ID OAT_HUMAN Reviewed; 439 AA. AC P04181; D3DRF0; Q16068; Q16069; Q68CS0; Q6IAV9; Q9UD03; DT 20-MAR-1987, integrated into UniProtKB/Swiss-Prot. DT 20-MAR-1987, sequence version 1. DT 04-NOV-2026, entry version 254. DE RecName: Full=Ornithine aminotransferase, mitochondrial; DE EC=2.6.1.13 {ECO:0000269|PubMed:1737786, ECO:0000269|PubMed:23076989}; DE AltName: Full=Ornithine delta-aminotransferase; DE AltName: Full=Ornithine--oxo-acid aminotransferase; DE Contains: DE RecName: Full=Ornithine aminotransferase, hepatic form; DE Contains: DE RecName: Full=Ornithine aminotransferase, renal form; DE Flags: Precursor; GN Name=OAT; 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). RX PubMed=3456579; DOI=10.1073/pnas.83.5.1203; RA Inana G., Totsuka S., Redmond M., Dougherty T., Nagle J., Shiono T., RA Ohura T., Kominami E., Katunuma N.; RT "Molecular cloning of human ornithine aminotransferase mRNA."; RL Proc. Natl. Acad. Sci. U.S.A. 83:1203-1207(1986). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). RC TISSUE=Liver; RX PubMed=3816496; DOI=10.1089/dna.1.1986.5.493; RA Ramesh V., Shaffer M.M., Allaire J.M., Shih V.E., Gusella J.F.; RT "Investigation of gyrate atrophy using a cDNA clone for human ornithine RT aminotransferase."; RL DNA 5:493-501(1986). RN [3] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), PROTEIN SEQUENCE OF 36-40, AND RP PROTEOLYTIC PROCESSING. RC TISSUE=Kidney; RX PubMed=2507357; DOI=10.1016/0014-5793(89)81110-x; RA Kobayashi T., Nishii M., Takagi Y., Titani T., Matsuzawa T.; RT "Molecular cloning and nucleotide sequence analysis of mRNA for human RT kidney ornithine aminotransferase. An examination of ornithine RT aminotransferase isozymes between liver and kidney."; RL FEBS Lett. 255:300-304(1989). RN [4] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORM 1). RX PubMed=3170546; DOI=10.1016/s0021-9258(18)68219-5; RA Mitchell G.A., Looney J.E., Brody L.C., Steel G., Suchanek M., RA Engelhardt J.F., Willard H.F., Valle D.; RT "Human ornithine-delta-aminotransferase. cDNA cloning and analysis of the RT structural gene."; RL J. Biol. Chem. 263:14288-14295(1988). RN [5] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC TISSUE=Placenta; RX PubMed=2373169; DOI=10.1016/0014-4835(90)90126-f; RA Zintz C.B., Inana G.; RT "Analysis of the human ornithine aminotransferase gene family."; RL Exp. Eye Res. 50:759-770(1990). RN [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2). RC TISSUE=Brain, Brain cortex, and Subthalamic nucleus; 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 [7] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RA Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.; RT "Cloning of human full open reading frames in Gateway(TM) system entry RT vector (pDONR201)."; RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases. RN [8] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2). RC TISSUE=Brain cortex; RX PubMed=17974005; DOI=10.1186/1471-2164-8-399; RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U., RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D., RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A., RA Wiemann S., Schupp I.; RT "The full-ORF clone resource of the German cDNA consortium."; RL BMC Genomics 8:399-399(2007). RN [9] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=15164054; DOI=10.1038/nature02462; RA Deloukas P., Earthrowl M.E., Grafham D.V., Rubenfield M., French L., RA Steward C.A., Sims S.K., Jones M.C., Searle S., Scott C., Howe K., RA Hunt S.E., Andrews T.D., Gilbert J.G.R., Swarbreck D., Ashurst J.L., RA Taylor A., Battles J., Bird C.P., Ainscough R., Almeida J.P., RA Ashwell R.I.S., Ambrose K.D., Babbage A.K., Bagguley C.L., Bailey J., RA Banerjee R., Bates K., Beasley H., Bray-Allen S., Brown A.J., Brown J.Y., RA Burford D.C., Burrill W., Burton J., Cahill P., Camire D., Carter N.P., RA Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S., Corby