COX7B_HUMAN
ID COX7B_HUMAN Reviewed; 80 AA.
AC P24311; B2R4M3; Q6ICR1;
DT 01-MAR-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1994, sequence version 2.
DT 03-AUG-2022, entry version 180.
DE RecName: Full=Cytochrome c oxidase subunit 7B, mitochondrial;
DE AltName: Full=Cytochrome c oxidase polypeptide VIIb;
DE Flags: Precursor;
GN Name=COX7B;
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].
RX PubMed=8382530; DOI=10.1016/0167-4781(93)90301-s;
RA Sadlock J.E., Lightowlers R.N., Capaldi R.A., Schon E.A.;
RT "Isolation of a cDNA specifying subunit VIIb of human cytochrome c
RT oxidase.";
RL Biochim. Biophys. Acta 1172:223-225(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
RA Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
RA Phelan M., Farmer A.;
RT "Cloning of human full-length CDSs in BD Creator(TM) system donor vector.";
RL Submitted (AUG-2003) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
RT "Cloning of human full open reading frames in Gateway(TM) system entry
RT vector (pDONR201).";
RL Submitted (MAY-2004) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Halleck A., Ebert L., Mkoundinya M., Schick M., Eisenstein S., Neubert P.,
RA Kstrang K., Schatten R., Shen B., Henze S., Mar W., Korn B., Zuo D., Hu Y.,
RA LaBaer J.;
RT "Cloning of human full open reading frames in Gateway(TM) system entry
RT vector (pDONR201).";
RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
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 GENOMIC DNA].
RX PubMed=15772651; DOI=10.1038/nature03440;
RA Ross M.T., Grafham D.V., Coffey A.J., Scherer S., McLay K., Muzny D.,
RA Platzer M., Howell G.R., Burrows C., Bird C.P., Frankish A., Lovell F.L.,
RA Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G., Jones M.C.,
RA Hurles M.E., Andrews T.D., Scott C.E., Searle S., Ramser J., Whittaker A.,
RA Deadman R., Carter N.P., Hunt S.E., Chen R., Cree A., Gunaratne P.,
RA Havlak P., Hodgson A., Metzker M.L., Richards S., Scott G., Steffen D.,
RA Sodergren E., Wheeler D.A., Worley K.C., Ainscough R., Ambrose K.D.,
RA Ansari-Lari M.A., Aradhya S., Ashwell R.I., Babbage A.K., Bagguley C.L.,
RA Ballabio A., Banerjee R., Barker G.E., Barlow K.F., Barrett I.P.,
RA Bates K.N., Beare D.M., Beasley H., Beasley O., Beck A., Bethel G.,
RA Blechschmidt K., Brady N., Bray-Allen S., Bridgeman A.M., Brown A.J.,
RA Brown M.J., Bonnin D., Bruford E.A., Buhay C., Burch P., Burford D.,
RA Burgess J., Burrill W., Burton J., Bye J.M., Carder C., Carrel L.,
RA Chako J., Chapman J.C., Chavez D., Chen E., Chen G., Chen Y., Chen Z.,
RA Chinault C., Ciccodicola A., Clark S.Y., Clarke G., Clee C.M., Clegg S.,
RA Clerc-Blankenburg K., Clifford K., Cobley V., Cole C.G., Conquer J.S.,
RA Corby N., Connor R.E., David R., Davies J., Davis C., Davis J., Delgado O.,
RA Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S., Draper H.,
RA Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I., Eades T.,
RA Ellwood M., Emery-Cohen A., Errington H., Evans K.L., Faulkner L.,
RA Francis F., Frankland J., Fraser A.E., Galgoczy P., Gilbert J., Gill R.,
RA Gloeckner G., Gregory S.G., Gribble S., Griffiths C., Grocock R., Gu Y.,
RA Gwilliam R., Hamilton C., Hart E.A., Hawes A., Heath P.D., Heitmann K.,
RA Hennig S., Hernandez J., Hinzmann B., Ho S., Hoffs M., Howden P.J.,
RA Huckle E.J., Hume J., Hunt P.J., Hunt A.R., Isherwood J., Jacob L.,
RA Johnson D., Jones S., de Jong P.J., Joseph S.S., Keenan S., Kelly S.,
RA Kershaw J.K., Khan Z., Kioschis P., Klages S., Knights A.J., Kosiura A.,
RA Kovar-Smith C., Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L.,
RA Liu W., Lloyd C., Lloyd D.M., Loulseged H., Loveland J.E., Lovell J.D.,
RA Lozado R., Lu J., Lyne R., Ma J., Maheshwari M., Matthews L.H.,
RA McDowall J., McLaren S., McMurray A., Meidl P., Meitinger T., Milne S.,
RA Miner G., Mistry S.L., Morgan M., Morris S., Mueller I., Mullikin J.C.,
RA Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N., Okwuonu G., Palmer S.,
RA Pandian R., Parker D., Parrish J., Pasternak S., Patel D., Pearce A.V.,
