ID   ALAT2_HUMAN             Reviewed;         523 AA.
AC   Q8TD30; Q8N9E2;
DT   25-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2002, sequence version 1.
DT   27-MAR-2024, entry version 160.
DE   RecName: Full=Alanine aminotransferase 2;
DE            Short=ALT2;
DE            EC=2.6.1.2;
DE   AltName: Full=Glutamate pyruvate transaminase 2;
DE            Short=GPT 2;
DE   AltName: Full=Glutamic--alanine transaminase 2;
DE   AltName: Full=Glutamic--pyruvic transaminase 2;
GN   Name=GPT2; Synonyms=AAT2, ALT2;
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] (ISOFORM 1), FUNCTION, CATALYTIC ACTIVITY, AND
RP   TISSUE SPECIFICITY.
RC   TISSUE=Adipose tissue;
RX   PubMed=11863375; DOI=10.1006/geno.2002.6722;
RA   Yang R.-Z., Blaileanu G., Hansen B.C., Shuldiner A.R., Gong D.-W.;
RT   "cDNA cloning, genomic structure, chromosomal mapping, and functional
RT   expression of a novel human alanine aminotransferase.";
RL   Genomics 79:445-450(2002).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC   TISSUE=Hippocampus;
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].
RX   PubMed=15616553; DOI=10.1038/nature03187;
RA   Martin J., Han C., Gordon L.A., Terry A., Prabhakar S., She X., Xie G.,
RA   Hellsten U., Chan Y.M., Altherr M., Couronne O., Aerts A., Bajorek E.,
RA   Black S., Blumer H., Branscomb E., Brown N.C., Bruno W.J., Buckingham J.M.,
RA   Callen D.F., Campbell C.S., Campbell M.L., Campbell E.W., Caoile C.,
RA   Challacombe J.F., Chasteen L.A., Chertkov O., Chi H.C., Christensen M.,
RA   Clark L.M., Cohn J.D., Denys M., Detter J.C., Dickson M.,
RA   Dimitrijevic-Bussod M., Escobar J., Fawcett J.J., Flowers D., Fotopulos D.,
RA   Glavina T., Gomez M., Gonzales E., Goodstein D., Goodwin L.A., Grady D.L.,
RA   Grigoriev I., Groza M., Hammon N., Hawkins T., Haydu L., Hildebrand C.E.,
RA   Huang W., Israni S., Jett J., Jewett P.B., Kadner K., Kimball H.,
RA   Kobayashi A., Krawczyk M.-C., Leyba T., Longmire J.L., Lopez F., Lou Y.,
RA   Lowry S., Ludeman T., Manohar C.F., Mark G.A., McMurray K.L., Meincke L.J.,
RA   Morgan J., Moyzis R.K., Mundt M.O., Munk A.C., Nandkeshwar R.D.,
RA   Pitluck S., Pollard M., Predki P., Parson-Quintana B., Ramirez L., Rash S.,
RA   Retterer J., Ricke D.O., Robinson D.L., Rodriguez A., Salamov A.,
RA   Saunders E.H., Scott D., Shough T., Stallings R.L., Stalvey M.,
RA   Sutherland R.D., Tapia R., Tesmer J.G., Thayer N., Thompson L.S., Tice H.,
RA   Torney D.C., Tran-Gyamfi M., Tsai M., Ulanovsky L.E., Ustaszewska A.,
RA   Vo N., White P.S., Williams A.L., Wills P.L., Wu J.-R., Wu K., Yang J.,
RA   DeJong P., Bruce D., Doggett N.A., Deaven L., Schmutz J., Grimwood J.,
RA   Richardson P., Rokhsar D.S., Eichler E.E., Gilna P., Lucas S.M.,
RA   Myers R.M., Rubin E.M., Pennacchio L.A.;
RT   "The sequence and analysis of duplication-rich human chromosome 16.";
RL   Nature 432:988-994(2004).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   TISSUE=Lung;
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   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   [6]
RP   INVOLVEMENT IN NEDSPM, VARIANT NEDSPM ARG-153, AND CHARACTERIZATION OF
RP   VARIANT NEDSPM ARG-153.