N., RA Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L., Frankish A., RA Frankland J.A., Garner P., Garnett J., Gribble S., Griffiths C., RA Grocock R., Gustafson E., Hammond S., Harley J.L., Hart E., Heath P.D., RA Ho T.P., Hopkins B., Horne J., Howden P.J., Huckle E., Hynds C., RA Johnson C., Johnson D., Kana A., Kay M., Kimberley A.M., Kershaw J.K., RA Kokkinaki M., Laird G.K., Lawlor S., Lee H.M., Leongamornlert D.A., RA Laird G., Lloyd C., Lloyd D.M., Loveland J., Lovell J., McLaren S., RA McLay K.E., McMurray A., Mashreghi-Mohammadi M., Matthews L., Milne S., RA Nickerson T., Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V., RA Peck A.I., Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A., RA Ross M.T., Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M., RA Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W., Tracey A., RA Tromans A., Tsolas J., Wall M., Walsh J., Wang H., Weinstock K., West A.P., RA Willey D.L., Whitehead S.L., Wilming L., Wray P.W., Young L., Chen Y., RA Lovering R.C., Moschonas N.K., Siebert R., Fechtel K., Bentley D., RA Durbin R.M., Hubbard T., Doucette-Stamm L., Beck S., Smith D.R., Rogers J.; RT "The DNA sequence and comparative analysis of human chromosome 10."; RL Nature 429:375-381(2004). RN [10] 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 [11] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RC TISSUE=Placenta, and Uterus; 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 [12] RP NUCLEOTIDE SEQUENCE [MRNA] OF 50-58 AND 328-336 (ISOFORM 1). RX PubMed=1682785; RA Ramesh V., Gusella J.F., Shih V.E.; RT "Molecular pathology of gyrate atrophy of the choroid and retina due to RT ornithine aminotransferase deficiency."; RL Mol. Biol. Med. 8:81-93(1991). RN [13] RP PARTIAL PROTEIN SEQUENCE, PYRIDOXAL PHOSPHATE AT LYS-292, AND PROTEOLYTIC RP PROCESSING. RX PubMed=3754226; DOI=10.1016/0014-5793(86)81219-4; RA Simmaco M., John R.A., Barra D., Bossa F.; RT "The primary structure of ornithine aminotransferase. Identification of RT active-site sequence and site of post-translational proteolysis."; RL FEBS Lett. 199:39-42(1986). RN [14] 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 [15] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Liver; RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014; RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., RA Ye M., Zou H.; RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver RT phosphoproteome."; RL J. Proteomics 96:253-262(2014). RN [16] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=25944712; DOI=10.1002/pmic.201400617; RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D., RA Lane L., Bairoch A., Van Dorsselaer A., Carapito C.; RT "N-terminome analysis of the human mitochondrial proteome."; RL Proteomics 15:2519-2524(2015). RN [17] RP X-RAY CRYSTALLOGRAPHY. RX PubMed=9309222; DOI=10.1016/s0969-2126(97)00258-x; RA Shah S.A., Shen B.W., Brunger A.T.; RT "Human ornithine aminotransferase complexed with L-canaline and gabaculine: RT structural basis for substrate recognition."; RL Structure 5:1067-1075(1997). RN [18] RP X-RAY CRYSTALLOGRAPHY, AND COFACTOR. RX PubMed=9514741; DOI=10.1006/jmbi.1997.1583; RA Shen B.W., Hennig M., Hohenester E., Jansonius J.N., Schirmer T.; RT "Crystal structure of human recombinant ornithine aminotransferase."; RL J. Mol. Biol. 277:81-102(1998). RN [19] RP X-RAY CRYSTALLOGRAPHY. RX PubMed=9878407; DOI=10.1006/jmbi.1998.2289; RA Storici P., Capitani G., Mueller R., Schirmer T., Jansonius J.N.; RT "Crystal structure of human ornithine aminotransferase complexed with the RT highly specific and potent inhibitor 5-fluoromethylornithine."; RL J. Mol. Biol. 285:297-309(1999). RN [20] RP VARIANTS GACR LYS-54 AND MET-332. RX PubMed=3375240; DOI=10.1073/pnas.85.11.3777; RA Ramesh V., McClatchey A.I., Ramesh N., Benoit L.A., Berson E.L., Shih V.E., RA Gusella J.F.; RT "Molecular basis of ornithine aminotransferase deficiency