BCS1_HUMAN
ID BCS1_HUMAN Reviewed; 419 AA.
AC Q9Y276; B3KTW9; Q7Z2V7;
DT 29-MAR-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1999, sequence version 1.
DT 03-AUG-2022, entry version 181.
DE RecName: Full=Mitochondrial chaperone BCS1;
DE Short=h-BCS1;
DE AltName: Full=BCS1-like protein;
GN Name=BCS1L; Synonyms=BCS1;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RC TISSUE=Brain;
RX PubMed=9878253; DOI=10.1006/geno.1998.5580;
RA Petruzzella V., Tiranti V., Fernandez P., Ianna P., Carrozzo R.,
RA Zeviani M.;
RT "Identification and characterization of human cDNAs specific to BCS1,
RT PET112, SCO1, COX15, and COX11, five genes involved in the formation and
RT function of the mitochondrial respiratory chain.";
RL Genomics 54:494-504(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], AND VARIANTS MC3DN1 LEU-99; PRO-155; ASN-277
RP AND MET-353.
RX PubMed=11528392; DOI=10.1038/ng706;
RA de Lonlay P., Valnot I., Barrientos A., Gorbatyuk M., Tzagoloff A.,
RA Taanman J.-W., Benayoun E., Chretien D., Kadhom N., Lombes A.,
RA Ogier de Baulny H., Niaudet P., Munnich A., Rustin P., Roetig A.;
RT "A mutant mitochondrial respiratory chain assembly protein causes complex
RT III deficiency in patients with tubulopathy, encephalopathy and liver
RT failure.";
RL Nat. Genet. 29:57-60(2001).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], AND VARIANTS GRACILE GLY-78;
RP GLN-144 AND ALA-327.
RX PubMed=12215968; DOI=10.1086/342773;
RA Visapaeae I., Fellman V., Vesa J., Dasvarma A., Hutton J.L., Kumar V.,
RA Payne G.S., Makarow M., Van Coster R., Taylor R.W., Turnbull D.M.,
RA Suomalainen A., Peltonen L.;
RT "GRACILE syndrome, a lethal metabolic disorder with iron overload, is
RT caused by a point mutation in BCS1L.";
RL Am. J. Hum. Genet. 71:863-876(2002).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain;
RX PubMed=9110174; DOI=10.1101/gr.7.4.353;
RA Yu W., Andersson B., Worley K.C., Muzny D.M., Ding Y., Liu W.,
RA Ricafrente J.Y., Wentland M.A., Lennon G., Gibbs R.A.;
RT "Large-scale concatenation cDNA sequencing.";
RL Genome Res. 7:353-358(1997).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Small intestine;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D.,
RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Muscle;
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 [9]
RP INTERACTION WITH LETM1, FUNCTION, SUBCELLULAR LOCATION, AND
RP CHARACTERIZATION OF VARIANT MC3DN1 PRO-155.
RX PubMed=18628306; DOI=10.1242/jcs.026625;
RA Tamai S., Iida H., Yokota S., Sayano T., Kiguchiya S., Ishihara N.,
RA Hayashi J., Mihara K., Oka T.;
RT "Characterization of the mitochondrial protein LETM1, which maintains the
RT mitochondrial tubular shapes and interacts with the AAA-ATPase BCS1L.";
RL J. Cell Sci. 121:2588-2600(2008).
RN [10]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-181, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [12]
RP CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION
RP BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25944712; DOI=10.1002/pmic.201400617;
RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D.,
RA Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
RT "N-terminome analysis of the human mitochondrial proteome.";
RL Proteomics 15:2519-2524(2015).
RN [13]
RP VARIANT MC3DN1 CYS-45.
RX PubMed=12910490; DOI=10.1002/ajmg.a.20171;
RA De Meirleir L., Seneca S., Damis E., Sepulchre B., Hoorens A., Gerlo E.,
RA Garcia Silva M.T., Hernandez E.M., Lissens W., Van Coster R.;
RT "Clinical and diagnostic characteristics of complex III deficiency due to
RT mutations in the BCS1L gene.";
RL Am. J. Med. Genet. A 121:126-131(2003).
RN [14]
RP VARIANTS MC3DN1 CYS-73; CYS-183; CYS-184 AND ILE-368.
RX PubMed=17403714; DOI=10.1093/hmg/ddm072;
RA Fernandez-Vizarra E., Bugiani M., Goffrini P., Carrara F., Farina L.,
RA Procopio E., Donati A., Uziel G., Ferrero I., Zeviani M.;
RT "Impaired complex III assembly associated with BCS1L gene mutations in
RT isolated mitochondrial encephalopathy.";
RL Hum. Mol. Genet. 16:1241-1252(2007).
