QCR2_HUMAN
ID QCR2_HUMAN Reviewed; 453 AA.
AC P22695; B3KSN4; Q9BQ05;
DT 01-AUG-1991, integrated into UniProtKB/Swiss-Prot.
DT 11-JUL-2002, sequence version 3.
DT 03-AUG-2022, entry version 213.
DE RecName: Full=Cytochrome b-c1 complex subunit 2, mitochondrial;
DE AltName: Full=Complex III subunit 2;
DE AltName: Full=Core protein II;
DE AltName: Full=Ubiquinol-cytochrome-c reductase complex core protein 2;
DE Flags: Precursor;
GN Name=UQCRC2;
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], AND VARIANT GLN-183.
RX PubMed=2547763; DOI=10.1016/s0021-9258(18)80022-9;
RA Hosokawa Y., Suzuki H., Toda H., Nishikimi M., Ozawa T.;
RT "Complementary DNA encoding core protein II of human mitochondrial
RT cytochrome bc1 complex. Substantial diversity in deduced primary structure
RT from its yeast counterpart.";
RL J. Biol. Chem. 264:13483-13488(1989).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Uterus;
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 [3]
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Lung, and Skin;
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 [5]
RP PROTEIN SEQUENCE OF 43-60; 71-84 AND 200-217, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RC TISSUE=Brain, and Cajal-Retzius cell;
RA Lubec G., Vishwanath V.;
RL Submitted (MAR-2007) to UniProtKB.
RN [6]
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 [7]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [8]
RP IDENTIFICATION 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 [9]
RP FUNCTION.
RX PubMed=29243944; DOI=10.1080/15384101.2017.1417707;
RA Fernandez-Vizarra E., Zeviani M.;
RT "Mitochondrial complex III Rieske Fe-S protein processing and assembly.";
RL Cell Cycle 17:681-687(2018).
RN [10]
RP IDENTIFICATION BY MASS SPECTROMETRY, AND INTERACTION WITH RAB5IF.
RX PubMed=31536960; DOI=10.1016/j.isci.2019.08.057;
RA Moutaoufik M.T., Malty R., Amin S., Zhang Q., Phanse S., Gagarinova A.,
RA Zilocchi M., Hoell L., Minic Z., Gagarinova M., Aoki H., Stockwell J.,
RA Jessulat M., Goebels F., Broderick K., Scott N.E., Vlasblom J., Musso G.,
RA Prasad B., Lamantea E., Garavaglia B., Rajput A., Murayama K., Okazaki Y.,
RA Foster L.J., Bader G.D., Cayabyab F.S., Babu M.;
RT "Rewiring of the Human Mitochondrial Interactome during Neuronal
RT Reprogramming Reveals Regulators of the Respirasome and Neurogenesis.";
RL IScience 19:1114-1132(2019).
RN [11]
RP STRUCTURE BY ELECTRON MICROSCOPY (3.40 ANGSTROMS).
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 VARIANT [LARGE SCALE ANALYSIS] TYR-208.
RX PubMed=16959974; DOI=10.1126/science.1133427;
RA Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D.,
RA Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P.,
RA Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V.,
RA Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H.,
RA Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W.,
RA Velculescu V.E.;
RT "The consensus coding sequences of human breast and colorectal cancers.";
RL Science 314:268-274(2006).
RN [13]
RP VARIANT MC3DN5 TRP-183.
RX PubMed=23281071; DOI=10.1002/humu.22257;
RA Miyake N., Yano S., Sakai C., Hatakeyama H., Matsushima Y., Shiina M.,
RA Watanabe Y., Bartley J., Abdenur J.E., Wang R.Y., Chang R., Tsurusaki Y.,
RA Doi H., Nakashima M., Saitsu H., Ogata K., Goto Y., Matsumoto N.;
RT "Mitochondrial complex III deficiency caused by a homozygous UQCRC2
RT mutation presenting with neonatal-onset recurrent metabolic
RT decompensation.";
RL Hum. Mutat. 34:446-452(2013).
