Q86XE5 (HOGA1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Probable 4-hydroxy-2-oxoglutarate aldolase, mitochondrial
EC=4.1.3.16

Alternative name(s):
Dihydrodipicolinate synthase-like
Short name=DHDPS-like protein
Probable 2-keto-4-hydroxyglutarate aldolase
Short name=Probable KHG-aldolase
Protein 569272

Gene names

Name:	HOGA1
Synonyms:	C10orf65, DHDPSL

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	327 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)

Function	Catalyzes the final step in the metabolic pathway of hydroxyproline Probable. Ref.6
Catalytic activity	4-hydroxy-2-oxoglutarate = pyruvate + glyoxylate.
Enzyme regulation	Inhibited by divalent cations By similarity.
Subunit structure	Homotetramer By similarity.
Subcellular location	Mitochondrion By similarity.
Involvement in disease	Hyperoxaluria primary 3 (HP3) [MIM:613616]: A disorder phenotypically similar to hyperoxaluria type 1 and type 2. It is characterized by increase in urinary oxalate excretion and mild glycolic aciduria. Clinical manifestations include calcium oxalate urolithiasis, hematuria, pain, and/or urinary tract infection. Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.6
Sequence similarities	Belongs to the DapA family.
Sequence caution	The sequence CAC84901.1 differs from that shown. Reason: Erroneous gene model prediction. The sequence CAI15457.1 differs from that shown. Reason: Erroneous gene model prediction.

Ontologies

Keywords
Cellular component	Mitochondrion
Coding sequence diversity	Alternative splicing
Disease	Disease mutation
Domain	Transit peptide
Ligand	Schiff base
Molecular function	Lyase
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	4-hydroxyproline catabolic process Inferred from direct assay PubMed 21998747. Source: BHF-UCL glyoxylate catabolic process Inferred from mutant phenotype Ref.6. Source: UniProtKB oxalate metabolic process Inferred from mutant phenotype PubMed 21896830. Source: BHF-UCL pyruvate biosynthetic process Inferred from direct assay PubMed 21998747. Source: BHF-UCL
Cellular_component	mitochondrion Inferred from sequence or structural similarity PubMed 21998747. Source: BHF-UCL
Molecular_function	4-hydroxy-2-oxoglutarate aldolase activity Inferred from sequence or structural similarity. Source: UniProtKB protein homodimerization activity Inferred from direct assay PubMed 21998747. Source: BHF-UCL
Complete GO annotation...

Alternative products

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

Isoform 1 (identifier: Q86XE5-1)

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: Q86XE5-3)

The sequence of this isoform differs from the canonical sequence as follows:
     71-233: Missing.

Note: No experimental confirmation available.

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Transit peptide

1 – 25

25

Mitochondrion Potential

Chain

26 – 327

302

Probable 4-hydroxy-2-oxoglutarate aldolase, mitochondrial

PRO_0000273346

Regions

Region

77 – 78

2

Substrate binding By similarity

Sites

Active site

196

1

Schiff-base intermediate with substrate By similarity

Site

168

1

Involved in proton transfer during cleavage By similarity

Natural variations

Alternative sequence

71 – 233

163

Missing in isoform 2.

VSP_022515

Natural variant

257

1

C → G in HP3. Ref.6

VAR_064035

Natural variant

287

1

G → V in HP3. Ref.6

VAR_064036

Natural variant

315

1

Missing in HP3. Ref.6

VAR_064037

Secondary structure

1

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327

Helix Strand Turn

Details...

