NIT2_MOUSE
ID NIT2_MOUSE Reviewed; 276 AA.
AC Q9JHW2; Q9CTG9;
DT 26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 142.
DE RecName: Full=Omega-amidase NIT2 {ECO:0000303|PubMed:19596042};
DE EC=3.5.1.3 {ECO:0000269|PubMed:19596042, ECO:0000269|PubMed:28373563};
DE AltName: Full=Nitrilase homolog 2 {ECO:0000305};
GN Name=Nit2 {ECO:0000303|PubMed:19596042}; Synonyms=D16Ertd502e;
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 [MRNA].
RX PubMed=10959838; DOI=10.1016/s0960-9822(00)00621-7;
RA Pace H.C., Hodawadekar S.C., Draganescu A., Huang J., Bieganowski P.,
RA Pekarsky Y., Croce C.M., Brenner C.;
RT "Crystal structure of the worm NitFhit Rosetta stone protein reveals a Nit
RT tetramer binding two Fhit dimers.";
RL Curr. Biol. 10:907-917(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J, and FVB/N; TISSUE=Mammary tumor;
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 [4]
RP FUNCTION, CATALYTIC ACTIVITY, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=19596042; DOI=10.1016/j.biochi.2009.07.002;
RA Jaisson S., Veiga-da-Cunha M., Van Schaftingen E.;
RT "Molecular identification of omega-amidase, the enzyme that is functionally
RT coupled with glutamine transaminases, as the putative tumor suppressor
RT Nit2.";
RL Biochimie 91:1066-1071(2009).
RN [5]
RP SUBUNIT.
RX PubMed=19595734; DOI=10.1016/j.biochi.2009.07.003;
RA Krasnikov B.F., Chien C.-H., Nostramo R., Pinto J.T., Nieves E.,
RA Callaway M., Sun J., Huebner K., Cooper A.J.L.;
RT "Identification of the putative tumor suppressor Nit2 as omega-amidase, an
RT enzyme metabolically linked to glutamine and asparagine transamination.";
RL Biochimie 91:1072-1080(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 ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-68, SUCCINYLATION [LARGE SCALE
RP ANALYSIS] AT LYS-68; LYS-123 AND LYS-130, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic fibroblast, and 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 [8]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-68, AND IDENTIFICATION BY MASS
RP 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 [9]
RP CATALYTIC ACTIVITY, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=28373563; DOI=10.1073/pnas.1613736114;
RA Peracchi A., Veiga-da-Cunha M., Kuhara T., Ellens K.W., Paczia N.,
RA Stroobant V., Seliga A.K., Marlaire S., Jaisson S., Bommer G.T., Sun J.,
RA Huebner K., Linster C.L., Cooper A.J.L., Van Schaftingen E.;
RT "Nit1 is a metabolite repair enzyme that hydrolyzes deaminated
RT glutathione.";
RL Proc. Natl. Acad. Sci. U.S.A. 114:E3233-E3242(2017).
RN [10]
RP X-RAY CRYSTALLOGRAPHY (1.49 ANGSTROMS), AND HOMODIMERIZATION.
RX PubMed=19053248; DOI=10.1021/bi801786y;
RA Barglow K.T., Saikatendu K.S., Bracey M.H., Huey R., Morris G.M.,
RA Olson A.J., Stevens R.C., Cravatt B.F.;
RT "Functional proteomic and structural insights into molecular recognition in
RT the nitrilase family enzymes.";
RL Biochemistry 47:13514-13523(2008).
