RNH2C_HUMAN
ID RNH2C_HUMAN Reviewed; 164 AA.
AC Q8TDP1; Q9H7F5;
DT 05-SEP-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2002, sequence version 1.
DT 03-AUG-2022, entry version 141.
DE RecName: Full=Ribonuclease H2 subunit C;
DE Short=RNase H2 subunit C;
DE AltName: Full=Aicardi-Goutieres syndrome 3 protein;
DE Short=AGS3;
DE AltName: Full=RNase H1 small subunit;
DE AltName: Full=Ribonuclease HI subunit C;
GN Name=RNASEH2C; Synonyms=AYP1;
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].
RA Frank P., Bogusch A., Grimm R., Wintersberger U.;
RT "Cloning of the cDNA encoding the small subunit of human RNase HI.";
RL Submitted (OCT-2000) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
RA Lim H.N., Oakenfull E.A., Hawkins J.R.;
RT "Evidence that the T6 pseudogene upstream of human SRY is derived from the
RT transcript of a novel autosomal gene, AYP1.";
RL Submitted (FEB-2001) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Adipose tissue;
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=B-cell;
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 ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
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 ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22223895; DOI=10.1074/mcp.m111.015131;
RA Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T.,
RA Giglione C.;
RT "Comparative large-scale characterisation of plant vs. mammal proteins
RT reveals similar and idiosyncratic N-alpha acetylation features.";
RL Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
RN [8]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-3, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [10]
RP X-RAY CRYSTALLOGRAPHY (3.1 ANGSTROMS), FUNCTION, AND SUBUNIT.
RX PubMed=21177858; DOI=10.1074/jbc.m110.181974;
RA Figiel M., Chon H., Cerritelli S.M., Cybulska M., Crouch R.J., Nowotny M.;
RT "The structural and biochemical characterization of human RNase H2 complex
RT reveals the molecular basis for substrate recognition and Aicardi-Goutieres
RT syndrome defects.";
RL J. Biol. Chem. 286:10540-10550(2011).
RN [11]
RP VARIANTS AGS3 HIS-13; TRP-69; LEU-76; LEU-138; ILE-143 AND SER-151.
RX PubMed=17846997; DOI=10.1086/521373;
RA Rice G., Patrick T., Parmar R., Taylor C.F., Aeby A., Aicardi J.,
RA Artuch R., Montalto S.A., Bacino C.A., Barroso B., Baxter P., Benko W.S.,
RA Bergmann C., Bertini E., Biancheri R., Blair E.M., Blau N., Bonthron D.T.,
RA Briggs T., Brueton L.A., Brunner H.G., Burke C.J., Carr I.M.,
RA Carvalho D.R., Chandler K.E., Christen H.J., Corry P.C., Cowan F.M.,
RA Cox H., D'Arrigo S., Dean J., De Laet C., De Praeter C., Dery C.,
RA Ferrie C.D., Flintoff K., Frints S.G., Garcia-Cazorla A., Gener B.,
RA Goizet C., Goutieres F., Green A.J., Guet A., Hamel B.C., Hayward B.E.,
RA Heiberg A., Hennekam R.C., Husson M., Jackson A.P., Jayatunga R.,
RA Jiang Y.H., Kant S.G., Kao A., King M.D., Kingston H.M., Klepper J.,
RA van der Knaap M.S., Kornberg A.J., Kotzot D., Kratzer W., Lacombe D.,
RA Lagae L., Landrieu P.G., Lanzi G., Leitch A., Lim M.J., Livingston J.H.,
RA Lourenco C.M., Lyall E.G., Lynch S.A., Lyons M.J., Marom D., McClure J.P.,
RA McWilliam R., Melancon S.B., Mewasingh L.D., Moutard M.L., Nischal K.K.,
RA Ostergaard J.R., Prendiville J., Rasmussen M., Rogers R.C., Roland D.,
RA Rosser E.M., Rostasy K., Roubertie A., Sanchis A., Schiffmann R.,
RA Scholl-Burgi S., Seal S., Shalev S.A., Corcoles C.S., Sinha G.P., Soler D.,
RA Spiegel R., Stephenson J.B., Tacke U., Tan T.Y., Till M., Tolmie J.L.,
RA Tomlin P., Vagnarelli F., Valente E.M., Van Coster R.N., Van der Aa N.,
RA Vanderver A., Vles J.S., Voit T., Wassmer E., Weschke B., Whiteford M.L.,
RA Willemsen M.A., Zankl A., Zuberi S.M., Orcesi S., Fazzi E., Lebon P.,
RA Crow Y.J.;
RT "Clinical and molecular phenotype of Aicardi-Goutieres syndrome.";
RL Am. J. Hum. Genet. 81:713-725(2007).
