SubmitCancel

Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

Q96EM0

- T3HPD_HUMAN

UniProt

Q96EM0 - T3HPD_HUMAN

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein
Trans-L-3-hydroxyproline dehydratase
Gene
L3HYPDH, C14orf149
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

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.1 Publication

Catalytic activityi

Trans-3-hydroxy-L-proline = 1-pyrroline 2-carboxylate + H2O.1 Publication

Kineticsi

  1. KM=7.23 mM for trans-3-hydroxy-L-proline1 Publication

Vmax=39.5 µmol/min/mg enzyme

pH dependencei

Optimum pH is 8.0.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei104 – 1041Proton acceptor By similarity
Binding sitei269 – 2691Substrate By similarity

GO - Molecular functioni

  1. hydro-lyase activity Source: UniProtKB
  2. trans-L-3-hydroxyproline dehydratase activity Source: UniProtKB-EC

GO - Biological processi

  1. metabolic process Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Lyase

Names & Taxonomyi

Protein namesi
Recommended name:
Trans-L-3-hydroxyproline dehydratase (EC:4.2.1.77)
Alternative name(s):
Trans-3-hydroxy-l-proline dehydratase
Gene namesi
Name:L3HYPDH
Synonyms:C14orf149
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 14

Organism-specific databases

HGNCiHGNC:20488. L3HYPDH.

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi273 – 2731T → C: Restores racemase activity and catalyzes racemization of L-proline to D-proline at low level. 1 Publication

Organism-specific databases

PharmGKBiPA134961537.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 354354Trans-L-3-hydroxyproline dehydratase
PRO_0000288949Add
BLAST

Proteomic databases

MaxQBiQ96EM0.
PaxDbiQ96EM0.
PRIDEiQ96EM0.

PTM databases

PhosphoSiteiQ96EM0.

Expressioni

Tissue specificityi

Ubiquitously expressed.1 Publication

Gene expression databases

ArrayExpressiQ96EM0.
BgeeiQ96EM0.
CleanExiHS_C14orf149.
GenevestigatoriQ96EM0.

Organism-specific databases

HPAiHPA056694.

Interactioni

Subunit structurei

Homodimer By similarity.

Protein-protein interaction databases

BioGridi125210. 1 interaction.
STRINGi9606.ENSP00000247194.

Structurei

3D structure databases

ProteinModelPortaliQ96EM0.
SMRiQ96EM0. Positions 20-354.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni105 – 1062Substrate binding By similarity
Regioni274 – 2752Substrate binding By similarity

Sequence similaritiesi

Belongs to the proline racemase family.

Phylogenomic databases

eggNOGiCOG3938.
HOGENOMiHOG000084336.
HOVERGENiHBG057443.
InParanoidiQ96EM0.
OMAiFVACEGG.
OrthoDBiEOG75F4DB.
PhylomeDBiQ96EM0.
TreeFamiTF329167.

Family and domain databases

InterProiIPR008794. Pro_racemase_fam.
[Graphical view]
PfamiPF05544. Pro_racemase. 1 hit.
[Graphical view]
PIRSFiPIRSF029792. Pro_racemase. 1 hit.

Sequencei

Sequence statusi: Complete.