CC -!- FUNCTION: Has omega-amidase activity (PubMed:19596042,
CC PubMed:28373563). The role of omega-amidase is to remove potentially
CC toxic intermediates by converting 2-oxoglutaramate and 2-oxosuccinamate
CC to biologically useful 2-oxoglutarate and oxaloacetate, respectively
CC (PubMed:19596042). Can also hydrolyze gamma-monomethyl-alpha-
CC ketoglutarate in vitro (PubMed:19596042). {ECO:0000269|PubMed:19596042,
CC ECO:0000269|PubMed:28373563}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a monoamide of a dicarboxylate + H2O = a dicarboxylate +
CC NH4(+); Xref=Rhea:RHEA:11716, ChEBI:CHEBI:15377, ChEBI:CHEBI:28938,
CC ChEBI:CHEBI:28965, ChEBI:CHEBI:77450; EC=3.5.1.3;
CC Evidence={ECO:0000269|PubMed:19596042, ECO:0000269|PubMed:28373563};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:11717;
CC Evidence={ECO:0000269|PubMed:19596042, ECO:0000269|PubMed:28373563};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2-oxoglutaramate + H2O = 2-oxoglutarate + NH4(+);
CC Xref=Rhea:RHEA:32963, ChEBI:CHEBI:15377, ChEBI:CHEBI:16769,
CC ChEBI:CHEBI:16810, ChEBI:CHEBI:28938; EC=3.5.1.3;
CC Evidence={ECO:0000269|PubMed:19596042, ECO:0000269|PubMed:28373563};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:32964;
CC Evidence={ECO:0000269|PubMed:19596042, ECO:0000269|PubMed:28373563};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2-oxosuccinamate + H2O = NH4(+) + oxaloacetate;
CC Xref=Rhea:RHEA:59412, ChEBI:CHEBI:15377, ChEBI:CHEBI:16452,
CC ChEBI:CHEBI:28938, ChEBI:CHEBI:57735; EC=3.5.1.3;
CC Evidence={ECO:0000269|PubMed:19596042};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:59413;
CC Evidence={ECO:0000269|PubMed:19596042};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.195 mM for 2-oxoglutaramate (at pH 8.5)
CC {ECO:0000269|PubMed:19596042};
CC KM=0.25 mM for 2-oxoglutaramate (at pH 8.5)
CC {ECO:0000269|PubMed:28373563};
CC KM=1.48 mM for glutaramate (at pH 7.2) {ECO:0000269|PubMed:19596042};
CC KM=1.27 mM for glutaramate (at pH 8.5) {ECO:0000269|PubMed:19596042};
CC KM=0.14 mM for succinamate (at pH 8.5) {ECO:0000269|PubMed:19596042};
CC KM=0.017 mM for 2-oxosuccinamate (at pH 8.5)
CC {ECO:0000269|PubMed:19596042};
CC KM=0.003 mM for 2-oxosuccinamate (at pH 7.2)
CC {ECO:0000269|PubMed:19596042};
CC KM=0.012 mM for gamma-monomethyl-alpha-ketoglutarate (at pH 7.2)
CC {ECO:0000269|PubMed:19596042};
CC Vmax=32.0 umol/min/mg enzyme with 2-oxoglutaramate as substrate (at
CC pH 8.5) {ECO:0000269|PubMed:19596042};
CC Vmax=19.4 umol/min/mg enzyme with 2-oxoglutaramate as substrate (at
CC pH 8.5) {ECO:0000269|PubMed:28373563};
CC Vmax=1.6 umol/min/mg enzyme with 2-oxosuccinamate as substrate (at pH
CC 8.5) {ECO:0000269|PubMed:19596042};
CC Vmax=16 umol/min/mg enzyme with glutaramate as substrate (at pH 8.5)
CC {ECO:0000269|PubMed:19596042};
CC Vmax=5.1 umol/min/mg enzyme with succinamate as substrate (at pH 8.5)
CC {ECO:0000269|PubMed:19596042};
CC Vmax=245.2 umol/min/mg enzyme with gamma-monomethyl-alpha-
CC ketoglutarate as substrate (at pH 7.2) {ECO:0000269|PubMed:19596042};
CC Vmax=7.5 umol/min/mg enzyme with glutaramate as substrate (at pH 7.2)
CC {ECO:0000269|PubMed:19596042};
CC Vmax=3.6 umol/min/mg enzyme with succinamate as substrate (at pH 7.2)
CC {ECO:0000269|PubMed:19596042};
CC Vmax=2.1 umol/min/mg enzyme with 2-oxosuccinamate as substrate (at pH
CC 7.2) {ECO:0000269|PubMed:19596042};
CC Note=In solution, 2-oxoglutaramate is in equilibrium with a cyclic
CC form (2-hydroxy-5-oxoproline), and at pH 8.0 or above, the rate of
CC ring opening is no longer limiting for the omega-amidase reaction
CC (PubMed:19596042). kcat is 10.7 sec(-1) with 2-oxoglutaramate as
CC substrate (PubMed:28373563). {ECO:0000269|PubMed:19596042,
CC ECO:0000269|PubMed:28373563};
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:19053248,
CC ECO:0000305|PubMed:19595734}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q9NQR4}.