RX   PubMed=25758935; DOI=10.1007/s10545-015-9824-x;
RA   Celis K., Shuldiner S., Haverfield E.V., Cappell J., Yang R., Gong D.W.,
RA   Chung W.K.;
RT   "Loss of function mutation in glutamic pyruvate transaminase 2 (GPT2)
RT   causes developmental encephalopathy.";
RL   J. Inherit. Metab. Dis. 38:941-948(2015).
RN   [7]
RP   X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 49-523 IN COMPLEX WITH PYRIDOXAL
RP   PHOSPHATE, AND COFACTOR.
RG   Structural genomics consortium (SGC);
RT   "Human glutamate pyruvate transaminase 2.";
RL   Submitted (AUG-2009) to the PDB data bank.
CC   -!- FUNCTION: Catalyzes the reversible transamination between alanine and
CC       2-oxoglutarate to form pyruvate and glutamate.
CC       {ECO:0000269|PubMed:11863375}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=2-oxoglutarate + L-alanine = L-glutamate + pyruvate;
CC         Xref=Rhea:RHEA:19453, ChEBI:CHEBI:15361, ChEBI:CHEBI:16810,
CC         ChEBI:CHEBI:29985, ChEBI:CHEBI:57972; EC=2.6.1.2;
CC         Evidence={ECO:0000269|PubMed:11863375};
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000269|Ref.7};
CC   -!- PATHWAY: Amino-acid degradation; L-alanine degradation via transaminase
CC       pathway; pyruvate from L-alanine: step 1/1.
CC   -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q8TD30-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q8TD30-2; Sequence=VSP_020008;
CC   -!- TISSUE SPECIFICITY: Expressed at high levels in muscle, adipose tissue,
CC       kidney and brain and at lower levels in the liver and breast.
CC       {ECO:0000269|PubMed:11863375}.
CC   -!- DISEASE: Neurodevelopmental disorder with spastic paraplegia and
CC       microcephaly (NEDSPM) [MIM:616281]: An autosomal recessive syndrome
CC       characterized by severe psychomotor developmental delay, dysarthria,
CC       walking difficulties, moderately to severely impaired intellectual
CC       development, poor or absent speech, and progressive microcephaly.
CC       {ECO:0000269|PubMed:25758935}. Note=The disease is caused by variants
CC       affecting the gene represented in this entry.
CC   -!- SIMILARITY: Belongs to the class-I pyridoxal-phosphate-dependent
CC       aminotransferase family. Alanine aminotransferase subfamily.
CC       {ECO:0000305}.
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DR   EMBL; AY029173; AAK31794.2; -; mRNA.
DR   EMBL; AK094971; BAC04465.1; -; mRNA.
DR   EMBL; AC018845; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BC062555; AAH62555.1; -; mRNA.
DR   CCDS; CCDS10725.1; -. [Q8TD30-1]
DR   CCDS; CCDS45478.1; -. [Q8TD30-2]
DR   RefSeq; NP_001135938.1; NM_001142466.2. [Q8TD30-2]
DR   RefSeq; NP_597700.1; NM_133443.3. [Q8TD30-1]
DR   PDB; 3IHJ; X-ray; 2.30 A; A=49-523.
DR   PDBsum; 3IHJ; -.
DR   AlphaFoldDB; Q8TD30; -.
DR   SMR; Q8TD30; -.
DR   BioGRID; 124217; 37.
DR   IntAct; Q8TD30; 11.
DR   MINT; Q8TD30; -.
DR   STRING; 9606.ENSP00000345282; -.
DR   DrugBank; DB00160; Alanine.
DR   DrugBank; DB00142; Glutamic acid.
DR   DrugBank; DB00780; Phenelzine.
