NOVA1_HUMAN
ID NOVA1_HUMAN Reviewed; 507 AA.
AC P51513; A8K0S4; A8K4Q7; D3DS81; D3DS82; Q6B004;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 13-FEB-2019, sequence version 2.
DT 03-AUG-2022, entry version 180.
DE RecName: Full=RNA-binding protein Nova-1 {ECO:0000305};
DE AltName: Full=Neuro-oncological ventral antigen 1;
DE AltName: Full=Onconeural ventral antigen 1;
DE AltName: Full=Paraneoplastic Ri antigen;
DE AltName: Full=Ventral neuron-specific protein 1;
GN Name=NOVA1 {ECO:0000312|HGNC:HGNC:7886};
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] (ISOFORMS 1 AND 2), AND TISSUE SPECIFICITY.
RC TISSUE=Cerebellum, and Hippocampus;
RX PubMed=8398153; DOI=10.1016/0896-6273(93)90077-5;
RA Buckanovich R.J., Posner J.B., Darnell R.B.;
RT "Nova, the paraneoplastic Ri antigen, is homologous to an RNA-binding
RT protein and is specifically expressed in the developing motor system.";
RL Neuron 11:657-672(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Amygdala;
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 (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Brain;
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 NUCLEOTIDE SEQUENCE [MRNA] OF 1-34.
RC TISSUE=Fetal brain;
RA Dmitrenko V.V., Garifulin O.M., Shostak K.A., Smikodub A.I., Kavsan V.M.;
RL Submitted (APR-1996) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP MISCELLANEOUS.
RX PubMed=8558240; DOI=10.1523/jneurosci.16-03-01114.1996;
RA Buckanovich R.J., Yang Y.Y., Darnell R.B.;
RT "The onconeural antigen Nova-1 is a neuron-specific RNA-binding protein,
RT the activity of which is inhibited by paraneoplastic antibodies.";
RL J. Neurosci. 16:1114-1122(1996).
RN [7]
RP FUNCTION, AND DOMAIN.
RX PubMed=10811881; DOI=10.1073/pnas.090553997;
RA Jensen K.B., Musunuru K., Lewis H.A., Burley S.K., Darnell R.B.;
RT "The tetranucleotide UCAY directs the specific recognition of RNA by the
RT Nova K-homology 3 domain.";
RL Proc. Natl. Acad. Sci. U.S.A. 97:5740-5745(2000).
RN [8]
RP IDENTIFICATION BY MASS 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 [9]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT "System-wide temporal characterization of the proteome and phosphoproteome
RT of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [10]
RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 421-492.
RX PubMed=10368286; DOI=10.1016/s0969-2126(99)80025-2;
RA Lewis H.A., Chen H., Edo C., Buckanovich R.J., Yang Y.Y.-L., Musunuru K.,
RA Zhong R., Darnell R.B., Burley S.K.;
RT "Crystal structures of Nova-1 and Nova-2 K-homology RNA-binding domains.";
RL Structure 7:191-203(1999).
CC -!- FUNCTION: Functions to regulate alternative splicing in neurons by
CC binding pre-mRNA in a sequence-specific manner to activate exon
CC inclusion or exclusion. It binds specifically to the sequences 5'-YCAY-
CC 3' and regulates splicing in only a subset of regulated exons
CC (PubMed:10811881). Binding to an exonic 5'-YCAY-3' cluster changes the
CC protein complexes assembled on pre-mRNA, blocking U1 snRNP binding and
CC exon inclusion, whereas binding to an intronic 5'-YCAY-3' cluster
CC enhances spliceosome assembly and exon inclusion. Binding to 5'-YCAY-3'
CC clusters results in a local and asymmetric action to regulate
CC spliceosome assembly and alternative splicing in neurons. Binding to an
CC exonic 5'-YCAY-3' cluster changed the protein complexes assembled on
CC pre-mRNA, blocking U1 snRNP (small nuclear ribonucleoprotein) binding
CC and exon inclusion, whereas binding to an intronic 5'-YCAY-3' cluster
CC enhanced spliceosome assembly and exon inclusion. With NOVA1, they
CC perform unique biological functions in different brain areas and cell
CC types. Autoregulates its own expression by acting as a splicing
CC repressor. Acts to activate the inclusion of exon E3A in the glycine
CC receptor alpha-2 chain and of exon E9 in gamma-aminobutyric-acid
CC receptor gamma-2 subunit via a distal downstream UCAU-rich intronic
CC splicing enhancer. Acts to regulate a novel glycine receptor alpha-2
CC chain splice variant (alpha-2N) in developing spinal cord (By
CC similarity). {ECO:0000250|UniProtKB:Q9JKN6,
CC ECO:0000269|PubMed:10811881}.