Beta strand

37 – 39

3

Helix

54 – 64

11

Beta strand

70 – 76

7

Helix

77 – 79

3

Helix

81 – 83

3

Helix

86 – 98

13

Beta strand

104 – 109

6

Helix

115 – 127

13

Beta strand

131 – 136

6

Helix

142 – 144

3

Helix

147 – 160

14

Beta strand

165 – 169

5

Helix

171 – 174

4

Helix

180 – 187

8

Beta strand

192 – 197

6

Helix

202 – 211

10

Turn

212 – 214

3

Beta strand

218 – 223

6

Helix

224 – 226

3

Helix

227 – 233

7

Beta strand

237 – 239

3

Helix

241 – 244

4

Helix

247 – 258

12

Helix

262 – 278

17

Turn

279 – 283

5

Helix

284 – 295

12

Helix

311 – 322

12

Turn

323 – 325

3

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified June 1, 2003. Version 1. Checksum: 2DC011E4F9FD32C9	FASTA	327	35,249
	10 20 30 40 50 60 MLGPQVWSSV RQGLSRSLSR NVGVWASGEG KKVDIAGIYP PVTTPFTATA EVDYGKLEEN 70 80 90 100 110 120 LHKLGTFPFR GFVVQGSNGE FPFLTSSERL EVVSRVRQAM PKNRLLLAGS GCESTQATVE 130 140 150 160 170 180 MTVSMAQVGA DAAMVVTPCY YRGRMSSAAL IHHYTKVADL SPIPVVLYSV PANTGLDLPV 190 200 210 220 230 240 DAVVTLSQHP NIVGMKDSGG DVTRIGLIVH KTRKQDFQVL AGSAGFLMAS YALGAVGGVC 250 260 270 280 290 300 ALANVLGAQV CQLERLCCTG QWEDAQKLQH RLIEPNAAVT RRFGIPGLKK IMDWFGYYGG 310 320 PCRAPLQELS PAEEEALRMD FTSNGWL
	Isoform 2 [UniParc]. Checksum: 5DC5ADF3B9A891B4	FASTA	164	17,954
	10 20 30 40 50 60 MLGPQVWSSV RQGLSRSLSR NVGVWASGEG KKVDIAGIYP PVTTPFTATA EVDYGKLEEN 70 80 90 100 110 120 LHKLGTFPFR GAVGGVCALA NVLGAQVCQL ERLCCTGQWE DAQKLQHRLI EPNAAVTRRF 130 140 150 160 GIPGLKKIMD WFGYYGGPCR APLQELSPAE EEALRMDFTS NGWL

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"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] (ISOFORM 1). Tissue: Urinary bladder.
[2]	"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].
[3]	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].
[4]	"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] (ISOFORMS 1 AND 2). Tissue: Hippocampus and Kidney.
[5]	"Homo sapiens gene 569272." Moschonas N.K. Submitted (APR-2001) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-279 (ISOFORM 1).
[6]	"Mutations in DHDPSL are responsible for primary hyperoxaluria type III." Belostotsky R., Seboun E., Idelson G.H., Milliner D.S., Becker-Cohen R., Rinat C., Monico C.G., Feinstein S., Ben-Shalom E., Magen D., Weissman I., Charon C., Frishberg Y. Am. J. Hum. Genet. 87:392-399(2010) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, VARIANTS HP3 GLY-257; VAL-287 AND GLU-315 DEL.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

AK289440 mRNA. Translation: BAF82129.1.
AL355315 Genomic DNA. Translation: CAI15454.1.
AL355315 Genomic DNA. Translation: CAI15455.1.
AL355315 Genomic DNA. Translation: CAI15457.1. Sequence problems.
CH471066 Genomic DNA. Translation: EAW49912.1.
BC011916 mRNA. Translation: AAH11916.1.
BC045550 mRNA. Translation: AAH45550.1.
BC057821 mRNA. Translation: AAH57821.1.
AJ312051 Genomic DNA. Translation: CAC84901.1. Sequence problems.

IPI

IPI00061760.
IPI00642544.

RefSeq

NP_001128142.1. NM_001134670.1.
NP_612422.2. NM_138413.3.

UniGene

Hs.180346.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
3S5N	X-ray	2.50	A	26-327	[»]
3S5O	X-ray	1.97	A	26-327	[»]

ProteinModelPortal

Q86XE5.

ModBase

Search...

PTM databases

PhosphoSite

Q86XE5.

Polymorphism databases

DMDM

74750531.

Proteomic databases

PaxDb

Q86XE5.

PRIDE

Q86XE5.

Protocols and materials databases

DNASU

112817.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000370646; ENSP00000359680; ENSG00000241935.
ENST00000370647; ENSP00000359681; ENSG00000241935.

GeneID

112817.

KEGG

hsa:112817.

UCSC

uc001kny.3. human.
uc001knz.3. human.

Organism-specific databases

CTD

112817.

GeneCards

GC10P099354.

HGNC

HGNC:25155. HOGA1.

HPA

HPA039466.

MIM

613597. gene.
613616. phenotype.

neXtProt

NX_Q86XE5.

Orphanet

93600. Primary hyperoxaluria type 3.

PharmGKB

PA165548441.

GenAtlas

Search...

Phylogenomic databases

eggNOG

COG0329.

HOVERGEN

HBG081405.

InParanoid

Q86XE5.

OMA

GCESTRA.

PhylomeDB

Q86XE5.

Gene expression databases

Bgee

Q86XE5.

CleanEx

HS_C10orf65.

Genevestigator

Q86XE5.

Family and domain databases

Gene3D

3.20.20.70. 1 hit.

InterPro

IPR013785. Aldolase_TIM.
IPR002220. Dihydrodipicolinate_synth-like.
IPR020625. Dihydrodipicolinate_synth_AS.
[Graphical view]

PANTHER

PTHR12128. PTHR12128. 1 hit.

Pfam

PF00701. DHDPS. 1 hit.
[Graphical view]

PIRSF

PIRSF001365. DHDPS. 1 hit.

PRINTS

PR00146. DHPICSNTHASE.

PROSITE

PS00665. DHDPS_1. False negative.
PS00666. DHDPS_2. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

BindingDB

Q86XE5.

ChEMBL

CHEMBL5996.

ChiTaRS

HOGA1. human.

GenomeRNAi

112817.

NextBio

78673.

SOURCE

Search...

Entry information

Entry name

HOGA1_HUMAN

Accession

Primary (citable) accession number: Q86XE5
Secondary accession number(s): A8K075 , Q5T680, Q5T684, Q711P0, Q8N9F2, Q96EV5

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 23, 2007
Last sequence update:	June 1, 2003
Last modified:	May 29, 2013
This is version 92 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.