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 (By similarity). The 2 core subunits UQCRC1/QCR1
CC and UQCRC2/QCR2 are homologous to the 2 mitochondrial-processing
CC peptidase (MPP) subunits beta-MPP and alpha-MPP respectively, and they
CC seem to have preserved their MPP processing properties (By similarity).
CC May be involved in the in situ processing of UQCRFS1 into the mature
CC Rieske protein and its mitochondrial targeting sequence (MTS)/subunit 9
CC when incorporated into complex III (Probable).
CC {ECO:0000250|UniProtKB:P07257, ECO:0000250|UniProtKB:P23004,
CC ECO:0000305|PubMed:29243944}.
CC -!- SUBUNIT: Component of the ubiquinol-cytochrome c oxidoreductase
CC (cytochrome b-c1 complex, complex III, CIII), a multisubunit enzyme
CC composed of 11 subunits. The complex is composed of 3 respiratory
CC subunits cytochrome b, cytochrome c1 and Rieske protein UQCRFS1, 2 core
CC protein subunits UQCRC1/QCR1 and UQCRC2/QCR2, and 6 low-molecular
CC weight protein subunits UQCRH/QCR6, UQCRB/QCR7, UQCRQ/QCR8,
CC UQCR10/QCR9, UQCR11/QCR10 and subunit 9, the cleavage product of Rieske
CC protein UQCRFS1 (By similarity). The complex exists as an obligatory
CC dimer and forms supercomplexes (SCs) in the inner mitochondrial
CC membrane with NADH-ubiquinone oxidoreductase (complex I, CI) and
CC cytochrome c oxidase (complex IV, CIV), resulting in different
CC assemblies (supercomplex SCI(1)III(2)IV(1) and megacomplex
CC MCI(2)III(2)IV(2)) (PubMed:28844695). Interacts with RAB5IF
CC (PubMed:31536960). Interacts with STMP1 (By similarity).
CC {ECO:0000250|UniProtKB:P23004, ECO:0000250|UniProtKB:Q9DB77,
CC ECO:0000269|PubMed:28844695, ECO:0000269|PubMed:31536960}.
CC -!- INTERACTION:
CC P22695; Q15027: ACAP1; NbExp=3; IntAct=EBI-1051424, EBI-751746;
CC P22695; O00555: CACNA1A; NbExp=2; IntAct=EBI-1051424, EBI-766279;
CC P22695; Q8N7T0: hCG_1820408; NbExp=3; IntAct=EBI-1051424, EBI-25858908;
CC P22695; Q9H2C1: LHX5; NbExp=3; IntAct=EBI-1051424, EBI-25835523;
CC P22695; Q13573: SNW1; NbExp=3; IntAct=EBI-1051424, EBI-632715;
CC -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane
CC {ECO:0000250|UniProtKB:P07257}; Peripheral membrane protein
CC {ECO:0000250|UniProtKB:P07257}; Matrix side
CC {ECO:0000250|UniProtKB:P07257}.
CC -!- DISEASE: Mitochondrial complex III deficiency, nuclear 5 (MC3DN5)
CC [MIM:615160]: 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:23281071}. Note=The disease is caused
CC by variants affecting the gene represented in this entry.
CC -!- SIMILARITY: Belongs to the peptidase M16 family. UQCRC2/QCR2 subfamily.
CC {ECO:0000305}.
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DR EMBL; J04973; AAA35710.1; -; mRNA.
DR EMBL; AK094006; BAG52796.1; -; mRNA.
DR EMBL; CH471249; EAW50592.1; -; Genomic_DNA.
DR EMBL; BC003136; AAH03136.1; -; mRNA.
DR EMBL; BC000484; AAH00484.1; -; mRNA.
DR CCDS; CCDS10601.1; -.
DR PIR; A32629; A32629.
DR RefSeq; NP_003357.2; NM_003366.3.
DR PDB; 5XTE; EM; 3.40 A; K/W=35-453.
DR PDB; 5XTH; EM; 3.90 A; AK/AW=35-453.
DR PDB; 5XTI; EM; 17.40 A; AK/AW=35-453.
DR PDBsum; 5XTE; -.
DR PDBsum; 5XTH; -.