in B-6-responsive RT and -nonresponsive forms of gyrate atrophy."; RL Proc. Natl. Acad. Sci. U.S.A. 85:3777-3780(1988). RN [21] RP VARIANT GACR TYR-319. RX PubMed=2793865; DOI=10.1016/s0021-9258(18)71513-5; RA Inana G., Chambers C., Hotta Y., Inouye L., Filpula D., Pulford S., RA Shiono T.; RT "Point mutation affecting processing of the ornithine aminotransferase RT precursor protein in gyrate atrophy."; RL J. Biol. Chem. 264:17432-17436(1989). RN [22] RP VARIANTS GACR THR-180; LEU-241; PRO-250; ASP-353 AND ARG-394. RX PubMed=1612597; DOI=10.1016/0888-7543(92)90258-t; RA Michaud J., Brody L.C., Steel G., Fontaine G., Martin L.S., Valle D., RA Mitchell G.; RT "Strand-separating conformational polymorphism analysis: efficacy of RT detection of point mutations in the human ornithine delta-aminotransferase RT gene."; RL Genomics 13:389-394(1992). RN [23] RP VARIANTS GACR HIS-55; LYS-89; PHE-93; LEU-154; THR-180; ALA-184 DEL; RP LEU-241; CYS-245; PRO-250; ILE-267; PRO-270; LYS-271; ASP-353; ALA-375; RP ARG-394; PRO-402 AND LEU-417, VARIANT PHE-437, CHARACTERIZATION OF VARIANTS RP GACR HIS-55; LYS-89; PHE-93; LEU-154; THR-180; ALA-184 DEL; LEU-241; RP CYS-245; PRO-250; ILE-267; PRO-270; LYS-271; ASP-353; ALA-375; ARG-394; RP PRO-402 AND LEU-417, FUNCTION, CATALYTIC ACTIVITY, AND PATHWAY. RX PubMed=1737786; DOI=10.1016/s0021-9258(19)50731-1; RA Brody L.C., Mitchell G.A., Obie C., Michaud J., Steel G., Fontaine G., RA Robert M.-F., Sipila I., Kaiser-Kupfer M., Valle D.; RT "Ornithine delta-aminotransferase mutations in gyrate atrophy. Allelic RT heterogeneity and functional consequences."; RL J. Biol. Chem. 267:3302-3307(1992). RN [24] RP VARIANT GACR VAL-226. RX PubMed=7887415; RA Michaud J., Thompson G.N., Brody L.C., Steel G., Obie C., Fontaine G., RA Schappert K., Keith C.G., Valle D., Mitchell G.A.; RT "Pyridoxine-responsive gyrate atrophy of the choroid and retina: clinical RT and biochemical correlates of the mutation A226V."; RL Am. J. Hum. Genet. 56:616-622(1995). RN [25] RP VARIANT GACR GLU-90. RX PubMed=7668253; RA Kobayashi T., Ogawa H., Kasahara M., Shiozawa Z., Matsuzawa T.; RT "A single amino acid substitution within the mature sequence of ornithine RT aminotransferase obstructs mitochondrial entry of the precursor."; RL Am. J. Hum. Genet. 57:284-291(1995). RN [26] RP VARIANTS GACR ASP-51; ARG-104; GLN-199; LYS-318; MET-332; TYR-394; LEU-417; RP ASN-436 AND PHE-437, CHARACTERIZATION OF ASP-51; ARG-104; GLN-199; VAL-226; RP LYS-318; MET-332; TYR-394; LEU-402; LEU-417; ASN-436 AND PHE-437, FUNCTION, RP CATALYTIC ACTIVITY, PATHWAY, SUBUNIT, AND SUBCELLULAR LOCATION. RX PubMed=23076989; DOI=10.1002/humu.22233; RA Doimo M., Desbats M.A., Baldoin M.C., Lenzini E., Basso G., Murphy E., RA Graziano C., Seri M., Burlina A., Sartori G., Trevisson E., Salviati L.; RT "Functional analysis of missense mutations of OAT, causing gyrate atrophy RT of choroid and retina."; RL Hum. Mutat. 34:229-236(2013). CC -!- FUNCTION: Catalyzes the reversible interconversion of L-ornithine and CC 2-oxoglutarate to L-glutamate semialdehyde and L-glutamate. CC {ECO:0000269|PubMed:1737786, ECO:0000269|PubMed:23076989}. CC -!- CATALYTIC ACTIVITY: CC Reaction=L-ornithine + 2-oxoglutarate = L-glutamate 5-semialdehyde + L- CC glutamate; Xref=Rhea:RHEA:25160, ChEBI:CHEBI:16810, CC ChEBI:CHEBI:29985, ChEBI:CHEBI:46911, ChEBI:CHEBI:58066; EC=2.6.1.13; CC Evidence={ECO:0000269|PubMed:1737786, ECO:0000269|PubMed:23076989}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:25161; CC Evidence={ECO:0000305|PubMed:1737786}; CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:25162; CC Evidence={ECO:0000305|PubMed:1737786}; CC -!- COFACTOR: CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326; CC Evidence={ECO:0000269|PubMed:9514741}; CC -!- PATHWAY: Amino-acid biosynthesis; L-proline biosynthesis; L-glutamate CC 5-semialdehyde from L-ornithine: step 1/1. {ECO:0000305|PubMed:1737786, CC ECO:0000305|PubMed:23076989}. CC -!