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Protein

Probable proline dehydrogenase 2

Gene

Prodh2

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Converts proline to delta-1-pyrroline-5-carboxylate.Curated

Catalytic activityi

L-proline + a quinone = (S)-1-pyrroline-5-carboxylate + a quinol.

Cofactori

FADBy similarity

Pathwayi: L-proline degradation into L-glutamate

This protein is involved in step 1 of the subpathway that synthesizes L-glutamate from L-proline.
Proteins known to be involved in the 2 steps of the subpathway in this organism are:
  1. Probable proline dehydrogenase 2 (Prodh2), Proline dehydrogenase 1, mitochondrial (Prodh)
  2. Delta-1-pyrroline-5-carboxylate dehydrogenase, mitochondrial (Aldh4a1)
This subpathway is part of the pathway L-proline degradation into L-glutamate, which is itself part of Amino-acid degradation.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes L-glutamate from L-proline, the pathway L-proline degradation into L-glutamate and in Amino-acid degradation.

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Biological processi

Proline metabolism

Keywords - Ligandi

FAD, Flavoprotein

Enzyme and pathway databases

UniPathwayiUPA00261; UER00373.

Names & Taxonomyi

Protein namesi
Recommended name:
Probable proline dehydrogenase 2 (EC:1.5.5.2)
Alternative name(s):
Kidney and liver proline oxidase 1
MmPOX1
Probable proline oxidase 2
Proline oxidase-like protein
Short name:
PO
Short name:
Proline oxidase
Gene namesi
Name:Prodh2
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 7

Organism-specific databases

MGIiMGI:1929093. Prodh2.

Subcellular locationi

GO - Cellular componenti

  • mitochondrial inner membrane Source: MGI
  • mitochondrion Source: MGI
Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 456456Probable proline dehydrogenase 2PRO_0000308624Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei310 – 3101N6-acetyllysineCombined sources
Modified residuei320 – 3201N6-acetyllysineCombined sources

Keywords - PTMi

Acetylation

Proteomic databases

MaxQBiQ8VCZ9.
PaxDbiQ8VCZ9.
PRIDEiQ8VCZ9.

PTM databases

iPTMnetiQ8VCZ9.
PhosphoSiteiQ8VCZ9.
SwissPalmiQ8VCZ9.

Expressioni

Developmental stagei

Expressed in liver at E14. Expression level increases at P5 and decreases after P21.1 Publication

Inductioni

In liver, by TCF1 and HNF4A.1 Publication

Gene expression databases

BgeeiQ8VCZ9.
CleanExiMM_PRODH2.
ExpressionAtlasiQ8VCZ9. baseline and differential.
GenevisibleiQ8VCZ9. MM.

Interactioni

Protein-protein interaction databases

IntActiQ8VCZ9. 1 interaction.
MINTiMINT-4119643.
STRINGi10090.ENSMUSP00000062214.

Structurei

3D structure databases

ProteinModelPortaliQ8VCZ9.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the proline oxidase family.Curated

Phylogenomic databases

eggNOGiKOG0186. Eukaryota.
COG0506. LUCA.
GeneTreeiENSGT00390000006265.
HOGENOMiHOG000233406.
HOVERGENiHBG108294.
InParanoidiQ8VCZ9.
KOiK11394.
OMAiTGNILMQ.
OrthoDBiEOG7RZ5Q2.
PhylomeDBiQ8VCZ9.
TreeFamiTF313544.

Family and domain databases

Gene3Di3.20.20.220. 2 hits.
InterProiIPR029041. FAD-linked_oxidoreductase-like.
IPR002872. Proline_DH_dom.
IPR015659. Proline_oxidase.
[Graphical view]
PANTHERiPTHR13914. PTHR13914. 1 hit.
PfamiPF01619. Pro_dh. 1 hit.
[Graphical view]
SUPFAMiSSF51730. SSF51730. 2 hits.

Sequencei

Sequence statusi: Complete.

Q8VCZ9-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MIWTRLPLYG PSKPSTGGWQ PLRFDGGAFH VKGTAELARA LLVLRLCAWP
60 70 80 90 100
PLVTHGLAFQ AWSQRLLGSR LSGALLRASI YGQFVAGETA EEVRNCVGQL
110 120 130 140 150
QALGLQPLLA VPTEEEPDST AKTSEVWYEE NLSAMLRCVD LSRALVDAHG
160 170 180 190 200
PARNSLMQLK VTALASTRLC KELSAWIQRP RGSSELSPER LAEAMDSGRN
210 220 230 240 250
LQLSCLSTEQ NQHLQASLSR LHRVAQHARA KCVRLLVDAE YTFINPALSL
260 270 280 290 300
LVAALAVRWN SPEEGGPWVW NTYQAYLKDT HQRLEQDAEA AHKAGLAFGV
310 320 330 340 350
KLVRGAYLDK ERSMTQLQGK EDCTQPDYEA TSRSYSRCLE LMLRCVSNHG
360 370 380 390 400
PPCHLMVASH NEESVRQATK RMWELGIPLD GPVCFGQLLG MCDHVSLALG
410 420 430 440 450
QAGYMVYKSI PYGCLEEVIP YLIRRAQENR SVLQGARREQ ALLSQELWRR