DR PDBsum; 5XTI; -.
DR AlphaFoldDB; P22695; -.
DR SMR; P22695; -.
DR BioGRID; 113231; 312.
DR ComplexPortal; CPX-560; Mitochondrial respiratory chain complex III.
DR IntAct; P22695; 75.
DR MINT; P22695; -.
DR STRING; 9606.ENSP00000268379; -.
DR DrugBank; DB07763; (5S)-3-ANILINO-5-(2,4-DIFLUOROPHENYL)-5-METHYL-1,3-OXAZOLIDINE-2,4-DIONE.
DR DrugBank; DB07778; (S)-famoxadone.
DR DrugBank; DB04141; 2-Hexyloxy-6-Hydroxymethyl-Tetrahydro-Pyran-3,4,5-Triol.
DR DrugBank; DB08453; 2-Nonyl-4-quinolinol 1-oxide.
DR DrugBank; DB04799; 6-Hydroxy-5-undecyl-4,7-benzothiazoledione.
DR DrugBank; DB07401; Azoxystrobin.
DR DrugBank; DB08330; METHYL (2Z)-3-METHOXY-2-{2-[(E)-2-PHENYLVINYL]PHENYL}ACRYLATE.
DR DrugBank; DB08690; Ubiquinone Q2.
DR MEROPS; M16.974; -.
DR CarbonylDB; P22695; -.
DR GlyGen; P22695; 2 sites, 1 O-linked glycan (2 sites).
DR iPTMnet; P22695; -.
DR MetOSite; P22695; -.
DR PhosphoSitePlus; P22695; -.
DR SwissPalm; P22695; -.
DR BioMuta; UQCRC2; -.
DR DMDM; 21903482; -.
DR REPRODUCTION-2DPAGE; IPI00305383; -.
DR UCD-2DPAGE; P22695; -.
DR CPTAC; CPTAC-138; -.
DR CPTAC; CPTAC-139; -.
DR EPD; P22695; -.
DR jPOST; P22695; -.
DR MassIVE; P22695; -.
DR MaxQB; P22695; -.
DR PaxDb; P22695; -.
DR PeptideAtlas; P22695; -.
DR PRIDE; P22695; -.
DR ProteomicsDB; 54028; -.
DR TopDownProteomics; P22695; -.
DR Antibodypedia; 1267; 245 antibodies from 30 providers.
DR DNASU; 7385; -.
DR Ensembl; ENST00000268379.9; ENSP00000268379.4; ENSG00000140740.11.
DR GeneID; 7385; -.
DR KEGG; hsa:7385; -.
DR MANE-Select; ENST00000268379.9; ENSP00000268379.4; NM_003366.4; NP_003357.2.
DR UCSC; uc002djx.4; human.
DR CTD; 7385; -.
DR DisGeNET; 7385; -.
DR GeneCards; UQCRC2; -.
DR HGNC; HGNC:12586; UQCRC2.
DR HPA; ENSG00000140740; Tissue enhanced (skeletal muscle, tongue).
DR MalaCards; UQCRC2; -.
DR MIM; 191329; gene.
DR MIM; 615160; phenotype.
DR neXtProt; NX_P22695; -.
DR OpenTargets; ENSG00000140740; -.
DR Orphanet; 1460; Isolated complex III deficiency.
DR PharmGKB; PA37217; -.
DR VEuPathDB; HostDB:ENSG00000140740; -.
DR eggNOG; KOG2583; Eukaryota.
DR GeneTree; ENSGT00940000154915; -.
DR HOGENOM; CLU_009902_0_0_1; -.
DR InParanoid; P22695; -.
DR OMA; WVGEFFT; -.
DR OrthoDB; 1000258at2759; -.
DR PhylomeDB; P22695; -.
DR TreeFam; TF105033; -.
DR BioCyc; MetaCyc:HS06753-MON; -.
DR PathwayCommons; P22695; -.
DR Reactome; R-HSA-611105; Respiratory electron transport.
DR SignaLink; P22695; -.
DR SIGNOR; P22695; -.