RN [15]
RP VARIANTS BJS ARG-35; TRP-114; HIS-183; CYS-184; GLU-302 AND HIS-306,
RP VARIANTS MC3DN1 LEU-99; PRO-155; ASN-277 AND MET-353, AND VARIANTS GRACILE
RP GLY-78; GLN-144 AND ALA-327.
RX PubMed=17314340; DOI=10.1056/nejmoa055262;
RA Hinson J.T., Fantin V.R., Schoenberger J., Breivik N., Siem G.,
RA McDonough B., Sharma P., Keogh I., Godinho R., Santos F., Esparza A.,
RA Nicolau Y., Selvaag E., Cohen B.H., Hoppel C.L., Tranebjaerg L.,
RA Eavey R.D., Seidman J.G., Seidman C.E.;
RT "Missense mutations in the BCS1L gene as a cause of the Bjoernstad
RT syndrome.";
RL N. Engl. J. Med. 356:809-819(2007).
RN [16]
RP VARIANT MC3DN1 ALA-50.
RX PubMed=19162478; DOI=10.1016/j.nmd.2008.11.016;
RA Blazquez A., Gil-Borlado M.C., Moran M., Verdu A., Cazorla-Calleja M.R.,
RA Martin M.A., Arenas J., Ugalde C.;
RT "Infantile mitochondrial encephalomyopathy with unusual phenotype caused by
RT a novel BCS1L mutation in an isolated complex III-deficient patient.";
RL Neuromuscul. Disord. 19:143-146(2009).
RN [17]
RP VARIANT BJS ASN-301.
RX PubMed=24172246; DOI=10.1038/jhg.2013.101;
RA Siddiqi S., Siddiq S., Mansoor A., Oostrik J., Ahmad N., Kazmi S.A.,
RA Kremer H., Qamar R., Schraders M.;
RT "Novel mutation in AAA domain of BCS1L causing Bjornstad syndrome.";
RL J. Hum. Genet. 58:819-821(2013).
RN [18]
RP VARIANT MC3DN1 ARG-129.
RX PubMed=22991165; DOI=10.1007/s10545-012-9536-4;
RA Al-Owain M., Colak D., Albakheet A., Al-Younes B., Al-Humaidi Z.,
RA Al-Sayed M., Al-Hindi H., Al-Sugair A., Al-Muhaideb A., Rahbeeni Z.,
RA Al-Sehli A., Al-Fadhli F., Ozand P.T., Taylor R.W., Kaya N.;
RT "Clinical and biochemical features associated with BCS1L mutation.";
RL J. Inherit. Metab. Dis. 36:813-820(2013).
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.
CC {ECO:0000269|PubMed:18628306}.
CC -!- SUBUNIT: Interacts with LETM1. {ECO:0000269|PubMed:18628306}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane
CC {ECO:0000269|PubMed:18628306, ECO:0000269|PubMed:9878253}; Single-pass
CC membrane protein {ECO:0000269|PubMed:18628306,
CC ECO:0000269|PubMed:9878253}.
CC -!- TISSUE SPECIFICITY: Ubiquitous. {ECO:0000269|PubMed:9878253}.
CC -!- DISEASE: GRACILE syndrome (GRACILE) [MIM:603358]: GRACILE stands for
CC 'growth retardation, aminoaciduria, cholestasis, iron overload, lactic
CC acidosis, and early death'. It is a recessively inherited lethal
CC disease characterized by fetal growth retardation, lactic acidosis,
CC aminoaciduria, cholestasis, and abnormalities in iron metabolism.
CC {ECO:0000269|PubMed:12215968, ECO:0000269|PubMed:17314340}. Note=The
CC disease is caused by variants affecting the gene represented in this
CC entry.
CC -!- DISEASE: Mitochondrial complex III deficiency, nuclear 1 (MC3DN1)
CC [MIM:124000]: A disorder of the mitochondrial respiratory chain
CC resulting in a highly variable phenotype depending on which tissues are
CC affected. Clinical features include mitochondrial encephalopathy,
CC psychomotor retardation, ataxia, severe failure to thrive, liver
CC dysfunction, renal tubulopathy, muscle weakness and exercise
CC intolerance. {ECO:0000269|PubMed:11528392, ECO:0000269|PubMed:12910490,
CC ECO:0000269|PubMed:17314340, ECO:0000269|PubMed:17403714,
CC ECO:0000269|PubMed:18628306, ECO:0000269|PubMed:19162478,
CC ECO:0000269|PubMed:22991165}. Note=The disease is caused by variants
CC affecting the gene represented in this entry.
