PROD1_ARATH
ID PROD1_ARATH Reviewed; 499 AA.
AC P92983; P92945; Q8VXV1; Q944L2; Q96281;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 30-MAY-2000, sequence version 2.
DT 03-AUG-2022, entry version 154.
DE RecName: Full=Proline dehydrogenase 1, mitochondrial;
DE EC=1.5.5.2 {ECO:0000305|PubMed:8776899};
DE AltName: Full=Osmotic stress-induced proline dehydrogenase;
DE AltName: Full=Proline oxidase;
DE AltName: Full=Protein EARLY RESPONSIVE TO DEHYDRATION 5;
DE Flags: Precursor;
GN Name=POX1; Synonyms=ERD5, PRO1, PRODH1; OrderedLocusNames=At3g30775;
GN ORFNames=MIF6.16, MIF6.19;
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND INDUCTION.
RC STRAIN=cv. Columbia;
RX PubMed=9003320; DOI=10.1007/pl00008600;
RA Peng Z., Lu Q., Verma D.P.S.;
RT "Reciprocal regulation of delta 1-pyrroline-5-carboxylate synthetase and
RT proline dehydrogenase genes controls proline levels during and after
RT osmotic stress in plants.";
RL Mol. Gen. Genet. 253:334-341(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=cv. Columbia; TISSUE=Root;
RX PubMed=8710950; DOI=10.1073/pnas.93.16.8787;
RA Verbruggen N., Hua X.J., May M., van Montagu M.;
RT "Environmental and developmental signals modulate proline homeostasis:
RT evidence for a negative transcriptional regulator.";
RL Proc. Natl. Acad. Sci. U.S.A. 93:8787-8791(1996).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA], AND CATALYTIC ACTIVITY.
RC STRAIN=cv. Columbia;
RX PubMed=8776899; DOI=10.2307/3870304;
RA Kiyosue T., Yoshiba Y., Yamaguchi-Shinozaki K., Shinozaki K.;
RT "A nuclear gene encoding mitochondrial proline dehydrogenase, an enzyme
RT involved in proline metabolism, is upregulated by proline but downregulated
RT by dehydration in Arabidopsis.";
RL Plant Cell 8:1323-1335(1996).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10819329; DOI=10.1093/dnares/7.2.131;
RA Sato S., Nakamura Y., Kaneko T., Katoh T., Asamizu E., Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 3. I. Sequence
RT features of the regions of 4,504,864 bp covered by sixty P1 and TAC
RT clones.";
RL DNA Res. 7:131-135(2000).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10907853; DOI=10.1093/dnares/7.3.217;
RA Kaneko T., Katoh T., Sato S., Nakamura Y., Asamizu E., Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 3. II. Sequence
RT features of the 4,251,695 bp regions covered by 90 P1, TAC and BAC
RT clones.";
RL DNA Res. 7:217-221(2000).
RN [6]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
RX PubMed=27862469; DOI=10.1111/tpj.13415;
RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA Town C.D.;
RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT genome.";
RL Plant J. 89:789-804(2017).
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=14593172; DOI=10.1126/science.1088305;
RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA Ecker J.R.;
RT "Empirical analysis of transcriptional activity in the Arabidopsis
RT genome.";
RL Science 302:842-846(2003).
RN [8]
RP FUNCTION, TISSUE SPECIFICITY, SUBCELLULAR LOCATION, AND INDUCTION.
RX PubMed=9847097; DOI=10.1104/pp.118.4.1233;
RA Nakashima K., Satoh R., Kiyosue T., Yamaguchi-Shinozaki K., Shinozaki K.;
RT "A gene encoding proline dehydrogenase is not only induced by proline and
RT hypoosmolarity, but is also developmentally regulated in the reproductive
RT organs of Arabidopsis.";
RL Plant Physiol. 118:1233-1241(1998).
RN [9]
RP DISRUPTION PHENOTYPE.
RX PubMed=12773641; DOI=10.1093/pcp/pcg066;
RA Nanjo T., Fujita M., Seki M., Kato T., Tabata S., Shinozaki K.;
RT "Toxicity of free proline revealed in an arabidopsis T-DNA-tagged mutant
RT deficient in proline dehydrogenase.";
RL Plant Cell Physiol. 44:541-548(2003).
RN [10]
RP INDUCTION BY BZIP53.