DR BioGRID-ORCS; 7385; 396 hits in 1087 CRISPR screens.
DR ChiTaRS; UQCRC2; human.
DR GeneWiki; UQCRC2; -.
DR GenomeRNAi; 7385; -.
DR Pharos; P22695; Tbio.
DR PRO; PR:P22695; -.
DR Proteomes; UP000005640; Chromosome 16.
DR RNAct; P22695; protein.
DR Bgee; ENSG00000140740; Expressed in heart right ventricle and 208 other tissues.
DR ExpressionAtlas; P22695; baseline and differential.
DR Genevisible; P22695; HS.
DR GO; GO:0005743; C:mitochondrial inner membrane; IDA:ComplexPortal.
DR GO; GO:0005750; C:mitochondrial respiratory chain complex III; IDA:UniProtKB.
DR GO; GO:0005751; C:mitochondrial respiratory chain complex IV; IDA:UniProtKB.
DR GO; GO:0005739; C:mitochondrion; IDA:HPA.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0046872; F:metal ion binding; IEA:InterPro.
DR GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro.
DR GO; GO:0009060; P:aerobic respiration; TAS:ProtInc.
DR GO; GO:0045333; P:cellular respiration; IC:ComplexPortal.
DR GO; GO:0006122; P:mitochondrial electron transport, ubiquinol to cytochrome c; IC:ComplexPortal.
DR GO; GO:0006119; P:oxidative phosphorylation; TAS:ProtInc.
DR GO; GO:0006508; P:proteolysis; IEA:InterPro.
DR InterPro; IPR011249; Metalloenz_LuxS/M16.
DR InterPro; IPR011765; Pept_M16_N.
DR InterPro; IPR001431; Pept_M16_Zn_BS.
DR InterPro; IPR007863; Peptidase_M16_C.
DR Pfam; PF00675; Peptidase_M16; 1.
DR Pfam; PF05193; Peptidase_M16_C; 1.
DR SUPFAM; SSF63411; SSF63411; 2.
DR PROSITE; PS00143; INSULINASE; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Direct protein sequencing; Disease variant;
KW Electron transport; Membrane; Mitochondrion; Mitochondrion inner membrane;
KW Primary mitochondrial disease; Reference proteome; Respiratory chain;
KW Transit peptide; Transport.
FT TRANSIT 1..14
FT /note="Mitochondrion"
FT CHAIN 15..453
FT /note="Cytochrome b-c1 complex subunit 2, mitochondrial"
FT /id="PRO_0000026791"
FT MOD_RES 66
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q9DB77"
FT MOD_RES 199
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q9DB77"
FT MOD_RES 250
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q9DB77"
FT VARIANT 148
FT /note="R -> S (in dbSNP:rs2228473)"
FT /id="VAR_029336"
FT VARIANT 183
FT /note="R -> Q (in dbSNP:rs4850)"
FT /evidence="ECO:0000269|PubMed:2547763"
FT /id="VAR_034582"
FT VARIANT 183
FT /note="R -> W (in MC3DN5; dbSNP:rs374661051)"
FT /evidence="ECO:0000269|PubMed:23281071"
FT /id="VAR_069709"
FT VARIANT 208
FT /note="F -> Y (in a colorectal cancer sample; somatic
FT mutation)"
FT /evidence="ECO:0000269|PubMed:16959974"
FT /id="VAR_036479"
FT VARIANT 254
FT /note="R -> H (in dbSNP:rs11863893)"