RA Pearson D.M., Pelan S.E., Perez L., Porter K.M., Ramsey Y., Reichwald K.,
RA Rhodes S., Ridler K.A., Schlessinger D., Schueler M.G., Sehra H.K.,
RA Shaw-Smith C., Shen H., Sheridan E.M., Shownkeen R., Skuce C.D.,
RA Smith M.L., Sotheran E.C., Steingruber H.E., Steward C.A., Storey R.,
RA Swann R.M., Swarbreck D., Tabor P.E., Taudien S., Taylor T., Teague B.,
RA Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S., Tromans A.C.,
RA d'Urso M., Verduzco D., Villasana D., Waldron L., Wall M., Wang Q.,
RA Warren J., Warry G.L., Wei X., West A., Whitehead S.L., Whiteley M.N.,
RA Wilkinson J.E., Willey D.L., Williams G., Williams L., Williamson A.,
RA Williamson H., Wilming L., Woodmansey R.L., Wray P.W., Yen J., Zhang J.,
RA Zhou J., Zoghbi H., Zorilla S., Buck D., Reinhardt R., Poustka A.,
RA Rosenthal A., Lehrach H., Meindl A., Minx P.J., Hillier L.W., Willard H.F.,
RA Wilson R.K., Waterston R.H., Rice C.M., Vaudin M., Coulson A., Nelson D.L.,
RA Weinstock G., Sulston J.E., Durbin R.M., Hubbard T., Gibbs R.A., Beck S.,
RA Rogers J., Bentley D.R.;
RT "The DNA sequence of the human X chromosome.";
RL Nature 434:325-337(2005).
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 (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Ovary;
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 PROTEIN SEQUENCE OF 25-43.
RC TISSUE=Heart;
RX PubMed=1309697; DOI=10.1111/j.1432-1033.1992.tb19847.x;
RA van Kuilenburg A.B.P., van Beeumen J.J., van der Meer N.M., Muijsers A.O.;
RT "Subunits VIIa,b,c of human cytochrome c oxidase. Identification of both
RT 'heart-type' and 'liver-type' isoforms of subunit VIIa in human heart.";
RL Eur. J. Biochem. 203:193-199(1992).
RN [10]
RP FUNCTION, AND INVOLVEMENT IN LSDMCA2.
RX PubMed=23122588; DOI=10.1016/j.ajhg.2012.09.016;
RA Indrieri A., van Rahden V.A., Tiranti V., Morleo M., Iaconis D.,
RA Tammaro R., D'Amato I., Conte I., Maystadt I., Demuth S., Zvulunov A.,
RA Kutsche K., Zeviani M., Franco B.;
RT "Mutations in COX7B cause microphthalmia with linear skin lesions, an
RT unconventional mitochondrial disease.";
RL Am. J. Hum. Genet. 91:942-949(2012).
RN [11]
RP STRUCTURE BY ELECTRON MICROSCOPY (3.90 ANGSTROMS), AND SUBUNIT.
RX PubMed=28844695; DOI=10.1016/j.cell.2017.07.050;
RA Guo R., Zong S., Wu M., Gu J., Yang M.;
RT "Architecture of human mitochondrial respiratory megacomplex I2III2IV2.";
RL Cell 170:1247-1257(2017).
RN [12]
RP STRUCTURE BY ELECTRON MICROSCOPY (3.60 ANGSTROMS) OF 30-78.
RX PubMed=30030519; DOI=10.1038/s41422-018-0071-1;
RA Zong S., Wu M., Gu J., Liu T., Guo R., Yang M.;
RT "Structure of the intact 14-subunit human cytochrome c oxidase.";
RL Cell Res. 28:1026-1034(2018).
CC -!- FUNCTION: Component of the cytochrome c oxidase, the last enzyme in the
CC mitochondrial electron transport chain which drives oxidative
CC phosphorylation. The respiratory chain contains 3 multisubunit
CC complexes succinate dehydrogenase (complex II, CII), ubiquinol-
CC cytochrome c oxidoreductase (cytochrome b-c1 complex, complex III,
CC CIII) and cytochrome c oxidase (complex IV, CIV), that cooperate to
CC transfer electrons derived from NADH and succinate to molecular oxygen,
CC creating an electrochemical gradient over the inner membrane that
CC drives transmembrane transport and the ATP synthase. Cytochrome c
CC oxidase is the component of the respiratory chain that catalyzes the
CC reduction of oxygen to water. Electrons originating from reduced
CC cytochrome c in the intermembrane space (IMS) are transferred via the
CC dinuclear copper A center (CU(A)) of subunit 2 and heme A of subunit 1
CC to the active site in subunit 1, a binuclear center (BNC) formed by
CC heme A3 and copper B (CU(B)). The BNC reduces molecular oxygen to 2
CC water molecules using 4 electrons from cytochrome c in the IMS and 4
CC protons from the mitochondrial matrix (By similarity). Plays a role in
CC proper central nervous system (CNS) development in vertebrates
CC (PubMed:23122588). {ECO:0000250|UniProtKB:P13183,
CC ECO:0000269|PubMed:23122588}.
