SYAC_MOUSE
ID SYAC_MOUSE Reviewed; 968 AA.
AC Q8BGQ7; Q8BXR0;
DT 10-MAY-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 154.
DE RecName: Full=Alanine--tRNA ligase, cytoplasmic {ECO:0000255|HAMAP-Rule:MF_03133};
DE EC=6.1.1.7 {ECO:0000255|HAMAP-Rule:MF_03133, ECO:0000269|PubMed:27622773};
DE AltName: Full=Alanyl-tRNA synthetase {ECO:0000255|HAMAP-Rule:MF_03133};
DE Short=AlaRS {ECO:0000255|HAMAP-Rule:MF_03133};
DE AltName: Full=Protein sticky {ECO:0000303|PubMed:16906134};
DE Short=Sti {ECO:0000303|PubMed:16906134};
GN Name=Aars1; Synonyms=Aars {ECO:0000312|MGI:MGI:2384560};
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=Mammary gland, and Retina;
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 MRNA].
RC STRAIN=FVB/N; TISSUE=Liver;
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 [3]
RP ISGYLATION.
RX PubMed=16139798; DOI=10.1016/j.bbrc.2005.08.132;
RA Giannakopoulos N.V., Luo J.K., Papov V., Zou W., Lenschow D.J.,
RA Jacobs B.S., Borden E.C., Li J., Virgin H.W., Zhang D.E.;
RT "Proteomic identification of proteins conjugated to ISG15 in mouse and
RT human cells.";
RL Biochem. Biophys. Res. Commun. 336:496-506(2005).
RN [4]
RP FUNCTION, INVOLVEMENT IN STI, VARIANT STI GLU-734, AND CHARACTERIZATION OF
RP VARIANT STI GLU-734.
RX PubMed=16906134; DOI=10.1038/nature05096;
RA Lee J.W., Beebe K., Nangle L.A., Jang J., Longo-Guess C.M., Cook S.A.,
RA Davisson M.T., Sundberg J.P., Schimmel P., Ackerman S.L.;
RT "Editing-defective tRNA synthetase causes protein misfolding and
RT neurodegeneration.";
RL Nature 443:50-55(2006).
RN [5]
RP FUNCTION IN EDITING ACTIVITY ON MISCHARGED TRNA(ALA).
RX PubMed=20010690; DOI=10.1038/nature08612;
RA Guo M., Chong Y.E., Shapiro R., Beebe K., Yang X.L., Schimmel P.;
RT "Paradox of mistranslation of serine for alanine caused by AlaRS
RT recognition dilemma.";
RL Nature 462:808-812(2009).
RN [6]
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 [7]
RP FUNCTION, CATALYTIC ACTIVITY, AND MUTAGENESIS OF CYS-723.
RX PubMed=25422440; DOI=10.1073/pnas.1420196111;
RA Liu Y., Satz J.S., Vo M.N., Nangle L.A., Schimmel P., Ackerman S.L.;
RT "Deficiencies in tRNA synthetase editing activity cause
RT cardioproteinopathy.";
RL Proc. Natl. Acad. Sci. U.S.A. 111:17570-17575(2014).
RN [8]
RP CATALYTIC ACTIVITY, FUNCTION, AND MUTAGENESIS OF ALA-448.
RX PubMed=27622773; DOI=10.1021/jacs.6b07121;
RA Sun L., Gomes A.C., He W., Zhou H., Wang X., Pan D.W., Schimmel P., Pan T.,
RA Yang X.L.;
RT "Evolutionary Gain of Alanine Mischarging to Noncognate tRNAs with a G4:U69
RT Base Pair.";
RL J. Am. Chem. Soc. 138:12948-12955(2016).
RN [9]
RP FUNCTION, AND INTERACTION WITH ANKRD16.
RX PubMed=29769718; DOI=10.1038/s41586-018-0137-8;
RA Vo M.N., Terrey M., Lee J.W., Roy B., Moresco J.J., Sun L., Fu H., Liu Q.,
RA Weber T.G., Yates J.R. III, Fredrick K., Schimmel P., Ackerman S.L.;
RT "ANKRD16 prevents neuron loss caused by an editing-defective tRNA
RT synthetase.";
RL Nature 557:510-515(2018).