- SUBUNIT: Homohexamer. {ECO:0000269|PubMed:23076989}. CC -!- INTERACTION: CC P04181; P05067: APP; NbExp=3; IntAct=EBI-721662, EBI-77613; CC -!- SUBCELLULAR LOCATION: Mitochondrion matrix CC {ECO:0000269|PubMed:23076989}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=1; CC IsoId=P04181-1; Sequence=Displayed; CC Name=2; CC IsoId=P04181-2; Sequence=VSP_043085; CC -!- DISEASE: Gyrate atrophy of choroid and retina (GACR) [MIM:258870]: An CC autosomal recessive disorder clinically characterized by a triad of CC progressive chorioretinal degeneration, early cataract formation, and CC type II muscle fiber atrophy. Characteristic chorioretinal atrophy with CC progressive constriction of the visual fields leads to blindness at the CC latest during the sixth decade of life. Patients generally have normal CC intelligence. {ECO:0000269|PubMed:1612597, ECO:0000269|PubMed:1737786, CC ECO:0000269|PubMed:23076989, ECO:0000269|PubMed:2793865, CC ECO:0000269|PubMed:3375240, ECO:0000269|PubMed:7668253, CC ECO:0000269|PubMed:7887415}. Note=The disease is caused by variants CC affecting the gene represented in this entry. CC -!- SIMILARITY: Belongs to the class-III pyridoxal-phosphate-dependent CC aminotransferase family. {ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; M12267; AAA59956.1; -; mRNA. DR EMBL; M14963; AAA59959.1; -; mRNA. DR EMBL; Y07511; CAA68809.1; -; mRNA. DR EMBL; M23204; AAA36386.1; -; mRNA. DR EMBL; M23205; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; M88760; AAA59958.1; ALT_SEQ; Genomic_DNA. DR EMBL; M29927; AAA59957.1; -; Genomic_DNA. DR EMBL; M29919; AAA59957.1; JOINED; Genomic_DNA. DR EMBL; M29920; AAA59957.1; JOINED; Genomic_DNA. DR EMBL; M29921; AAA59957.1; JOINED; Genomic_DNA. DR EMBL; M29922; AAA59957.1; JOINED; Genomic_DNA. DR EMBL; M29923; AAA59957.1; JOINED; Genomic_DNA. DR EMBL; M29924; AAA59957.1; JOINED; Genomic_DNA. DR EMBL; M29925; AAA59957.1; JOINED; Genomic_DNA. DR EMBL; M29926; AAA59957.1; JOINED; Genomic_DNA. DR EMBL; AK296032; BAH12241.1; -; mRNA. DR EMBL; AK312561; BAG35458.1; -; mRNA. DR EMBL; AK315947; BAH14318.1; -; mRNA. DR EMBL; CR457045; CAG33326.1; -; mRNA. DR EMBL; CR749808; CAH18668.1; -; mRNA. DR EMBL; AL445237; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CH471066; EAW49271.1; -; Genomic_DNA. DR EMBL; CH471066; EAW49272.1; -; Genomic_DNA. DR EMBL; BC000964; AAH00964.1; -; mRNA. DR EMBL; BC016928; AAH16928.1; -; mRNA. DR EMBL; S66418; AAB20298.1; -; mRNA. DR EMBL; S66421; AAB20297.1; -; mRNA. DR CCDS; CCDS53586.1; -. [P04181-2] DR CCDS; CCDS7639.1; -. [P04181-1] DR PIR; A30806; XNHUO. DR PIR; I55360; I55360. DR RefSeq; NP_000265.1; NM_000274.4. [P04181-1] DR RefSeq; NP_001165285.1; NM_001171814.2. [P04181-2] DR RefSeq; NP_001309894.1; NM_001322965.2. [P04181-1] DR RefSeq; NP_001309895.1; NM_001322966.2. [P04181-1] DR RefSeq; NP_001309896.1; NM_001322967.2. [P04181-1] DR RefSeq; NP_001309897.1; NM_001322968.2. [P04181-1] DR RefSeq; NP_001309898.1; NM_001322969.2. [P04181-1] DR RefSeq; NP_001309899.1; NM_001322970.2. [P04181-1] DR RefSeq; NP_001309900.1; NM_001322971.2. DR PDB; 10LW; X-ray; 1.93 A; A/B/C=1-439. DR PDB; 10LX; X-ray; 1.83 A; A/B/C=1-439. DR PDB; 1GBN; X-ray; 2.30 A; A/B/C=38-439. DR PDB; 1OAT; X-ray; 2.50 A; A/B/C=1-439. DR PDB; 2BYJ; X-ray; 3.02 A; A/B/C=1-439. DR PDB; 2BYL; X-ray; 2.15 A; A/B/C=1-439. DR PDB; 2CAN; X-ray; 2.30 A; A/B/C=38-439. DR PDB; 2OAT; X-ray; 1.95 A; A/B/C=1-439. DR PDB; 5VWO; X-ray; 1.77 A; A/B/C=36-439. DR PDB; 6HX7; X-ray; 1.80 A; A/B/C=26-439. DR PDB; 6OIA; X-ray; 1.78 A; A/B/C=36-439. DR PDB; 6V8C; X-ray; 1.90 A; A/B/C=36-439. DR PDB; 6V8D; X-ray; 2.25 A; A/B/C=36-439. DR PDB; 7JX9; X-ray; 1.96 A; A/B/C=36-439. DR PDB; 7LK0; X-ray; 1.96 A; A/B/C=36-439. DR PDB; 7LK1; X-ray; 1.79 A; A/B/C=36-439. DR PDB; 7LNM; X-ray; 2.00 A; B/C/E/F/I/J=36-439. DR PDB; 7LOM; X-ray; 2.10 A; A/B/C=36-439. DR PDB; 7LON; X-ray; 1.95 A; A/B/C=36-439. DR PDB; 