Q96EM0-1 [UniParc]FASTAAdd to Basket

« Hide

MESALAVPRL PPHDPGTPVL SVVDMHTGGE PLRIVLAGCP EVSGPTLLAK    50
RRYMRQHLDH VRRRLMFEPR GHRDMYGAVL VPSELPDAHL GVLFLHNEGY 100
SSMCGHAVLA LGRFALDFGL VPAPPAGTRE ARVNIHCPCG LVTAFVACED 150
GRSHGPVRFH SVPAFVLATD LMVDVPGHGK VMVDIAYGGA FYAFVTAEKL 200
GLDICSAKTR DLVDAASAVT EAVKAQFKIN HPDSEDLAFL YGTILTDGKD 250
AYTKEPTTNI CVFADEQVDR SPTGSGVTAR IALQYHKGLL ELNQMRAFKS 300
SATGSVFTGK AVREAKCGDF KAVIVEVSGQ AHYTGTASFI IEDDDPLRDG 350
FLLK 354
Length:354
Mass (Da):38,138
Last modified:May 18, 2010 - v2
Checksum:iD279EE0B7C679969
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti42 – 421V → A.
Corresponds to variant rs17096291 [ dbSNP | Ensembl ].
VAR_032540
Natural varianti125 – 1251P → S.
Corresponds to variant rs35622288 [ dbSNP | Ensembl ].
VAR_062192
Natural varianti315 – 3151A → V.
Corresponds to variant rs1046701 [ dbSNP | Ensembl ].
VAR_032541
Natural varianti341 – 3411I → V.
Corresponds to variant rs8660 [ dbSNP | Ensembl ].
VAR_032542

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti9 – 91R → W in AAH12131. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AK058165 mRNA. Translation: BAB71696.1.
AL159140 Genomic DNA. No translation available.
BC012131 mRNA. Translation: AAH12131.1.
CCDSiCCDS9739.1.
RefSeqiNP_653182.1. NM_144581.1.
UniGeneiHs.729061.

Genome annotation databases

EnsembliENST00000247194; ENSP00000247194; ENSG00000126790.
GeneIDi112849.
KEGGihsa:112849.
UCSCiuc001xee.1. human.

Polymorphism databases

DMDMi296452868.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AK058165 mRNA. Translation: BAB71696.1 .
AL159140 Genomic DNA. No translation available.
BC012131 mRNA. Translation: AAH12131.1 .
CCDSi CCDS9739.1.
RefSeqi NP_653182.1. NM_144581.1.
UniGenei Hs.729061.

3D structure databases

ProteinModelPortali Q96EM0.
SMRi Q96EM0. Positions 20-354.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 125210. 1 interaction.
STRINGi 9606.ENSP00000247194.

Chemistry

DrugBanki DB00172. L-Proline.

PTM databases

PhosphoSitei Q96EM0.

Polymorphism databases

DMDMi 296452868.

Proteomic databases

MaxQBi Q96EM0.
PaxDbi Q96EM0.
PRIDEi Q96EM0.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000247194 ; ENSP00000247194 ; ENSG00000126790 .
GeneIDi 112849.
KEGGi hsa:112849.
UCSCi uc001xee.1. human.

Organism-specific databases

CTDi 112849.
GeneCardsi GC14M059928.
HGNCi HGNC:20488. L3HYPDH.
HPAi HPA056694.
MIMi 614811. gene.
neXtProti NX_Q96EM0.
PharmGKBi PA134961537.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG3938.
HOGENOMi HOG000084336.
HOVERGENi HBG057443.
InParanoidi Q96EM0.
OMAi FVACEGG.
OrthoDBi EOG75F4DB.
PhylomeDBi Q96EM0.
TreeFami TF329167.

Miscellaneous databases

GenomeRNAii 112849.
NextBioi 78685.
PROi Q96EM0.
SOURCEi Search...

Gene expression databases

ArrayExpressi Q96EM0.
Bgeei Q96EM0.
CleanExi HS_C14orf149.
Genevestigatori Q96EM0.

Family and domain databases

InterProi IPR008794. Pro_racemase_fam.
[Graphical view ]
Pfami PF05544. Pro_racemase. 1 hit.
[Graphical view ]
PIRSFi PIRSF029792. Pro_racemase. 1 hit.
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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. 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.

Entry informationi

Entry nameiT3HPD_HUMAN
AccessioniPrimary (citable) accession number: Q96EM0
Secondary accession number(s): Q96LJ5
Entry historyi
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 statusiReviewed (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.

Miscellaneousi

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 (1 Publication).

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Human chromosome 14
    Human chromosome 14: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi