FAAA_MOUSE
ID FAAA_MOUSE Reviewed; 419 AA.
AC P35505; Q3TY87; Q9QW65;
DT 01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 2.
DT 03-AUG-2022, entry version 170.
DE RecName: Full=Fumarylacetoacetase;
DE Short=FAA;
DE EC=3.7.1.2 {ECO:0000269|PubMed:11154690, ECO:0000269|PubMed:11209059};
DE AltName: Full=Beta-diketonase;
DE AltName: Full=Fumarylacetoacetate hydrolase;
GN Name=Fah;
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=1741389; DOI=10.1073/pnas.89.4.1363;
RA Klebig M.L., Russell L.B., Rinchik E.M.;
RT "Murine fumarylacetoacetate hydrolase (Fah) gene is disrupted by a
RT neonatally lethal albino deletion that defines the hepatocyte-specific
RT developmental regulation 1 (hsdr-1) locus.";
RL Proc. Natl. Acad. Sci. U.S.A. 89:1363-1367(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=C57BL/6J; TISSUE=Liver;
RX PubMed=1524868; DOI=10.1016/0885-4505(92)90044-y;
RA Grompe M., Al-Dhalimy M.;
RT "Nucleotide sequence of a cDNA encoding murine fumarylacetoacetate
RT hydrolase.";
RL Biochem. Med. Metab. Biol. 48:26-31(1992).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=1644288; DOI=10.1101/gad.6.8.1430;
RA Ruppert S., Kelsey G., Schedl A., Schmid E., Thies E., Schutz G.;
RT "Deficiency of an enzyme of tyrosine metabolism underlies altered gene
RT expression in newborn liver of lethal albino mice.";
RL Genes Dev. 6:1430-1443(1992).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Spleen, and Visual cortex;
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=FVB/N; TISSUE=Kidney;
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 [6]
RP MUTAGENESIS OF GLU-201, AND CATALYTIC ACTIVITY.
RX PubMed=11209059; DOI=10.1073/pnas.98.2.641;
RA Aponte J.L., Sega G.A., Hauser L.J., Dhar M.S., Withrow C.M.,
RA Carpenter D.A., Rinchik E.M., Culiat C.T., Johnson D.K.;
RT "Point mutations in the murine fumarylacetoacetate hydrolase gene: animal
RT models for the human genetic disorder hereditary tyrosinemia type 1.";
RL Proc. Natl. Acad. Sci. U.S.A. 98:641-645(2001).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-84 AND SER-92, AND
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 [8]
RP X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) IN COMPLEX WITH PRODUCTS AND CALCIUM,
RP COFACTOR, ACTIVE SITE, AND SUBUNIT.
RX PubMed=10508789; DOI=10.1016/s0969-2126(99)80170-1;
RA Timm D.E., Mueller H.A., Bhanumoorthy P., Harp J.M., Bunick G.J.;
RT "Crystal structure and mechanism of a carbon-carbon bond hydrolase.";
RL Structure 7:1023-1033(1999).
RN [9]
RP X-RAY CRYSTALLOGRAPHY (1.3 ANGSTROMS) IN COMPLEX WITH INHIBITOR; CALCIUM
RP AND MAGNESIUM, SUBUNIT, CATALYTIC ACTIVITY, AND COFACTOR.
RX PubMed=11154690; DOI=10.1074/jbc.m007621200;
RA Bateman R.L., Bhanumoorthy P., Witte J.F., McClard R.W., Grompe M.,
RA Timm D.E.;
RT "Mechanistic inferences from the crystal structure of fumarylacetoacetate
RT hydrolase with a bound phosphorus-based inhibitor.";
RL J. Biol. Chem. 276:15284-15291(2001).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=4-fumarylacetoacetate + H2O = acetoacetate + fumarate + H(+);
CC Xref=Rhea:RHEA:10244, ChEBI:CHEBI:13705, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:18034, ChEBI:CHEBI:29806; EC=3.7.1.2;
CC Evidence={ECO:0000269|PubMed:11154690, ECO:0000269|PubMed:11209059};
CC -!- COFACTOR:
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC Evidence={ECO:0000269|PubMed:11154690, ECO:0000305|PubMed:10508789};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000269|PubMed:11154690};
CC -!- PATHWAY: Amino-acid degradation; L-phenylalanine degradation;
CC acetoacetate and fumarate from L-phenylalanine: step 6/6.
