P5CR3_MOUSE
ID P5CR3_MOUSE Reviewed; 274 AA.
AC Q9DCC4; Q8R0P9; Q9D0X2;
DT 18-MAR-2008, integrated into UniProtKB/Swiss-Prot.
DT 18-MAR-2008, sequence version 2.
DT 03-AUG-2022, entry version 144.
DE RecName: Full=Pyrroline-5-carboxylate reductase 3 {ECO:0000250|UniProtKB:Q53H96};
DE Short=P5C reductase 3;
DE Short=P5CR 3;
DE EC=1.5.1.2 {ECO:0000250|UniProtKB:Q53H96};
DE AltName: Full=Pyrroline-5-carboxylate reductase-like protein;
GN Name=Pycr3 {ECO:0000250|UniProtKB:Q53H96}; Synonyms=Pycrl;
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 MRNA].
RC STRAIN=FVB/N; TISSUE=Colon;
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 [3]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC and Spleen;
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).
CC -!- FUNCTION: Enzyme that catalyzes the last step in proline biosynthesis.
CC Proline is synthesized from either glutamate or ornithine; both are
CC converted to pyrroline-5-carboxylate (P5C), and then to proline via
CC pyrroline-5-carboxylate reductases (PYCRs). PYCRL is exclusively linked
CC to the conversion of ornithine to proline.
CC {ECO:0000250|UniProtKB:Q53H96}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-proline + NADP(+) = 1-pyrroline-5-carboxylate + 2 H(+) +
CC NADPH; Xref=Rhea:RHEA:14109, ChEBI:CHEBI:15378, ChEBI:CHEBI:15893,
CC ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:60039; EC=1.5.1.2;
CC Evidence={ECO:0000250|UniProtKB:Q53H96};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-proline + NAD(+) = 1-pyrroline-5-carboxylate + 2 H(+) +
CC NADH; Xref=Rhea:RHEA:14105, ChEBI:CHEBI:15378, ChEBI:CHEBI:15893,
CC ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, ChEBI:CHEBI:60039; EC=1.5.1.2;
CC Evidence={ECO:0000250|UniProtKB:Q53H96};
CC -!- PATHWAY: Amino-acid biosynthesis; L-proline biosynthesis; L-proline
CC from L-glutamate 5-semialdehyde: step 1/1.
CC {ECO:0000250|UniProtKB:Q53H96}.
CC -!- SUBUNIT: Homodecamer; composed of 5 homodimers.
CC {ECO:0000250|UniProtKB:P32322}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q53H96}.
CC -!- SIMILARITY: Belongs to the pyrroline-5-carboxylate reductase family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAB23252.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AK002912; BAB22451.1; -; mRNA.
DR EMBL; AK004291; BAB23252.1; ALT_FRAME; mRNA.
DR EMBL; BC026536; AAH26536.1; -; mRNA.
DR CCDS; CCDS37109.1; -.
DR RefSeq; NP_079688.2; NM_025412.2.
DR AlphaFoldDB; Q9DCC4; -.
DR SMR; Q9DCC4; -.
DR BioGRID; 211286; 19.
DR IntAct; Q9DCC4; 2.
DR MINT; Q9DCC4; -.
DR STRING; 10090.ENSMUSP00000049605; -.
DR iPTMnet; Q9DCC4; -.
DR PhosphoSitePlus; Q9DCC4; -.
DR SwissPalm; Q9DCC4; -.
DR REPRODUCTION-2DPAGE; IPI00153234; -.
DR REPRODUCTION-2DPAGE; Q9DCC4; -.
DR EPD; Q9DCC4; -.
DR jPOST; Q9DCC4; -.
DR MaxQB; Q9DCC4; -.
DR PaxDb; Q9DCC4; -.
DR PeptideAtlas; Q9DCC4; -.
DR PRIDE; Q9DCC4; -.
DR ProteomicsDB; 287756; -.
DR Antibodypedia; 28003; 207 antibodies from 20 providers.
DR DNASU; 66194; -.
DR Ensembl; ENSMUST00000053918; ENSMUSP00000049605; ENSMUSG00000022571.
DR GeneID; 66194; -.
DR KEGG; mmu:66194; -.
DR UCSC; uc007whq.1; mouse.
DR CTD; 66194; -.
DR MGI; MGI:1913444; Pycrl.
DR VEuPathDB; HostDB:ENSMUSG00000022571; -.
DR eggNOG; KOG3124; Eukaryota.
DR GeneTree; ENSGT00950000183044; -.
DR HOGENOM; CLU_042344_3_1_1; -.
DR InParanoid; Q9DCC4; -.
