ID   BCS1_BOVIN              Reviewed;         419 AA.
AC   Q5E9H5;
DT   17-APR-2007, integrated into UniProtKB/Swiss-Prot.
DT   15-MAR-2005, sequence version 1.
DT   03-AUG-2022, entry version 113.
DE   RecName: Full=Mitochondrial chaperone BCS1;
DE   AltName: Full=BCS1-like protein;
GN   Name=BCS1L;
OS   Bos taurus (Bovine).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC   Bovinae; Bos.
OX   NCBI_TaxID=9913;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX   PubMed=16305752; DOI=10.1186/1471-2164-6-166;
RA   Harhay G.P., Sonstegard T.S., Keele J.W., Heaton M.P., Clawson M.L.,
RA   Snelling W.M., Wiedmann R.T., Van Tassell C.P., Smith T.P.L.;
RT   "Characterization of 954 bovine full-CDS cDNA sequences.";
RL   BMC Genomics 6:166-166(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=Hereford; TISSUE=Hypothalamus;
RG   NIH - Mammalian Gene Collection (MGC) project;
RL   Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Chaperone necessary for the assembly of mitochondrial
CC       respiratory chain complex III. Plays an important role in the
CC       maintenance of mitochondrial tubular networks, respiratory chain
CC       assembly and formation of the LETM1 complex (By similarity).
CC       {ECO:0000250}.
CC   -!- SUBUNIT: Interacts with LETM1. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane {ECO:0000250};
CC       Single-pass membrane protein {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the AAA ATPase family. BCS1 subfamily.
CC       {ECO:0000305}.
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DR   EMBL; BT020945; AAX08962.1; -; mRNA.
DR   EMBL; BC103135; AAI03136.1; -; mRNA.
DR   RefSeq; NP_001015671.1; NM_001015671.1.
DR   RefSeq; XP_005202918.1; XM_005202861.2.
DR   RefSeq; XP_005202919.1; XM_005202862.1.
DR   RefSeq; XP_010800664.1; XM_010802362.2.
DR   AlphaFoldDB; Q5E9H5; -.
DR   SMR; Q5E9H5; -.
DR   STRING; 9913.ENSBTAP00000004967; -.
DR   PaxDb; Q5E9H5; -.
DR   Ensembl; ENSBTAT00000004967; ENSBTAP00000004967; ENSBTAG00000003813.
DR   GeneID; 539713; -.
DR   KEGG; bta:539713; -.
DR   CTD; 617; -.
DR   VEuPathDB; HostDB:ENSBTAG00000003813; -.
DR   VGNC; VGNC:26456; BCS1L.
DR   eggNOG; KOG0743; Eukaryota.
DR   GeneTree; ENSGT00390000005415; -.
DR   HOGENOM; CLU_010189_6_2_1; -.
DR   InParanoid; Q5E9H5; -.
DR   OMA; EWRQFGH; -.
DR   OrthoDB; 532729at2759; -.
DR   TreeFam; TF315009; -.
DR   Proteomes; UP000009136; Chromosome 2.
DR   Bgee; ENSBTAG00000003813; Expressed in oocyte and 107 other tissues.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005743; C:mitochondrial inner membrane; IBA:GO_Central.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0016887; F:ATP hydrolysis activity; IEA:Ensembl.
DR   GO; GO:0033617; P:mitochondrial cytochrome c oxidase assembly; IEA:Ensembl.
DR   GO; GO:0032981; P:mitochondrial respiratory chain complex I assembly; IEA:Ensembl.
DR   GO; GO:0034551; P:mitochondrial respiratory chain complex III assembly; IBA:GO_Central.
DR   GO; GO:0032979; P:protein insertion into mitochondrial inner membrane from matrix; IBA:GO_Central.
DR   Gene3D; 3.40.50.300; -; 1.
DR   InterPro; IPR003593; AAA+_ATPase.
DR   InterPro; IPR003959; ATPase_AAA_core.
DR   InterPro; IPR003960; ATPase_AAA_CS.
DR   InterPro; IPR014851; BCS1_N.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   Pfam; PF00004; AAA; 1.
DR   Pfam; PF08740; BCS1_N; 1.
DR   SMART; SM00382; AAA; 1.
DR   SMART; SM01024; BCS1_N; 1.
DR   SUPFAM; SSF52540; SSF52540; 1.
DR   PROSITE; PS00674; AAA; 1.
PE   2: Evidence at transcript level;
KW   ATP-binding; Chaperone; Membrane; Mitochondrion;
KW   Mitochondrion inner membrane; Nucleotide-binding; Phosphoprotein;
KW   Reference proteome; Transmembrane; Transmembrane helix.
FT   CHAIN           1..419
FT                   /note="Mitochondrial chaperone BCS1"
FT                   /id="PRO_0000284062"
FT   TOPO_DOM        1..15
FT                   /note="Mitochondrial intermembrane"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        16..32
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        33..419
FT                   /note="Mitochondrial matrix"
FT                   /evidence="ECO:0000255"
FT   BINDING         230..237
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255"
FT   MOD_RES         181
FT                   /note="Phosphotyrosine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9Y276"
SQ   SEQUENCE   419 AA;  47504 MW;  584E714A1DB753FA CRC64;
     MPLSDFVLAL KDNPYFGAGF GLVGVGTALA LARKGAQLGL VAFRRHYMIT LEVPARDRSY
     AWLLSWLTRH STRTQHLSVE TTYLQHESGR ISTKFEFVPS PGNHFIWYQG KWIRVERSRE
     MQMIDLQTGT PWESVTFTAL GTDRKVFFNI LEEARELALQ QEEGKTVMYT AVGSEWRPFG
     YPRRRRPLNS VVLEQGVTER IVRDIREFID NPKWYIDRGI PYRRGYLLYG PPGCGKSSFI
     TALAGELQHS ICLLSLTDSS LSDDRLNHLL SVAPQQSLVL LEDVDAAFLS RDLAAENPIK
     YQGLGRLTFS GLLNALDGVA STEARIVFMT TNHIDRLDPA LIRPGRVDMK EYVGHCSRWQ
     LTQMFQRFYP GQATSLAENF ADRVLQATTQ ISPAQVQGYF MLYKNDPAGA IQNAESLRR