CC -!- FUNCTION: Catalyzes the attachment of alanine to tRNA(Ala) in a two-
CC step reaction: alanine is first activated by ATP to form Ala-AMP and
CC then transferred to the acceptor end of tRNA(Ala) (PubMed:16906134,
CC PubMed:20010690, PubMed:25422440, PubMed:27622773). Also edits
CC incorrectly charged tRNA(Ala) via its editing domain (PubMed:16906134,
CC PubMed:20010690, PubMed:25422440, PubMed:29769718). {ECO:0000255|HAMAP-
CC Rule:MF_03133, ECO:0000269|PubMed:16906134,
CC ECO:0000269|PubMed:20010690, ECO:0000269|PubMed:25422440,
CC ECO:0000269|PubMed:27622773, ECO:0000269|PubMed:29769718}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-alanine + tRNA(Ala) = AMP + diphosphate + L-alanyl-
CC tRNA(Ala); Xref=Rhea:RHEA:12540, Rhea:RHEA-COMP:9657, Rhea:RHEA-
CC COMP:9923, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:57972,
CC ChEBI:CHEBI:78442, ChEBI:CHEBI:78497, ChEBI:CHEBI:456215; EC=6.1.1.7;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_03133,
CC ECO:0000269|PubMed:27622773};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_03133};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000255|HAMAP-Rule:MF_03133};
CC -!- SUBUNIT: Monomer (By similarity). Interacts with ANKRD16; the
CC interaction is direct (PubMed:29769718). {ECO:0000255|HAMAP-
CC Rule:MF_03133, ECO:0000269|PubMed:29769718}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03133}.
CC -!- DOMAIN: Consists of three domains; the N-terminal catalytic domain, the
CC editing domain and the C-terminal C-Ala domain. The editing domain
CC removes incorrectly charged amino acids, while the C-Ala domain, along
CC with tRNA(Ala), serves as a bridge to cooperatively bring together the
CC editing and aminoacylation centers thus stimulating deacylation of
CC misacylated tRNAs. {ECO:0000255|HAMAP-Rule:MF_03133}.
CC -!- PTM: ISGylated. {ECO:0000255|HAMAP-Rule:MF_03133,
CC ECO:0000269|PubMed:16139798}.
CC -!- DISEASE: Note=In sticky (sti); homozygous mice display an unkempt
CC sticky appearance of fur and show cerebellar Purkinje cell loss and
CC ataxia. Defects are caused by impaired ability to edit incorrectly
CC charged tRNA(Ala), resulting in a two-fold increase in Ser-mischarged
CC tRNA(Ala). This results in formation of ubiquitinated protein
CC aggregates in cerebellar Purkinje cells and degeneration of these
CC neurons. {ECO:0000269|PubMed:16906134}.
CC -!- MISCELLANEOUS: Was named 'sticky' because of the sticky characteristics
CC of the fur in mice homozygous for the Glu-734 variant.
CC {ECO:0000303|PubMed:16906134}.
CC -!- SIMILARITY: Belongs to the class-II aminoacyl-tRNA synthetase family.
CC {ECO:0000255|HAMAP-Rule:MF_03133}.
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DR EMBL; AK044451; BAC31927.1; -; mRNA.
DR EMBL; AK085725; BAC39520.1; -; mRNA.
DR EMBL; BC033273; AAH33273.1; -; mRNA.
DR CCDS; CCDS40478.1; -.
DR RefSeq; NP_666329.2; NM_146217.4.
DR RefSeq; XP_006530984.1; XM_006530921.2.
DR RefSeq; XP_006530985.1; XM_006530922.1.
DR RefSeq; XP_006530987.1; XM_006530924.1.
DR RefSeq; XP_017168237.1; XM_017312748.1.
DR AlphaFoldDB; Q8BGQ7; -.
DR SMR; Q8BGQ7; -.
DR BioGRID; 231572; 27.
DR IntAct; Q8BGQ7; 4.
DR STRING; 10090.ENSMUSP00000034441; -.
DR iPTMnet; Q8BGQ7; -.
DR PhosphoSitePlus; Q8BGQ7; -.
DR SwissPalm; Q8BGQ7; -.
DR EPD; Q8BGQ7; -.
DR jPOST; Q8BGQ7; -.
DR MaxQB; Q8BGQ7; -.
DR PaxDb; Q8BGQ7; -.
DR PeptideAtlas; Q8BGQ7; -.
DR PRIDE; Q8BGQ7; -.
DR ProteomicsDB; 254614; -.
DR Antibodypedia; 29958; 227 antibodies from 28 providers.
DR DNASU; 234734; -.
DR Ensembl; ENSMUST00000034441; ENSMUSP00000034441; ENSMUSG00000031960.
DR GeneID; 234734; -.
DR KEGG; mmu:234734; -.
DR UCSC; uc009nlo.2; mouse.
DR CTD; 234734; -.
DR MGI; MGI:2384560; Aars.
