PROD_MOUSE
ID PROD_MOUSE Reviewed; 599 AA.
AC Q9WU79; A0JLW6; Q3UNR4; Q9QX61;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 05-APR-2011, sequence version 2.
DT 03-AUG-2022, entry version 145.
DE RecName: Full=Proline dehydrogenase 1, mitochondrial;
DE EC=1.5.5.2;
DE AltName: Full=Proline oxidase;
DE Flags: Precursor;
GN Name=Prodh; Synonyms=Pro1;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Kidney;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 5-599.
RC STRAIN=C57BL/6J, and PRO/Re; TISSUE=Cerebellum;
RX PubMed=10192398; DOI=10.1038/7777;
RA Gogos J.A., Santha M., Takacs Z., Beck K.D., Luine V., Lucas L.R.,
RA Nadler J.V., Karayiorgou M.;
RT "The gene encoding proline dehydrogenase modulates sensorimotor gating in
RT mice.";
RL Nat. Genet. 21:434-439(1999).
RN [5]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 7-599.
RA Lin W.-W., Hu C.A., Valle D.;
RL Submitted (NOV-1996) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 56-599.
RC TISSUE=Brain;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [7]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, and Lung;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [8]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-356; LYS-367 AND LYS-485, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=23576753; DOI=10.1073/pnas.1302961110;
RA Rardin M.J., Newman J.C., Held J.M., Cusack M.P., Sorensen D.J., Li B.,
RA Schilling B., Mooney S.D., Kahn C.R., Verdin E., Gibson B.W.;
RT "Label-free quantitative proteomics of the lysine acetylome in mitochondria
RT identifies substrates of SIRT3 in metabolic pathways.";
RL Proc. Natl. Acad. Sci. U.S.A. 110:6601-6606(2013).
CC -!- FUNCTION: Converts proline to delta-1-pyrroline-5-carboxylate.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a quinone + L-proline = (S)-1-pyrroline-5-carboxylate + a
CC quinol + H(+); Xref=Rhea:RHEA:23784, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:17388, ChEBI:CHEBI:24646, ChEBI:CHEBI:60039,
CC ChEBI:CHEBI:132124; EC=1.5.5.2;
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC -!- PATHWAY: Amino-acid degradation; L-proline degradation into L-
CC glutamate; L-glutamate from L-proline: step 1/2.
CC -!- SUBCELLULAR LOCATION: Mitochondrion matrix.
CC -!- TISSUE SPECIFICITY: Expressed in liver, kidney, heart and to a lesser
CC extent in brain, lung and muscle.
CC -!- DISEASE: Note=Pro/re mice that have a premature termination on Prodh
CC are sluggish in their movement.
CC -!- SIMILARITY: Belongs to the proline oxidase family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAD24776.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=AAI25328.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=EDK97501.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AK144068; BAE25683.1; -; mRNA.
DR EMBL; AC087064; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH466521; EDK97501.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AF120279; AAD24776.1; ALT_INIT; mRNA.
DR EMBL; U80020; AAF21467.1; -; mRNA.
DR EMBL; BC125327; AAI25328.1; ALT_INIT; mRNA.
DR CCDS; CCDS37278.1; -.
DR RefSeq; NP_035302.2; NM_011172.2.
DR AlphaFoldDB; Q9WU79; -.
DR STRING; 10090.ENSMUSP00000003620; -.
DR iPTMnet; Q9WU79; -.
DR PhosphoSitePlus; Q9WU79; -.
DR SwissPalm; Q9WU79; -.
DR EPD; Q9WU79; -.
DR jPOST; Q9WU79; -.
DR MaxQB; Q9WU79; -.
DR PaxDb; Q9WU79; -.
DR PeptideAtlas; Q9WU79; -.
DR PRIDE; Q9WU79; -.
DR ProteomicsDB; 289843; -.
DR DNASU; 19125; -.
DR Ensembl; ENSMUST00000003620; ENSMUSP00000003620; ENSMUSG00000003526.
DR GeneID; 19125; -.
DR KEGG; mmu:19125; -.
DR UCSC; uc007ymu.1; mouse.
DR CTD; 5625; -.
DR MGI; MGI:97770; Prodh.
DR VEuPathDB; HostDB:ENSMUSG00000003526; -.
DR eggNOG; KOG0186; Eukaryota.
DR GeneTree; ENSGT00390000006265; -.
DR InParanoid; Q9WU79; -.
DR OMA; YLNEASC; -.
DR OrthoDB; 948528at2759; -.