RN [12]
RP VARIANTS AGS3 TRP-69 AND ILE-143, FUNCTION, TISSUE SPECIFICITY, AND
RP INTERACTION WITH RNASEH2A AND RNASEH2B.
RX PubMed=16845400; DOI=10.1038/ng1842;
RA Crow Y.J., Leitch A., Hayward B.E., Garner A., Parmar R., Griffith E.,
RA Ali M., Semple C., Aicardi J., Babul-Hirji R., Baumann C., Baxter P.,
RA Bertini E., Chandler K.E., Chitayat D., Cau D., Dery C., Fazzi E.,
RA Goizet C., King M.D., Klepper J., Lacombe D., Lanzi G., Lyall H.,
RA Martinez-Frias M.L., Mathieu M., McKeown C., Monier A., Oade Y.,
RA Quarrell O.W., Rittey C.D., Rogers R.C., Sanchis A., Stephenson J.B.P.,
RA Tacke U., Till M., Tolmie J.L., Tomlin P., Voit T., Weschke B., Woods C.G.,
RA Lebon P., Bonthron D.T., Ponting C.P., Jackson A.P.;
RT "Mutations in genes encoding ribonuclease H2 subunits cause Aicardi-
RT Goutieres syndrome and mimic congenital viral brain infection.";
RL Nat. Genet. 38:910-916(2006).
RN [13]
RP VARIANTS AGS3 TYR-39 AND TRP-69.
RX PubMed=20131292; DOI=10.1002/art.27367;
RA Ramantani G., Kohlhase J., Hertzberg C., Innes A.M., Engel K., Hunger S.,
RA Borozdin W., Mah J.K., Ungerath K., Walkenhorst H., Richardt H.H.,
RA Buckard J., Bevot A., Siegel C., von Stuelpnagel C., Ikonomidou C.,
RA Thomas K., Proud V., Niemann F., Wieczorek D., Haeusler M., Niggemann P.,
RA Baltaci V., Conrad K., Lebon P., Lee-Kirsch M.A.;
RT "Expanding the phenotypic spectrum of lupus erythematosus in Aicardi-
RT Goutieres syndrome.";
RL Arthritis Rheum. 62:1469-1477(2010).
CC -!- FUNCTION: Non catalytic subunit of RNase H2, an endonuclease that
CC specifically degrades the RNA of RNA:DNA hybrids. Participates in DNA
CC replication, possibly by mediating the removal of lagging-strand
CC Okazaki fragment RNA primers during DNA replication. Mediates the
CC excision of single ribonucleotides from DNA:RNA duplexes.
CC {ECO:0000269|PubMed:16845400, ECO:0000269|PubMed:21177858}.
CC -!- SUBUNIT: The RNase H2 complex is a heterotrimer composed of the
CC catalytic subunit RNASEH2A and the non-catalytic subunits RNASEH2B and
CC RNASEH2C. {ECO:0000269|PubMed:21177858}.
CC -!- INTERACTION:
CC Q8TDP1; P04792: HSPB1; NbExp=3; IntAct=EBI-9027335, EBI-352682;
CC Q8TDP1; O60333-2: KIF1B; NbExp=3; IntAct=EBI-9027335, EBI-10975473;
CC Q8TDP1; Q08AM6: VAC14; NbExp=3; IntAct=EBI-9027335, EBI-2107455;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Widely expressed. {ECO:0000269|PubMed:16845400}.
CC -!- DISEASE: Aicardi-Goutieres syndrome 3 (AGS3) [MIM:610329]: A form of
CC Aicardi-Goutieres syndrome, a genetically heterogeneous disease
CC characterized by cerebral atrophy, leukoencephalopathy, intracranial
CC calcifications, chronic cerebrospinal fluid (CSF) lymphocytosis,
CC increased CSF alpha-interferon, and negative serologic investigations
CC for common prenatal infection. Clinical features as thrombocytopenia,
CC hepatosplenomegaly and elevated hepatic transaminases along with
CC intermittent fever may erroneously suggest an infective process. Severe
CC neurological dysfunctions manifest in infancy as progressive
CC microcephaly, spasticity, dystonic posturing and profound psychomotor
CC retardation. Death often occurs in early childhood.