CC -!- SIMILARITY: Belongs to the carbon-nitrogen hydrolase superfamily.
CC NIT1/NIT2 family. {ECO:0000305}.
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DR EMBL; AF284573; AAF87102.1; -; mRNA.
DR EMBL; AK003604; BAB22884.1; -; mRNA.
DR EMBL; AK004535; BAB23354.1; -; mRNA.
DR EMBL; BC020153; AAH20153.1; -; mRNA.
DR CCDS; CCDS37363.1; -.
DR RefSeq; NP_075664.1; NM_023175.1.
DR PDB; 2W1V; X-ray; 1.49 A; A/B=1-276.
DR PDBsum; 2W1V; -.
DR AlphaFoldDB; Q9JHW2; -.
DR SMR; Q9JHW2; -.
DR BioGRID; 206703; 1.
DR STRING; 10090.ENSMUSP00000023432; -.
DR iPTMnet; Q9JHW2; -.
DR PhosphoSitePlus; Q9JHW2; -.
DR SwissPalm; Q9JHW2; -.
DR REPRODUCTION-2DPAGE; IPI00119945; -.
DR EPD; Q9JHW2; -.
DR jPOST; Q9JHW2; -.
DR MaxQB; Q9JHW2; -.
DR PaxDb; Q9JHW2; -.
DR PeptideAtlas; Q9JHW2; -.
DR PRIDE; Q9JHW2; -.
DR ProteomicsDB; 293566; -.
DR Antibodypedia; 32221; 256 antibodies from 24 providers.
DR DNASU; 52633; -.
DR Ensembl; ENSMUST00000023432; ENSMUSP00000023432; ENSMUSG00000022751.
DR GeneID; 52633; -.
DR KEGG; mmu:52633; -.
DR UCSC; uc007zna.1; mouse.
DR CTD; 56954; -.
DR MGI; MGI:1261838; Nit2.
DR VEuPathDB; HostDB:ENSMUSG00000022751; -.
DR eggNOG; KOG0806; Eukaryota.
DR GeneTree; ENSGT00550000074838; -.
DR HOGENOM; CLU_030130_1_0_1; -.
DR InParanoid; Q9JHW2; -.
DR OMA; GNTYRES; -.
DR OrthoDB; 1154369at2759; -.
DR PhylomeDB; Q9JHW2; -.
DR TreeFam; TF300747; -.
DR BioCyc; MetaCyc:MON-18738; -.
DR Reactome; R-MMU-6798695; Neutrophil degranulation.
DR BioGRID-ORCS; 52633; 1 hit in 71 CRISPR screens.
DR ChiTaRS; Nit2; mouse.
DR EvolutionaryTrace; Q9JHW2; -.
DR PRO; PR:Q9JHW2; -.
DR Proteomes; UP000000589; Chromosome 16.
DR RNAct; Q9JHW2; protein.
DR Bgee; ENSMUSG00000022751; Expressed in right kidney and 237 other tissues.
DR ExpressionAtlas; Q9JHW2; baseline and differential.
DR Genevisible; Q9JHW2; MM.
DR GO; GO:0005813; C:centrosome; ISO:MGI.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0005739; C:mitochondrion; HDA:MGI.
DR GO; GO:0106008; F:2-oxoglutaramate amidase activity; IEA:RHEA.
DR GO; GO:0050152; F:omega-amidase activity; ISO:MGI.
DR GO; GO:0006528; P:asparagine metabolic process; ISO:MGI.
DR GO; GO:0006541; P:glutamine metabolic process; ISO:MGI.
DR GO; GO:0006107; P:oxaloacetate metabolic process; ISO:MGI.
DR CDD; cd07572; nit; 1.
DR Gene3D; 3.60.110.10; -; 1.
DR InterPro; IPR003010; C-N_Hydrolase.
DR InterPro; IPR036526; C-N_Hydrolase_sf.
DR InterPro; IPR045254; Nit1/2_C-N_Hydrolase.
DR Pfam; PF00795; CN_hydrolase; 1.
DR SUPFAM; SSF56317; SSF56317; 1.
DR PROSITE; PS50263; CN_HYDROLASE; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Cytoplasm; Hydrolase; Phosphoprotein;
KW Reference proteome.