DR VEuPathDB; HostDB:ENSMUSG00000031960; -.
DR eggNOG; KOG0188; Eukaryota.
DR GeneTree; ENSGT00940000157335; -.
DR HOGENOM; CLU_004485_5_0_1; -.
DR InParanoid; Q8BGQ7; -.
DR OMA; YHHTMFE; -.
DR OrthoDB; 129373at2759; -.
DR PhylomeDB; Q8BGQ7; -.
DR TreeFam; TF300737; -.
DR BioGRID-ORCS; 234734; 24 hits in 73 CRISPR screens.
DR ChiTaRS; Aars; mouse.
DR PRO; PR:Q8BGQ7; -.
DR Proteomes; UP000000589; Chromosome 8.
DR RNAct; Q8BGQ7; protein.
DR Bgee; ENSMUSG00000031960; Expressed in vault of skull and 260 other tissues.
DR ExpressionAtlas; Q8BGQ7; baseline and differential.
DR Genevisible; Q8BGQ7; MM.
DR GO; GO:0005737; C:cytoplasm; ISO:MGI.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0005739; C:mitochondrion; IBA:GO_Central.
DR GO; GO:0004813; F:alanine-tRNA ligase activity; IDA:UniProtKB.
DR GO; GO:0016597; F:amino acid binding; ISO:MGI.
DR GO; GO:0002161; F:aminoacyl-tRNA editing activity; IDA:UniProtKB.
DR GO; GO:0005524; F:ATP binding; ISO:MGI.
DR GO; GO:0002196; F:Ser-tRNA(Ala) hydrolase activity; IDA:UniProtKB.
DR GO; GO:0045182; F:translation regulator activity; IMP:MGI.
DR GO; GO:0000049; F:tRNA binding; ISO:MGI.
DR GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0006419; P:alanyl-tRNA aminoacylation; IDA:UniProtKB.
DR GO; GO:0021680; P:cerebellar Purkinje cell layer development; IMP:MGI.
DR GO; GO:0043524; P:negative regulation of neuron apoptotic process; IMP:MGI.
DR GO; GO:0050905; P:neuromuscular process; IMP:MGI.
DR GO; GO:0050885; P:neuromuscular process controlling balance; IMP:MGI.
DR GO; GO:0051402; P:neuron apoptotic process; IMP:MGI.
DR GO; GO:0140018; P:regulation of cytoplasmic translational fidelity; IMP:MGI.
DR GO; GO:0006400; P:tRNA modification; IDA:UniProtKB.
DR Gene3D; 3.30.930.10; -; 1.
DR HAMAP; MF_00036_B; Ala_tRNA_synth_B; 1.
DR InterPro; IPR045864; aa-tRNA-synth_II/BPL/LPL.
DR InterPro; IPR002318; Ala-tRNA-lgiase_IIc.
DR InterPro; IPR018162; Ala-tRNA-ligase_IIc_anticod-bd.
DR InterPro; IPR018165; Ala-tRNA-synth_IIc_core.
DR InterPro; IPR018164; Ala-tRNA-synth_IIc_N.
DR InterPro; IPR023033; Ala_tRNA_ligase_euk/bac.
DR InterPro; IPR003156; DHHA1_dom.
DR InterPro; IPR018163; Thr/Ala-tRNA-synth_IIc_edit.
DR InterPro; IPR009000; Transl_B-barrel_sf.
DR InterPro; IPR012947; tRNA_SAD.
DR Pfam; PF02272; DHHA1; 1.
DR Pfam; PF01411; tRNA-synt_2c; 1.
DR Pfam; PF07973; tRNA_SAD; 1.
DR PRINTS; PR00980; TRNASYNTHALA.
DR SMART; SM00863; tRNA_SAD; 1.
DR SUPFAM; SSF101353; SSF101353; 1.
DR SUPFAM; SSF50447; SSF50447; 1.
DR SUPFAM; SSF55186; SSF55186; 1.
DR SUPFAM; SSF55681; SSF55681; 1.
DR TIGRFAMs; TIGR00344; alaS; 1.
DR PROSITE; PS50860; AA_TRNA_LIGASE_II_ALA; 1.
PE 1: Evidence at protein level;
KW Acetylation; Aminoacyl-tRNA synthetase; ATP-binding; Cytoplasm;
KW Disease variant; Ligase; Metal-binding; Nucleotide-binding; Phosphoprotein;
KW Protein biosynthesis; Reference proteome; RNA-binding; tRNA-binding;
KW Ubl conjugation; Zinc.