CC -!- DISEASE: Bjoernstad syndrome (BJS) [MIM:262000]: An autosomal recessive
CC disease characterized by congenital sensorineural hearing loss and
CC twisted hairs (pili torti). Pili torti is a condition in which the hair
CC shafts are flattened at irregular intervals and twisted 180 degrees
CC from the normal axis, making the hair extremely brittle.
CC {ECO:0000269|PubMed:17314340, ECO:0000269|PubMed:24172246}. Note=The
CC disease is caused by variants affecting the gene represented in this
CC entry.
CC -!- SIMILARITY: Belongs to the AAA ATPase family. BCS1 subfamily.
CC {ECO:0000305}.
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DR EMBL; AF026849; AAD08638.1; -; mRNA.
DR EMBL; AF346835; AAK29417.1; -; Genomic_DNA.
DR EMBL; AF516670; AAN05490.1; -; Genomic_DNA.
DR EMBL; AF038195; AAB97365.1; -; mRNA.
DR EMBL; AK096210; BAG53231.1; -; mRNA.
DR EMBL; BX571752; CAE11877.1; -; mRNA.
DR EMBL; CH471063; EAW70634.1; -; Genomic_DNA.
DR EMBL; BC000416; AAH00416.1; -; mRNA.
DR EMBL; BC007500; AAH07500.1; -; mRNA.
DR CCDS; CCDS2419.1; -.
DR RefSeq; NP_001073335.1; NM_001079866.1.
DR RefSeq; NP_001244271.1; NM_001257342.1.
DR RefSeq; NP_001244272.1; NM_001257343.1.
DR RefSeq; NP_001244273.1; NM_001257344.1.
DR RefSeq; NP_001305765.1; NM_001318836.1.
DR RefSeq; NP_001307646.1; NM_001320717.1.
DR RefSeq; NP_004319.1; NM_004328.4.
DR RefSeq; XP_006712741.1; XM_006712678.1.
DR RefSeq; XP_016860120.1; XM_017004631.1.
DR RefSeq; XP_016860121.1; XM_017004632.1.
DR AlphaFoldDB; Q9Y276; -.
DR SMR; Q9Y276; -.
DR BioGRID; 107087; 105.
DR IntAct; Q9Y276; 26.
DR MINT; Q9Y276; -.
DR STRING; 9606.ENSP00000413908; -.
DR TCDB; 3.A.28.1.5; the aaa-atpase, bcs1 (bcs1) family.
DR GlyGen; Q9Y276; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q9Y276; -.
DR PhosphoSitePlus; Q9Y276; -.
DR BioMuta; BCS1L; -.
DR DMDM; 46397351; -.
DR EPD; Q9Y276; -.
DR jPOST; Q9Y276; -.
DR MassIVE; Q9Y276; -.
DR MaxQB; Q9Y276; -.
DR PaxDb; Q9Y276; -.
DR PeptideAtlas; Q9Y276; -.
DR PRIDE; Q9Y276; -.
DR ProteomicsDB; 85679; -.
DR Antibodypedia; 34281; 125 antibodies from 22 providers.
DR DNASU; 617; -.
DR Ensembl; ENST00000359273.8; ENSP00000352219.3; ENSG00000074582.15.
DR Ensembl; ENST00000392109.5; ENSP00000375957.1; ENSG00000074582.15.
DR Ensembl; ENST00000392110.6; ENSP00000375958.2; ENSG00000074582.15.
DR Ensembl; ENST00000392111.7; ENSP00000375959.2; ENSG00000074582.15.
DR Ensembl; ENST00000412366.5; ENSP00000406494.1; ENSG00000074582.15.
DR Ensembl; ENST00000431802.5; ENSP00000413908.1; ENSG00000074582.15.
DR Ensembl; ENST00000439945.5; ENSP00000404999.1; ENSG00000074582.15.
DR GeneID; 617; -.
DR KEGG; hsa:617; -.
DR MANE-Select; ENST00000359273.8; ENSP00000352219.3; NM_001079866.2; NP_001073335.1.
DR UCSC; uc002vip.4; human.
DR CTD; 617; -.
DR DisGeNET; 617; -.
DR GeneCards; BCS1L; -.
DR GeneReviews; BCS1L; -.
DR HGNC; HGNC:1020; BCS1L.
