Q9WU79 (PROD_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Proline dehydrogenase 1, mitochondrial
EC=1.5.99.8

Alternative name(s):
Proline oxidase

Gene names

Name:	Prodh
Synonyms:	Pro1

Organism

Mus musculus (Mouse)

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length	599 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at transcript level

General annotation (Comments)

Function	Converts proline to delta-1-pyrroline-5-carboxylate.
Catalytic activity	L-proline + acceptor = (S)-1-pyrroline-5-carboxylate + reduced acceptor.
Cofactor	FAD.
Pathway	Amino-acid degradation; L-proline degradation into L-glutamate; L-glutamate from L-proline: step 1/2.
Subcellular location	Mitochondrion matrix.
Tissue specificity	Expressed in liver, kidney, heart and to a lesser extent in brain, lung and muscle.
Involvement in disease	Note=Pro/re mice that have a premature termination on Prodh are sluggish in their movement.
Sequence similarities	Belongs to the proline oxidase family.
Sequence caution	The sequence AAD24776.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended. The sequence AAI25328.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended. The sequence EDK97501.1 differs from that shown. Reason: Erroneous gene model prediction.

Ontologies

Keywords
Biological process	Proline metabolism
Cellular component	Mitochondrion
Domain	Transit peptide
Ligand	FAD Flavoprotein
Molecular function	Oxidoreductase
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	glutamate biosynthetic process Inferred from electronic annotation. Source: InterPro proline catabolic process Inferred from electronic annotation. Source: InterPro
Cellular component	mitochondrial inner membrane Inferred from direct assay. Source: MGI mitochondrial matrix Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	proline dehydrogenase 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
	Transit peptide	1 – ?		Mitochondrion Potential
	Chain	? – 599		Proline dehydrogenase 1, mitochondrial		PRO_0000025801
Experimental info
	Sequence conflict	7 – 8	2	FL → HE in AAF21467. Ref.5
	Sequence conflict	303	1	E → V in BAE25683. Ref.1
	Sequence conflict	379	1	D → G in BAE25683. Ref.1
	Sequence conflict	436	1	F → S in AAD24776. Ref.4
	Sequence conflict	443	1	G → R in AAD24776. Ref.4

Sequences

	Sequence		Length	Mass (Da)
	Q9WU79 [UniParc]. Last modified April 5, 2011. Version 2. Checksum: 528AA436920CE5DD	FASTA	599	68,036
	10 20 30 40 50 60 MALKRVFLLR SVAPRVAALS TKPQAQEQPP ASPEALRGCG AAKAVRPPVP AVDFTNTQEA 70 80 90 100 110 120 YRSRRSWELV RNLLVLRLCA SPVLLAHHEQ LFQVARKLLG QRMFERLMKM TFYGHFVAGE 130 140 150 160 170 180 DQESIRPLIR HNKAFGVGFI LDYGVEEDLS PEEAERKEME SCTSEAERDG SGANKREKQY 190 200 210 220 230 240 QVHPAFGDRR DGVISARTYF YANEAKCDNY MENLLQCIKA SGGASDGGFS AIKLTALGRP 250 260 270 280 290 300 QFLLQFSDVL TRWRRFFHQM AAEQGQAGRA AVDTKLEVAV LQDSIAKMGI ASRAEIEGWF 310 320 330 340 350 360 TPETLGVSGT VDLLDWNSLI DSRTRLSRHL VVPNVQTGQL EPLLSRFTEE EEQQMKRMLQ 370 380 390 400 410 420 RMDVLAKKAK EAGVRLMIDA EQSYFQPAIS RLTLEMQRRF NVDKPFIFNT FQCYLKDAYD 430 440 450 460 470 480 NVTLDMELAR REGWCFGAKL VRGAYMAQER VRAAEIGYED PINPTYEATN AMYHRCLNYV 490 500 510 520 530 540 LEELKHSTKA EVMVASHNED TVHFTLCRMK EIGLHPADGQ VCFGQLLGMC DQISFPLGQA 550 560 570 580 590 GFPVYKYVPY GPVMEVLPYL SRRALENSSI MKGAQRERQL LWQELRRRLR TGSLFHHPA

References

	« Hide 'large scale' referencesShow 'large scale' references »
[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: 16141072] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: C57BL/6J. Tissue: Kidney.
[2]	"Lineage-specific biology revealed by a finished genome assembly of the mouse." Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S. , Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K., Eichler E.E., Ponting C.P. PLoS Biol. 7:E1000112-E1000112(2009) [PubMed: 19468303] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: C57BL/6.
[3]	Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C. Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[4]	"The gene encoding proline dehydrogenase modulates sensorimotor gating in mice." Gogos J.A., Santha M., Takacs Z., Beck K.D., Luine V., Lucas L.R., Nadler J.V., Karayiorgou M. Nat. Genet. 21:434-439(1999) [PubMed: 10192398] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 5-599. Strain: C57BL/6 and PRO/Re. Tissue: Cerebellum.
[5]	Lin W.-W., Hu C.A., Valle D. Submitted (NOV-1996) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 7-599.
[6]	"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: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 56-599. Tissue: Brain.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AK144068 mRNA. Translation: BAE25683.1. AC087064 Genomic DNA. No translation available. CH466521 Genomic DNA. Translation: EDK97501.1. Sequence problems. AF120279 mRNA. Translation: AAD24776.1. Different initiation. U80020 mRNA. Translation: AAF21467.1. BC125327 mRNA. Translation: AAI25328.1. Different initiation.
IPI	IPI00322760.
RefSeq	NP_035302.2. NM_011172.2.
UniGene	Mm.28456.
3D structure databases
ProteinModelPortal	Q9WU79.
ModBase	Search...
Protein-protein interaction databases
STRING	Q9WU79.
PTM databases
PhosphoSite	Q9WU79.
Proteomic databases
PRIDE	Q9WU79.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENSMUST00000003620; ENSMUSP00000003620; ENSMUSG00000003526. ENSMUST00000136776; ENSMUSP00000117597; ENSMUSG00000003526.
GeneID	19125.
KEGG	mmu:19125.
Organism-specific databases
CTD	5625.
MGI	MGI:97770. Prodh.
Phylogenomic databases
GeneTree	ENSGT00390000006265.
HOVERGEN	HBG008262.
InParanoid	Q9WU79.
OMA	YASEAKC.
OrthoDB	EOG41G35C.
Gene expression databases
ArrayExpress	Q9WU79.
Bgee	Q9WU79.
CleanEx	MM_PRODH.
Genevestigator	Q9WU79.
GermOnline	ENSMUSG00000003526. Mus musculus.
Family and domain databases
InterPro	IPR002872. Proline_DH. IPR015659. Proline_oxidase. [Graphical view]
KO	K00318.
PANTHER	PTHR13914. Proline_oxidase. 1 hit.
Pfam	PF01619. Pro_dh. 1 hit. [Graphical view]
ProtoNet	Search...
Other
SOURCE	Search...

Entry information

Entry name

PROD_MOUSE

Accession

Primary (citable) accession number: Q9WU79
Secondary accession number(s): A0JLW6, Q3UNR4, Q9QX61

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 30, 2000
Last sequence update:	April 5, 2011
Last modified:	November 16, 2011
This is version 76 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program