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:10508789,
CC ECO:0000269|PubMed:11154690}.
CC -!- TISSUE SPECIFICITY: Mainly in liver and kidney.
CC -!- SIMILARITY: Belongs to the FAH family. {ECO:0000305}.
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DR EMBL; M84145; AAA37591.1; -; mRNA.
DR EMBL; Z11774; CAA77819.1; -; mRNA.
DR EMBL; AK143759; BAE25527.1; -; mRNA.
DR EMBL; AK158808; BAE34676.1; -; mRNA.
DR EMBL; BC010767; AAH10767.1; -; mRNA.
DR CCDS; CCDS21418.1; -.
DR PIR; A40219; A40219.
DR PIR; A56825; A56825.
DR RefSeq; NP_034306.2; NM_010176.4.
DR PDB; 1HYO; X-ray; 1.30 A; A/B=1-419.
DR PDB; 1QCN; X-ray; 1.90 A; A/B=1-419.
DR PDB; 1QCO; X-ray; 1.90 A; A/B=1-419.
DR PDB; 1QQJ; X-ray; 1.55 A; A/B=1-419.
DR PDB; 2HZY; X-ray; 1.35 A; A/B=1-419.
DR PDBsum; 1HYO; -.
DR PDBsum; 1QCN; -.
DR PDBsum; 1QCO; -.
DR PDBsum; 1QQJ; -.
DR PDBsum; 2HZY; -.
DR AlphaFoldDB; P35505; -.
DR SMR; P35505; -.
DR BioGRID; 199589; 1.
DR IntAct; P35505; 1.
DR STRING; 10090.ENSMUSP00000032865; -.
DR iPTMnet; P35505; -.
DR PhosphoSitePlus; P35505; -.
DR SwissPalm; P35505; -.
DR SWISS-2DPAGE; P35505; -.
DR CPTAC; non-CPTAC-3643; -.
DR CPTAC; non-CPTAC-3803; -.
DR EPD; P35505; -.
DR jPOST; P35505; -.
DR MaxQB; P35505; -.
DR PaxDb; P35505; -.
DR PeptideAtlas; P35505; -.
DR PRIDE; P35505; -.
DR ProteomicsDB; 267702; -.
DR Antibodypedia; 27851; 304 antibodies from 28 providers.
DR DNASU; 14085; -.
DR Ensembl; ENSMUST00000032865; ENSMUSP00000032865; ENSMUSG00000030630.
DR GeneID; 14085; -.
DR KEGG; mmu:14085; -.
DR UCSC; uc009iej.3; mouse.
DR CTD; 2184; -.
DR MGI; MGI:95482; Fah.
DR VEuPathDB; HostDB:ENSMUSG00000030630; -.
DR eggNOG; KOG2843; Eukaryota.
DR GeneTree; ENSGT00390000008646; -.
DR HOGENOM; CLU_026207_2_0_1; -.
DR InParanoid; P35505; -.
DR OMA; YWTAAQQ; -.
DR OrthoDB; 980065at2759; -.
DR PhylomeDB; P35505; -.
DR TreeFam; TF315211; -.
DR BRENDA; 3.7.1.2; 3474.
DR Reactome; R-MMU-8963684; Tyrosine catabolism.
DR UniPathway; UPA00139; UER00341.
DR BioGRID-ORCS; 14085; 0 hits in 72 CRISPR screens.
DR ChiTaRS; Fah; mouse.
DR EvolutionaryTrace; P35505; -.
DR PRO; PR:P35505; -.
DR Proteomes; UP000000589; Chromosome 7.
DR RNAct; P35505; protein.
DR Bgee; ENSMUSG00000030630; Expressed in left lobe of liver and 236 other tissues.
DR ExpressionAtlas; P35505; baseline and differential.
DR Genevisible; P35505; MM.
DR GO; GO:0004334; F:fumarylacetoacetase activity; IMP:MGI.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0006527; P:arginine catabolic process; IMP:MGI.
DR GO; GO:1902000; P:homogentisate catabolic process; IBA:GO_Central.
DR GO; GO:0006559; P:L-phenylalanine catabolic process; IBA:GO_Central.
DR GO; GO:0006629; P:lipid metabolic process; IEA:UniProtKB-KW.
DR GO; GO:0006572; P:tyrosine catabolic process; IBA:GO_Central.
DR Gene3D; 2.30.30.230; -; 1.
