ID A0A2K6GPH6_PROCO Unreviewed; 353 AA.
AC A0A2K6GPH6;
DT 28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT 28-MAR-2018, sequence version 1.
DT 24-JAN-2024, entry version 30.
DE RecName: Full=Mitochondrial import inner membrane translocase subunit TIM50 {ECO:0000256|RuleBase:RU365079};
GN Name=TIMM50 {ECO:0000313|Ensembl:ENSPCOP00000028146.1};
OS Propithecus coquereli (Coquerel's sifaka) (Propithecus verreauxi
OS coquereli).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Strepsirrhini; Lemuriformes;
OC Indriidae; Propithecus.
OX NCBI_TaxID=379532 {ECO:0000313|Ensembl:ENSPCOP00000028146.1, ECO:0000313|Proteomes:UP000233160};
RN [1] {ECO:0000313|Ensembl:ENSPCOP00000028146.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
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.
CC {ECO:0000256|RuleBase:RU365079}.
CC -!- SUBUNIT: Component of the TIM23 complex.
CC {ECO:0000256|RuleBase:RU365079}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004167}; Single-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004167}. Mitochondrion
CC inner membrane {ECO:0000256|ARBA:ARBA00004434,
CC ECO:0000256|RuleBase:RU365079}; Single-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004434, ECO:0000256|RuleBase:RU365079}.
CC -!- SIMILARITY: Belongs to the TIM50 family.
CC {ECO:0000256|ARBA:ARBA00006344, ECO:0000256|RuleBase:RU365079}.
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DR AlphaFoldDB; A0A2K6GPH6; -.
DR Ensembl; ENSPCOT00000039027.1; ENSPCOP00000028146.1; ENSPCOG00000026662.1.
DR GeneTree; ENSGT01040000240503; -.
DR Proteomes; UP000233160; Unplaced.
DR GO; GO:0005744; C:TIM23 mitochondrial import inner membrane translocase complex; IEA:UniProtKB-UniRule.
DR GO; GO:0004722; F:protein serine/threonine phosphatase activity; IEA:UniProt.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR CDD; cd07521; HAD_FCP1-like; 1.
DR Gene3D; 3.40.50.1000; HAD superfamily/HAD-like; 1.
DR InterPro; IPR004274; FCP1_dom.
DR InterPro; IPR036412; HAD-like_sf.
DR InterPro; IPR023214; HAD_sf.
DR PANTHER; PTHR12210; DULLARD PROTEIN PHOSPHATASE; 1.
DR PANTHER; PTHR12210:SF3; MITOCHONDRIAL IMPORT INNER MEMBRANE TRANSLOCASE SUBUNIT TIM50; 1.
DR Pfam; PF03031; NIF; 1.
DR SMART; SM00577; CPDc; 1.
DR SUPFAM; SSF56784; HAD-like; 1.
DR PROSITE; PS50969; FCP1; 1.
PE 3: Inferred from homology;
KW Membrane {ECO:0000256|RuleBase:RU365079};
KW Mitochondrion {ECO:0000256|ARBA:ARBA00023128,
KW ECO:0000256|RuleBase:RU365079};
KW Mitochondrion inner membrane {ECO:0000256|ARBA:ARBA00022792};
KW Protein transport {ECO:0000256|ARBA:ARBA00022927,
KW ECO:0000256|RuleBase:RU365079};
KW Reference proteome {ECO:0000313|Proteomes:UP000233160};
KW Transit peptide {ECO:0000256|ARBA:ARBA00022946,
KW ECO:0000256|RuleBase:RU365079};
KW Translocation {ECO:0000256|ARBA:ARBA00023010,
KW ECO:0000256|RuleBase:RU365079};
KW Transmembrane {ECO:0000256|RuleBase:RU365079};
KW Transmembrane helix {ECO:0000256|RuleBase:RU365079};
KW Transport {ECO:0000256|RuleBase:RU365079}.
FT TRANSMEM 66..87
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU365079"
FT DOMAIN 143..286
FT /note="FCP1 homology"
FT /evidence="ECO:0000259|PROSITE:PS50969"
FT REGION 24..59
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 353 AA; 39572 MW; 4902AFCE56453BEE CRC64;
MAASAALFSR LRGGLRLGAR GLCTRLATPP PRTPDQAAEI GSRGGTKAQG PQQQPRSEGP
SYAKKVALWL AGLLGAGGTV SVVYIFGNNP VDETGAKIPD EFDNDPILVQ QLRRTYKYFK
DYRQMIIEPT SPCLLPDPLQ EPYYQPPYTL VLELTGVLLH PEWSLATGWR FKKRPGIETL
FQQLAPLYEI VIFTSETGMT AFPLIDSVDP HGFISYRLFR DATRYMDGHH VKDISCLNRD
PARVVVVDCK KEAFSLQPYN GVALRPWDGN SDDRVLLDLS AFLKTIALNG VEDVRTVLEH
YALEDDPLAA FKQRQSRLEQ EEQQRLAELS KSNKQNLLFG SLTSRLWPRS KQP
//