CC -!- SUBUNIT: Interacts with PTBP2; the interaction is direct.
CC {ECO:0000250|UniProtKB:Q9JKN6}.
CC -!- INTERACTION:
CC P51513; P18507: GABRG2; NbExp=2; IntAct=EBI-726123, EBI-9008430;
CC P51513; P50406: HTR6; NbExp=9; IntAct=EBI-726123, EBI-1182222;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q9JKN6}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=P51513-4; Sequence=Displayed;
CC Name=2; Synonyms=Tumor;
CC IsoId=P51513-2; Sequence=VSP_060047, VSP_060048;
CC Name=3;
CC IsoId=P51513-5; Sequence=VSP_060046;
CC -!- TISSUE SPECIFICITY: Expressed in cerebellum, brain stem, hippocampus,
CC and frontal cortex. {ECO:0000269|PubMed:8398153}.
CC -!- DOMAIN: The KH domain consists of approximately 70 amino acids and
CC includes a conserved hydrophobic core, an invariant Gly-X-X-Gly motif,
CC and an additional variable segment (PubMed:10811881). The third KH
CC domain (KH3) binds a hairpin RNA loop containing the 5'-UCAY-3' motif
CC on targeted molecules (PubMed:10811881). RNA binding by KH3 requires
CC residues C-terminal to the KH domain (PubMed:10811881).
CC {ECO:0000269|PubMed:10811881, ECO:0000303|PubMed:10811881}.
CC -!- MISCELLANEOUS: Target antigen in a human paraneoplastic motor disorder,
CC paraneoplastic opsoclonus-myoclonus ataxia (POMA). POMA antibodies
CC block NOVAl RNA binding. {ECO:0000305|PubMed:8558240}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA16022.1; Type=Miscellaneous discrepancy; Note=Probable cloning artifact leading to an insertion into the sequence.; Evidence={ECO:0000305};
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DR EMBL; U04840; AAA16022.1; ALT_SEQ; mRNA.
DR EMBL; AK289639; BAF82328.1; -; mRNA.
DR EMBL; AK291022; BAF83711.1; -; mRNA.
DR EMBL; AL079343; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL132716; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471078; EAW65990.1; -; Genomic_DNA.
DR EMBL; CH471078; EAW65991.1; -; Genomic_DNA.
DR EMBL; CH471078; EAW65992.1; -; Genomic_DNA.
DR EMBL; CH471078; EAW65993.1; -; Genomic_DNA.
DR EMBL; CH471078; EAW65995.1; -; Genomic_DNA.
DR EMBL; BC075038; AAH75038.1; -; mRNA.
DR EMBL; BC075039; AAH75039.1; -; mRNA.
DR EMBL; Z70771; CAA94810.1; -; mRNA.
DR CCDS; CCDS32060.1; -. [P51513-5]
DR CCDS; CCDS32061.1; -. [P51513-4]
DR CCDS; CCDS9635.1; -. [P51513-2]
DR PIR; I38489; I38489.
DR RefSeq; NP_002506.2; NM_002515.2. [P51513-4]
DR RefSeq; NP_006480.2; NM_006489.2. [P51513-5]
DR RefSeq; NP_006482.1; NM_006491.2. [P51513-2]
DR PDB; 1DT4; X-ray; 2.60 A; A=421-492.
DR PDB; 2ANN; X-ray; 2.30 A; A=49-246.
DR PDB; 2ANR; X-ray; 1.94 A; A=49-246.
DR PDBsum; 1DT4; -.
DR PDBsum; 2ANN; -.
DR PDBsum; 2ANR; -.
DR AlphaFoldDB; P51513; -.
DR SMR; P51513; -.
DR BioGRID; 110919; 14.
DR IntAct; P51513; 14.
DR MINT; P51513; -.
DR STRING; 9606.ENSP00000438875; -.
DR iPTMnet; P51513; -.
DR PhosphoSitePlus; P51513; -.
DR BioMuta; NOVA1; -.
DR DMDM; 1709303; -.
DR EPD; P51513; -.
DR jPOST; P51513; -.
DR MassIVE; P51513; -.
DR MaxQB; P51513; -.
DR PaxDb; P51513; -.
DR PeptideAtlas; P51513; -.
DR PRIDE; P51513; -.
