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Protein

Trans-L-3-hydroxyproline dehydratase

Gene

L3hypdh

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 3 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).1 Publication

Catalytic activityi

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

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei104 – 1041Proton acceptorBy similarity
Binding sitei269 – 2691SubstrateBy similarity

GO - Molecular functioni

  • hydro-lyase activity Source: UniProtKB
  • trans-L-3-hydroxyproline dehydratase activity Source: UniProtKB-EC

GO - Biological processi

  • 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
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 12

Organism-specific databases

MGIiMGI:1914467. L3hypdh.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 354354Trans-L-3-hydroxyproline dehydratasePRO_0000288950Add
BLAST

Proteomic databases

EPDiQ9CXA2.
MaxQBiQ9CXA2.
PaxDbiQ9CXA2.
PRIDEiQ9CXA2.

PTM databases

PhosphoSiteiQ9CXA2.

Expressioni

Gene expression databases

BgeeiQ9CXA2.
CleanExiMM_2810055F11RIK.
GenevisibleiQ9CXA2. MM.

Interactioni

Subunit structurei

Homodimer.By similarity

Protein-protein interaction databases

IntActiQ9CXA2. 1 interaction.
MINTiMINT-4123759.
STRINGi10090.ENSMUSP00000019862.

Structurei

3D structure databases

ProteinModelPortaliQ9CXA2.
SMRiQ9CXA2. Positions 19-354.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

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

Sequence similaritiesi

Belongs to the proline racemase family.Curated

Phylogenomic databases

eggNOGiENOG410IIC6. Eukaryota.
COG3938. LUCA.
GeneTreeiENSGT00390000002032.
HOGENOMiHOG000084336.
HOVERGENiHBG057443.
InParanoidiQ9CXA2.
KOiK18384.
OMAiARMAQWY.
OrthoDBiEOG75F4DB.
PhylomeDBiQ9CXA2.
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.

Q9CXA2-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MEAALAVTRL PPNDPRTPAL SVVDMHTGGE PLRIVHAGCP EVAGPTLLAK
60 70 80 90 100
RRYMRQHLDY IRRRLVFEPR GHRDMYGAIL VPSELPDAHL GVLFLHNEGY
110 120 130 140 150
SSMCGHAVLA LGRFALDFGL VPAPPKGARE AQVNIHCPCG LVTAFVECEG
160 170 180 190 200
GRSCGPVRFH SVPAFVLASD LTVDVPGHGK VLVDIAYGGA FYAFVSAEKL
210 220 230 240 250
GLDVCSAKTR DLVDAASALT GAVKAQFKIN HPESEDLGFL YGSILTDGKD
260 270 280 290 300
AYSEEATTNI CVFADEQVDR SPTGSGVTAR IALQYHKGLL QLNQTRAFKS
310 320 330 340 350
SATGSVFTGC AVREAKCGDF KAVIVEVAGQ AHYTGTANLT VEDGDPLRDG

FLLK
Length:354
Mass (Da):37,804
Last modified:June 1, 2001 - v1
Checksum:iB993BF8E7BFA3505
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti13 – 131N → H in AAH04753 (PubMed:15489334).Curated
Sequence conflicti15 – 151P → S in AAH04753 (PubMed:15489334).Curated
Sequence conflicti81 – 811V → M in AAH04753 (PubMed:15489334).Curated
Sequence conflicti126 – 1261K → E in AAH04753 (PubMed:15489334).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK018449 mRNA. Translation: BAB31217.1.
CR974486 Genomic DNA. Translation: CAX15363.1.
BC004753 mRNA. Translation: AAH04753.1.
CCDSiCCDS25966.1.
RefSeqiNP_080314.1. NM_026038.2.
UniGeneiMm.286120.

Genome annotation databases

EnsembliENSMUST00000019862; ENSMUSP00000019862; ENSMUSG00000019718.
GeneIDi67217.
KEGGimmu:67217.
UCSCiuc007nvd.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK018449 mRNA. Translation: BAB31217.1.
CR974486 Genomic DNA. Translation: CAX15363.1.
BC004753 mRNA. Translation: AAH04753.1.
CCDSiCCDS25966.1.
RefSeqiNP_080314.1. NM_026038.2.
UniGeneiMm.286120.

3D structure databases

ProteinModelPortaliQ9CXA2.
SMRiQ9CXA2. Positions 19-354.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiQ9CXA2. 1 interaction.
MINTiMINT-4123759.
STRINGi10090.ENSMUSP00000019862.

PTM databases

PhosphoSiteiQ9CXA2.

Proteomic databases

EPDiQ9CXA2.
MaxQBiQ9CXA2.
PaxDbiQ9CXA2.
PRIDEiQ9CXA2.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000019862; ENSMUSP00000019862; ENSMUSG00000019718.
GeneIDi67217.
KEGGimmu:67217.
UCSCiuc007nvd.1. mouse.

Organism-specific databases

CTDi112849.
MGIiMGI:1914467. L3hypdh.

Phylogenomic databases

eggNOGiENOG410IIC6. Eukaryota.
COG3938. LUCA.
GeneTreeiENSGT00390000002032.
HOGENOMiHOG000084336.
HOVERGENiHBG057443.
InParanoidiQ9CXA2.
KOiK18384.
OMAiARMAQWY.
OrthoDBiEOG75F4DB.
PhylomeDBiQ9CXA2.
TreeFamiTF329167.

Miscellaneous databases

PROiQ9CXA2.
SOURCEiSearch...

Gene expression databases

BgeeiQ9CXA2.
CleanExiMM_2810055F11RIK.
GenevisibleiQ9CXA2. MM.

Family and domain databases

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

Publicationsi

« Hide 'large scale' publications
  1. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: C57BL/6J.
    Tissue: Lung.
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: C57BL/6J.
  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].
    Strain: FVB/N.
    Tissue: Mammary tumor.
  4. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Brown adipose tissue, Heart, Kidney, Liver and Lung.
  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.

Entry informationi

Entry nameiT3HPD_MOUSE
AccessioniPrimary (citable) accession number: Q9CXA2
Secondary accession number(s): B8JJ82, Q99KB5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 29, 2007
Last sequence update: June 1, 2001
Last modified: June 8, 2016
This is version 88 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

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.By similarity

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.