DR   DrugBank; DB00114; Pyridoxal phosphate.
DR   GlyGen; Q8TD30; 1 site, 1 O-linked glycan (1 site).
DR   iPTMnet; Q8TD30; -.
DR   PhosphoSitePlus; Q8TD30; -.
DR   SwissPalm; Q8TD30; -.
DR   BioMuta; GPT2; -.
DR   DMDM; 74730602; -.
DR   EPD; Q8TD30; -.
DR   jPOST; Q8TD30; -.
DR   MassIVE; Q8TD30; -.
DR   MaxQB; Q8TD30; -.
DR   PaxDb; 9606-ENSP00000345282; -.
DR   PeptideAtlas; Q8TD30; -.
DR   ProteomicsDB; 74226; -. [Q8TD30-1]
DR   ProteomicsDB; 74227; -. [Q8TD30-2]
DR   Pumba; Q8TD30; -.
DR   Antibodypedia; 28066; 261 antibodies from 29 providers.
DR   DNASU; 84706; -.
DR   Ensembl; ENST00000340124.9; ENSP00000345282.4; ENSG00000166123.14. [Q8TD30-1]
DR   Ensembl; ENST00000440783.2; ENSP00000413804.2; ENSG00000166123.14. [Q8TD30-2]
DR   GeneID; 84706; -.
DR   KEGG; hsa:84706; -.
DR   MANE-Select; ENST00000340124.9; ENSP00000345282.4; NM_133443.4; NP_597700.1.
DR   UCSC; uc002eel.4; human. [Q8TD30-1]
DR   AGR; HGNC:18062; -.
DR   CTD; 84706; -.
DR   DisGeNET; 84706; -.
DR   GeneCards; GPT2; -.
DR   HGNC; HGNC:18062; GPT2.
DR   HPA; ENSG00000166123; Tissue enhanced (pancreas, skeletal muscle, tongue).
DR   MalaCards; GPT2; -.
DR   MIM; 138210; gene.
DR   MIM; 616281; phenotype.
DR   neXtProt; NX_Q8TD30; -.
DR   OpenTargets; ENSG00000166123; -.
DR   Orphanet; 477673; Postnatal microcephaly-infantile hypotonia-spastic diplegia-dysarthria-intellectual disability syndrome.
DR   PharmGKB; PA28948; -.
DR   VEuPathDB; HostDB:ENSG00000166123; -.
DR   eggNOG; KOG0258; Eukaryota.
DR   GeneTree; ENSGT00940000159061; -.
DR   HOGENOM; CLU_014254_3_1_1; -.
DR   InParanoid; Q8TD30; -.
DR   OMA; KARETSC; -.
DR   OrthoDB; 5472891at2759; -.
DR   PhylomeDB; Q8TD30; -.
DR   TreeFam; TF300839; -.
DR   BioCyc; MetaCyc:HS09332-MONOMER; -.
DR   PathwayCommons; Q8TD30; -.
DR   Reactome; R-HSA-8964540; Alanine metabolism. [Q8TD30-1]
DR   SignaLink; Q8TD30; -.
DR   SIGNOR; Q8TD30; -.
DR   UniPathway; UPA00528; UER00586.
DR   BioGRID-ORCS; 84706; 14 hits in 1080 CRISPR screens.
DR   ChiTaRS; GPT2; human.
DR   EvolutionaryTrace; Q8TD30; -.
DR   GenomeRNAi; 84706; -.
DR   Pharos; Q8TD30; Tbio.
DR   PRO; PR:Q8TD30; -.
DR   Proteomes; UP000005640; Chromosome 16.
DR   RNAct; Q8TD30; Protein.
DR   Bgee; ENSG00000166123; Expressed in lower esophagus mucosa and 170 other cell types or tissues.
DR   ExpressionAtlas; Q8TD30; baseline and differential.
DR   GO; GO:0005759; C:mitochondrial matrix; TAS:Reactome.