7T9Z; X-ray; 2.15 A; A/B/C=1-439. DR PDB; 7TA0; X-ray; 2.33 A; A/B/C=1-439. DR PDB; 7TA1; X-ray; 2.20 A; A/B/C/D/E/F=1-439. DR PDB; 7TED; X-ray; 2.63 A; A/B/C/D/E/F/G/H/I=36-439. DR PDB; 7TEV; X-ray; 1.91 A; A/B/C=36-439. DR PDB; 7TFP; X-ray; 2.71 A; A/B/C=36-439. DR PDB; 8EZ1; X-ray; 1.91 A; A/B/C=36-439. DR PDB; 8V9M; X-ray; 1.61 A; A/B/C=36-439. DR AlphaFoldDB; P04181; -. DR SMR; P04181; -. DR BioGRID; 110996; 245. DR FunCoup; P04181; 2045. DR IntAct; P04181; 78. DR NDEx; IQUERY-CP-OAT; 6 NDEx IQuery Curated Pathways. DR STRING; 9606.ENSP00000357838; -. DR BindingDB; P04181; -. DR ChEMBL; CHEMBL5954; -. DR DrugBank; DB02821; Canaline. DR DrugBank; DB02054; Gabaculine. DR DrugBank; DB00129; Ornithine. DR DrugBank; DB00114; Pyridoxal phosphate. DR CarbonylDB; P04181; -. DR GlyCosmos; P04181; 2 sites, 1 glycan. DR GlyGen; P04181; 2 sites, 1 O-linked glycan (2 sites). DR iPTMnet; P04181; -. DR MetOSite; P04181; -. DR PhosphoSitePlus; P04181; -. DR SwissPalm; P04181; -. DR BioMuta; OAT; -. DR DMDM; 129018; -. DR REPRODUCTION-2DPAGE; IPI00022334; -. DR jPOST; P04181; -. DR MassIVE; P04181; -. DR PaxDb; 9606-ENSP00000357838; -. DR PeptideAtlas; P04181; -. DR ProteomicsDB; 51672; -. [P04181-1] DR ProteomicsDB; 51673; -. [P04181-2] DR Pumba; P04181; -. DR Antibodypedia; 32371; 296 antibodies from 34 providers. DR DNASU; 4942; -. DR Ensembl; ENST00000368845.6; ENSP00000357838.5; ENSG00000065154.13. [P04181-1] DR Ensembl; ENST00000539214.5; ENSP00000439042.1; ENSG00000065154.13. [P04181-2] DR Ensembl; ENST00000858831.1; ENSP00000528890.1; ENSG00000065154.13. [P04181-1] DR Ensembl; ENST00000858833.1; ENSP00000528892.1; ENSG00000065154.13. [P04181-1] DR Ensembl; ENST00000858834.1; ENSP00000528893.1; ENSG00000065154.13. [P04181-1] DR Ensembl; ENST00000858835.1; ENSP00000528894.1; ENSG00000065154.13. [P04181-1] DR Ensembl; ENST00000858836.1; ENSP00000528895.1; ENSG00000065154.13. [P04181-1] DR Ensembl; ENST00000858838.1; ENSP00000528897.1; ENSG00000065154.13. [P04181-1] DR Ensembl; ENST00000858839.1; ENSP00000528898.1; ENSG00000065154.13. [P04181-1] DR Ensembl; ENST00000858840.1; ENSP00000528899.1; ENSG00000065154.13. [P04181-1] DR Ensembl; ENST00000921311.1; ENSP00000591370.1; ENSG00000065154.13. [P04181-1] DR Ensembl; ENST00000921312.1; ENSP00000591371.1; ENSG00000065154.13. [P04181-1] DR Ensembl; ENST00000921315.1; ENSP00000591374.1; ENSG00000065154.13. [P04181-1] DR Ensembl; ENST00000921319.1; ENSP00000591378.1; ENSG00000065154.13. [P04181-1] DR Ensembl; ENST00000971961.1; ENSP00000642019.1; ENSG00000065154.13. [P04181-1] DR Ensembl; ENST00000971962.1; ENSP00000642021.1; ENSG00000065154.13. [P04181-1] DR Ensembl; ENST00000971963.1; ENSP00000642022.1; ENSG00000065154.13. [P04181-1] DR GeneID; 4942; -. DR KEGG; hsa:4942; -. DR MANE-Select; ENST00000368845.6; ENSP00000357838.5; NM_000274.4; NP_000265.1. DR UCSC; uc001lhp.4; human. [P04181-1] DR AGR; HGNC:8091; -. DR ClinPGx; PA31880; -. DR CTD; 4942; -. DR DisGeNET; 4942; -. DR GeneCards; OAT; -. DR HGNC; HGNC:8091; OAT. DR HPA; ENSG00000065154; Tissue enhanced (intestine). DR MalaCards; OAT; -. DR MIM; 258870; phenotype. DR MIM; 613349; gene. DR OpenTargets; ENSG00000065154; -. DR Orphanet; 414; Gyrate atrophy of choroid and retina. DR VEuPathDB; HostDB:ENSG00000065154; -. DR eggNOG; KOG1402; Eukaryota. DR GeneTree; ENSGT00630000089895; -. DR HOGENOM; CLU_016922_10_3_1; -. DR InParanoid; P04181; -. DR OMA; AADCGNH; -. DR OrthoDB; 425114at2759; -. DR PAN-GO; P04181; 6 GO annotations based on evolutionary models. DR PhylomeDB; P04181; -. DR BioCyc; MetaCyc:HS00832-MONOMER; -. DR BRENDA; 2.6.1.13; 2681. DR PathwayCommons; P04181; -. DR Reactome; R-HSA-8964539; Glutamate and glutamine metabolism. DR SABIO-RK; P04181; -. DR SignaLink; P04181; -. DR SIGNOR; P04181; -. DR UniPathway; UPA00098; UER00358. DR Agora; ENSG00000065154; -. DR BioGRID-ORCS; 4942; 11 hits in 1165 CRISPR screens. DR CD-CODE; 91857CE7; Nucleolus. DR ChiTaRS; OAT; human. DR