QCR1_MOUSE
ID QCR1_MOUSE Reviewed; 480 AA.
AC Q9CZ13; Q3TV75; Q9CWL6;
DT 20-JUN-2001, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 2.
DT 03-AUG-2022, entry version 177.
DE RecName: Full=Cytochrome b-c1 complex subunit 1, mitochondrial;
DE AltName: Full=Complex III subunit 1;
DE AltName: Full=Core protein I;
DE AltName: Full=Ubiquinol-cytochrome-c reductase complex core protein 1;
DE Flags: Precursor;
GN Name=Uqcrc1;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Bone marrow, and Embryo;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP PROTEIN SEQUENCE OF 59-80; 86-99; 112-134; 143-163; 214-222; 229-248;
RP 256-276; 379-390; 397-442; 448-470 AND 473-479, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RC STRAIN=C57BL/6J; TISSUE=Brain, and Hippocampus;
RA Lubec G., Kang S.U., Klug S., Yang J.W., Zigmond M.;
RL Submitted (JUL-2007) to UniProtKB.
RN [4]
RP SUBUNIT.
RX PubMed=19026783; DOI=10.1016/j.molcel.2008.10.021;
RA Acin-Perez R., Fernandez-Silva P., Peleato M.L., Perez-Martos A.,
RA Enriquez J.A.;
RT "Respiratory active mitochondrial supercomplexes.";
RL Mol. Cell 32:529-539(2008).
RN [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [6]
RP SUCCINYLATION [LARGE SCALE ANALYSIS] AT LYS-163, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=23806337; DOI=10.1016/j.molcel.2013.06.001;
RA Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y.,
RA Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.;
RT "SIRT5-mediated lysine desuccinylation impacts diverse metabolic
RT pathways.";
RL Mol. Cell 50:919-930(2013).
RN [7]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-111; LYS-138; LYS-163 AND
RP LYS-248, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=23576753; DOI=10.1073/pnas.1302961110;
RA Rardin M.J., Newman J.C., Held J.M., Cusack M.P., Sorensen D.J., Li B.,
RA Schilling B., Mooney S.D., Kahn C.R., Verdin E., Gibson B.W.;
RT "Label-free quantitative proteomics of the lysine acetylome in mitochondria
RT identifies substrates of SIRT3 in metabolic pathways.";
RL Proc. Natl. Acad. Sci. U.S.A. 110:6601-6606(2013).
RN [8]
RP TISSUE SPECIFICITY, AND DISRUPTION PHENOTYPE.
RX PubMed=30666338; DOI=10.1007/s00018-019-03007-6;
RA Shan W., Li J., Xu W., Li H., Zuo Z.;
RT "Critical role of UQCRC1 in embryo survival, brain ischemic tolerance and
RT normal cognition in mice.";
RL Cell. Mol. Life Sci. 76:1381-1396(2019).
RN [9]
RP INTERACTION WITH BRAWNIN.
RX PubMed=32161263; DOI=10.1038/s41467-020-14999-2;
RA Zhang S., Reljic B., Liang C., Kerouanton B., Francisco J.C., Peh J.H.,
RA Mary C., Jagannathan N.S., Olexiouk V., Tang C., Fidelito G., Nama S.,
RA Cheng R.K., Wee C.L., Wang L.C., Duek Roggli P., Sampath P., Lane L.,
RA Petretto E., Sobota R.M., Jesuthasan S., Tucker-Kellogg L., Reversade B.,
RA Menschaert G., Sun L., Stroud D.A., Ho L.;
RT "Mitochondrial peptide BRAWNIN is essential for vertebrate respiratory
RT complex III assembly.";
RL Nat. Commun. 11:1312-1312(2020).
RN [10]
RP INTERACTION WITH STMP1.
RX PubMed=35101990; DOI=10.1073/pnas.2120476119;
RA Makarewich C.A., Munir A.Z., Bezprozvannaya S., Gibson A.M., Young Kim S.,
RA Martin-Sandoval M.S., Mathews T.P., Szweda L.I., Bassel-Duby R.,
RA Olson E.N.;
RT "The cardiac-enriched microprotein mitolamban regulates mitochondrial
RT respiratory complex assembly and function in mice.";
RL Proc. Natl. Acad. Sci. U.S.A. 119:0-0(2022).
