BCS1_MOUSE
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 03-AUG-2022, entry version 145.
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, Pancreas,
RC 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 SMR; Q9CZP5; -.
DR BioGRID; 211741; 2.
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; Q9CZP5; -.
DR PeptideAtlas; Q9CZP5; -.
DR PRIDE; Q9CZP5; -.
DR ProteomicsDB; 265168; -.
DR Antibodypedia; 34281; 125 antibodies from 22 providers.
DR DNASU; 66821; -.
DR Ensembl; ENSMUST00000027358; ENSMUSP00000027358; ENSMUSG00000026172.
DR Ensembl; ENSMUST00000113732; ENSMUSP00000109361; ENSMUSG00000026172.
DR Ensembl; ENSMUST00000113733; ENSMUSP00000109362; ENSMUSG00000026172.
DR GeneID; 66821; -.
DR KEGG; mmu:66821; -.
DR UCSC; uc007bmq.2; mouse.
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; EWRQFGH; -.
DR OrthoDB; 532729at2759; -.
DR PhylomeDB; Q9CZP5; -.
DR TreeFam; TF315009; -.
DR BioGRID-ORCS; 66821; 23 hits in 57 CRISPR screens.
DR PRO; PR:Q9CZP5; -.
DR Proteomes; UP000000589; Chromosome 1.
DR RNAct; Q9CZP5; protein.
DR Bgee; ENSMUSG00000026172; Expressed in interventricular septum and 243 other tissues.
DR Genevisible; Q9CZP5; MM.
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: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 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 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