CC -!- PATHWAY: Energy metabolism; oxidative phosphorylation.
CC {ECO:0000250|UniProtKB:P13183}.
CC -!- SUBUNIT: Component of the cytochrome c oxidase (complex IV, CIV), a
CC multisubunit enzyme composed of 14 subunits. The complex is composed of
CC a catalytic core of 3 subunits MT-CO1, MT-CO2 and MT-CO3, encoded in
CC the mitochondrial DNA, and 11 supernumerary subunits COX4I1 (or
CC COX4I2), COX5A, COX5B, COX6A1 (or COX6A2), COX6B1 (or COX6B2), COX6C,
CC COX7A2 (or COX7A1), COX7B, COX7C, COX8A and NDUFA4, which are encoded
CC in the nuclear genome (PubMed:30030519). The complex exists as a
CC monomer or a dimer and forms supercomplexes (SCs) in the inner
CC mitochondrial membrane with NADH-ubiquinone oxidoreductase (complex I,
CC CI) and ubiquinol-cytochrome c oxidoreductase (cytochrome b-c1 complex,
CC complex III, CIII), resulting in different assemblies (supercomplex
CC SCI(1)III(2)IV(1) and megacomplex MCI(2)III(2)IV(2)) (PubMed:28844695).
CC {ECO:0000269|PubMed:28844695, ECO:0000269|PubMed:30030519}.
CC -!- INTERACTION:
CC P24311; Q14749: GNMT; NbExp=3; IntAct=EBI-2684371, EBI-744239;
CC -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane
CC {ECO:0000269|PubMed:30030519}; Single-pass membrane protein
CC {ECO:0000269|PubMed:30030519}.
CC -!- DISEASE: Linear skin defects with multiple congenital anomalies 2
CC (LSDMCA2) [MIM:300887]: A distinct form of aplasia cutis congenita
CC presenting as multiple linear skin defects on the face and neck
CC associated with poor growth, microcephaly, and facial dysmorphism.
CC Additional features include intellectual disability, nail dystrophy,
CC short stature and cardiac abnormalities. {ECO:0000269|PubMed:23122588}.
CC Note=The disease is caused by variants affecting the gene represented
CC in this entry.
CC -!- SIMILARITY: Belongs to the cytochrome c oxidase VIIb family.
CC {ECO:0000305}.
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DR EMBL; Z14244; CAA78613.1; -; mRNA.
DR EMBL; BT009767; AAP88769.1; -; mRNA.
DR EMBL; CR450332; CAG29328.1; -; mRNA.
DR EMBL; CR542124; CAG46921.1; -; mRNA.
DR EMBL; AK311879; BAG34820.1; -; mRNA.
DR EMBL; AL356235; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471104; EAW98607.1; -; Genomic_DNA.
DR EMBL; BC018386; AAH18386.1; -; mRNA.
DR CCDS; CCDS14437.1; -.
DR PIR; S29856; OSHU7B.
DR RefSeq; NP_001857.1; NM_001866.2.
DR PDB; 5Z62; EM; 3.60 A; K=30-78.
DR PDBsum; 5Z62; -.
DR AlphaFoldDB; P24311; -.
DR SMR; P24311; -.
DR BioGRID; 107742; 19.
DR ComplexPortal; CPX-6123; Mitochondrial respiratory chain complex IV.
DR IntAct; P24311; 5.
DR STRING; 9606.ENSP00000417656; -.
DR DrugBank; DB02659; Cholic Acid.
DR DrugBank; DB04464; N-Formylmethionine.
DR iPTMnet; P24311; -.
DR PhosphoSitePlus; P24311; -.
DR BioMuta; COX7B; -.
DR DMDM; 461804; -.
DR EPD; P24311; -.
DR jPOST; P24311; -.
DR MassIVE; P24311; -.
DR MaxQB; P24311; -.
DR PaxDb; P24311; -.
DR PeptideAtlas; P24311; -.
DR PRIDE; P24311; -.
DR ProteomicsDB; 54196; -.
DR TopDownProteomics; P24311; -.
DR Antibodypedia; 44006; 93 antibodies from 23 providers.
DR DNASU; 1349; -.
DR Ensembl; ENST00000650309.2; ENSP00000497474.1; ENSG00000131174.7.
DR GeneID; 1349; -.
DR KEGG; hsa:1349; -.
