F8E12DAC1 CRC64;
MLSIARVSLL RNARMVPVHA MQMRPVVVRR SLHNGSLLLQ KKNEKNEAPK SILDDDMLAR
AGVEVEGNEA GSKDKSGRAG EAGESAEQDD STGDKGSGKK KRSRKSSTDI KRERYANWFY
ILSLLGLASG ALSMARDWDS DESEELKKEI PNGYTPALMY KRMKRRWESI FTFFQEPPFP
DLLPPPPPPP YQRPLTLVLS LEDLLVHSEW TQQSGWRTAK RPGVDYFLGY LSQYYEIVLF
SSNYMMYAEK IAEKLDPIHA FITYNLFKEH CLYKDGVHIK DLSKLNRDLG KVLIIDTDEN
SFKLQPENAI YLEPWDGKAD DRLLRLIPFL EYLATQQVSD VRPILKSFPD NKNIPEAFEK
RVQVLKEKFE RDERVKNDKN LFLKLLGIGL IGTKPKFPLD LIREEGEKNY VRFMKLVEEE
KEKIKLQQQA MGQQTFTLKD YVEGNIPTPE EQLKLQMEKQ QEIEAQFEEQ KKLKAQQGSK