DR Gene3D; 3.90.850.10; -; 1.
DR InterPro; IPR005959; Fumarylacetoacetase.
DR InterPro; IPR011234; Fumarylacetoacetase-like_C.
DR InterPro; IPR036663; Fumarylacetoacetase_C_sf.
DR InterPro; IPR015377; Fumarylacetoacetase_N.
DR InterPro; IPR036462; Fumarylacetoacetase_N_sf.
DR PANTHER; PTHR43069; PTHR43069; 1.
DR Pfam; PF01557; FAA_hydrolase; 1.
DR Pfam; PF09298; FAA_hydrolase_N; 1.
DR SUPFAM; SSF56529; SSF56529; 1.
DR SUPFAM; SSF63433; SSF63433; 1.
DR TIGRFAMs; TIGR01266; fum_ac_acetase; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Calcium; Hydrolase; Lipid metabolism; Magnesium;
KW Metal-binding; Phenylalanine catabolism; Phosphoprotein;
KW Reference proteome; Tyrosine catabolism.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:P16930"
FT CHAIN 2..419
FT /note="Fumarylacetoacetase"
FT /id="PRO_0000156826"
FT ACT_SITE 133
FT /note="Proton acceptor"
FT /evidence="ECO:0000305|PubMed:10508789"
FT BINDING 126
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000269|PubMed:10508789,
FT ECO:0000269|PubMed:11154690"
FT BINDING 128
FT /ligand="substrate"
FT /evidence="ECO:0000305|PubMed:10508789"
FT BINDING 142
FT /ligand="substrate"
FT /evidence="ECO:0000305|PubMed:10508789"
FT BINDING 199
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000269|PubMed:10508789,
FT ECO:0000269|PubMed:11154690"
FT BINDING 201
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000269|PubMed:10508789,
FT ECO:0000269|PubMed:11154690"
FT BINDING 233
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000269|PubMed:10508789,
FT ECO:0000269|PubMed:11154690"
FT BINDING 233
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000269|PubMed:11154690"
FT BINDING 240
FT /ligand="substrate"
FT /evidence="ECO:0000305|PubMed:10508789"
FT BINDING 244
FT /ligand="substrate"
FT /evidence="ECO:0000305|PubMed:10508789"
FT BINDING 253
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000269|PubMed:11154690"
FT BINDING 257
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000269|PubMed:11154690"
FT BINDING 350
FT /ligand="substrate"
FT /evidence="ECO:0000305|PubMed:10508789"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0000250|UniProtKB:P16930"
FT MOD_RES 84
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 92
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 309
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P16930"
FT MOD_RES 417
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P25093"
FT MUTAGEN 201
FT /note="E->G: Decrease in activity."
FT /evidence="ECO:0000269|PubMed:11209059"
FT CONFLICT 129..130
FT /note="SS -> PF (in Ref. 2; CAA77819)"
FT /evidence="ECO:0000305"
FT CONFLICT 307
FT /note="G -> R (in Ref. 3; no nucleotide entry)"
FT /evidence="ECO:0000305"
FT CONFLICT 376
FT /note="E -> G (in Ref. 1; AAA37591 and 5; AAH10767)"
FT /evidence="ECO:0000305"
FT STRAND 2..4
FT /evidence="ECO:0007829|PDB:1QQJ"
FT TURN 14..16
FT /evidence="ECO:0007829|PDB:1HYO"
FT STRAND 19..23
FT /evidence="ECO:0007829|PDB:1HYO"
FT STRAND 31..36