CC {ECO:0000269|PubMed:16845400, ECO:0000269|PubMed:17846997,
CC ECO:0000269|PubMed:20131292}. Note=The disease is caused by variants
CC affecting the gene represented in this entry.
CC -!- MISCELLANEOUS: The T6 pseudogene located upstream of SRY on chromosome
CC Y is derived from the transcript of this gene.
CC -!- SIMILARITY: Belongs to the RNase H2 subunit C family. {ECO:0000305}.
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DR EMBL; AF312034; AAL87739.1; -; mRNA.
DR EMBL; AF346605; AAO49176.1; -; Genomic_DNA.
DR EMBL; AF346606; AAO49177.1; -; mRNA.
DR EMBL; AK024627; BAB14937.1; -; mRNA.
DR EMBL; BC023588; AAH23588.1; -; mRNA.
DR CCDS; CCDS8111.1; -.
DR RefSeq; NP_115569.2; NM_032193.3.
DR PDB; 3P56; X-ray; 4.06 A; C/F=1-164.
DR PDB; 3PUF; X-ray; 3.10 A; C/F/I/L/O/R=1-164.
DR PDBsum; 3P56; -.
DR PDBsum; 3PUF; -.
DR AlphaFoldDB; Q8TDP1; -.
DR SMR; Q8TDP1; -.
DR BioGRID; 123916; 20.
DR ComplexPortal; CPX-745; RNase H2 complex.
DR IntAct; Q8TDP1; 7.
DR STRING; 9606.ENSP00000308193; -.
DR iPTMnet; Q8TDP1; -.
DR PhosphoSitePlus; Q8TDP1; -.
DR BioMuta; RNASEH2C; -.
DR DMDM; 74730607; -.
DR EPD; Q8TDP1; -.
DR jPOST; Q8TDP1; -.
DR MassIVE; Q8TDP1; -.
DR MaxQB; Q8TDP1; -.
DR PaxDb; Q8TDP1; -.
DR PeptideAtlas; Q8TDP1; -.
DR PRIDE; Q8TDP1; -.
DR Antibodypedia; 44295; 141 antibodies from 24 providers.
DR DNASU; 84153; -.
DR Ensembl; ENST00000308418.10; ENSP00000308193.5; ENSG00000172922.11.
DR Ensembl; ENST00000531596.6; ENSP00000435717.2; ENSG00000172922.11.
DR Ensembl; ENST00000534482.6; ENSP00000432081.2; ENSG00000172922.11.
DR Ensembl; ENST00000644142.1; ENSP00000493695.1; ENSG00000172922.11.
DR GeneID; 84153; -.
DR KEGG; hsa:84153; -.
DR MANE-Select; ENST00000308418.10; ENSP00000308193.5; NM_032193.4; NP_115569.2.
DR UCSC; uc001ofn.4; human.
DR CTD; 84153; -.
DR DisGeNET; 84153; -.
DR GeneCards; RNASEH2C; -.
DR GeneReviews; RNASEH2C; -.
DR HGNC; HGNC:24116; RNASEH2C.
DR HPA; ENSG00000172922; Low tissue specificity.
DR MalaCards; RNASEH2C; -.
DR MIM; 610329; phenotype.
DR MIM; 610330; gene.
DR neXtProt; NX_Q8TDP1; -.
DR OpenTargets; ENSG00000172922; -.
DR Orphanet; 51; Aicardi-Goutieres syndrome.
DR PharmGKB; PA162401445; -.
DR VEuPathDB; HostDB:ENSG00000172922; -.
DR eggNOG; ENOG502SBKV; Eukaryota.
DR GeneTree; ENSGT00390000001568; -.
DR InParanoid; Q8TDP1; -.
DR OMA; YFNNYTR; -.
DR OrthoDB; 1542008at2759; -.
DR PhylomeDB; Q8TDP1; -.
DR TreeFam; TF324370; -.
DR BioCyc; MetaCyc:HS16149-MON; -.
DR BRENDA; 3.1.26.4; 2681.
DR PathwayCommons; Q8TDP1; -.
DR SignaLink; Q8TDP1; -.
DR BioGRID-ORCS; 84153; 196 hits in 1091 CRISPR screens.
DR ChiTaRS; RNASEH2C; human.
DR EvolutionaryTrace; Q8TDP1; -.
DR GenomeRNAi; 84153; -.
DR Pharos; Q8TDP1; Tbio.
DR PRO; PR:Q8TDP1; -.
DR Proteomes; UP000005640; Chromosome 11.
DR RNAct; Q8TDP1; protein.
