ID A0A1S3NQC1_SALSA Unreviewed; 399 AA.
AC A0A1S3NQC1;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 28.
DE RecName: Full=Mitochondrial import inner membrane translocase subunit TIM50 {ECO:0000256|RuleBase:RU365079};
GN Name=LOC106580763 {ECO:0000313|RefSeq:XP_014017623.1};
OS Salmo salar (Atlantic salmon).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Protacanthopterygii; Salmoniformes;
OC Salmonidae; Salmoninae; Salmo.
OX NCBI_TaxID=8030 {ECO:0000313|Proteomes:UP000087266, ECO:0000313|RefSeq:XP_014017623.1};
RN [1] {ECO:0000313|RefSeq:XP_014017623.1}
RP IDENTIFICATION.
RC TISSUE=Muscle {ECO:0000313|RefSeq:XP_014017623.1};
RG RefSeq;
RL Submitted (NOV-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 RefSeq; XP_014017623.1; XM_014162148.1.
DR AlphaFoldDB; A0A1S3NQC1; -.
DR STRING; 8030.ENSSSAP00000087812; -.
DR PaxDb; 8030-ENSSSAP00000087812; -.
DR GeneID; 106580763; -.
DR KEGG; sasa:106580763; -.
DR OrthoDB; 11362at2759; -.
DR Proteomes; UP000087266; Chromosome ssa20.
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|ARBA:ARBA00022792};
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:UP000087266};
KW Transit peptide {ECO:0000256|ARBA:ARBA00022946,
KW ECO:0000256|RuleBase:RU365079};
KW Translocation {ECO:0000256|ARBA:ARBA00023010,
KW ECO:0000256|RuleBase:RU365079}; Transport {ECO:0000256|RuleBase:RU365079}.
FT DOMAIN 190..333
FT /note="FCP1 homology"
FT /evidence="ECO:0000259|PROSITE:PS50969"
FT REGION 73..107
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 89..107
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 399 AA; 44861 MW; B24CC668A3CB2C76 CRC64;
MFTGSVPFKM SATSMFPMCV RASRGLLRLR NGGRGGSNST GVDLIRALST EKPPTGDGSA
TGGLAQAILQ ERLQQQQKSQ GQPPPEGDGD SEQKQDQGED KKQKENTAYA KKMVMRLAGL
MGIGGAVGMV YVFGSNSVDE QGNTIPDQFD NDAPVIQQLR RTFKYFQDYR QMIIEPTSPK
LLPDPLREPY YQPPYTLVLE LTDVLLHPEW SLATGWRFKK RPGIDYLFQQ LAPLYEIVIF
TAETGMTAYP LIDSIDPQGF VMYRLFRDAT RYMEGYHVKD VSCLNRDTSK VIVVDCKREA
FSLQPFNGMA LTKWDGNSED RTLYDLAHFL KTIALSGVDD VRSVLENYAL EDDPIEAFKR
RQAQLAQEEE QRLAELAQPK KQGISLGSIA GRFWRSKQQ
//