FT /evidence="ECO:0007829|PDB:1HYO"
FT STRAND 39..42
FT /evidence="ECO:0007829|PDB:1HYO"
FT TURN 43..46
FT /evidence="ECO:0007829|PDB:1HYO"
FT HELIX 47..49
FT /evidence="ECO:0007829|PDB:1HYO"
FT TURN 53..57
FT /evidence="ECO:0007829|PDB:1HYO"
FT HELIX 59..63
FT /evidence="ECO:0007829|PDB:1HYO"
FT STRAND 64..67
FT /evidence="ECO:0007829|PDB:1HYO"
FT HELIX 68..73
FT /evidence="ECO:0007829|PDB:1HYO"
FT HELIX 75..89
FT /evidence="ECO:0007829|PDB:1HYO"
FT TURN 90..94
FT /evidence="ECO:0007829|PDB:1QCN"
FT HELIX 95..98
FT /evidence="ECO:0007829|PDB:1HYO"
FT HELIX 100..106
FT /evidence="ECO:0007829|PDB:1HYO"
FT STRAND 107..110
FT /evidence="ECO:0007829|PDB:1HYO"
FT STRAND 114..116
FT /evidence="ECO:0007829|PDB:1HYO"
FT STRAND 124..127
FT /evidence="ECO:0007829|PDB:1HYO"
FT HELIX 131..142
FT /evidence="ECO:0007829|PDB:1HYO"
FT HELIX 144..146
FT /evidence="ECO:0007829|PDB:1HYO"
FT TURN 150..154
FT /evidence="ECO:0007829|PDB:1HYO"
FT STRAND 158..160
FT /evidence="ECO:0007829|PDB:1HYO"
FT STRAND 166..168
FT /evidence="ECO:0007829|PDB:1HYO"
FT STRAND 177..180
FT /evidence="ECO:0007829|PDB:1HYO"
FT STRAND 189..192
FT /evidence="ECO:0007829|PDB:1HYO"
FT STRAND 199..206
FT /evidence="ECO:0007829|PDB:1HYO"
FT HELIX 218..221
FT /evidence="ECO:0007829|PDB:1HYO"
FT HELIX 222..224
FT /evidence="ECO:0007829|PDB:1HYO"
FT STRAND 225..232
FT /evidence="ECO:0007829|PDB:1HYO"
FT HELIX 237..243
FT /evidence="ECO:0007829|PDB:1HYO"
FT TURN 245..247
FT /evidence="ECO:0007829|PDB:1HYO"
FT HELIX 251..254
FT /evidence="ECO:0007829|PDB:1HYO"
FT STRAND 257..259
FT /evidence="ECO:0007829|PDB:1HYO"
FT STRAND 263..265
FT /evidence="ECO:0007829|PDB:1HYO"
FT HELIX 266..269
FT /evidence="ECO:0007829|PDB:1HYO"
FT HELIX 270..272
FT /evidence="ECO:0007829|PDB:1HYO"
FT HELIX 285..287
FT /evidence="ECO:0007829|PDB:1HYO"
FT STRAND 298..304
FT /evidence="ECO:0007829|PDB:1HYO"
FT STRAND 312..318
FT /evidence="ECO:0007829|PDB:1HYO"
FT HELIX 319..321
FT /evidence="ECO:0007829|PDB:2HZY"
FT HELIX 326..334
FT /evidence="ECO:0007829|PDB:1HYO"
FT STRAND 345..347
FT /evidence="ECO:0007829|PDB:1HYO"
FT HELIX 356..358
FT /evidence="ECO:0007829|PDB:1HYO"
FT HELIX 362..365
FT /evidence="ECO:0007829|PDB:1HYO"
FT TURN 366..370
FT /evidence="ECO:0007829|PDB:1HYO"
FT STRAND 373..376
FT /evidence="ECO:0007829|PDB:2HZY"
FT STRAND 380..383
FT /evidence="ECO:0007829|PDB:1HYO"
FT STRAND 389..397
FT /evidence="ECO:0007829|PDB:1HYO"
FT STRAND 402..413
FT /evidence="ECO:0007829|PDB:1HYO"
SQ SEQUENCE 419 AA; 46176 MW; 771C247377B59102 CRC64;
MSFIPVAEDS DFPIQNLPYG VFSTQSNPKP RIGVAIGDQI LDLSVIKHLF TGPALSKHQH
VFDETTLNNF MGLGQAAWKE ARASLQNLLS ASQARLRDDK ELRQRAFTSQ ASATMHLPAT
IGDYTDFYSS RQHATNVGIM FRGKENALLP NWLHLPVGYH GRASSIVVSG TPIRRPMGQM
RPDNSKPPVY GACRLLDMEL EMAFFVGPGN RFGEPIPISK AHEHIFGMVL MNDWSARDIQ
QWEYVPLGPF LGKSFGTTIS PWVVPMDALM PFVVPNPKQD PKPLPYLCHS QPYTFDINLS
VSLKGEGMSQ AATICRSNFK HMYWTMLQQL THHSVNGCNL RPGDLLASGT ISGSDPESFG
SMLELSWKGT KAIDVEQGQT RTFLLDGDEV IITGHCQGDG YRVGFGQCAG KVLPALSPA