DR HPA; ENSG00000074582; Low tissue specificity.
DR MalaCards; BCS1L; -.
DR MIM; 124000; phenotype.
DR MIM; 262000; phenotype.
DR MIM; 603358; phenotype.
DR MIM; 603647; gene.
DR neXtProt; NX_Q9Y276; -.
DR OpenTargets; ENSG00000074582; -.
DR Orphanet; 123; Bjoernstad syndrome.
DR Orphanet; 53693; GRACILE syndrome.
DR Orphanet; 1460; Isolated complex III deficiency.
DR Orphanet; 254902; Renal tubulopathy-encephalopathy-liver failure syndrome.
DR PharmGKB; PA25327; -.
DR VEuPathDB; HostDB:ENSG00000074582; -.
DR eggNOG; KOG0743; Eukaryota.
DR GeneTree; ENSGT00390000005415; -.
DR HOGENOM; CLU_010189_6_2_1; -.
DR InParanoid; Q9Y276; -.
DR OMA; EWRQFGH; -.
DR OrthoDB; 532729at2759; -.
DR PhylomeDB; Q9Y276; -.
DR TreeFam; TF315009; -.
DR PathwayCommons; Q9Y276; -.
DR Reactome; R-HSA-1268020; Mitochondrial protein import.
DR SignaLink; Q9Y276; -.
DR SIGNOR; Q9Y276; -.
DR BioGRID-ORCS; 617; 334 hits in 1083 CRISPR screens.
DR GeneWiki; BCS1L; -.
DR GenomeRNAi; 617; -.
DR Pharos; Q9Y276; Tbio.
DR PRO; PR:Q9Y276; -.
DR Proteomes; UP000005640; Chromosome 2.
DR RNAct; Q9Y276; protein.
DR Bgee; ENSG00000074582; Expressed in body of pancreas and 192 other tissues.
DR ExpressionAtlas; Q9Y276; baseline and differential.
DR Genevisible; Q9Y276; HS.
DR GO; GO:0005743; C:mitochondrial inner membrane; IBA:GO_Central.
DR GO; GO:0005750; C:mitochondrial respiratory chain complex III; TAS:ProtInc.
DR GO; GO:0005739; C:mitochondrion; IDA:UniProtKB.
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; IMP:UniProtKB.
DR GO; GO:0032981; P:mitochondrial respiratory chain complex I assembly; IMP:UniProtKB.
DR GO; GO:0034551; P:mitochondrial respiratory chain complex III assembly; IMP:UniProtKB.
DR GO; GO:0007005; P:mitochondrion organization; IMP:UniProtKB.
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 ATP-binding; Chaperone; Deafness; Disease variant; Membrane; Mitochondrion;
KW Mitochondrion inner membrane; Nucleotide-binding; Phosphoprotein;
KW Primary mitochondrial disease; Reference proteome; Transmembrane;
KW Transmembrane helix.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:25944712"
FT CHAIN 2..419
FT /note="Mitochondrial chaperone BCS1"
FT /id="PRO_0000084772"
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..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:0007744|PubMed:23186163"
FT VARIANT 35
FT /note="G -> R (in BJS; with mild mitochondrial complex III
FT deficiency; dbSNP:rs121908579)"
FT /evidence="ECO:0000269|PubMed:17314340"
FT /id="VAR_032086"
FT VARIANT 45
FT /note="R -> C (in MC3DN1; dbSNP:rs121908575)"
FT /evidence="ECO:0000269|PubMed:12910490"
FT /id="VAR_032087"
FT VARIANT 50
FT /note="T -> A (in MC3DN1; dbSNP:rs121908580)"
FT /evidence="ECO:0000269|PubMed:19162478"
FT /id="VAR_064615"
FT VARIANT 73
FT /note="R -> C (in MC3DN1; dbSNP:rs140812286)"
FT /evidence="ECO:0000269|PubMed:17403714"
FT /id="VAR_064616"
FT VARIANT 78
FT /note="S -> G (in GRACILE; dbSNP:rs28937590)"
FT /evidence="ECO:0000269|PubMed:12215968,
FT ECO:0000269|PubMed:17314340"
FT /id="VAR_018149"