DR ProteomicsDB; 12757; -.
DR ProteomicsDB; 56316; -. [P51513-2]
DR ProteomicsDB; 56318; -. [P51513-4]
DR TopDownProteomics; P51513-2; -. [P51513-2]
DR Antibodypedia; 133; 261 antibodies from 34 providers.
DR DNASU; 4857; -.
DR Ensembl; ENST00000344429.9; ENSP00000342387.5; ENSG00000139910.20. [P51513-2]
DR Ensembl; ENST00000465357.6; ENSP00000447391.1; ENSG00000139910.20. [P51513-5]
DR Ensembl; ENST00000539517.7; ENSP00000438875.2; ENSG00000139910.20. [P51513-4]
DR GeneID; 4857; -.
DR KEGG; hsa:4857; -.
DR MANE-Select; ENST00000539517.7; ENSP00000438875.2; NM_002515.3; NP_002506.2.
DR UCSC; uc001wpy.4; human. [P51513-4]
DR CTD; 4857; -.
DR DisGeNET; 4857; -.
DR GeneCards; NOVA1; -.
DR HGNC; HGNC:7886; NOVA1.
DR HPA; ENSG00000139910; Tissue enhanced (brain).
DR MIM; 602157; gene.
DR neXtProt; NX_P51513; -.
DR OpenTargets; ENSG00000139910; -.
DR PharmGKB; PA31688; -.
DR VEuPathDB; HostDB:ENSG00000139910; -.
DR eggNOG; KOG2191; Eukaryota.
DR GeneTree; ENSGT00940000155573; -.
DR HOGENOM; CLU_022670_1_1_1; -.
DR InParanoid; P51513; -.
DR OMA; MTTLANY; -.
DR OrthoDB; 1167935at2759; -.
DR PhylomeDB; P51513; -.
DR TreeFam; TF316981; -.
DR PathwayCommons; P51513; -.
DR SignaLink; P51513; -.
DR BioGRID-ORCS; 4857; 13 hits in 1073 CRISPR screens.
DR ChiTaRS; NOVA1; human.
DR EvolutionaryTrace; P51513; -.
DR GeneWiki; NOVA1; -.
DR GenomeRNAi; 4857; -.
DR Pharos; P51513; Tbio.
DR PRO; PR:P51513; -.
DR Proteomes; UP000005640; Chromosome 14.
DR RNAct; P51513; protein.
DR Bgee; ENSG00000139910; Expressed in cortical plate and 169 other tissues.
DR ExpressionAtlas; P51513; baseline and differential.
DR Genevisible; P51513; HS.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA:HPA.
DR GO; GO:0005730; C:nucleolus; IDA:HPA.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0003730; F:mRNA 3'-UTR binding; IEA:Ensembl.
DR GO; GO:0003729; F:mRNA binding; ISS:UniProtKB.
DR GO; GO:0003723; F:RNA binding; HDA:UniProtKB.
DR GO; GO:1990825; F:sequence-specific mRNA binding; IDA:UniProtKB.
DR GO; GO:0000398; P:mRNA splicing, via spliceosome; IBA:GO_Central.
DR GO; GO:0120163; P:negative regulation of cold-induced thermogenesis; ISS:YuBioLab.
DR GO; GO:0007399; P:nervous system development; IEA:UniProtKB-KW.
DR GO; GO:0000381; P:regulation of alternative mRNA splicing, via spliceosome; ISS:UniProtKB.
DR GO; GO:0010468; P:regulation of gene expression; IBA:GO_Central.
DR GO; GO:0051252; P:regulation of RNA metabolic process; IBA:GO_Central.
DR GO; GO:0006396; P:RNA processing; TAS:ProtInc.
DR GO; GO:0008380; P:RNA splicing; TAS:ProtInc.
DR Gene3D; 3.30.1370.10; -; 3.
DR InterPro; IPR004087; KH_dom.
DR InterPro; IPR004088; KH_dom_type_1.
DR InterPro; IPR036612; KH_dom_type_1_sf.
DR InterPro; IPR033086; NOVA1.
DR PANTHER; PTHR10288:SF229; PTHR10288:SF229; 1.
DR Pfam; PF00013; KH_1; 3.
DR SMART; SM00322; KH; 3.
DR SUPFAM; SSF54791; SSF54791; 3.
DR PROSITE; PS50084; KH_TYPE_1; 3.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; mRNA processing; mRNA splicing;
KW Neurogenesis; Nucleus; Phosphoprotein; Reference proteome; Repeat;
KW RNA-binding.