LLGRTA
Length:456
Mass (Da):50,723
Last modified:March 1, 2002 - v1
Checksum:iCD02C1474AADBD56
GO

Sequence cautioni

The sequence AAF21466.1 differs from that shown. Reason: Erroneous initiation. Curated
The sequence AAQ13907.1 differs from that shown. Reason: Erroneous initiation. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti337 – 3371R → H in AAF21466 (Ref. 1) Curated
Sequence conflicti416 – 4161E → K in AAF21466 (Ref. 1) Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U80019 mRNA. Translation: AAF21466.1. Different initiation.
AF222851 mRNA. Translation: AAQ13907.1. Different initiation.
AK050141 mRNA. Translation: BAC34090.1.
BC018182 mRNA. Translation: AAH18182.1.
CCDSiCCDS21093.1.
RefSeqiNP_062419.2. NM_019546.5.
UniGeneiMm.270525.

Genome annotation databases

EnsembliENSMUST00000058280; ENSMUSP00000062214; ENSMUSG00000036892.
GeneIDi56189.
KEGGimmu:56189.
UCSCiuc009geo.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U80019 mRNA. Translation: AAF21466.1. Different initiation.
AF222851 mRNA. Translation: AAQ13907.1. Different initiation.
AK050141 mRNA. Translation: BAC34090.1.
BC018182 mRNA. Translation: AAH18182.1.
CCDSiCCDS21093.1.
RefSeqiNP_062419.2. NM_019546.5.
UniGeneiMm.270525.

3D structure databases

ProteinModelPortaliQ8VCZ9.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiQ8VCZ9. 1 interaction.
MINTiMINT-4119643.
STRINGi10090.ENSMUSP00000062214.

PTM databases

iPTMnetiQ8VCZ9.
PhosphoSiteiQ8VCZ9.
SwissPalmiQ8VCZ9.

Proteomic databases

MaxQBiQ8VCZ9.
PaxDbiQ8VCZ9.
PRIDEiQ8VCZ9.

Protocols and materials databases

DNASUi56189.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000058280; ENSMUSP00000062214; ENSMUSG00000036892.
GeneIDi56189.
KEGGimmu:56189.
UCSCiuc009geo.1. mouse.

Organism-specific databases

CTDi58510.
MGIiMGI:1929093. Prodh2.

Phylogenomic databases

eggNOGiKOG0186. Eukaryota.
COG0506. LUCA.
GeneTreeiENSGT00390000006265.
HOGENOMiHOG000233406.
HOVERGENiHBG108294.
InParanoidiQ8VCZ9.
KOiK11394.
OMAiTGNILMQ.
OrthoDBiEOG7RZ5Q2.
PhylomeDBiQ8VCZ9.
TreeFamiTF313544.

Enzyme and pathway databases

UniPathwayiUPA00261; UER00373.

Miscellaneous databases

PROiQ8VCZ9.
SOURCEiSearch...

Gene expression databases

BgeeiQ8VCZ9.
CleanExiMM_PRODH2.
ExpressionAtlasiQ8VCZ9. baseline and differential.
GenevisibleiQ8VCZ9. MM.

Family and domain databases

Gene3Di3.20.20.220. 2 hits.
InterProiIPR029041. FAD-linked_oxidoreductase-like.
IPR002872. Proline_DH_dom.
IPR015659. Proline_oxidase.
[Graphical view]
PANTHERiPTHR13914. PTHR13914. 1 hit.
PfamiPF01619. Pro_dh. 1 hit.
[Graphical view]
SUPFAMiSSF51730. SSF51730. 2 hits.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. Lin W.-W., Hu C.A., Valle D.
    Submitted (NOV-1996) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  2. Yang Q., Tian Y., Wallner E.I., Kanwar Y.S.
    Submitted (JAN-2000) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  3. "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: Liver.
  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].
    Strain: FVB/N.
    Tissue: Liver.
  5. "Hepatocyte nuclear factors 1alpha and 4alpha control expression of proline oxidase in adult liver."
    Kamiya A., Inoue Y., Kodama T., Gonzalez F.J.
    FEBS Lett. 578:63-68(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: INDUCTION BY TCF1 AND HNF4A, DEVELOPMENTAL STAGE.
  6. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Kidney and Liver.
  7. "Label-free quantitative proteomics of the lysine acetylome in mitochondria identifies substrates of SIRT3 in metabolic pathways."
    Rardin M.J., Newman J.C., Held J.M., Cusack M.P., Sorensen D.J., Li B., Schilling B., Mooney S.D., Kahn C.R., Verdin E., Gibson B.W.
    Proc. Natl. Acad. Sci. U.S.A. 110:6601-6606(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-310 AND LYS-320, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.

Entry informationi

Entry nameiPROD2_MOUSE
AccessioniPrimary (citable) accession number: Q8VCZ9
Secondary accession number(s): Q2V058, Q9QX62
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 23, 2007
Last sequence update: March 1, 2002
Last modified: June 8, 2016
This is version 96 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. 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.