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. May be involved
CC in the in situ processing of UQCRFS1 into the mature Rieske protein and
CC its mitochondrial targeting sequence (MTS)/subunit 9 when incorporated
CC into complex III (By similarity). Seems to play an important role in
CC the maintenance of proper mitochondrial function in nigral dopaminergic
CC neurons (By similarity). {ECO:0000250|UniProtKB:P07256,
CC ECO:0000250|UniProtKB:P31800, ECO:0000250|UniProtKB:P31930}.
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:19026783). Interacts with BRAWNIN
CC (PubMed:32161263). Interacts with STMP1 (PubMed:35101990).
CC {ECO:0000250|UniProtKB:P31800, ECO:0000269|PubMed:19026783,
CC ECO:0000269|PubMed:32161263, ECO:0000269|PubMed:35101990}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane
CC {ECO:0000250|UniProtKB:P07256}; Peripheral membrane protein
CC {ECO:0000250|UniProtKB:P07256}; Matrix side
CC {ECO:0000250|UniProtKB:P07256}.
CC -!- TISSUE SPECIFICITY: Expressed in neurons and astrocytes of the cerebral
CC cortex and hippocampus (at protein level).
CC {ECO:0000269|PubMed:30666338}.
CC -!- PTM: Acetylation of Lys-138 is observed in liver mitochondria from
CC fasted mice but not from fed mice.
CC -!- DISRUPTION PHENOTYPE: Results in early embryonic lethality.
CC {ECO:0000269|PubMed:30666338}.
CC -!- SIMILARITY: Belongs to the peptidase M16 family. UQCRC1/QCR1 subfamily.
CC {ECO:0000305}.
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DR EMBL; AK013128; BAB28666.1; -; mRNA.
DR EMBL; AK010553; BAB27022.1; -; mRNA.
DR EMBL; AK151764; BAE30670.1; -; mRNA.
DR EMBL; AK160337; BAE35744.1; -; mRNA.
DR EMBL; CH466560; EDL21324.1; -; Genomic_DNA.
DR CCDS; CCDS23540.1; -.
DR RefSeq; NP_079683.2; NM_025407.2.
DR PDB; 7O37; EM; 3.20 A; A/L=35-480.
DR PDB; 7O3C; EM; 3.30 A; A/L=35-480.
DR PDB; 7O3E; EM; 3.60 A; A/L=35-480.
DR PDB; 7O3H; EM; 2.60 A; A/L=35-480.
DR PDBsum; 7O37; -.
DR PDBsum; 7O3C; -.
DR PDBsum; 7O3E; -.
DR PDBsum; 7O3H; -.
DR AlphaFoldDB; Q9CZ13; -.
DR SMR; Q9CZ13; -.
DR BioGRID; 204459; 58.
DR ComplexPortal; CPX-563; Mitochondrial respiratory chain complex III.
DR CORUM; Q9CZ13; -.
DR IntAct; Q9CZ13; 11.
DR MINT; Q9CZ13; -.
DR STRING; 10090.ENSMUSP00000026743; -.
DR MEROPS; M16.975; -.
DR MEROPS; M16.981; -.
DR iPTMnet; Q9CZ13; -.
DR PhosphoSitePlus; Q9CZ13; -.
DR SwissPalm; Q9CZ13; -.
DR REPRODUCTION-2DPAGE; IPI00111885; -.
DR REPRODUCTION-2DPAGE; Q9CZ13; -.
DR UCD-2DPAGE; Q9CZ13; -.
DR EPD; Q9CZ13; -.
DR jPOST; Q9CZ13; -.
DR MaxQB; Q9CZ13; -.
DR PaxDb; Q9CZ13; -.
DR PeptideAtlas; Q9CZ13; -.
DR PRIDE; Q9CZ13; -.
DR ProteomicsDB; 301902; -.
DR TopDownProteomics; Q9CZ13; -.
DR Antibodypedia; 1257; 374 antibodies from 29 providers.
DR DNASU; 22273; -.
DR Ensembl; ENSMUST00000026743; ENSMUSP00000026743; ENSMUSG00000025651.
DR GeneID; 22273; -.
DR KEGG; mmu:22273; -.
DR UCSC; uc009rrg.1; mouse.