FT CHAIN 1..968
FT /note="Alanine--tRNA ligase, cytoplasmic"
FT /id="PRO_0000075282"
FT BINDING 77
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P49588"
FT BINDING 95
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P49588"
FT BINDING 176
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P49588"
FT BINDING 214..216
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P49588"
FT BINDING 216
FT /ligand="L-alanine"
FT /ligand_id="ChEBI:CHEBI:57972"
FT /evidence="ECO:0000250|UniProtKB:P49588"
FT BINDING 239
FT /ligand="L-alanine"
FT /ligand_id="ChEBI:CHEBI:57972"
FT /evidence="ECO:0000250|UniProtKB:P49588"
FT BINDING 243
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P49588"
FT BINDING 605
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03133"
FT BINDING 609
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03133"
FT BINDING 723
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03133"
FT BINDING 727
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03133"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0000250|UniProtKB:P49588, ECO:0000255|HAMAP-
FT Rule:MF_03133"
FT MOD_RES 399
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P49588"
FT MOD_RES 555
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P49588"
FT MOD_RES 876
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P49588"
FT VARIANT 734
FT /note="A -> E (in sti; homozygous mice display an unkempt
FT sticky appearance of fur and show cerebellar Purkinje cell
FT loss and ataxia; defects are caused by impaired ability to
FT edit incorrectly charged tRNA, resulting in formation of
FT ubiquitinated protein aggregates in cerebellar Purkinje
FT cells and degeneration of these neurons)"
FT /evidence="ECO:0000269|PubMed:16906134"
FT MUTAGEN 448
FT /note="A->Q: Decreases misincorporation of Cys instead of
FT Ala."
FT /evidence="ECO:0000269|PubMed:27622773"
FT MUTAGEN 723
FT /note="C->A: Homozygous embryos die at midgestation.
FT Defects are caused by a dramatic increase in production of
FT Ser-mischarged tRNA(Ala)."
FT /evidence="ECO:0000269|PubMed:25422440"
FT CONFLICT 369
FT /note="E -> D (in Ref. 1; BAC31927)"
FT /evidence="ECO:0000305"
FT CONFLICT 630
FT /note="A -> T (in Ref. 1; BAC31927)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 968 AA; 106909 MW; 7CDF2556C81A89EC CRC64;
MDATLTAREI RERFINFFRR NEHTYVHSSA TIPLDDPTLL FANAGMNQFK PIFLNTIDPS
HPMAKLSRAA NTQKCIRAGG KHNDLDDVGK DVYHHTFFEM LGSWSFGDYF KELACKMALE
LLTQEFGIPV ERLYVTYFGG DEAAGLEPDL ECRQIWQNLG LDEARILPGN MKDNFWEMGD
TGPCGPCSEI HYDRIGGRDA AHLVNQDDPN VLEIWNLVFI QYNRESDGVL KPLPKKSIDT
GMGLERLVSV LQNKMSNYDT DLFMPYFEAI QKGTGARPYT GKVGAEDADG IDMAYRVLAD
HARTITVALA DGGRPDNTGR GYVLRRILRR AVRYSHEKLN ASRGFFATLV DVVVQSLGDA
FPELKKDPEM VKDIINEEEV QFLKTLSRGR RILDRKIQSL GDCKTIPGDT AWLLYDTYGF
PVDLTGLIAE EKGLVVDMNG FEEERRLAQL KSQGKGAGDE DLIMLDIYAI EELRAKGLEA
TDDSPKYNYQ SDSSGSYVFE CTVATVLALR REKMFVDEVV TGQECGVVLD KTCFYAEQGG
QIYDEGYLVK VDDSSEDKTE FTVKNAQVRG GYVLHIGTIY GNLKVGDQVR LFIDEPRRRP
VMSNHTATHI LNFALRSVLG EADQKGSLVA PDRLRFDFTA KGAMSTQQIK KAEEIVNGMI
EAAKPVYTQD CPLAAAKAIQ GLRAVFDETY PDPVRVVSIG VPVSELLDDP CGPAGSLTSV
EFCGGTHLRN SSHAGAFVIV TEEAIAKGIR RIVAVTGAEA QKALRKSETL KKSLSAMEAK
VKAQTAPNKD VQREIADLGE ALATAVIPQW QKDEQRETLK SLKKVMDDLD RASKADVQKR
VLEKTKQLID SNPNQPLVIL EMESGASAKA LNEALKLFKT HSPQTSAMLF TVDNEAGKIT
CLCQVPQNAA NRGLKASEWV QQVSGLMDGK GGGKDMSAQA TGKNVGCLQE ALQLATSFAQ
LRLGDVKN