DR PhylomeDB; Q9WU79; -.
DR TreeFam; TF313544; -.
DR BRENDA; 1.5.5.2; 3474.
DR Reactome; R-MMU-70688; Proline catabolism.
DR UniPathway; UPA00261; UER00373.
DR BioGRID-ORCS; 19125; 4 hits in 72 CRISPR screens.
DR ChiTaRS; Prodh; mouse.
DR PRO; PR:Q9WU79; -.
DR Proteomes; UP000000589; Chromosome 16.
DR RNAct; Q9WU79; protein.
DR Bgee; ENSMUSG00000003526; Expressed in adult mammalian kidney and 72 other tissues.
DR ExpressionAtlas; Q9WU79; baseline and differential.
DR Genevisible; Q9WU79; MM.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; ISO:MGI.
DR GO; GO:0005743; C:mitochondrial inner membrane; HDA:MGI.
DR GO; GO:0005759; C:mitochondrial matrix; IEA:UniProtKB-SubCell.
DR GO; GO:0005739; C:mitochondrion; IDA:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0016597; F:amino acid binding; ISO:MGI.
DR GO; GO:0071949; F:FAD binding; ISS:UniProtKB.
DR GO; GO:0004657; F:proline dehydrogenase activity; ISS:UniProtKB.
DR GO; GO:0010942; P:positive regulation of cell death; ISO:MGI.
DR GO; GO:0010133; P:proline catabolic process to glutamate; IBA:GO_Central.
DR InterPro; IPR029041; FAD-linked_oxidoreductase-like.
DR InterPro; IPR002872; Proline_DH_dom.
DR InterPro; IPR015659; Proline_oxidase.
DR PANTHER; PTHR13914; PTHR13914; 1.
DR Pfam; PF01619; Pro_dh; 1.
DR SUPFAM; SSF51730; SSF51730; 1.
PE 1: Evidence at protein level;
KW Acetylation; FAD; Flavoprotein; Mitochondrion; Oxidoreductase;
KW Proline metabolism; Reference proteome; Transit peptide.
FT TRANSIT 1..?
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN ?..599
FT /note="Proline dehydrogenase 1, mitochondrial"
FT /id="PRO_0000025801"
FT REGION 20..39
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 152..180
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 356
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:23576753"
FT MOD_RES 367
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:23576753"
FT MOD_RES 485
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:23576753"
FT CONFLICT 7..8
FT /note="FL -> HE (in Ref. 5; AAF21467)"
FT /evidence="ECO:0000305"
FT CONFLICT 303
FT /note="E -> V (in Ref. 1; BAE25683)"
FT /evidence="ECO:0000305"
FT CONFLICT 379
FT /note="D -> G (in Ref. 1; BAE25683)"
FT /evidence="ECO:0000305"
FT CONFLICT 436
FT /note="F -> S (in Ref. 4; AAD24776)"
FT /evidence="ECO:0000305"
FT CONFLICT 443
FT /note="G -> R (in Ref. 4; AAD24776)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 599 AA; 68036 MW; 528AA436920CE5DD CRC64;
MALKRVFLLR SVAPRVAALS TKPQAQEQPP ASPEALRGCG AAKAVRPPVP AVDFTNTQEA
YRSRRSWELV RNLLVLRLCA SPVLLAHHEQ LFQVARKLLG QRMFERLMKM TFYGHFVAGE
DQESIRPLIR HNKAFGVGFI LDYGVEEDLS PEEAERKEME SCTSEAERDG SGANKREKQY
QVHPAFGDRR DGVISARTYF YANEAKCDNY MENLLQCIKA SGGASDGGFS AIKLTALGRP
QFLLQFSDVL TRWRRFFHQM AAEQGQAGRA AVDTKLEVAV LQDSIAKMGI ASRAEIEGWF
TPETLGVSGT VDLLDWNSLI DSRTRLSRHL VVPNVQTGQL EPLLSRFTEE EEQQMKRMLQ
RMDVLAKKAK EAGVRLMIDA EQSYFQPAIS RLTLEMQRRF NVDKPFIFNT FQCYLKDAYD
NVTLDMELAR REGWCFGAKL VRGAYMAQER VRAAEIGYED PINPTYEATN AMYHRCLNYV
LEELKHSTKA EVMVASHNED TVHFTLCRMK EIGLHPADGQ VCFGQLLGMC DQISFPLGQA
GFPVYKYVPY GPVMEVLPYL SRRALENSSI MKGAQRERQL LWQELRRRLR TGSLFHHPA
