P04181 (OAT_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Ornithine aminotransferase, mitochondrial
EC=2.6.1.13

Alternative name(s):
Ornithine delta-aminotransferase
Ornithine--oxo-acid aminotransferase

Cleaved into the following 2 chains:

1. Ornithine aminotransferase, hepatic form
2. Ornithine aminotransferase, renal form

Gene names

Name:

OAT

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	439 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

Catalytic activity	L-ornithine + a 2-oxo acid = L-glutamate 5-semialdehyde + an L-amino acid.
Cofactor	Pyridoxal phosphate.
Pathway	Amino-acid biosynthesis; L-proline biosynthesis; L-glutamate 5-semialdehyde from L-ornithine: step 1/1.
Subunit structure	Homotetramer.
Subcellular location	Mitochondrion matrix.
Involvement in disease	Hyperornithinemia with gyrate atrophy of choroid and retina (HOGA) [MIM:258870]: A disorder clinically characterized by a triad of progressive chorioretinal degeneration, early cataract formation, and type II muscle fiber atrophy. Characteristic chorioretinal atrophy with progressive constriction of the visual fields leads to blindness at the latest during the sixth decade of life. Patients generally have normal intelligence. Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.18 Ref.19 Ref.20 Ref.21 Ref.22 Ref.23
Sequence similarities	Belongs to the class-III pyridoxal-phosphate-dependent aminotransferase family.

Ontologies

Keywords
Cellular component	Mitochondrion
Coding sequence diversity	Alternative splicing Polymorphism
Disease	Disease mutation
Domain	Transit peptide
Ligand	Pyridoxal phosphate
Molecular function	Aminotransferase Transferase
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	L-proline biosynthetic process Inferred from electronic annotation. Source: UniProtKB-UniPathway cellular amino acid biosynthetic process Traceable author statement. Source: Reactome cellular nitrogen compound metabolic process Traceable author statement. Source: Reactome protein hexamerization Inferred from direct assay PubMed 97454792. Source: UniProtKB visual perception Traceable author statement Ref.19. Source: ProtInc
Cellular_component	mitochondrial matrix Traceable author statement. Source: Reactome
Molecular_function	ornithine-oxo-acid transaminase activity Inferred from experiment. Source: Reactome pyridoxal phosphate binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
EIF6	P56537	1	EBI-721662,EBI-372243

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: P04181-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

Isoform 2 (identifier: P04181-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1-138: Missing.

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Transit peptide

1 – 35

35

Mitochondrion; in renal form Ref.3

Transit peptide

1 – 25

25

Mitochondrion; in hepatic form

Chain

26 – 439

414

Ornithine aminotransferase, hepatic form

PRO_0000001262

Chain

36 – 439

404

Ornithine aminotransferase, renal form

PRO_0000001263

Amino acid modifications

Modified residue

292

1

N6-(pyridoxal phosphate)lysine Ref.13

Natural variations

Alternative sequence

1 – 138

138

Missing in isoform 2.

VSP_043085

Natural variant

54

1

N → K in HOGA. Ref.18

VAR_000565

Natural variant

55

1

Y → H in HOGA. Ref.21

VAR_000566

Natural variant

89

1

N → K in HOGA. Ref.21

VAR_000567

Natural variant

90

1

Q → E in HOGA; mistargeted, accumulates in cytoplasm. Ref.23

VAR_015648

Natural variant

93

1

C → F in HOGA. Ref.21

VAR_000568

Natural variant

154

1

R → L in HOGA; complete loss of activity. Ref.21

VAR_000569

Natural variant

180

1

R → T in HOGA; complete loss of activity. Ref.20 Ref.21

VAR_000570

Natural variant

184

1

Missing in HOGA. Ref.21

VAR_000571

Natural variant

226

1

A → V in HOGA. Ref.22

VAR_000572

Natural variant

241

1

P → L in HOGA. Ref.20 Ref.21

VAR_000573

Natural variant

245

1

Y → C in HOGA. Ref.21

VAR_000574

Natural variant

250

1

R → P in HOGA. Ref.20 Ref.21

VAR_000575

Natural variant

267

1

T → I in HOGA. Ref.21

VAR_000576

Natural variant

270

1

A → P in HOGA.