EvolutionaryTrace; P04181; -. DR GenomeRNAi; 4942; -. DR Pharos; P04181; Tchem. DR PRO; PR:P04181; -. DR Proteomes; UP000005640; Chromosome 10. DR RNAct; P04181; protein. DR Bgee; ENSG00000065154; Expressed in jejunal mucosa and 208 other cell types or tissues. DR ExpressionAtlas; P04181; baseline and differential. DR GO; GO:0005759; C:mitochondrial matrix; IDA:UniProtKB. DR GO; GO:0005739; C:mitochondrion; IDA:HPA. DR GO; GO:0042802; F:identical protein binding; IPI:UniProtKB. DR GO; GO:0004587; F:L-ornithine transaminase activity; IMP:UniProtKB. DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro. DR GO; GO:0006527; P:L-arginine catabolic process; IBA:GO_Central. DR GO; GO:0055129; P:L-proline biosynthetic process; IEA:UniProtKB-UniPathway. DR GO; GO:0007601; P:visual perception; TAS:ProtInc. DR CDD; cd00610; OAT_like; 1. DR FunFam; 3.40.640.10:FF:000011; Ornithine aminotransferase; 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; IPR005814; Aminotrans_3. DR InterPro; IPR049704; Aminotrans_3_PPA_site. DR InterPro; IPR050103; Class-III_PLP-dep_AT. DR InterPro; IPR010164; Orn_aminotrans. DR InterPro; IPR015424; PyrdxlP-dep_Trfase. DR InterPro; IPR015421; PyrdxlP-dep_Trfase_major. DR InterPro; IPR015422; PyrdxlP-dep_Trfase_small. DR NCBIfam; TIGR01885; Orn_aminotrans; 1. DR PANTHER; PTHR11986; AMINOTRANSFERASE CLASS III; 1. DR PANTHER; PTHR11986:SF18; ORNITHINE AMINOTRANSFERASE, MITOCHONDRIAL; 1. DR Pfam; PF00202; Aminotran_3; 1. DR PIRSF; PIRSF000521; Transaminase_4ab_Lys_Orn; 1. DR SUPFAM; SSF53383; PLP-dependent transferases; 1. DR PROSITE; PS00600; AA_TRANSFER_CLASS_3; 1. PE 1: Evidence at protein level; KW 3D-structure; Acetylation; Alternative splicing; Aminotransferase; KW Direct protein sequencing; Disease variant; Mitochondrion; KW Proteomics identification; Pyridoxal phosphate; Reference proteome; KW Transferase; Transit peptide. FT TRANSIT 1..35 FT /note="Mitochondrion; in renal form" FT /evidence="ECO:0000269|PubMed:2507357" FT TRANSIT 1..25 FT /note="Mitochondrion; in hepatic form" FT CHAIN 26..439 FT /note="Ornithine aminotransferase, hepatic form" FT /id="PRO_0000001262" FT CHAIN 36..439 FT /note="Ornithine aminotransferase, renal form" FT /id="PRO_0000001263" FT MOD_RES 49 FT /note="N6-acetyllysine" FT /evidence="ECO:0000250|UniProtKB:P29758" FT MOD_RES 66 FT /note="N6-acetyllysine" FT /evidence="ECO:0000250|UniProtKB:P29758" FT MOD_RES 102 FT /note="N6-succinyllysine" FT /evidence="ECO:0000250|UniProtKB:P29758" FT MOD_RES 107 FT /note="N6-acetyllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:P29758" FT MOD_RES 107 FT /note="N6-succinyllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:P29758" FT MOD_RES 292 FT /note="N6-(pyridoxal phosphate)lysine" FT /evidence="ECO:0000269|PubMed:3754226" FT MOD_RES 362 FT /note="N6-acetyllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:P29758" FT MOD_RES 362 FT /note="N6-succinyllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:P29758" FT MOD_RES 386 FT /note="N6-acetyllysine" FT /evidence="ECO:0000250|UniProtKB:P29758" FT MOD_RES 392 FT /note="N6-acetyllysine" FT /evidence="ECO:0000250|UniProtKB:P29758" FT MOD_RES 405 FT /note="N6-acetyllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:P29758" FT MOD_RES 405 FT /note="N6-succinyllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:P29758" FT MOD_RES 421 FT /note="N6-acetyllysine" FT /evidence="ECO:0000250|UniProtKB:P29758" FT VAR_SEQ 1..138 FT /note="Missing (in isoform 2)" FT /evidence="ECO:0000303|PubMed:14702039, FT ECO:0000303|PubMed:17974005" FT /id="VSP_043085" FT VARIANT 51 FT /note="G -> D (in GACR; loss of protein stability; loss of FT ornithine aminotransferase activity; dbSNP:rs11553554)" FT /evidence="ECO:0000269|PubMed:23076989" FT /id="VAR_071924" FT VARIANT 54 FT /note="N -> K (in GACR; dbSNP:rs121965048)" FT /evidence="ECO:0000269|PubMed:3375240" FT /id="VAR_000565" FT VARIANT 55 FT /note="Y -> H (in