DR   GO; GO:0004021; F:L-alanine:2-oxoglutarate aminotransferase activity; IDA:UniProtKB.
DR   GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR   GO; GO:0006103; P:2-oxoglutarate metabolic process; IDA:UniProtKB.
DR   GO; GO:0009058; P:biosynthetic process; IEA:InterPro.
DR   GO; GO:0042853; P:L-alanine catabolic process; IEA:UniProtKB-UniPathway.
DR   GO; GO:0042851; P:L-alanine metabolic process; IDA:UniProtKB.
DR   CDD; cd00609; AAT_like; 1.
DR   Gene3D; 1.10.287.1970; -; 1.
DR   Gene3D; 3.90.1150.10; Aspartate Aminotransferase, domain 1; 1.
DR   Gene3D; 3.40.640.10; Type I PLP-dependent aspartate aminotransferase-like (Major domain); 1.
DR   InterPro; IPR045088; ALAT1/2-like.
DR   InterPro; IPR004839; Aminotransferase_I/II.
DR   InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR   InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR   InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR   PANTHER; PTHR11751; ALANINE AMINOTRANSFERASE; 1.
DR   PANTHER; PTHR11751:SF311; ALANINE AMINOTRANSFERASE 2; 1.
DR   Pfam; PF00155; Aminotran_1_2; 1.
DR   SUPFAM; SSF53383; PLP-dependent transferases; 1.
DR   Genevisible; Q8TD30; HS.
PE   1: Evidence at protein level;
KW   3D-structure; Acetylation; Alternative splicing; Aminotransferase;
KW   Disease variant; Intellectual disability; Pyridoxal phosphate;
KW   Reference proteome; Transferase.
FT   CHAIN           1..523
FT                   /note="Alanine aminotransferase 2"
FT                   /id="PRO_0000247532"
FT   REGION          1..25
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         341
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT   MOD_RES         415
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:Q8BGT5"
FT   MOD_RES         505
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:Q8BGT5"
FT   MOD_RES         512
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:Q8BGT5"
FT   VAR_SEQ         1..100
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:14702039"
FT                   /id="VSP_020008"
FT   VARIANT         153
FT                   /note="S -> R (in NEDSPM; loss of function mutation;
FT                   dbSNP:rs786203999)"
FT                   /evidence="ECO:0000269|PubMed:25758935"
FT                   /id="VAR_073379"
FT   CONFLICT        284
FT                   /note="D -> G (in Ref. 4; BAC04465)"
FT                   /evidence="ECO:0000305"
FT   STRAND          49..52
FT                   /evidence="ECO:0007829|PDB:3IHJ"
FT   TURN            53..56
FT                   /evidence="ECO:0007829|PDB:3IHJ"
FT   STRAND          57..64
FT                   /evidence="ECO:0007829|PDB:3IHJ"
FT   HELIX           67..80
FT                   /evidence="ECO:0007829|PDB:3IHJ"
FT   STRAND          86..89
FT                   /evidence="ECO:0007829|PDB:3IHJ"
FT   HELIX           107..117
FT                   /evidence="ECO:0007829|PDB:3IHJ"
FT   HELIX           119..123
FT                   /evidence="ECO:0007829|PDB:3IHJ"
FT   STRAND          125..127
FT                   /evidence="ECO:0007829|PDB:3IHJ"
FT   HELIX           129..141
FT                   /evidence="ECO:0007829|PDB:3IHJ"
FT   HELIX           157..170
FT                   /evidence="ECO:0007829|PDB:3IHJ"