VAR_000577

Natural variant

271

1

R → K in HOGA. Ref.21

VAR_000578

Natural variant

319

1

H → Y in HOGA. Ref.19

VAR_000579

Natural variant

332

1

V → M in HOGA. Ref.18

VAR_000580

Natural variant

353

1

G → D in HOGA. Ref.20 Ref.21

VAR_000581

Natural variant

375

1

G → A in HOGA. Ref.21

VAR_000582

Natural variant

394

1

C → R in HOGA. Ref.20 Ref.21

VAR_000583

Natural variant

402

1

L → P in HOGA. Ref.21

VAR_000584

Natural variant

417

1

P → L in HOGA. Ref.21

VAR_000585

Natural variant

437

1

L → F. Ref.21
Corresponds to variant rs1800456 [ dbSNP | Ensembl ].

VAR_000586

Secondary structure

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439

Helix Strand Turn

Details...

Helix

40 – 50

11

Beta strand

61 – 67

7

Beta strand

69 – 72

4

Beta strand

77 – 82

6

Helix

83 – 86

4

Turn

87 – 90

4

Helix

95 – 105

11

Beta strand

115 – 119

5

Helix

120 – 131

12

Beta strand

134 – 141

8

Helix

142 – 159

18

Beta strand

169 – 173

5

Helix

182 – 185

4

Helix

191 – 194

4

Beta strand

204 – 207

4

Helix

212 – 218

7

Beta strand

224 – 229

6

Beta strand

231 – 233

3

Turn

234 – 237

4

Helix

245 – 255

11

Beta strand

259 – 263

5

Turn

265 – 272

8

Beta strand

273 – 276

4

Helix

277 – 281

5

Beta strand

286 – 290

5

Helix

292 – 295

4

Beta strand

302 – 306

5

Helix

308 – 311

4

Helix

327 – 342

16

Helix

345 – 360

16

Turn

365 – 367

3

Beta strand

368 – 374

7

Beta strand

377 – 382

6

Helix

390 – 399

10

Beta strand

406 – 414

9

Helix

422 – 437

16

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified March 20, 1987. Version 1. Checksum: E9D0636824A83220	FASTA	439	48,535
	10 20 30 40 50 60 MFSKLAHLQR FAVLSRGVHS SVASATSVAT KKTVQGPPTS DDIFEREYKY GAHNYHPLPV 70 80 90 100 110 120 ALERGKGIYL WDVEGRKYFD FLSSYSAVNQ GHCHPKIVNA LKSQVDKLTL TSRAFYNNVL 130 140 150 160 170 180 GEYEEYITKL FNYHKVLPMN TGVEAGETAC KLARKWGYTV KGIQKYKAKI VFAAGNFWGR 190 200 210 220 230 240 TLSAISSSTD PTSYDGFGPF MPGFDIIPYN DLPALERALQ DPNVAAFMVE PIQGEAGVVV 250 260 270 280 290 300 PDPGYLMGVR ELCTRHQVLF IADEIQTGLA RTGRWLAVDY ENVRPDIVLL GKALSGGLYP 310 320 330 340 350 360 VSAVLCDDDI MLTIKPGEHG STYGGNPLGC RVAIAALEVL EEENLAENAD KLGIILRNEL 370 380 390 400 410 420 MKLPSDVVTA VRGKGLLNAI VIKETKDWDA WKVCLRLRDN GLLAKPTHGD IIRFAPPLVI 430 KEDELRESIE IINKTILSF
	Isoform 2 [UniParc]. Checksum: 9CFA7F66DDB264F0	FASTA	301	32,853
	10 20 30 40 50 60 MNTGVEAGET ACKLARKWGY TVKGIQKYKA KIVFAAGNFW GRTLSAISSS TDPTSYDGFG 70 80 90 100 110 120 PFMPGFDIIP YNDLPALERA LQDPNVAAFM VEPIQGEAGV VVPDPGYLMG VRELCTRHQV 130 140 150 160 170 180 LFIADEIQTG LARTGRWLAV DYENVRPDIV LLGKALSGGL YPVSAVLCDD DIMLTIKPGE 190 200 210 220 230 240 HGSTYGGNPL GCRVAIAALE VLEEENLAEN ADKLGIILRN ELMKLPSDVV TAVRGKGLLN 250 260 270 280 290 300 AIVIKETKDW DAWKVCLRLR DNGLLAKPTH GDIIRFAPPL VIKEDELRES IEIINKTILS F