FT CHAIN 1..507
FT /note="RNA-binding protein Nova-1"
FT /id="PRO_0000050116"
FT DOMAIN 49..116
FT /note="KH 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00117"
FT DOMAIN 171..237
FT /note="KH 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00117"
FT DOMAIN 421..488
FT /note="KH 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00117"
FT REGION 1..44
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 139..171
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 419..503
FT /note="Required for RNA binding"
FT /evidence="ECO:0000269|PubMed:10811881"
FT MOTIF 27..43
FT /note="Bipartite nuclear localization signal"
FT /evidence="ECO:0000255"
FT COMPBIAS 20..34
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 154
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9JKN6"
FT VAR_SEQ 150..173
FT /note="Missing (in isoform 3)"
FT /id="VSP_060046"
FT VAR_SEQ 174..181
FT /note="VKIIVPNS -> KHNISWIS (in isoform 2)"
FT /id="VSP_060047"
FT VAR_SEQ 182..507
FT /note="Missing (in isoform 2)"
FT /id="VSP_060048"
FT STRAND 50..57
FT /evidence="ECO:0007829|PDB:2ANR"
FT HELIX 58..65
FT /evidence="ECO:0007829|PDB:2ANR"
FT HELIX 67..69
FT /evidence="ECO:0007829|PDB:2ANR"
FT HELIX 70..79
FT /evidence="ECO:0007829|PDB:2ANR"
FT STRAND 82..85
FT /evidence="ECO:0007829|PDB:2ANR"
FT STRAND 95..104
FT /evidence="ECO:0007829|PDB:2ANR"
FT HELIX 106..120
FT /evidence="ECO:0007829|PDB:2ANR"
FT HELIX 145..148
FT /evidence="ECO:0007829|PDB:2ANR"
FT STRAND 174..179
FT /evidence="ECO:0007829|PDB:2ANR"
FT HELIX 180..187
FT /evidence="ECO:0007829|PDB:2ANR"
FT HELIX 189..191
FT /evidence="ECO:0007829|PDB:2ANR"
FT HELIX 192..200
FT /evidence="ECO:0007829|PDB:2ANR"
FT STRAND 204..207
FT /evidence="ECO:0007829|PDB:2ANR"
FT STRAND 218..226
FT /evidence="ECO:0007829|PDB:2ANR"
FT HELIX 227..242
FT /evidence="ECO:0007829|PDB:2ANR"
FT STRAND 422..429
FT /evidence="ECO:0007829|PDB:1DT4"
FT TURN 430..433
FT /evidence="ECO:0007829|PDB:1DT4"
FT HELIX 434..437
FT /evidence="ECO:0007829|PDB:1DT4"
FT HELIX 439..441
FT /evidence="ECO:0007829|PDB:1DT4"
FT HELIX 442..451
FT /evidence="ECO:0007829|PDB:1DT4"
FT STRAND 454..457
FT /evidence="ECO:0007829|PDB:1DT4"
FT STRAND 469..476
FT /evidence="ECO:0007829|PDB:1DT4"
FT HELIX 478..491
FT /evidence="ECO:0007829|PDB:1DT4"
SQ SEQUENCE 507 AA; 51727 MW; DBF455477988CDCA CRC64;
MMAAAPIQQN GTHTGVPIDL DPPDSRKRPL EAPPEAGSTK RTNTGEDGQY FLKVLIPSYA
AGSIIGKGGQ TIVQLQKETG ATIKLSKSKD FYPGTTERVC LIQGTVEALN AVHGFIAEKI
REMPQNVAKT EPVSILQPQT TVNPDRIKQT LPSSPTTTKS SPSDPMTTSR ANQVKIIVPN
STAGLIIGKG GATVKAVMEQ SGAWVQLSQK PDGINLQERV VTVSGEPEQN RKAVELIIQK
IQEDPQSGSC LNISYANVTG PVANSNPTGS PYANTAEVLP TAAAAAGLLG HANLAGVAAF
PAVLSGFTGN DLVAITSALN TLASYGYNLN TLGLGLSQAA ATGALAAAAA SANPAAAAAN
LLATYASEAS ASGSTAGGTA GTFALGSLAA ATAATNGYFG AASPLAASAI LGTEKSTDGS
KDVVEIAVPE NLVGAILGKG GKTLVEYQEL TGARIQISKK GEFVPGTRNR KVTITGTPAA
TQAAQYLITQ RITYEQGVRA ANPQKVG