RC STRAIN=cv. Columbia;
RX PubMed=16810321; DOI=10.1038/sj.emboj.7601206;
RA Weltmeier F., Ehlert A., Mayer C.S., Dietrich K., Wang X., Schuetze K.,
RA Alonso R., Harter K., Vicente-Carbajosa J., Droege-Laser W.;
RT "Combinatorial control of Arabidopsis proline dehydrogenase transcription
RT by specific heterodimerisation of bZIP transcription factors.";
RL EMBO J. 25:3133-3143(2006).
RN [11]
RP INDUCTION.
RX PubMed=17106685; DOI=10.1007/s00425-006-0429-3;
RA Ribarits A., Abdullaev A., Tashpulatov A., Richter A., Heberle-Bors E.,
RA Touraev A.;
RT "Two tobacco proline dehydrogenases are differentially regulated and play a
RT role in early plant development.";
RL Planta 225:1313-1324(2007).
RN [12]
RP FUNCTION, INDUCTION, TISSUE SPECIFICITY, SUBCELLULAR LOCATION, AND
RP DISRUPTION PHENOTYPE.
RX PubMed=20403182; DOI=10.1186/1471-2229-10-70;
RA Funck D., Eckard S., Mueller G.;
RT "Non-redundant functions of two proline dehydrogenase isoforms in
RT Arabidopsis.";
RL BMC Plant Biol. 10:70-70(2010).
RN [13]
RP IDENTIFICATION BY MASS SPECTROMETRY, AND CLEAVAGE OF TRANSIT PEPTIDE AFTER
RP PHE-72.
RX PubMed=25732537; DOI=10.1093/jxb/erv064;
RA Carrie C., Venne A.S., Zahedi R.P., Soll J.;
RT "Identification of cleavage sites and substrate proteins for two
RT mitochondrial intermediate peptidases in Arabidopsis thaliana.";
RL J. Exp. Bot. 66:2691-2708(2015).
CC -!- FUNCTION: Converts proline to delta-1-pyrroline-5-carboxylate.
CC {ECO:0000269|PubMed:20403182, ECO:0000269|PubMed:9847097}.
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 Evidence={ECO:0000305|PubMed:8776899};
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 {ECO:0000269|PubMed:20403182,
CC ECO:0000269|PubMed:9847097, ECO:0000305|PubMed:25732537}.
CC -!- TISSUE SPECIFICITY: Ubiquitous. Highest expression in pollen grains, in
CC the stigma and in developing embryos. {ECO:0000269|PubMed:20403182,
CC ECO:0000269|PubMed:9847097}.
CC -!- INDUCTION: Down-regulated by salt or drought stress. Up-regulated by
CC proline, hypoosmolarity or rehydration (PubMed:17106685,
CC PubMed:20403182, PubMed:9003320, PubMed:9847097). Activated by BZIP53
CC (PubMed:16810321). {ECO:0000269|PubMed:16810321,
CC ECO:0000269|PubMed:17106685, ECO:0000269|PubMed:20403182,
CC ECO:0000269|PubMed:9003320, ECO:0000269|PubMed:9847097}.
CC -!- DISRUPTION PHENOTYPE: No visible phenotype when grown under normal
CC conditions. Proline hypersensitivity. {ECO:0000269|PubMed:12773641,
CC ECO:0000269|PubMed:20403182}.
CC -!- SIMILARITY: Belongs to the proline oxidase family. {ECO:0000305}.
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DR EMBL; U59508; AAB40615.1; -; mRNA.
DR EMBL; X97075; CAA65783.1; -; mRNA.
DR EMBL; D83025; BAA11682.1; -; mRNA.
DR EMBL; AB028614; BAB02917.1; -; Genomic_DNA.
DR EMBL; AP001296; BAB02917.1; JOINED; Genomic_DNA.
DR EMBL; CP002686; AEE77659.1; -; Genomic_DNA.
DR EMBL; CP002686; ANM65921.1; -; Genomic_DNA.
DR EMBL; AF428306; AAL16138.1; -; mRNA.
DR EMBL; AY074571; AAL67111.1; -; mRNA.
DR RefSeq; NP_001319672.1; NM_001339059.1.
DR RefSeq; NP_189701.3; NM_113981.6.
DR AlphaFoldDB; P92983; -.
DR SMR; P92983; -.
DR BioGRID; 8159; 1.
DR IntAct; P92983; 2.
DR STRING; 3702.AT3G30775.1; -.
DR PaxDb; P92983; -.
DR PRIDE; P92983; -.
DR ProteomicsDB; 226217; -.
DR DNASU; 822833; -.
DR EnsemblPlants; AT3G30775.1; AT3G30775.1; AT3G30775.
DR EnsemblPlants; AT3G30775.2; AT3G30775.2; AT3G30775.