FT /id="VAR_034583"
FT CONFLICT 360
FT /note="T -> R (in Ref. 1; AAA35710)"
FT /evidence="ECO:0000305"
FT STRAND 48..51
FT /evidence="ECO:0007829|PDB:5XTE"
FT STRAND 57..66
FT /evidence="ECO:0007829|PDB:5XTE"
FT HELIX 69..71
FT /evidence="ECO:0007829|PDB:5XTE"
FT HELIX 79..83
FT /evidence="ECO:0007829|PDB:5XTE"
FT HELIX 85..88
FT /evidence="ECO:0007829|PDB:5XTE"
FT STRAND 91..93
FT /evidence="ECO:0007829|PDB:5XTE"
FT HELIX 96..106
FT /evidence="ECO:0007829|PDB:5XTE"
FT STRAND 109..114
FT /evidence="ECO:0007829|PDB:5XTE"
FT STRAND 119..126
FT /evidence="ECO:0007829|PDB:5XTE"
FT HELIX 127..129
FT /evidence="ECO:0007829|PDB:5XTE"
FT HELIX 130..142
FT /evidence="ECO:0007829|PDB:5XTE"
FT HELIX 148..154
FT /evidence="ECO:0007829|PDB:5XTE"
FT HELIX 157..165
FT /evidence="ECO:0007829|PDB:5XTE"
FT HELIX 169..181
FT /evidence="ECO:0007829|PDB:5XTE"
FT STRAND 182..184
FT /evidence="ECO:0007829|PDB:5XTE"
FT HELIX 185..187
FT /evidence="ECO:0007829|PDB:5XTE"
FT HELIX 194..196
FT /evidence="ECO:0007829|PDB:5XTE"
FT TURN 197..199
FT /evidence="ECO:0007829|PDB:5XTE"
FT HELIX 202..212
FT /evidence="ECO:0007829|PDB:5XTE"
FT TURN 215..217
FT /evidence="ECO:0007829|PDB:5XTE"
FT STRAND 218..225
FT /evidence="ECO:0007829|PDB:5XTE"
FT HELIX 227..233
FT /evidence="ECO:0007829|PDB:5XTE"
FT HELIX 234..238
FT /evidence="ECO:0007829|PDB:5XTE"
FT STRAND 257..259
FT /evidence="ECO:0007829|PDB:5XTE"
FT STRAND 265..275
FT /evidence="ECO:0007829|PDB:5XTE"
FT STRAND 278..280
FT /evidence="ECO:0007829|PDB:5XTE"
FT HELIX 281..292
FT /evidence="ECO:0007829|PDB:5XTE"
FT HELIX 308..314
FT /evidence="ECO:0007829|PDB:5XTE"
FT STRAND 321..328
FT /evidence="ECO:0007829|PDB:5XTE"
FT STRAND 334..343
FT /evidence="ECO:0007829|PDB:5XTE"
FT TURN 344..346
FT /evidence="ECO:0007829|PDB:5XTE"
FT HELIX 347..362
FT /evidence="ECO:0007829|PDB:5XTE"
FT HELIX 368..387
FT /evidence="ECO:0007829|PDB:5XTE"
FT HELIX 389..402
FT /evidence="ECO:0007829|PDB:5XTE"
FT HELIX 409..418
FT /evidence="ECO:0007829|PDB:5XTE"
FT HELIX 421..433
FT /evidence="ECO:0007829|PDB:5XTE"
FT STRAND 437..440
FT /evidence="ECO:0007829|PDB:5XTE"
SQ SEQUENCE 453 AA; 48443 MW; BFA655C24C07AF52 CRC64;
MKLLTRAGSF SRFYSLKVAP KVKATAAPAG APPQPQDLEF TKLPNGLVIA SLENYSPVSR
IGLFIKAGSR YEDFSNLGTT HLLRLTSSLT TKGASSFKIT RGIEAVGGKL SVTATRENMA
YTVECLRGDV DILMEFLLNV TTAPEFRRWE VADLQPQLKI DKAVAFQNPQ THVIENLHAA
AYRNALANPL YCPDYRIGKV TSEELHYFVQ NHFTSARMAL IGLGVSHPVL KQVAEQFLNM
RGGLGLSGAK ANYRGGEIRE QNGDSLVHAA FVAESAVAGS AEANAFSVLQ HVLGAGPHVK
RGSNTTSHLH QAVAKATQQP FDVSAFNASY SDSGLFGIYT ISQATAAGDV IKAAYNQVKT
IAQGNLSNTD VQAAKNKLKA GYLMSVESSE CFLEEVGSQA LVAGSYMPPS TVLQQIDSVA
NADIINAAKK FVSGQKSMAA SGNLGHTPFV DEL
