Q96EM0 (T3HPD_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Trans-L-3-hydroxyproline dehydratase
EC=4.2.1.77

Alternative name(s):
Trans-3-hydroxy-l-proline dehydratase

Gene names

Name:	L3HYPDH
Synonyms:	C14orf149

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	354 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Catalyzes the dehydration of trans-3-hydroxy-L-proline to delta-1-pyrroline-2-carboxylate (Pyr2C). May be required to degrade trans-3-hydroxy-L-proline from the diet and originating from the degradation of proteins such as collagen-IV that contain it. Ref.5
Catalytic activity	Trans-3-hydroxy-L-proline = 1-pyrroline 2-carboxylate + H2O. Ref.5
Subunit structure	Homodimer By similarity.
Tissue specificity	Ubiquitously expressed. Ref.5
Miscellaneous	In contrast to the T.cruzi proline racemase enzyme, lacks the conserved Cys at position 273 which is replaced by a Thr residue, transforming the racemase activity into dehydratase activity (Ref.5).
Sequence similarities	Belongs to the proline racemase family.
Biophysicochemical properties	Kinetic parameters: KM=7.23 mM for trans-3-hydroxy-L-proline Ref.5 Vmax=39.5 µmol/min/mg enzyme pH dependence: Optimum pH is 8.0.

Ontologies

Keywords
Coding sequence diversity	Polymorphism
Molecular function	Lyase
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Molecular_function	hydro-lyase activity Inferred from direct assay Ref.5. Source: UniProtKB trans-L-3-hydroxyproline dehydratase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 354	354	Trans-L-3-hydroxyproline dehydratase		PRO_0000288949
Regions
	Region	105 – 106	2	Substrate binding By similarity
	Region	274 – 275	2	Substrate binding By similarity
Sites
	Active site	104	1	Proton acceptor By similarity
	Binding site	269	1	Substrate By similarity
Natural variations
	Natural variant	42	1	V → A. Corresponds to variant rs17096291 [ dbSNP | Ensembl ].		VAR_032540
	Natural variant	125	1	P → S. Corresponds to variant rs35622288 [ dbSNP | Ensembl ].		VAR_062192
	Natural variant	315	1	A → V. Corresponds to variant rs1046701 [ dbSNP | Ensembl ].		VAR_032541
	Natural variant	341	1	I → V. Corresponds to variant rs8660 [ dbSNP | Ensembl ].		VAR_032542
Experimental info
	Mutagenesis	273	1	T → C: Restores racemase activity and catalyzes racemization of L-proline to D-proline at low level. Ref.5
	Sequence conflict	9	1	R → W in AAH12131. Ref.3

Sequences

	Sequence		Length	Mass (Da)
	Q96EM0 [UniParc]. Last modified May 18, 2010. Version 2. Checksum: D279EE0B7C679969	FASTA	354	38,138
	10 20 30 40 50 60 MESALAVPRL PPHDPGTPVL SVVDMHTGGE PLRIVLAGCP EVSGPTLLAK RRYMRQHLDH 70 80 90 100 110 120 VRRRLMFEPR GHRDMYGAVL VPSELPDAHL GVLFLHNEGY SSMCGHAVLA LGRFALDFGL 130 140 150 160 170 180 VPAPPAGTRE ARVNIHCPCG LVTAFVACED GRSHGPVRFH SVPAFVLATD LMVDVPGHGK 190 200 210 220 230 240 VMVDIAYGGA FYAFVTAEKL GLDICSAKTR DLVDAASAVT EAVKAQFKIN HPDSEDLAFL 250 260 270 280 290 300 YGTILTDGKD AYTKEPTTNI CVFADEQVDR SPTGSGVTAR IALQYHKGLL ELNQMRAFKS 310 320 330 340 350 SATGSVFTGK AVREAKCGDF KAVIVEVSGQ AHYTGTASFI IEDDDPLRDG FLLK