DR MANE-Select; ENST00000650309.2; ENSP00000497474.1; NM_001866.3; NP_001857.1.
DR UCSC; uc004ecu.2; human.
DR CTD; 1349; -.
DR DisGeNET; 1349; -.
DR GeneCards; COX7B; -.
DR GeneReviews; COX7B; -.
DR HGNC; HGNC:2291; COX7B.
DR HPA; ENSG00000131174; Tissue enhanced (skeletal muscle, tongue).
DR MalaCards; COX7B; -.
DR MIM; 300885; gene.
DR MIM; 300887; phenotype.
DR neXtProt; NX_P24311; -.
DR OpenTargets; ENSG00000131174; -.
DR Orphanet; 2556; Microphthalmia with linear skin defects syndrome.
DR PharmGKB; PA26809; -.
DR VEuPathDB; HostDB:ENSG00000131174; -.
DR eggNOG; ENOG502S9DG; Eukaryota.
DR GeneTree; ENSGT00390000012178; -.
DR HOGENOM; CLU_172656_0_0_1; -.
DR InParanoid; P24311; -.
DR OMA; GATFCIT; -.
DR OrthoDB; 1571716at2759; -.
DR PhylomeDB; P24311; -.
DR TreeFam; TF105068; -.
DR BioCyc; MetaCyc:HS05498-MON; -.
DR PathwayCommons; P24311; -.
DR Reactome; R-HSA-5628897; TP53 Regulates Metabolic Genes.
DR Reactome; R-HSA-611105; Respiratory electron transport.
DR Reactome; R-HSA-9707564; Cytoprotection by HMOX1.
DR SignaLink; P24311; -.
DR SIGNOR; P24311; -.
DR UniPathway; UPA00705; -.
DR BioGRID-ORCS; 1349; 244 hits in 642 CRISPR screens.
DR ChiTaRS; COX7B; human.
DR GeneWiki; COX7B; -.
DR GenomeRNAi; 1349; -.
DR Pharos; P24311; Tbio.
DR PRO; PR:P24311; -.
DR Proteomes; UP000005640; Chromosome X.
DR RNAct; P24311; protein.
DR Bgee; ENSG00000131174; Expressed in heart right ventricle and 211 other tissues.
DR ExpressionAtlas; P24311; baseline and differential.
DR Genevisible; P24311; HS.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005743; C:mitochondrial inner membrane; TAS:Reactome.
DR GO; GO:0031966; C:mitochondrial membrane; IDA:ComplexPortal.
DR GO; GO:0005751; C:mitochondrial respiratory chain complex IV; IPI:ComplexPortal.
DR GO; GO:0005739; C:mitochondrion; IBA:GO_Central.
DR GO; GO:0045277; C:respiratory chain complex IV; IBA:GO_Central.
DR GO; GO:0004129; F:cytochrome-c oxidase activity; TAS:ProtInc.
DR GO; GO:0045333; P:cellular respiration; IC:ComplexPortal.
DR GO; GO:0007417; P:central nervous system development; IMP:UniProtKB.
DR GO; GO:0006123; P:mitochondrial electron transport, cytochrome c to oxygen; IC:ComplexPortal.
DR CDD; cd01403; Cyt_c_Oxidase_VIIb; 1.
DR Gene3D; 4.10.51.10; -; 1.
DR InterPro; IPR008433; Cyt_c_oxidase_suVIIB.
DR InterPro; IPR023272; Cyt_c_oxidase_suVIIB_dom_sf.
DR PANTHER; PTHR16716; PTHR16716; 1.
DR Pfam; PF05392; COX7B; 1.
DR SUPFAM; SSF81423; SSF81423; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Direct protein sequencing; Membrane; Mitochondrion;
KW Mitochondrion inner membrane; Reference proteome; Transit peptide;
KW Transmembrane; Transmembrane helix.
FT TRANSIT 1..24
FT /note="Mitochondrion"
FT /evidence="ECO:0000269|PubMed:1309697"
FT CHAIN 25..80
FT /note="Cytochrome c oxidase subunit 7B, mitochondrial"
FT /id="PRO_0000006158"
FT TOPO_DOM 25..32
FT /note="Mitochondrial matrix"
FT /evidence="ECO:0000269|PubMed:30030519"
FT TRANSMEM 33..59
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:P13183"
FT TOPO_DOM 60..80
FT /note="Mitochondrial intermembrane"
FT /evidence="ECO:0000269|PubMed:30030519"
FT CONFLICT 29
FT /note="R -> P (in Ref. 9; AA sequence)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 80 AA; 9161 MW; 1EE75BD1AA253E59 CRC64;
MFPLVKSALN RLQVRSIQQT MARQSHQKRT PDFHDKYGNA VLASGATFCI VTWTYVATQV
GIEWNLSPVG RVTPKEWRNQ
