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   27-MAR-2024, entry version 222.
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 type 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; 347.
DR   ComplexPortal; CPX-560; Mitochondrial respiratory chain complex III.
DR   IntAct; P22695; 79.
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   GlyCosmos; P22695; 2 sites, 1 glycan.
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   CPTAC; CPTAC-138; -.
DR   CPTAC; CPTAC-139; -.
DR   EPD; P22695; -.
DR   jPOST; P22695; -.
DR   MassIVE; P22695; -.
DR   MaxQB; P22695; -.
DR   PaxDb; 9606-ENSP00000268379; -.
DR   PeptideAtlas; P22695; -.
DR   ProteomicsDB; 54028; -.
DR   Pumba; P22695; -.
DR   TopDownProteomics; P22695; -.
DR   Antibodypedia; 1267; 274 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   AGR; HGNC:12586; -.
DR   CTD; 7385; -.
DR   DisGeNET; 7385; -.
DR   GeneCards; UQCRC2; -.
DR   HGNC; HGNC:12586; UQCRC2.
DR   HPA; ENSG00000140740; Tissue enhanced (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; APKFALY; -.
DR   OrthoDB; 314823at2759; -.
DR   PhylomeDB; P22695; -.
DR   TreeFam; TF105033; -.
DR   BioCyc; MetaCyc:HS06753-MONOMER; -.
DR   PathwayCommons; P22695; -.
DR   Reactome; R-HSA-611105; Respiratory electron transport.
DR   SignaLink; P22695; -.
DR   SIGNOR; P22695; -.
DR   BioGRID-ORCS; 7385; 427 hits in 1170 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 210 other cell types or tissues.
DR   ExpressionAtlas; P22695; baseline and differential.
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; NAS:ComplexPortal.
DR   GO; GO:0006122; P:mitochondrial electron transport, ubiquinol to cytochrome c; NAS:ComplexPortal.
DR   GO; GO:0006119; P:oxidative phosphorylation; TAS:ProtInc.
DR   GO; GO:0006508; P:proteolysis; IEA:InterPro.
DR   Gene3D; 3.30.830.10; Metalloenzyme, LuxS/M16 peptidase-like; 2.
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   PANTHER; PTHR11851:SF226; CYTOCHROME B-C1 COMPLEX SUBUNIT 2, MITOCHONDRIAL; 1.
DR   PANTHER; PTHR11851; METALLOPROTEASE; 1.
DR   Pfam; PF00675; Peptidase_M16; 1.
DR   Pfam; PF05193; Peptidase_M16_C; 1.
DR   SUPFAM; SSF63411; LuxS/MPP-like metallohydrolase; 2.
DR   PROSITE; PS00143; INSULINASE; 1.
DR   UCD-2DPAGE; P22695; -.
DR   Genevisible; P22695; HS.
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
//