DR CTD; 7384; -.
DR MGI; MGI:107876; Uqcrc1.
DR VEuPathDB; HostDB:ENSMUSG00000025651; -.
DR eggNOG; KOG0960; Eukaryota.
DR GeneTree; ENSGT00940000158931; -.
DR HOGENOM; CLU_009902_4_2_1; -.
DR InParanoid; Q9CZ13; -.
DR OMA; WSNPDNV; -.
DR OrthoDB; 638125at2759; -.
DR PhylomeDB; Q9CZ13; -.
DR TreeFam; TF105032; -.
DR Reactome; R-MMU-611105; Respiratory electron transport.
DR BioGRID-ORCS; 22273; 24 hits in 74 CRISPR screens.
DR ChiTaRS; Uqcrc1; mouse.
DR PRO; PR:Q9CZ13; -.
DR Proteomes; UP000000589; Chromosome 9.
DR RNAct; Q9CZ13; protein.
DR Bgee; ENSMUSG00000025651; Expressed in proximal tubule and 143 other tissues.
DR ExpressionAtlas; Q9CZ13; baseline and differential.
DR Genevisible; Q9CZ13; MM.
DR GO; GO:0005743; C:mitochondrial inner membrane; HDA:MGI.
DR GO; GO:0005750; C:mitochondrial respiratory chain complex III; ISO:MGI.
DR GO; GO:0005739; C:mitochondrion; IDA:MGI.
DR GO; GO:0043209; C:myelin sheath; HDA:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; IEA:InterPro.
DR GO; GO:0044877; F:protein-containing complex binding; ISO:MGI.
DR GO; GO:0031625; F:ubiquitin protein ligase binding; ISO:MGI.
DR GO; GO:0045333; P:cellular respiration; IC:ComplexPortal.
DR GO; GO:0006122; P:mitochondrial electron transport, ubiquinol to cytochrome c; IDA:MGI.
DR GO; GO:0034551; P:mitochondrial respiratory chain complex III assembly; ISS:UniProtKB.
DR GO; GO:0014823; P:response to activity; IEA:Ensembl.
DR GO; GO:0043279; P:response to alkaloid; IEA:Ensembl.
DR InterPro; IPR011249; Metalloenz_LuxS/M16.
DR InterPro; IPR011765; Pept_M16_N.
DR InterPro; IPR007863; Peptidase_M16_C.
DR Pfam; PF00675; Peptidase_M16; 1.
DR Pfam; PF05193; Peptidase_M16_C; 1.
DR SUPFAM; SSF63411; SSF63411; 2.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Direct protein sequencing; Electron transport;
KW Membrane; Mitochondrion; Mitochondrion inner membrane; Phosphoprotein;
KW Reference proteome; Respiratory chain; Transit peptide; Transport.
FT TRANSIT 1..34
FT /note="Mitochondrion"
FT /evidence="ECO:0000250"
FT CHAIN 35..480
FT /note="Cytochrome b-c1 complex subunit 1, mitochondrial"
FT /id="PRO_0000026787"
FT MOD_RES 111
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:23576753"
FT MOD_RES 138
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:23576753"
FT MOD_RES 163
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:23576753"
FT MOD_RES 163
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 212
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q68FY0"
FT MOD_RES 214
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q68FY0"
FT MOD_RES 248
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:23576753"
FT CONFLICT 223
FT /note="H -> N (in Ref. 1; BAB28666)"
FT /evidence="ECO:0000305"
FT CONFLICT 318
FT /note="Y -> C (in Ref. 1; BAB28666)"