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Molecular cloning of human ornithine aminotransferase mRNA." Inana G., Totsuka S., Redmond M., Dougherty T., Nagle J., Shiono T., Ohura T., Kominami E., Katunuma N. Proc. Natl. Acad. Sci. U.S.A. 83:1203-1207(1986) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
[2]	"Investigation of gyrate atrophy using a cDNA clone for human ornithine aminotransferase." Ramesh V., Shaffer M.M., Allaire J.M., Shih V.E., Gusella J.F. DNA 5:493-501(1986) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). Tissue: Liver.
[3]	"Molecular cloning and nucleotide sequence analysis of mRNA for human kidney ornithine aminotransferase. An examination of ornithine aminotransferase isozymes between liver and kidney." Kobayashi T., Nishii M., Takagi Y., Titani T., Matsuzawa T. FEBS Lett. 255:300-304(1989) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), PROTEIN SEQUENCE OF 36-40, PROTEOLYTIC PROCESSING. Tissue: Kidney.
[4]	"Human ornithine-delta-aminotransferase. cDNA cloning and analysis of the structural gene." Mitchell G.A., Looney J.E., Brody L.C., Steel G., Suchanek M., Engelhardt J.F., Willard H.F., Valle D. J. Biol. Chem. 263:14288-14295(1988) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORM 1).
[5]	"Analysis of the human ornithine aminotransferase gene family." Zintz C.B., Inana G. Exp. Eye Res. 50:759-770(1990) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Tissue: Placenta.
[6]	"Complete sequencing and characterization of 21,243 full-length human cDNAs." Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S. Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2). Tissue: Brain, Brain cortex and Subthalamic nucleus.
[7]	"Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201)." Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B. Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
[8]	"The full-ORF clone resource of the German cDNA consortium." Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U., Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A., Wiemann S., Schupp I. BMC Genomics 8:399-399(2007) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2). Tissue: Brain cortex.
[9]	"The DNA sequence and comparative analysis of human chromosome 10." Deloukas P., Earthrowl M.E., Grafham D.V., Rubenfield M., French L., Steward C.A., Sims S.K., Jones M.C., Searle S., Scott C., Howe K., Hunt S.E., Andrews T.D., Gilbert J.G.R., Swarbreck D., Ashurst J.L., Taylor A., Battles J. , Bird C.P., Ainscough R., Almeida J.P., Ashwell R.I.S., Ambrose K.D., Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Bates K., Beasley H., Bray-Allen S., Brown A.J., Brown J.Y., Burford D.C., Burrill W., Burton J., Cahill P., Camire D., Carter N.P., Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S., Corby N., Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L., Frankish A., Frankland J.A., Garner P., Garnett J., Gribble S., Griffiths C., Grocock R., Gustafson E., Hammond S., Harley J.L., Hart E., Heath P.D., Ho T.P., Hopkins B., Horne J., Howden P.J., Huckle E., Hynds C., Johnson C., Johnson D., Kana A., Kay M., Kimberley A.M., Kershaw J.K., Kokkinaki M., Laird G.K., Lawlor S., Lee H.M., Leongamornlert D.A., Laird G., Lloyd C., Lloyd D.M., Loveland J., Lovell J., McLaren S., McLay K.E., McMurray A., Mashreghi-Mohammadi M., Matthews L., Milne S., Nickerson T., Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V., Peck A.I., Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A., Ross M.T., Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M., Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W., Tracey A., Tromans A., Tsolas J., Wall M., Walsh J., Wang H., Weinstock K., West A.P., Willey D.L., Whitehead S.L., Wilming L., Wray P.W., Young L., Chen Y., Lovering R.C., Moschonas N.K., Siebert R., Fechtel K., Bentley D., Durbin R.M., Hubbard T., Doucette-Stamm L., Beck S., Smith D.R., Rogers J. Nature 429:375-381(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[10]	Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C. Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[11]	"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). Tissue: Placenta and Uterus.