FT CHAIN 1..276
FT /note="Omega-amidase NIT2"
FT /id="PRO_0000320254"
FT DOMAIN 4..248
FT /note="CN hydrolase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00054"
FT ACT_SITE 43
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00054"
FT ACT_SITE 112
FT /note="Proton donor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00054"
FT ACT_SITE 153
FT /note="Nucleophile"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00054"
FT MOD_RES 26
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9NQR4"
FT MOD_RES 68
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:23576753,
FT ECO:0007744|PubMed:23806337"
FT MOD_RES 68
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 123
FT /note="N6-succinyllysine"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 130
FT /note="N6-succinyllysine"
FT /evidence="ECO:0007744|PubMed:23806337"
FT STRAND 3..10
FT /evidence="ECO:0007829|PDB:2W1V"
FT HELIX 17..33
FT /evidence="ECO:0007829|PDB:2W1V"
FT STRAND 37..40
FT /evidence="ECO:0007829|PDB:2W1V"
FT TURN 43..46
FT /evidence="ECO:0007829|PDB:2W1V"
FT TURN 51..53
FT /evidence="ECO:0007829|PDB:2W1V"
FT HELIX 54..57
FT /evidence="ECO:0007829|PDB:2W1V"
FT STRAND 61..63
FT /evidence="ECO:0007829|PDB:2W1V"
FT HELIX 64..76
FT /evidence="ECO:0007829|PDB:2W1V"
FT STRAND 78..81
FT /evidence="ECO:0007829|PDB:2W1V"
FT STRAND 85..89
FT /evidence="ECO:0007829|PDB:2W1V"
FT STRAND 92..100
FT /evidence="ECO:0007829|PDB:2W1V"
FT STRAND 106..111
FT /evidence="ECO:0007829|PDB:2W1V"
FT STRAND 117..120
FT /evidence="ECO:0007829|PDB:2W1V"
FT TURN 121..123
FT /evidence="ECO:0007829|PDB:2W1V"
FT STRAND 124..127
FT /evidence="ECO:0007829|PDB:2W1V"
FT HELIX 128..130
FT /evidence="ECO:0007829|PDB:2W1V"
FT STRAND 140..142
FT /evidence="ECO:0007829|PDB:2W1V"
FT STRAND 147..150
FT /evidence="ECO:0007829|PDB:2W1V"
FT HELIX 153..157
FT /evidence="ECO:0007829|PDB:2W1V"
FT HELIX 159..167
FT /evidence="ECO:0007829|PDB:2W1V"
FT STRAND 170..176
FT /evidence="ECO:0007829|PDB:2W1V"
FT HELIX 183..199
FT /evidence="ECO:0007829|PDB:2W1V"
FT STRAND 202..206
FT /evidence="ECO:0007829|PDB:2W1V"
FT STRAND 214..216
FT /evidence="ECO:0007829|PDB:2W1V"
FT STRAND 223..225
FT /evidence="ECO:0007829|PDB:2W1V"
FT STRAND 231..234
FT /evidence="ECO:0007829|PDB:2W1V"
FT STRAND 237..247
FT /evidence="ECO:0007829|PDB:2W1V"
FT HELIX 248..257
FT /evidence="ECO:0007829|PDB:2W1V"
FT HELIX 260..262
FT /evidence="ECO:0007829|PDB:2W1V"
FT TURN 266..268
FT /evidence="ECO:0007829|PDB:2W1V"
FT STRAND 269..273
FT /evidence="ECO:0007829|PDB:2W1V"
SQ SEQUENCE 276 AA; 30502 MW; 740FDC44978326D6 CRC64;
MSTFRLALIQ LQVSSIKSDN LTRACSLVRE AAKQGANIVS LPECFNSPYG TTYFPDYAEK
IPGESTQKLS EVAKESSIYL IGGSIPEEDA GKLYNTCSVF GPDGSLLVKH RKIHLFDIDV
PGKITFQESK TLSPGDSFST FDTPYCKVGL GICYDMRFAE LAQIYAQRGC QLLVYPGAFN
LTTGPAHWEL LQRARAVDNQ VYVATASPAR DDKASYVAWG HSTVVDPWGQ VLTKAGTEET
ILYSDIDLKK LAEIRQQIPI LKQKRADLYT VESKKP