GACR; decreased protein abundance; FT dbSNP:rs121965037)" FT /evidence="ECO:0000269|PubMed:1737786" FT /id="VAR_000566" FT VARIANT 89 FT /note="N -> K (in GACR; no effect on protein abundance; FT dbSNP:rs386833602)" FT /evidence="ECO:0000269|PubMed:1737786" FT /id="VAR_000567" FT VARIANT 90 FT /note="Q -> E (in GACR; mistargeted, accumulates in FT cytoplasm; dbSNP:rs121965060)" FT /evidence="ECO:0000269|PubMed:7668253" FT /id="VAR_015648" FT VARIANT 93 FT /note="C -> F (in GACR; no effect on protein abundance; FT dbSNP:rs121965038)" FT /evidence="ECO:0000269|PubMed:1737786" FT /id="VAR_000568" FT VARIANT 104 FT /note="Q -> R (in GACR; loss of protein stability; loss of FT ornithine aminotransferase activity; dbSNP:rs386833604)" FT /evidence="ECO:0000269|PubMed:23076989" FT /id="VAR_071925" FT VARIANT 154 FT /note="R -> L (in GACR; no effect on protein abundance; FT loss of ornithine aminotransferase activity; FT dbSNP:rs121965039)" FT /evidence="ECO:0000269|PubMed:1737786" FT /id="VAR_000569" FT VARIANT 180 FT /note="R -> T (in GACR; no effect on protein abundance; FT loss of ornithine aminotransferase activity; FT dbSNP:rs121965040)" FT /evidence="ECO:0000269|PubMed:1612597, FT ECO:0000269|PubMed:1737786" FT /id="VAR_000570" FT VARIANT 184 FT /note="Missing (in GACR; no effect on protein abundance; FT loss of ornithine aminotransferase activity; FT dbSNP:rs121965035)" FT /evidence="ECO:0000269|PubMed:1737786" FT /id="VAR_000571" FT VARIANT 199 FT /note="P -> Q (in GACR; loss of protein stability; loss of FT ornithine aminotransferase activity; dbSNP:rs267606925)" FT /evidence="ECO:0000269|PubMed:23076989" FT /id="VAR_071926" FT VARIANT 226 FT /note="A -> V (in GACR; loss of protein stability; loss of FT ornithine aminotransferase activity; dbSNP:rs121965059)" FT /evidence="ECO:0000269|PubMed:23076989, FT ECO:0000269|PubMed:7887415" FT /id="VAR_000572" FT VARIANT 241 FT /note="P -> L (in GACR; no effect on protein abundance; FT dbSNP:rs121965051)" FT /evidence="ECO:0000269|PubMed:1612597, FT ECO:0000269|PubMed:1737786" FT /id="VAR_000573" FT VARIANT 245 FT /note="Y -> C (in GACR; no effect on protein abundance; FT dbSNP:rs121965046)" FT /evidence="ECO:0000269|PubMed:1737786" FT /id="VAR_000574" FT VARIANT 250 FT /note="R -> P (in GACR; no effect on protein abundance; FT dbSNP:rs121965052)" FT /evidence="ECO:0000269|PubMed:1612597, FT ECO:0000269|PubMed:1737786" FT /id="VAR_000575" FT VARIANT 267 FT /note="T -> I (in GACR; decreased protein abundance; FT dbSNP:rs386833618)" FT /evidence="ECO:0000269|PubMed:1737786" FT /id="VAR_000576" FT VARIANT 270 FT /note="A -> P (in GACR; decreased protein abundance in FT homozygous patient cells; dbSNP:rs121965041)" FT /evidence="ECO:0000269|PubMed:1737786" FT /id="VAR_000577" FT VARIANT 271 FT /note="R -> K (in GACR; no effect on protein abundance; FT loss of ornithine aminotransferase activity; FT dbSNP:rs121965042)" FT /evidence="ECO:0000269|PubMed:1737786" FT /id="VAR_000578" FT VARIANT 318 FT /note="E -> K (in GACR; loss of protein stability; loss of FT ornithine aminotransferase activity; dbSNP:rs386833621)" FT /evidence="ECO:0000269|PubMed:23076989" FT /id="VAR_071927" FT VARIANT 319 FT /note="H -> Y (in GACR; dbSNP:rs121965049)" FT /evidence="ECO:0000269|PubMed:2793865" FT /id="VAR_000579" FT VARIANT 332 FT /note="V -> M (in GACR; loss of protein stability; loss of FT ornithine aminotransferase activity; dbSNP:rs121965047)" FT /evidence="ECO:0000269|PubMed:23076989, FT ECO:0000269|PubMed:3375240" FT /id="VAR_000580" FT VARIANT 353 FT /note="G -> D (in GACR; decreased protein abundance; FT dbSNP:rs121965053)" FT /evidence="ECO:0000269|PubMed:1612597, FT ECO:0000269|PubMed:1737786" FT /id="VAR_000581" FT VARIANT 375 FT /note="G -> A (in GACR; decreased protein abundance; FT dbSNP:rs121965045)" FT /evidence="ECO:0000269|PubMed:1737786" FT /id="VAR_000582" FT VARIANT 394 FT /note="C -> R (in GACR; no effect on protein abundance; FT