[12]	"Molecular pathology of gyrate atrophy of the choroid and retina due to ornithine aminotransferase deficiency." Ramesh V., Gusella J.F., Shih V.E. Mol. Biol. Med. 8:81-93(1991) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 50-58 AND 328-336 (ISOFORM 1).
[13]	"The primary structure of ornithine aminotransferase. Identification of active-site sequence and site of post-translational proteolysis." Simmaco M., John R.A., Barra D., Bossa F. FEBS Lett. 199:39-42(1986) [PubMed] [Europe PMC] [Abstract] Cited for: PARTIAL PROTEIN SEQUENCE, PYRIDOXAL PHOSPHATE AT LYS-292, PROTEOLYTIC PROCESSING.
[14]	"Initial characterization of the human central proteome." Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J. BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[15]	"Human ornithine aminotransferase complexed with L-canaline and gabaculine: structural basis for substrate recognition." Shah S.A., Shen B.W., Brunger A.T. Structure 5:1067-1075(1997) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS).
[16]	"Crystal structure of human recombinant ornithine aminotransferase." Shen B.W., Hennig M., Hohenester E., Jansonius J.N., Schirmer T. J. Mol. Biol. 277:81-102(1998) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS).
[17]	"Crystal structure of human ornithine aminotransferase complexed with the highly specific and potent inhibitor 5-fluoromethylornithine." Storici P., Capitani G., Mueller R., Schirmer T., Jansonius J.N. J. Mol. Biol. 285:297-309(1999) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.95 ANGSTROMS).
[18]	"Molecular basis of ornithine aminotransferase deficiency in B-6-responsive and -nonresponsive forms of gyrate atrophy." Ramesh V., McClatchey A.I., Ramesh N., Benoit L.A., Berson E.L., Shih V.E., Gusella J.F. Proc. Natl. Acad. Sci. U.S.A. 85:3777-3780(1988) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANTS HOGA LYS-54 AND MET-332.
[19]	"Point mutation affecting processing of the ornithine aminotransferase precursor protein in gyrate atrophy." Inana G., Chambers C., Hotta Y., Inouye L., Filpula D., Pulford S., Shiono T. J. Biol. Chem. 264:17432-17436(1989) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT HOGA TYR-319.
[20]	"Strand-separating conformational polymorphism analysis: efficacy of detection of point mutations in the human ornithine delta-aminotransferase gene." Michaud J., Brody L.C., Steel G., Fontaine G., Martin L.S., Valle D., Mitchell G. Genomics 13:389-394(1992) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANTS HOGA THR-180; LEU-241; PRO-250; ASP-353 AND ARG-394.
[21]	"Ornithine delta-aminotransferase mutations in gyrate atrophy. Allelic heterogeneity and functional consequences." Brody L.C., Mitchell G.A., Obie C., Michaud J., Steel G., Fontaine G., Robert M.-F., Sipila I., Kaiser-Kupfer M., Valle D. J. Biol. Chem. 267:3302-3307(1992) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANTS HOGA HIS-55; LYS-89; PHE-93; LEU-154; THR-180; ALA-184 DEL; LEU-241; CYS-245; PRO-250; ILE-267; LYS-271; ASP-353; ALA-375; ARG-394; PRO-402 AND LEU-417, VARIANT PHE-437.
[22]	"Pyridoxine-responsive gyrate atrophy of the choroid and retina: clinical and biochemical correlates of the mutation A226V." Michaud J., Thompson G.N., Brody L.C., Steel G., Obie C., Fontaine G., Schappert K., Keith C.G., Valle D., Mitchell G.A. Am. J. Hum. Genet. 56:616-622(1995) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT HOGA VAL-226.
[23]	"A single amino acid substitution within the mature sequence of ornithine aminotransferase obstructs mitochondrial entry of the precursor." Kobayashi T., Ogawa H., Kasahara M., Shiozawa Z., Matsuzawa T. Am. J. Hum. Genet. 57:284-291(1995) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT HOGA GLU-90.
+	Additional computationally mapped references.