FT /evidence="ECO:0000305"
FT HELIX 38..43
FT /evidence="ECO:0007829|PDB:7O3H"
FT STRAND 49..52
FT /evidence="ECO:0007829|PDB:7O3H"
FT STRAND 58..63
FT /evidence="ECO:0007829|PDB:7O3H"
FT STRAND 67..76
FT /evidence="ECO:0007829|PDB:7O3H"
FT HELIX 79..81
FT /evidence="ECO:0007829|PDB:7O3H"
FT STRAND 84..86
FT /evidence="ECO:0007829|PDB:7O3H"
FT HELIX 89..96
FT /evidence="ECO:0007829|PDB:7O3H"
FT STRAND 101..104
FT /evidence="ECO:0007829|PDB:7O3H"
FT HELIX 107..115
FT /evidence="ECO:0007829|PDB:7O3H"
FT STRAND 119..124
FT /evidence="ECO:0007829|PDB:7O3H"
FT STRAND 129..137
FT /evidence="ECO:0007829|PDB:7O3H"
FT HELIX 140..152
FT /evidence="ECO:0007829|PDB:7O3H"
FT HELIX 158..175
FT /evidence="ECO:0007829|PDB:7O3H"
FT HELIX 179..191
FT /evidence="ECO:0007829|PDB:7O3H"
FT TURN 196..198
FT /evidence="ECO:0007829|PDB:7O3H"
FT HELIX 205..210
FT /evidence="ECO:0007829|PDB:7O3H"
FT HELIX 213..223
FT /evidence="ECO:0007829|PDB:7O3H"
FT HELIX 226..228
FT /evidence="ECO:0007829|PDB:7O3H"
FT STRAND 229..236
FT /evidence="ECO:0007829|PDB:7O3H"
FT HELIX 239..249
FT /evidence="ECO:0007829|PDB:7O3H"
FT STRAND 250..253
FT /evidence="ECO:0007829|PDB:7O37"
FT STRAND 258..260
FT /evidence="ECO:0007829|PDB:7O3H"
FT STRAND 273..278
FT /evidence="ECO:0007829|PDB:7O3H"
FT STRAND 282..292
FT /evidence="ECO:0007829|PDB:7O3H"
FT HELIX 300..311
FT /evidence="ECO:0007829|PDB:7O3H"
FT STRAND 313..315
FT /evidence="ECO:0007829|PDB:7O3C"
FT HELIX 321..323
FT /evidence="ECO:0007829|PDB:7O3H"
FT HELIX 327..335
FT /evidence="ECO:0007829|PDB:7O3H"
FT STRAND 339..348
FT /evidence="ECO:0007829|PDB:7O3H"
FT STRAND 351..360
FT /evidence="ECO:0007829|PDB:7O3H"
FT HELIX 362..364
FT /evidence="ECO:0007829|PDB:7O3H"
FT HELIX 365..381
FT /evidence="ECO:0007829|PDB:7O3H"
FT HELIX 385..402
FT /evidence="ECO:0007829|PDB:7O3H"
FT HELIX 406..418
FT /evidence="ECO:0007829|PDB:7O3H"
FT HELIX 426..434
FT /evidence="ECO:0007829|PDB:7O3H"
FT HELIX 438..448
FT /evidence="ECO:0007829|PDB:7O3H"
FT TURN 449..451
FT /evidence="ECO:0007829|PDB:7O3H"
FT STRAND 455..461
FT /evidence="ECO:0007829|PDB:7O3H"
FT STRAND 463..465
FT /evidence="ECO:0007829|PDB:7O3H"
FT HELIX 468..474
FT /evidence="ECO:0007829|PDB:7O3H"
SQ SEQUENCE 480 AA; 52852 MW; 8150C97C655A91C9 CRC64;
MAASAVCRAA CSGTQVLLRT RRSPALLRLP ALRGTATFAQ ALQSVPETQV SILDNGLRVA
SEQSSHATCT VGVWIDAGSR YETEKNNGAG YFLEHLAFKG TKNRPGNALE KEVESIGAHL
NAYSTREHTA YLIKALSKDL PKVVELLADI VQNSSLEDSQ IEKERDVILR EMQENDASMQ
NVVFDYLHAT AFQGTPLAQA VEGPSENVRR LSRTDLTDYL NRHYKAPRMV LAAAGGVEHQ
QLLDLAQKHL SSVSRVYEED AVPGLTPCRF TGSEIRHRDD ALPLAHVAIA VEGPGWANPD
NVTLQVANAI IGHYDCTYGG GVHLSSPLAS VAVANKLCQS FQTFNISYSD TGLLGAHFVC
DAMSIDDMVF FLQGQWMRLC TSATESEVTR GKNILRNALV SHLDGTTPVC EDIGRSLLTY
GRRIPLAEWE SRIQEVDAQM LRDICSKYFY DQCPAVAGYG PIEQLPDYNR IRSGMFWLRF
