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Q96EM0 (T3HPD_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 85. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length354 AA.
Sequence statusComplete.
Protein existenceEvidence 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 diversityPolymorphism
   Molecular functionLyase
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processmetabolic process

Inferred from direct assay Ref.5. Source: UniProtKB

   Molecular_functionhydro-lyase activity

Inferred from direct assay Ref.5. Source: UniProtKB

trans-L-3-hydroxyproline dehydratase activity

Inferred from electronic annotation. Source: UniProtKB-EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 354354Trans-L-3-hydroxyproline dehydratase
PRO_0000288949

Regions

Region105 – 1062Substrate binding By similarity
Region274 – 2752Substrate binding By similarity

Sites

Active site1041Proton acceptor By similarity
Binding site2691Substrate By similarity

Natural variations

Natural variant421V → A.
Corresponds to variant rs17096291 [ dbSNP | Ensembl ].
VAR_032540
Natural variant1251P → S.
Corresponds to variant rs35622288 [ dbSNP | Ensembl ].
VAR_062192
Natural variant3151A → V.
Corresponds to variant rs1046701 [ dbSNP | Ensembl ].
VAR_032541
Natural variant3411I → V.
Corresponds to variant rs8660 [ dbSNP | Ensembl ].
VAR_032542

Experimental info

Mutagenesis2731T → C: Restores racemase activity and catalyzes racemization of L-proline to D-proline at low level. Ref.5
Sequence conflict91R → W in AAH12131. Ref.3

Sequences

Sequence LengthMass (Da)Tools
Q96EM0 [UniParc].

Last modified May 18, 2010. Version 2.
Checksum: D279EE0B7C679969

FASTA35438,138
        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 

« Hide

References

« Hide '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. expand/collapse author list , 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. expand/collapse author list , 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.
CCDSCCDS9739.1.
RefSeqNP_653182.1. NM_144581.1.
UniGeneHs.729061.

3D structure databases

ProteinModelPortalQ96EM0.
SMRQ96EM0. Positions 20-354.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid125210. 1 interaction.
STRING9606.ENSP00000247194.

Chemistry

DrugBankDB00172. L-Proline.

PTM databases

PhosphoSiteQ96EM0.

Polymorphism databases

DMDM296452868.

Proteomic databases

MaxQBQ96EM0.
PaxDbQ96EM0.
PRIDEQ96EM0.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000247194; ENSP00000247194; ENSG00000126790.
GeneID112849.
KEGGhsa:112849.
UCSCuc001xee.1. human.

Organism-specific databases

CTD112849.
GeneCardsGC14M059928.
HGNCHGNC:20488. L3HYPDH.
HPAHPA056694.
MIM614811. gene.
neXtProtNX_Q96EM0.
PharmGKBPA134961537.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG3938.
HOGENOMHOG000084336.
HOVERGENHBG057443.
InParanoidQ96EM0.
OMAFVACEGG.
OrthoDBEOG75F4DB.
PhylomeDBQ96EM0.
TreeFamTF329167.

Gene expression databases

ArrayExpressQ96EM0.
BgeeQ96EM0.
CleanExHS_C14orf149.
GenevestigatorQ96EM0.

Family and domain databases

InterProIPR008794. Pro_racemase_fam.
[Graphical view]
PfamPF05544. Pro_racemase. 1 hit.
[Graphical view]
PIRSFPIRSF029792. Pro_racemase. 1 hit.
ProtoNetSearch...

Other

GenomeRNAi112849.
NextBio78685.
PROQ96EM0.
SOURCESearch...

Entry information

Entry nameT3HPD_HUMAN
AccessionPrimary (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: July 9, 2014
This is version 85 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny 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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 14

Human chromosome 14: entries, gene names and cross-references to MIM