DR OMA; AKQTCLG; -.
DR OrthoDB; 952695at2759; -.
DR PhylomeDB; Q9DCC4; -.
DR Reactome; R-MMU-8964539; Glutamate and glutamine metabolism.
DR UniPathway; UPA00098; UER00361.
DR BioGRID-ORCS; 66194; 1 hit in 75 CRISPR screens.
DR PRO; PR:Q9DCC4; -.
DR Proteomes; UP000000589; Chromosome 15.
DR RNAct; Q9DCC4; protein.
DR Bgee; ENSMUSG00000022571; Expressed in yolk sac and 248 other tissues.
DR Genevisible; Q9DCC4; MM.
DR GO; GO:0005829; C:cytosol; ISS:UniProtKB.
DR GO; GO:0045171; C:intercellular bridge; ISO:MGI.
DR GO; GO:0072686; C:mitotic spindle; ISO:MGI.
DR GO; GO:0004126; F:cytidine deaminase activity; ISO:MGI.
DR GO; GO:0004735; F:pyrroline-5-carboxylate reductase activity; ISS:UniProtKB.
DR GO; GO:0009972; P:cytidine deamination; ISO:MGI.
DR GO; GO:0055129; P:L-proline biosynthetic process; ISS:UniProtKB.
DR HAMAP; MF_01925; P5C_reductase; 1.
DR InterPro; IPR008927; 6-PGluconate_DH-like_C_sf.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR028939; P5C_Rdtase_cat_N.
DR InterPro; IPR029036; P5CR_dimer.
DR InterPro; IPR000304; Pyrroline-COOH_reductase.
DR PANTHER; PTHR11645; PTHR11645; 1.
DR Pfam; PF03807; F420_oxidored; 1.
DR Pfam; PF14748; P5CR_dimer; 1.
DR PIRSF; PIRSF000193; Pyrrol-5-carb_rd; 1.
DR SUPFAM; SSF48179; SSF48179; 1.
DR SUPFAM; SSF51735; SSF51735; 1.
DR TIGRFAMs; TIGR00112; proC; 1.
PE 1: Evidence at protein level;
KW Acetylation; Amino-acid biosynthesis; Cytoplasm; NADP; Oxidoreductase;
KW Proline biosynthesis; Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:Q53H96"
FT CHAIN 2..274
FT /note="Pyrroline-5-carboxylate reductase 3"
FT /id="PRO_0000324563"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000250|UniProtKB:Q53H96"
FT CONFLICT 59
FT /note="T -> N (in Ref. 1; BAB23252)"
FT /evidence="ECO:0000305"
FT CONFLICT 68
FT /note="N -> S (in Ref. 1; BAB22451)"
FT /evidence="ECO:0000305"
FT CONFLICT 92..93
FT /note="VT -> IN (in Ref. 1; BAB23252)"
FT /evidence="ECO:0000305"
FT CONFLICT 107..110
FT /note="LSTM -> HGTK (in Ref. 1; BAB23252)"
FT /evidence="ECO:0000305"
FT CONFLICT 120
FT /note="V -> A (in Ref. 1; BAB23252)"
FT /evidence="ECO:0000305"
FT CONFLICT 128
FT /note="P -> T (in Ref. 1; BAB23252)"
FT /evidence="ECO:0000305"
FT CONFLICT 152
FT /note="L -> I (in Ref. 1; BAB23252)"
FT /evidence="ECO:0000305"
FT CONFLICT 164
FT /note="E -> K (in Ref. 1; BAB23252)"
FT /evidence="ECO:0000305"
FT CONFLICT 190
FT /note="A -> G (in Ref. 1; BAB23252)"
FT /evidence="ECO:0000305"
FT CONFLICT 198
FT /note="M -> I (in Ref. 1; BAB23252)"
FT /evidence="ECO:0000305"
FT CONFLICT 268
FT /note="A -> V (in Ref. 1; BAB23252)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 274 AA; 28721 MW; E01FB7133B45BD7C CRC64;
MAATMSEPRR VGFVGAGRMA EAIARGLIQA GKVEAKQVLA SAPTDNNLCH FRALGCQTTH
SNHEVLQNCP LVIFATKPQV LPTVLAEVAP IVTTEHIIVS VAAGISLSTM EGLLPPNTRV
LRVSPNLPCV VQEGAMVMAR GHHAGNDDAE LLQNLLEACG QCIEVPESYV DIHTGLSGSG
VAFVCTFSEA LAEGAIKMGM PSGLAHRIAA QTLLGTAKML QQEGKHPAQL RTDVLTPAGT
TIHGLHALER GGFRAATMSA VEAATCRAKE LSKK