FT   TURN            171..173
FT                   /evidence="ECO:0007829|PDB:3IHJ"
FT   HELIX           178..180
FT                   /evidence="ECO:0007829|PDB:3IHJ"
FT   STRAND          181..186
FT                   /evidence="ECO:0007829|PDB:3IHJ"
FT   HELIX           187..198
FT                   /evidence="ECO:0007829|PDB:3IHJ"
FT   HELIX           203..205
FT                   /evidence="ECO:0007829|PDB:3IHJ"
FT   STRAND          206..214
FT                   /evidence="ECO:0007829|PDB:3IHJ"
FT   HELIX           218..225
FT                   /evidence="ECO:0007829|PDB:3IHJ"
FT   STRAND          229..234
FT                   /evidence="ECO:0007829|PDB:3IHJ"
FT   HELIX           237..239
FT                   /evidence="ECO:0007829|PDB:3IHJ"
FT   HELIX           245..255
FT                   /evidence="ECO:0007829|PDB:3IHJ"
FT   TURN            256..258
FT                   /evidence="ECO:0007829|PDB:3IHJ"
FT   STRAND          259..269
FT                   /evidence="ECO:0007829|PDB:3IHJ"
FT   TURN            271..273
FT                   /evidence="ECO:0007829|PDB:3IHJ"
FT   HELIX           279..292
FT                   /evidence="ECO:0007829|PDB:3IHJ"
FT   STRAND          295..299
FT                   /evidence="ECO:0007829|PDB:3IHJ"
FT   TURN            301..304
FT                   /evidence="ECO:0007829|PDB:3IHJ"
FT   HELIX           316..322
FT                   /evidence="ECO:0007829|PDB:3IHJ"
FT   HELIX           325..328
FT                   /evidence="ECO:0007829|PDB:3IHJ"
FT   STRAND          333..342
FT                   /evidence="ECO:0007829|PDB:3IHJ"
FT   STRAND          347..349
FT                   /evidence="ECO:0007829|PDB:3IHJ"
FT   STRAND          352..358
FT                   /evidence="ECO:0007829|PDB:3IHJ"
FT   HELIX           361..373
FT                   /evidence="ECO:0007829|PDB:3IHJ"
FT   HELIX           379..388
FT                   /evidence="ECO:0007829|PDB:3IHJ"
FT   HELIX           399..425
FT                   /evidence="ECO:0007829|PDB:3IHJ"
FT   STRAND          437..441
FT                   /evidence="ECO:0007829|PDB:3IHJ"
FT   HELIX           449..457
FT                   /evidence="ECO:0007829|PDB:3IHJ"
FT   HELIX           462..474
FT                   /evidence="ECO:0007829|PDB:3IHJ"
FT   HELIX           481..483
FT                   /evidence="ECO:0007829|PDB:3IHJ"
FT   STRAND          492..496
FT                   /evidence="ECO:0007829|PDB:3IHJ"
FT   HELIX           501..521
FT                   /evidence="ECO:0007829|PDB:3IHJ"
SQ   SEQUENCE   523 AA;  57904 MW;  4DD87814C62C7DEA CRC64;
     MQRAAALVRR GCGPRTPSSW GRSQSSAAAE ASAVLKVRPE RSRRERILTL ESMNPQVKAV
     EYAVRGPIVL KAGEIELELQ RGIKKPFTEV IRANIGDAQA MGQQPITFLR QVMALCTYPN
     LLDSPSFPED AKKRARRILQ ACGGNSLGSY SASQGVNCIR EDVAAYITRR DGGVPADPDN
     IYLTTGASDG ISTILKILVS GGGKSRTGVM IPIPQYPLYS AVISELDAIQ VNYYLDEENC
     WALNVNELRR AVQEAKDHCD PKVLCIINPG NPTGQVQSRK CIEDVIHFAW EEKLFLLADE
     VYQDNVYSPD CRFHSFKKVL YEMGPEYSSN VELASFHSTS KGYMGECGYR GGYMEVINLH
     PEIKGQLVKL LSVRLCPPVS GQAAMDIVVN PPVAGEESFE QFSREKESVL GNLAKKAKLT
     EDLFNQVPGI HCNPLQGAMY AFPRIFIPAK AVEAAQAHQM APDMFYCMKL LEETGICVVP
     GSGFGQREGT YHFRMTILPP VEKLKTVLQK VKDFHINFLE KYA
//