ID   BCS1_MOUSE              Reviewed;         418 AA.
AC   Q9CZP5;
DT   13-APR-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2001, sequence version 1.
DT   27-MAR-2024, entry version 154.
DE   RecName: Full=Mitochondrial chaperone BCS1;
DE   AltName: Full=BCS1-like protein;
GN   Name=Bcs1l;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Cecum, and Cerebellum;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA   Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA   Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA   Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA   Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA   Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA   Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA   Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA   Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA   Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA   Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA   Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA   Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA   Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA   Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA   Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA   Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA   Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA   Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA   Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA   van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA   Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA   Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA   Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA   Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA   Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA   Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA   Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA   Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Mammary tumor;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA project:
RT   the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3]
RP   PROTEIN SEQUENCE OF 2-11, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC   STRAIN=C57BL/6J; TISSUE=Brain;
RA   Lubec G., Kang S.U.;
RL   Submitted (APR-2007) to UniProtKB.
RN   [4]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung,
RC   Pancreas, Spleen, and Testis;
RX   PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA   Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA   Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT   "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL   Cell 143:1174-1189(2010).
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; AK012324; BAB28162.1; -; mRNA.
DR   EMBL; AK078925; BAC37464.1; -; mRNA.
DR   EMBL; AK079385; BAC37629.1; -; mRNA.
DR   EMBL; BC019781; AAH19781.1; -; mRNA.
DR   CCDS; CCDS15051.1; -.
DR   RefSeq; NP_001292581.1; NM_001305652.1.
DR   RefSeq; NP_080060.1; NM_025784.5.
DR   PDB; 6U1Y; X-ray; 2.17 A; A/B/C/D/E/F/G=151-418.
DR   PDB; 6UKO; X-ray; 4.40 A; A/B/C/D/E/F/G=1-418.
DR   PDB; 6UKP; EM; 3.81 A; A/B/C/D/E/F/G=1-418.
DR   PDB; 6UKS; EM; 3.20 A; A/B/C/D/E/F/G=1-418.
DR   PDBsum; 6U1Y; -.
DR   PDBsum; 6UKO; -.
DR   PDBsum; 6UKP; -.
DR   PDBsum; 6UKS; -.
DR   AlphaFoldDB; Q9CZP5; -.
DR   EMDB; EMD-20808; -.
DR   EMDB; EMD-20811; -.
DR   SMR; Q9CZP5; -.
DR   BioGRID; 211741; 3.
DR   IntAct; Q9CZP5; 1.
DR   MINT; Q9CZP5; -.
DR   STRING; 10090.ENSMUSP00000027358; -.
DR   iPTMnet; Q9CZP5; -.
DR   PhosphoSitePlus; Q9CZP5; -.
DR   SwissPalm; Q9CZP5; -.
DR   EPD; Q9CZP5; -.
DR   jPOST; Q9CZP5; -.
DR   MaxQB; Q9CZP5; -.
DR   PaxDb; 10090-ENSMUSP00000027358; -.
DR   PeptideAtlas; Q9CZP5; -.
DR   ProteomicsDB; 265168; -.
DR   Pumba; Q9CZP5; -.
DR   Antibodypedia; 34281; 137 antibodies from 22 providers.
DR   DNASU; 66821; -.
DR   Ensembl; ENSMUST00000027358.11; ENSMUSP00000027358.5; ENSMUSG00000026172.13.
DR   Ensembl; ENSMUST00000113732.2; ENSMUSP00000109361.2; ENSMUSG00000026172.13.
DR   Ensembl; ENSMUST00000113733.10; ENSMUSP00000109362.4; ENSMUSG00000026172.13.
DR   GeneID; 66821; -.
DR   KEGG; mmu:66821; -.
DR   UCSC; uc007bmq.2; mouse.
DR   AGR; MGI:1914071; -.
DR   CTD; 617; -.
DR   MGI; MGI:1914071; Bcs1l.
DR   VEuPathDB; HostDB:ENSMUSG00000026172; -.
DR   eggNOG; KOG0743; Eukaryota.
DR   GeneTree; ENSGT00390000005415; -.
DR   HOGENOM; CLU_010189_6_2_1; -.
DR   InParanoid; Q9CZP5; -.
DR   OMA; WMTLYQR; -.
DR   OrthoDB; 664379at2759; -.
DR   PhylomeDB; Q9CZP5; -.
DR   TreeFam; TF315009; -.
DR   BioGRID-ORCS; 66821; 23 hits in 60 CRISPR screens.
DR   PRO; PR:Q9CZP5; -.
DR   Proteomes; UP000000589; Chromosome 1.
DR   RNAct; Q9CZP5; Protein.
DR   Bgee; ENSMUSG00000026172; Expressed in interventricular septum and 246 other cell types or tissues.
DR   GO; GO:0005743; C:mitochondrial inner membrane; IBA:GO_Central.
DR   GO; GO:0005739; C:mitochondrion; IMP:MGI.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0016887; F:ATP hydrolysis activity; IDA:FlyBase.
DR   GO; GO:0008566; F:mitochondrial protein-transporting ATPase activity; NAS:FlyBase.
DR   GO; GO:0033617; P:mitochondrial cytochrome c oxidase assembly; ISO:MGI.
DR   GO; GO:0032981; P:mitochondrial respiratory chain complex I assembly; ISO:MGI.
DR   GO; GO:0034551; P:mitochondrial respiratory chain complex III assembly; IMP:MGI.
DR   GO; GO:0007005; P:mitochondrion organization; ISO:MGI.
DR   GO; GO:0032979; P:protein insertion into mitochondrial inner membrane from matrix; IBA:GO_Central.
DR   CDD; cd19510; RecA-like_BCS1; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 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   PANTHER; PTHR23070; BCS1 AAA-TYPE ATPASE; 1.