FT VARIANT 99
FT /note="P -> L (in MC3DN1; dbSNP:rs121908572)"
FT /evidence="ECO:0000269|PubMed:11528392,
FT ECO:0000269|PubMed:17314340"
FT /id="VAR_018159"
FT VARIANT 114
FT /note="R -> W (in BJS; dbSNP:rs778769841)"
FT /evidence="ECO:0000269|PubMed:17314340"
FT /id="VAR_032088"
FT VARIANT 129
FT /note="G -> R (in MC3DN1; dbSNP:rs1057521059)"
FT /evidence="ECO:0000269|PubMed:22991165"
FT /id="VAR_072243"
FT VARIANT 144
FT /note="R -> Q (in GRACILE; dbSNP:rs386833857)"
FT /evidence="ECO:0000269|PubMed:12215968,
FT ECO:0000269|PubMed:17314340"
FT /id="VAR_018160"
FT VARIANT 155
FT /note="R -> P (in MC3DN1; abolishes interaction with LETM1;
FT dbSNP:rs121908573)"
FT /evidence="ECO:0000269|PubMed:11528392,
FT ECO:0000269|PubMed:17314340, ECO:0000269|PubMed:18628306"
FT /id="VAR_018161"
FT VARIANT 183
FT /note="R -> C (in MC3DN1; causes a decreased incorporation
FT of the Rieske iron-sulfur protein UQCRFS1 into complex III;
FT dbSNP:rs144885874)"
FT /evidence="ECO:0000269|PubMed:17403714"
FT /id="VAR_064617"
FT VARIANT 183
FT /note="R -> H (in BJS; dbSNP:rs121908577)"
FT /evidence="ECO:0000269|PubMed:17314340"
FT /id="VAR_032089"
FT VARIANT 184
FT /note="R -> C (in MC3DN1 and BJS; with mild mitochondrial
FT complex III deficiency; causes a decreased incorporation of
FT the Rieske iron-sulfur protein UQCRFS1 into complex III;
FT dbSNP:rs121908578)"
FT /evidence="ECO:0000269|PubMed:17314340,
FT ECO:0000269|PubMed:17403714"
FT /id="VAR_032090"
FT VARIANT 277
FT /note="S -> N (in MC3DN1; dbSNP:rs121908571)"
FT /evidence="ECO:0000269|PubMed:11528392,
FT ECO:0000269|PubMed:17314340"
FT /id="VAR_018162"
FT VARIANT 301
FT /note="Y -> N (in BJS; dbSNP:rs587777278)"
FT /evidence="ECO:0000269|PubMed:24172246"
FT /id="VAR_072244"
FT VARIANT 302
FT /note="Q -> E (in BJS; dbSNP:rs1457171169)"
FT /evidence="ECO:0000269|PubMed:17314340"
FT /id="VAR_032091"
FT VARIANT 306
FT /note="R -> H (in BJS; dbSNP:rs1280810181)"
FT /evidence="ECO:0000269|PubMed:17314340"
FT /id="VAR_032092"
FT VARIANT 327
FT /note="V -> A (in GRACILE; dbSNP:rs386833858)"
FT /evidence="ECO:0000269|PubMed:12215968,
FT ECO:0000269|PubMed:17314340"
FT /id="VAR_018163"
FT VARIANT 353
FT /note="V -> M (in MC3DN1; dbSNP:rs121908574)"
FT /evidence="ECO:0000269|PubMed:11528392,
FT ECO:0000269|PubMed:17314340"
FT /id="VAR_018164"
FT VARIANT 368
FT /note="F -> I (in MC3DN1)"
FT /evidence="ECO:0000269|PubMed:17403714"
FT /id="VAR_064618"
FT CONFLICT 394
FT /note="A -> T (in Ref. 6; CAE11877)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 419 AA; 47534 MW; 7F0F98BA62F2CBB8 CRC64;
MPLSDFILAL KDNPYFGAGF GLVGVGTALA LARKGVQLGL VAFRRHYMIT LEVPARDRSY
AWLLSWLTRH STRTQHLSVE TSYLQHESGR ISTKFEFVPS PGNHFIWYRG KWIRVERSRE
MQMIDLQTGT PWESVTFTAL GTDRKVFFNI LEEARELALQ QEEGKTVMYT AVGSEWRPFG
YPRRRRPLNS VVLQQGLADR IVRDVQEFID NPKWYTDRGI PYRRGYLLYG PPGCGKSSFI
TALAGELEHS ICLLSLTDSS LSDDRLNHLL SVAPQQSLVL LEDVDAAFLS RDLAVENPVK
YQGLGRLTFS GLLNALDGVA STEARIVFMT TNHVDRLDPA LIRPGRVDLK EYVGYCSHWQ
LTQMFQRFYP GQAPSLAENF AEHVLRATNQ ISPAQVQGYF MLYKNDPVGA IHNAESLRR
