ID   QCR7_DERPT              Reviewed;         118 AA.
AC   A0A0K2GUJ4;
DT   07-OCT-2020, integrated into UniProtKB/Swiss-Prot.
DT   11-NOV-2015, sequence version 1.
DT   25-MAY-2022, entry version 14.
DE   RecName: Full=Cytochrome b-c1 complex subunit 7 {ECO:0000305};
DE   AltName: Full=Allergen Der p 24 {ECO:0000303|PubMed:31139345};
DE   AltName: Full=Complex III subunit 7 {ECO:0000305};
DE   AltName: Full=Complex III subunit VII {ECO:0000305};
DE   AltName: Full=Ubiquinol-cytochrome c reductase binding protein Der p 24 {ECO:0000303|PubMed:31139345};
DE            Short=UQCRB Der p 24 {ECO:0000303|PubMed:31139345};
DE   AltName: Full=Ubiquinol-cytochrome c reductase complex 14 kDa protein {ECO:0000305};
DE   AltName: Allergen=Der p 24.0101 {ECO:0000305};
OS   Dermatophagoides pteronyssinus (European house dust mite).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Chelicerata; Arachnida; Acari;
OC   Acariformes; Sarcoptiformes; Astigmata; Psoroptidia; Analgoidea;
OC   Pyroglyphidae; Dermatophagoidinae; Dermatophagoides.
OX   NCBI_TaxID=6956 {ECO:0000312|EMBL:ALA65345.1};
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 10-28 AND 79-90, ALLERGEN,
RP   REGION, AND 3D-STRUCTURE MODELING.
RX   PubMed=31139345; DOI=10.1186/s13601-019-0266-7;
RA   Cai Z.L., Chen J.J., Zhang Z., Hou Y.B., He Y.S., Sun J.L., Ji K.;
RT   "Identification of immunodominant IgE binding epitopes of Der p 24, a major
RT   allergen of Dermatophagoides pteronyssinus.";
RL   Clin. Transl. Allergy 9:28-28(2019).
CC   -!- FUNCTION: Component of the ubiquinol-cytochrome c oxidoreductase, a
CC       multisubunit transmembrane complex that is part of the mitochondrial
CC       electron transport chain which drives oxidative phosphorylation. The
CC       respiratory chain contains 3 multisubunit complexes succinate
CC       dehydrogenase (complex II, CII), ubiquinol-cytochrome c oxidoreductase
CC       (cytochrome b-c1 complex, complex III, CIII) and cytochrome c oxidase
CC       (complex IV, CIV), that cooperate to transfer electrons derived from
CC       NADH and succinate to molecular oxygen, creating an electrochemical
CC       gradient over the inner membrane that drives transmembrane transport
CC       and the ATP synthase. The cytochrome b-c1 complex catalyzes electron
CC       transfer from ubiquinol to cytochrome c, linking this redox reaction to
CC       translocation of protons across the mitochondrial inner membrane, with
CC       protons being carried across the membrane as hydrogens on the quinol.
CC       In the process called Q cycle, 2 protons are consumed from the matrix,
CC       4 protons are released into the intermembrane space and 2 electrons are
CC       passed to cytochrome c. {ECO:0000250|UniProtKB:Q871K1}.
CC   -!- SUBUNIT: Component of the ubiquinol-cytochrome c oxidoreductase
CC       (cytochrome b-c1 complex, complex III, CIII), a multisubunit enzyme
CC       composed of 3 respiratory subunits cytochrome b, cytochrome c1 and
CC       Rieske protein, 2 core protein subunits, and additional low-molecular
CC       weight protein subunits. The complex exists as an obligatory dimer and
CC       forms supercomplexes (SCs) in the inner mitochondrial membrane with
CC       cytochrome c oxidase (complex IV, CIV). {ECO:0000250|UniProtKB:P00128}.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane; Peripheral membrane
CC       protein; Matrix side {ECO:0000250|UniProtKB:P00128}.
CC   -!- ALLERGEN: Causes an allergic reaction in human. Recombinant protein
CC       binds to IgE in 100% of the 8 patients tested allergic to house dust
CC       mite (HDM). 50% of the 10 HDM-allergic patients tested have positive
CC       skin prick test (SPT) reactions to the recombinant protein.
CC       {ECO:0000269|PubMed:31139345}.
CC   -!- SIMILARITY: Belongs to the UQCRB/QCR7 family.
CC       {ECO:0000255|PIRNR:PIRNR000022}.
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DR   EMBL; KP893174; ALA65345.1; -; mRNA.
DR   AlphaFoldDB; A0A0K2GUJ4; -.
DR   SMR; A0A0K2GUJ4; -.
DR   Allergome; 11912; Der p 24.
DR   Allergome; 11913; Der p 24.0101.
DR   Proteomes; UP000515146; Unplaced.
DR   GO; GO:0099617; C:matrix side of mitochondrial inner membrane; ISS:UniProtKB.
DR   GO; GO:0005750; C:mitochondrial respiratory chain complex III; ISS:UniProtKB.
DR   GO; GO:0006122; P:mitochondrial electron transport, ubiquinol to cytochrome c; ISS:UniProtKB.
DR   Gene3D; 1.10.1090.10; -; 1.
DR   InterPro; IPR003197; QCR7.
DR   InterPro; IPR036544; QCR7_sf.
DR   PANTHER; PTHR12022; PTHR12022; 1.
DR   Pfam; PF02271; UCR_14kD; 1.
DR   PIRSF; PIRSF000022; Bc1_14K; 1.
DR   SUPFAM; SSF81524; SSF81524; 1.
PE   1: Evidence at protein level;
KW   Allergen; Direct protein sequencing; Electron transport; Membrane;
KW   Mitochondrion; Mitochondrion inner membrane; Reference proteome;
KW   Respiratory chain; Transport.
FT   CHAIN           1..118
FT                   /note="Cytochrome b-c1 complex subunit 7"
FT                   /id="PRO_0000451110"
FT   REGION          1..32
FT                   /note="IgE-binding. Immunodominant epitope; induces
FT                   specific IgE antibody production in mice. Causes
FT                   degranulation of rat basophilic leukemia (RBL) cells and
FT                   the release of beta-hexosaminidase from them"
FT                   /evidence="ECO:0000269|PubMed:31139345"
SQ   SEQUENCE   118 AA;  14465 MW;  66F57D296986C879 CRC64;
     MVHLTKTLRF INNPGFRKFY YGLQGYNKYG LYYDDFYDYT DPAHLEAVRR LPPDLYDQHT
     YRVIRASQLE ITKQFLPKEQ WPSYEEDMDK GRFLTPYLDE VMKEKKEKEE WVNFLSKD