DR   PANTHER; PTHR23070:SF232; MITOCHONDRIAL CHAPERONE BCS1; 1.
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; P-loop containing nucleoside triphosphate hydrolases; 1.
DR   PROSITE; PS00674; AAA; 1.
DR   Genevisible; Q9CZP5; MM.
PE   1: Evidence at protein level;
KW   3D-structure; ATP-binding; Chaperone; Direct protein sequencing; Membrane;
KW   Mitochondrion; Mitochondrion inner membrane; Nucleotide-binding;
KW   Phosphoprotein; Reference proteome; Transmembrane; Transmembrane helix.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000250|UniProtKB:Q9Y276"
FT   CHAIN           2..418
FT                   /note="Mitochondrial chaperone BCS1"
FT                   /id="PRO_0000084773"
FT   TOPO_DOM        2..15
FT                   /note="Mitochondrial intermembrane"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        16..32
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        33..418
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"
FT   STRAND          50..52
FT                   /evidence="ECO:0007829|PDB:6UKS"
FT   STRAND          56..59
FT                   /evidence="ECO:0007829|PDB:6UKS"
FT   HELIX           60..70
FT                   /evidence="ECO:0007829|PDB:6UKS"
FT   STRAND          80..84
FT                   /evidence="ECO:0007829|PDB:6UKS"
FT   HELIX           87..89
FT                   /evidence="ECO:0007829|PDB:6UKS"
FT   STRAND          92..96
FT                   /evidence="ECO:0007829|PDB:6UKS"
FT   STRAND          101..107
FT                   /evidence="ECO:0007829|PDB:6UKS"
FT   STRAND          109..117
FT                   /evidence="ECO:0007829|PDB:6UKS"
FT   STRAND          125..130
FT                   /evidence="ECO:0007829|PDB:6UKS"
FT   STRAND          136..140
FT                   /evidence="ECO:0007829|PDB:6UKS"
FT   HELIX           145..161
FT                   /evidence="ECO:0007829|PDB:6UKS"
FT   STRAND          163..166
FT                   /evidence="ECO:0007829|PDB:6UKS"
FT   STRAND          168..172
FT                   /evidence="ECO:0007829|PDB:6U1Y"
FT   STRAND          175..178
FT                   /evidence="ECO:0007829|PDB:6U1Y"
FT   HELIX           188..190
FT                   /evidence="ECO:0007829|PDB:6U1Y"
FT   HELIX           197..209
FT                   /evidence="ECO:0007829|PDB:6U1Y"
FT   HELIX           212..218
FT                   /evidence="ECO:0007829|PDB:6U1Y"
FT   STRAND          222..229
FT                   /evidence="ECO:0007829|PDB:6U1Y"
FT   HELIX           236..246
FT                   /evidence="ECO:0007829|PDB:6U1Y"
FT   STRAND          250..253
FT                   /evidence="ECO:0007829|PDB:6U1Y"
FT   HELIX           263..271
FT                   /evidence="ECO:0007829|PDB:6U1Y"
FT   STRAND          275..281
FT                   /evidence="ECO:0007829|PDB:6U1Y"
FT   HELIX           284..287
FT                   /evidence="ECO:0007829|PDB:6U1Y"
FT   STRAND          303..306
FT                   /evidence="ECO:0007829|PDB:6UKS"
FT   HELIX           309..316
FT                   /evidence="ECO:0007829|PDB:6U1Y"
FT   STRAND          317..320
FT                   /evidence="ECO:0007829|PDB:6UKS"
FT   STRAND          323..332
FT                   /evidence="ECO:0007829|PDB:6U1Y"
FT   HELIX           334..336
FT                   /evidence="ECO:0007829|PDB:6U1Y"
FT   HELIX           339..342
FT                   /evidence="ECO:0007829|PDB:6U1Y"
FT   TURN            344..346
FT                   /evidence="ECO:0007829|PDB:6U1Y"
FT   STRAND          348..352
FT                   /evidence="ECO:0007829|PDB:6U1Y"
FT   HELIX           358..368
FT                   /evidence="ECO:0007829|PDB:6U1Y"
FT   HELIX           374..387
FT                   /evidence="ECO:0007829|PDB:6U1Y"
FT   HELIX           393..400
FT                   /evidence="ECO:0007829|PDB:6U1Y"
FT   HELIX           407..412
FT                   /evidence="ECO:0007829|PDB:6U1Y"
FT   HELIX           414..417
FT                   /evidence="ECO:0007829|PDB:6U1Y"
SQ   SEQUENCE   418 AA;  47406 MW;  94905BA9B097F0DE CRC64;
     MPFSDFVLAL KDNPYFGAGF GLVGVGTALA MARKGAQLGL VAFRRHYMIT LEVPARDRSY
     AWLLSWLTRH STRTQHLSVE TSYLQHESGR ISTKFEFIPS PGNHFIWYQG KWIRVERNRD
     MQMVDLQTGT PWESVTFTAL GTDRKVFFNI LEEARALALQ QEEGKTVMYT AVGSEWRTFG
     YPRRRRPLDS VVLQQGLADR IVKDIREFID NPKWYIDRGI PYRRGYLLYG PPGCGKSSFI
     TALAGELEHS ICLLSLTDSS LSDDRLNHLL SVAPQQSLVL LEDVDAAFLS RDLAVENPIK
     YQGLGRLTFS GLLNALDGVA STEARIVFMT TNYIDRLDPA LIRPGRVDLK EYVGYCSHWQ
     LTQMFQRFYP GQAPSLAENF AEHVLKATSE ISPAQVQGYF MLYKNDPMGA VHNIESLR
//