DR Bgee; ENSG00000172922; Expressed in pancreatic ductal cell and 183 other tissues.
DR ExpressionAtlas; Q8TDP1; baseline and differential.
DR Genevisible; Q8TDP1; HS.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0032299; C:ribonuclease H2 complex; IDA:UniProtKB.
DR GO; GO:0006298; P:mismatch repair; IC:ComplexPortal.
DR GO; GO:0006401; P:RNA catabolic process; IDA:UniProtKB.
DR CDD; cd09271; RNase_H2-C; 1.
DR IDEAL; IID00602; -.
DR InterPro; IPR013924; RNase_H2_suC.
DR Pfam; PF08615; RNase_H2_suC; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Aicardi-Goutieres syndrome; Disease variant;
KW Nucleus; Phosphoprotein; Reference proteome.
FT CHAIN 1..164
FT /note="Ribonuclease H2 subunit C"
FT /id="PRO_0000248385"
FT REGION 91..112
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0007744|PubMed:19413330,
FT ECO:0007744|PubMed:22223895, ECO:0007744|PubMed:22814378"
FT MOD_RES 3
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT VARIANT 13
FT /note="R -> H (in AGS3; dbSNP:rs75328625)"
FT /evidence="ECO:0000269|PubMed:17846997"
FT /id="VAR_070618"
FT VARIANT 39
FT /note="D -> Y (in AGS3; dbSNP:rs773527127)"
FT /evidence="ECO:0000269|PubMed:20131292"
FT /id="VAR_070619"
FT VARIANT 69
FT /note="R -> W (in AGS3; dbSNP:rs78635798)"
FT /evidence="ECO:0000269|PubMed:16845400,
FT ECO:0000269|PubMed:17846997, ECO:0000269|PubMed:20131292"
FT /id="VAR_027287"
FT VARIANT 76
FT /note="P -> L (in AGS3; dbSNP:rs76091978)"
FT /evidence="ECO:0000269|PubMed:17846997"
FT /id="VAR_070620"
FT VARIANT 138
FT /note="P -> L (in AGS3)"
FT /evidence="ECO:0000269|PubMed:17846997"
FT /id="VAR_070621"
FT VARIANT 143
FT /note="K -> I (in AGS3; dbSNP:rs75146158)"
FT /evidence="ECO:0000269|PubMed:16845400,
FT ECO:0000269|PubMed:17846997"
FT /id="VAR_027288"
FT VARIANT 151
FT /note="P -> S (in AGS3; dbSNP:rs78464826)"
FT /evidence="ECO:0000269|PubMed:17846997"
FT /id="VAR_070622"
FT HELIX 9..12
FT /evidence="ECO:0007829|PDB:3PUF"
FT STRAND 13..16
FT /evidence="ECO:0007829|PDB:3PUF"
FT HELIX 19..22
FT /evidence="ECO:0007829|PDB:3PUF"
FT STRAND 29..36
FT /evidence="ECO:0007829|PDB:3PUF"
FT STRAND 39..41
FT /evidence="ECO:0007829|PDB:3PUF"
FT HELIX 44..47
FT /evidence="ECO:0007829|PDB:3PUF"
FT HELIX 49..51
FT /evidence="ECO:0007829|PDB:3PUF"
FT STRAND 56..63
FT /evidence="ECO:0007829|PDB:3PUF"
FT STRAND 66..70
FT /evidence="ECO:0007829|PDB:3PUF"
FT STRAND 72..74
FT /evidence="ECO:0007829|PDB:3PUF"
FT STRAND 79..86
FT /evidence="ECO:0007829|PDB:3PUF"
FT STRAND 119..131
FT /evidence="ECO:0007829|PDB:3PUF"
FT STRAND 133..136
FT /evidence="ECO:0007829|PDB:3PUF"
FT HELIX 143..147
FT /evidence="ECO:0007829|PDB:3PUF"
FT HELIX 150..157
FT /evidence="ECO:0007829|PDB:3PUF"
SQ SEQUENCE 164 AA; 17840 MW; 13D0F1D039963671 CRC64;
MESGDEAAIE RHRVHLRSAT LRDAVPATLH LLPCEVAVDG PAPVGRFFTP AIRQGPEGLE
VSFRGRCLRG EEVAVPPGLV GYVMVTEEKK VSMGKPDPLR DSGTDDQEEE PLERDFDRFI
GATANFSRFT LWGLETIPGP DAKVRGALTW PSLAAAIHAQ VPED