dbSNP:rs121965054)" FT /evidence="ECO:0000269|PubMed:1612597, FT ECO:0000269|PubMed:1737786" FT /id="VAR_000583" FT VARIANT 394 FT /note="C -> Y (in GACR; loss of protein stability; loss of FT ornithine aminotransferase activity; dbSNP:rs386833597)" FT /evidence="ECO:0000269|PubMed:23076989" FT /id="VAR_071928" FT VARIANT 402 FT /note="L -> P (in GACR; may affect protein stability; loss FT of ornithine aminotransferase activity; dbSNP:rs121965043)" FT /evidence="ECO:0000269|PubMed:1737786, FT ECO:0000269|PubMed:23076989" FT /id="VAR_000584" FT VARIANT 417 FT /note="P -> L (in GACR; loss of protein stability; loss of FT ornithine aminotransferase activity; dbSNP:rs121965044)" FT /evidence="ECO:0000269|PubMed:1737786, FT ECO:0000269|PubMed:23076989" FT /id="VAR_000585" FT VARIANT 436 FT /note="I -> N (in GACR; loss of protein stability; loss of FT ornithine aminotransferase activity; dbSNP:rs386833598)" FT /evidence="ECO:0000269|PubMed:23076989" FT /id="VAR_071929" FT VARIANT 437 FT /note="L -> F (in GACR; likely benign; no effect on protein FT stability; no effect on ornithine aminotransferase FT activity; dbSNP:rs1800456)" FT /evidence="ECO:0000269|PubMed:1737786, FT ECO:0000269|PubMed:23076989" FT /id="VAR_000586" FT HELIX 40..50 FT /evidence="ECO:0007829|PDB:8V9M" FT STRAND 62..67 FT /evidence="ECO:0007829|PDB:8V9M" FT STRAND 69..72 FT /evidence="ECO:0007829|PDB:8V9M" FT STRAND 77..82 FT /evidence="ECO:0007829|PDB:8V9M" FT HELIX 83..86 FT /evidence="ECO:0007829|PDB:8V9M" FT TURN 87..90 FT /evidence="ECO:0007829|PDB:8V9M" FT HELIX 95..105 FT /evidence="ECO:0007829|PDB:8V9M" FT STRAND 115..119 FT /evidence="ECO:0007829|PDB:5VWO" FT HELIX 120..131 FT /evidence="ECO:0007829|PDB:8V9M" FT STRAND 134..141 FT /evidence="ECO:0007829|PDB:8V9M" FT HELIX 142..156 FT /evidence="ECO:0007829|PDB:8V9M" FT HELIX 157..161 FT /evidence="ECO:0007829|PDB:8V9M" FT STRAND 169..173 FT /evidence="ECO:0007829|PDB:8V9M" FT HELIX 182..186 FT /evidence="ECO:0007829|PDB:8V9M" FT HELIX 191..194 FT /evidence="ECO:0007829|PDB:8V9M" FT STRAND 204..207 FT /evidence="ECO:0007829|PDB:8V9M" FT HELIX 212..218 FT /evidence="ECO:0007829|PDB:8V9M" FT STRAND 224..229 FT /evidence="ECO:0007829|PDB:8V9M" FT STRAND 231..233 FT /evidence="ECO:0007829|PDB:8V9M" FT TURN 234..237 FT /evidence="ECO:0007829|PDB:8V9M" FT HELIX 245..255 FT /evidence="ECO:0007829|PDB:8V9M" FT STRAND 259..263 FT /evidence="ECO:0007829|PDB:8V9M" FT TURN 265..272 FT /evidence="ECO:0007829|PDB:8V9M" FT STRAND 273..276 FT /evidence="ECO:0007829|PDB:8V9M" FT HELIX 277..281 FT /evidence="ECO:0007829|PDB:8V9M" FT STRAND 286..290 FT /evidence="ECO:0007829|PDB:8V9M" FT HELIX 292..295 FT /evidence="ECO:0007829|PDB:8V9M" FT STRAND 302..306 FT /evidence="ECO:0007829|PDB:8V9M" FT HELIX 308..311 FT /evidence="ECO:0007829|PDB:8V9M" FT TURN 322..325 FT /evidence="ECO:0007829|PDB:7TED" FT HELIX 327..342 FT /evidence="ECO:0007829|PDB:8V9M" FT HELIX 345..360 FT /evidence="ECO:0007829|PDB:8V9M" FT TURN 365..367 FT /evidence="ECO:0007829|PDB:8V9M" FT STRAND 368..374 FT /evidence="ECO:0007829|PDB:8V9M" FT STRAND 377..382 FT /evidence="ECO:0007829|PDB:8V9M" FT HELIX 390..399 FT /evidence="ECO:0007829|PDB:8V9M" FT STRAND 405..407 FT /evidence="ECO:0007829|PDB:7TA1" FT TURN 408..410 FT /evidence="ECO:0007829|PDB:8V9M" FT STRAND 411..414 FT /evidence="ECO:0007829|PDB:8V9M" FT HELIX 422..436 FT /evidence="ECO:0007829|PDB:8V9M" SQ SEQUENCE 439 AA; 48535 MW; E9D0636824A83220 CRC64; MFSKLAHLQR FAVLSRGVHS SVASATSVAT KKTVQGPPTS DDIFEREYKY GAHNYHPLPV ALERGKGIYL WDVEGRKYFD FLSSYSAVNQ GHCHPKIVNA LKSQVDKLTL TSRAFYNNVL GEYEEYITKL FNYHKVLPMN TGVEAGETAC KLARKWGYTV KGIQKYKAKI VFAAGNFWGR TLSAISSSTD PTSYDGFGPF MPGFDIIPYN DLPALERALQ DPNVAAFMVE PIQGEAGVVV PDPGYLMGVR ELCTRHQVLF IADEIQTGLA RTGRWLAVDY ENVRPDIVLL GKALSGGLYP VSAVLCDDDI MLTIKPGEHG STYGGNPLGC RVAIAALEVL EEENLAENAD KLGIILRNEL MKLPSDVVTA VRGKGLLNAI VIKETKDWDA WKVCLRLRDN GLLAKPTHGD IIRFAPPLVI KEDELRESIE IINKTILSF //