Web resources

GeneReviews

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

M12267 mRNA. Translation: AAA59956.1.
M14963 mRNA. Translation: AAA59959.1.
Y07511 mRNA. Translation: CAA68809.1.
M23204 mRNA. Translation: AAA36386.1.
M23205 Genomic DNA. No translation available.
M88760 Genomic DNA. Translation: AAA59958.1. Sequence problems.
M29927 , M29919, M29920, M29921, M29922, M29923, M29924, M29925, M29926 Genomic DNA. Translation: AAA59957.1.
AK296032 mRNA. Translation: BAH12241.1.
AK312561 mRNA. Translation: BAG35458.1.
AK315947 mRNA. Translation: BAH14318.1.
CR457045 mRNA. Translation: CAG33326.1.
CR749808 mRNA. Translation: CAH18668.1.
AL445237 Genomic DNA. Translation: CAI17293.1.
CH471066 Genomic DNA. Translation: EAW49271.1.
CH471066 Genomic DNA. Translation: EAW49272.1.
BC000964 mRNA. Translation: AAH00964.1.
BC016928 mRNA. Translation: AAH16928.1.
S66418 mRNA. Translation: AAB20298.1.
S66421 mRNA. Translation: AAB20297.1.

IPI

IPI00022334.
IPI00955490.

PIR

XNHUO. A30806.
I55360.

RefSeq

NP_000265.1. NM_000274.3.
NP_001165285.1. NM_001171814.1.

UniGene

Hs.523332.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1GBN	X-ray	2.30	A/B/C	38-439	[»]
1OAT	X-ray	2.50	A/B/C	1-439	[»]
2BYJ	X-ray	3.02	A/B/C	1-439	[»]
2BYL	X-ray	2.15	A/B/C	1-439	[»]
2CAN	X-ray	2.30	A/B/C	38-439	[»]
2OAT	X-ray	1.95	A/B/C	1-439	[»]

ProteinModelPortal

P04181.

ModBase

Search...

Protein-protein interaction databases

IntAct

P04181. 7 interactions.

MINT

MINT-1387274.

STRING

9606.ENSP00000357838.

PTM databases

PhosphoSite

P04181.

Polymorphism databases

DMDM

129018.

2D gel databases

REPRODUCTION-2DPAGE

IPI00022334.

Proteomic databases

PaxDb

P04181.

PeptideAtlas

P04181.

PRIDE

P04181.

Protocols and materials databases

DNASU

4942.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000368845; ENSP00000357838; ENSG00000065154.
ENST00000539214; ENSP00000439042; ENSG00000065154.

GeneID

4942.

KEGG

hsa:4942.

UCSC

uc001lhp.3. human.

Organism-specific databases

CTD

4942.

GeneCards

GC10M126075.

HGNC

HGNC:8091. OAT.

HPA

CAB033576.
HPA040098.

MIM

258870. phenotype.
613349. gene.

neXtProt

NX_P04181.

Orphanet

414. Gyrate atrophy of choroid and retina.

PharmGKB

PA31880.

GenAtlas

Search...

Phylogenomic databases

eggNOG

COG4992.

HOGENOM

HOG000020206.

HOVERGEN

HBG000434.

InParanoid

P04181.

KO

K00819.

OMA

VIPYNDL.

OrthoDB

EOG4MSCZ6.

PhylomeDB

P04181.

Enzyme and pathway databases

BioCyc

MetaCyc:HS00832-MONOMER.

Reactome

REACT_111217. Metabolism.

SABIO-RK

P04181.

UniPathway

UPA00098; UER00358.

Gene expression databases

Bgee

P04181.

CleanEx

HS_OAT.

Genevestigator

P04181.

GermOnline

ENSG00000065154. Homo sapiens.

Family and domain databases

Gene3D

3.40.640.10. 1 hit.
3.90.1150.10. 2 hits.

InterPro

IPR005814. Aminotrans_3.
IPR010164. Orn_aminotrans.
IPR015424. PyrdxlP-dep_Trfase.
IPR015421. PyrdxlP-dep_Trfase_major_sub1.
IPR015422. PyrdxlP-dep_Trfase_major_sub2.
[Graphical view]

PANTHER

PTHR11986. PTHR11986. 1 hit.

Pfam

PF00202. Aminotran_3. 1 hit.
[Graphical view]

SUPFAM

SSF53383. PyrdxlP-dep_Trfase_major. 1 hit.

TIGRFAMs

TIGR01885. Orn_aminotrans. 1 hit.

PROSITE

PS00600. AA_TRANSFER_CLASS_3. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

ChEMBL

CHEMBL5954.

DrugBank

DB00129. L-Ornithine.
DB00114. Pyridoxal Phosphate.

EvolutionaryTrace

P04181.

GenomeRNAi

4942.

NextBio

19041.

SOURCE

Search...

Entry information

Entry name

OAT_HUMAN

Accession

Primary (citable) accession number: P04181
Secondary accession number(s): D3DRF0 , Q16068, Q16069, Q68CS0, Q6IAV9, Q9UD03

Entry history

Integrated into UniProtKB/Swiss-Prot:	March 20, 1987
Last sequence update:	March 20, 1987
Last modified:	May 1, 2013
This is version 156 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.