DR GeneID; 822833; -.
DR Gramene; AT3G30775.1; AT3G30775.1; AT3G30775.
DR Gramene; AT3G30775.2; AT3G30775.2; AT3G30775.
DR KEGG; ath:AT3G30775; -.
DR Araport; AT3G30775; -.
DR TAIR; locus:2089706; AT3G30775.
DR eggNOG; KOG0186; Eukaryota.
DR HOGENOM; CLU_018202_3_0_1; -.
DR InParanoid; P92983; -.
DR OMA; WMQDAAD; -.
DR OrthoDB; 948528at2759; -.
DR PhylomeDB; P92983; -.
DR BioCyc; ARA:AT3G30775-MON; -.
DR BioCyc; MetaCyc:AT3G30775-MON; -.
DR BRENDA; 1.5.5.2; 399.
DR UniPathway; UPA00261; UER00373.
DR PRO; PR:P92983; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; P92983; baseline and differential.
DR Genevisible; P92983; AT.
DR GO; GO:0005739; C:mitochondrion; IDA:TAIR.
DR GO; GO:0071949; F:FAD binding; IBA:GO_Central.
DR GO; GO:0004657; F:proline dehydrogenase activity; IMP:TAIR.
DR GO; GO:0071456; P:cellular response to hypoxia; HEP:TAIR.
DR GO; GO:0042742; P:defense response to bacterium; IMP:TAIR.
DR GO; GO:0010133; P:proline catabolic process to glutamate; IBA:GO_Central.
DR GO; GO:0006979; P:response to oxidative stress; IEP:TAIR.
DR GO; GO:0009414; P:response to water deprivation; IGI:TAIR.
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 FAD; Flavoprotein; Mitochondrion; Oxidoreductase; Proline metabolism;
KW Reference proteome; Stress response; Transit peptide.
FT TRANSIT 1..72
FT /note="Mitochondrion"
FT /evidence="ECO:0000269|PubMed:25732537"
FT CHAIN 73..499
FT /note="Proline dehydrogenase 1, mitochondrial"
FT /id="PRO_0000025804"
FT CONFLICT 30
FT /note="A -> V (in Ref. 1; AAB40615)"
FT /evidence="ECO:0000305"
FT CONFLICT 46
FT /note="P -> T (in Ref. 1; AAB40615)"
FT /evidence="ECO:0000305"
FT CONFLICT 51
FT /note="H -> Q (in Ref. 1; AAB40615)"
FT /evidence="ECO:0000305"
FT CONFLICT 91
FT /note="A -> P (in Ref. 2; CAA65783)"
FT /evidence="ECO:0000305"
FT CONFLICT 355
FT /note="A -> R (in Ref. 3; BAA11682)"
FT /evidence="ECO:0000305"
FT CONFLICT 361
FT /note="L -> V (in Ref. 2; CAA65783)"
FT /evidence="ECO:0000305"
FT CONFLICT 398
FT /note="V -> A (in Ref. 7; AAL67111)"
FT /evidence="ECO:0000305"
FT CONFLICT 425
FT /note="K -> R (in Ref. 7; AAL16138)"
FT /evidence="ECO:0000305"
FT CONFLICT 477
FT /note="A -> P (in Ref. 1; AAB40615)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 499 AA; 54956 MW; 1428611A40EFC824 CRC64;
MATRLLRTNF IRRSYRLPAF SPVGPPTVTA STAVVPEILS FGQQAPEPPL HHPKPTEQSH
DGLDLSDQAR LFSSIPTSDL LRSTAVLHAA AIGPMVDLGT WVMSSKLMDA SVTRGMVLGL
VKSTFYDHFC AGEDADAAAE RVRSVYEATG LKGMLVYGVE HADDAVSCDD NMQQFIRTIE
AAKSLPTSHF SSVVVKITAI CPISLLKRVS DLLRWEYKSP NFKLSWKLKS FPVFSESSPL
YHTNSEPEPL TAEEERELEA AHGRIQEICR KCQESNVPLL IDAEDTILQP AIDYMAYSSA
IMFNADKDRP IVYNTIQAYL RDAGERLHLA VQNAEKENVP MGFKLVRGAY MSSEASLADS
LGCKSPVHDT IQDTHSCYND CMTFLMEKAS NGSGFGVVLA THNADSGRLA SRKASDLGID
KQNGKIEFAQ LYGMSDALSF GLKRAGFNVS KYMPFGPVAT AIPYLLRRAY ENRGMMATGA
HDRQLMRMEL KRRLIAGIA
