ID A0A3B3VVP5_9TELE Unreviewed; 388 AA.
AC A0A3B3VVP5;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 24-JAN-2024, entry version 23.
DE RecName: Full=Mitochondrial import inner membrane translocase subunit TIM50 {ECO:0000256|RuleBase:RU365079};
OS Poecilia latipinna (sailfin molly).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Atherinomorphae; Cyprinodontiformes; Poeciliidae; Poeciliinae;
OC Poecilia.
OX NCBI_TaxID=48699 {ECO:0000313|Ensembl:ENSPLAP00000029118.1, ECO:0000313|Proteomes:UP000261500};
RN [1] {ECO:0000313|Ensembl:ENSPLAP00000029118.1}
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; A0A3B3VVP5; -.
DR STRING; 48699.ENSPLAP00000029118; -.
DR Ensembl; ENSPLAT00000023763.1; ENSPLAP00000029118.1; ENSPLAG00000019062.1.
DR GeneTree; ENSGT01040000240503; -.
DR Proteomes; UP000261500; Unplaced.
DR GO; GO:0005744; C:TIM23 mitochondrial import inner membrane translocase complex; IEA:UniProtKB-UniRule.
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 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 99..119
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU365079"
FT DOMAIN 205..348
FT /note="FCP1 homology"
FT /evidence="ECO:0000259|PROSITE:PS50969"
FT REGION 64..93
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 78..93
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 388 AA; 43966 MW; 11E37F9CCCFDD382 CRC64;
MSAMFPMCVR ASRSLLRFQS GMSAASSPQQ VLDVIRTLST EKNPPGTGGA TGGLAQAILQ
ERLQQSQGQP PPEGDPGQKD GEQTEDRKQK ENSAYAKKMV LRLAGLMGVG GAASLVYIFD
PSDLMRRCAG GKKPSRGRHT LIIRHEEERT NSEDEQGNRI PDEFDKDPPV VQQLRRTYKY
FKDYRQMIIE PTSPKLLPDP LKEPYYQPPY TLVLELTDVL LHPEWSLSTG WRFKKRPGID
FLFQQLAPLY EIVIFTAETG MTAYPLIDTI DPQGFVMYRL FRDATRYMEG HHVKDVSCLN
RASSKVIVVD CKREAFQLQP FNGLALRKWD GNSDDRTLYD LANFLKAIAL SGVDDVRSVL
ENYALEDDPI EAFKHRQAQL AQVGRFWF
//