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]. Tissue: Testis.
[2]	"The DNA sequence and analysis of human chromosome 14." Heilig R., Eckenberg R., Petit J.-L., Fonknechten N., Da Silva C., Cattolico L., Levy M., Barbe V., De Berardinis V., Ureta-Vidal A., Pelletier E., Vico V., Anthouard V., Rowen L., Madan A., Qin S., Sun H., Du H. , Pepin K., Artiguenave F., Robert C., Cruaud C., Bruels T., Jaillon O., Friedlander L., Samson G., Brottier P., Cure S., Segurens B., Aniere F., Samain S., Crespeau H., Abbasi N., Aiach N., Boscus D., Dickhoff R., Dors M., Dubois I., Friedman C., Gouyvenoux M., James R., Madan A., Mairey-Estrada B., Mangenot S., Martins N., Menard M., Oztas S., Ratcliffe A., Shaffer T., Trask B., Vacherie B., Bellemere C., Belser C., Besnard-Gonnet M., Bartol-Mavel D., Boutard M., Briez-Silla S., Combette S., Dufosse-Laurent V., Ferron C., Lechaplais C., Louesse C., Muselet D., Magdelenat G., Pateau E., Petit E., Sirvain-Trukniewicz P., Trybou A., Vega-Czarny N., Bataille E., Bluet E., Bordelais I., Dubois M., Dumont C., Guerin T., Haffray S., Hammadi R., Muanga J., Pellouin V., Robert D., Wunderle E., Gauguet G., Roy A., Sainte-Marthe L., Verdier J., Verdier-Discala C., Hillier L.W., Fulton L., McPherson J., Matsuda F., Wilson R., Scarpelli C., Gyapay G., Wincker P., Saurin W., Quetier F., Waterston R., Hood L., Weissenbach J. Nature 421:601-607(2003) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[3]	"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]. Tissue: Skin.
[4]	"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].
[5]	"Identification of a human trans-3-Hydroxy-L-proline dehydratase, the first characterized member of a novel family of proline racemase-like enzymes." Visser W.F., Verhoeven-Duif N.M., de Koning T.J. J. Biol. Chem. 287:21654-21662(2012) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, TISSUE SPECIFICITY, MUTAGENESIS OF THR-273.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AK058165 mRNA. Translation: BAB71696.1. AL159140 Genomic DNA. No translation available. BC012131 mRNA. Translation: AAH12131.1.
IPI	IPI00386591.
RefSeq	NP_653182.1. NM_144581.1.
UniGene	Hs.729061.
3D structure databases
HSSP	HSSP built from PDB template 1W61 based on UniProtKB Q4DA80.
ProteinModelPortal	Q96EM0.
SMR	Q96EM0. Positions 20-354.
ModBase	Search...
Protein-protein interaction databases
STRING	9606.ENSP00000247194.
PTM databases
PhosphoSite	Q96EM0.
Polymorphism databases
DMDM	296452868.
Proteomic databases
PaxDb	Q96EM0.
PRIDE	Q96EM0.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000247194; ENSP00000247194; ENSG00000126790.
GeneID	112849.
KEGG	hsa:112849.
UCSC	uc001xee.1. human.
Organism-specific databases
CTD	112849.
GeneCards	GC14M059928.
HGNC	HGNC:20488. L3HYPDH.
MIM	614811. gene.
neXtProt	NX_Q96EM0.
PharmGKB	PA134961537.
GenAtlas	Search...
Phylogenomic databases
eggNOG	COG3938.
HOGENOM	HOG000084336.
HOVERGEN	HBG057443.
InParanoid	Q96EM0.
OMA	LERRAYC.
OrthoDB	EOG4WWRJW.
PhylomeDB	Q96EM0.
Gene expression databases
ArrayExpress	Q96EM0.
Bgee	Q96EM0.
CleanEx	HS_C14orf149.
Genevestigator	Q96EM0.
Family and domain databases
InterPro	IPR008794. Pro_racemase. [Graphical view]
Pfam	PF05544. Pro_racemase. 1 hit. [Graphical view]
PIRSF	PIRSF029792. Pro_racemase. 1 hit.
ProtoNet	Search...
Other
DrugBank	DB00172. L-Proline.
GenomeRNAi	112849.
NextBio	78685.
SOURCE	Search...

Entry information

Entry name

T3HPD_HUMAN

Accession

Primary (citable) accession number: Q96EM0
Secondary accession number(s): Q96LJ5

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 29, 2007
Last sequence update:	May 18, 2010
Last modified:	May 1, 2013
This is version 75 of the entry and version 2 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.