P5CR2_RAT
ID P5CR2_RAT Reviewed; 320 AA.
AC Q6AY23;
DT 01-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 13-SEP-2004, sequence version 1.
DT 03-AUG-2022, entry version 127.
DE RecName: Full=Pyrroline-5-carboxylate reductase 2;
DE Short=P5C reductase 2;
DE Short=P5CR 2;
DE EC=1.5.1.2;
GN Name=Pycr2;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Testis;
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).
CC -!- FUNCTION: Housekeeping enzyme that catalyzes the last step in proline
CC biosynthesis. In some cell types, such as erythrocytes, its primary
CC function may be the generation of NADP(+). Can utilize both NAD and
CC NADP. Has higher affinity for NADP, but higher catalytic efficiency
CC with NADH (By similarity). Involved in cellular response to oxidative
CC stress (By similarity). {ECO:0000250|UniProtKB:Q96C36}.
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:Q96C36};
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:Q96C36};
CC -!- PATHWAY: Amino-acid biosynthesis; L-proline biosynthesis; L-proline
CC from L-glutamate 5-semialdehyde: step 1/1.
CC -!- SUBUNIT: Homodecamer; composed of 5 homodimers. Interacts with LTO1.
CC {ECO:0000250|UniProtKB:Q96C36}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q96C36}.
CC Mitochondrion {ECO:0000250|UniProtKB:Q96C36}.
CC -!- SIMILARITY: Belongs to the pyrroline-5-carboxylate reductase family.
CC {ECO:0000305}.
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DR EMBL; BC079222; AAH79222.1; -; mRNA.
DR RefSeq; NP_001012208.1; NM_001012208.1.
DR AlphaFoldDB; Q6AY23; -.
DR SMR; Q6AY23; -.
DR IntAct; Q6AY23; 2.
DR MINT; Q6AY23; -.
DR STRING; 10116.ENSRNOP00000004379; -.
DR iPTMnet; Q6AY23; -.
DR PhosphoSitePlus; Q6AY23; -.
DR jPOST; Q6AY23; -.
DR PaxDb; Q6AY23; -.
DR PRIDE; Q6AY23; -.
DR GeneID; 364064; -.
DR KEGG; rno:364064; -.
DR CTD; 29920; -.
DR RGD; 1310074; Pycr2.
DR VEuPathDB; HostDB:ENSRNOG00000003267; -.
DR eggNOG; KOG3124; Eukaryota.
DR HOGENOM; CLU_042344_3_0_1; -.
DR InParanoid; Q6AY23; -.
DR OMA; EQICTPK; -.
DR OrthoDB; 952695at2759; -.
DR PhylomeDB; Q6AY23; -.
DR Reactome; R-RNO-8964539; Glutamate and glutamine metabolism.
DR SABIO-RK; Q6AY23; -.
DR UniPathway; UPA00098; UER00361.
DR PRO; PR:Q6AY23; -.
DR Proteomes; UP000002494; Chromosome 13.
DR Bgee; ENSRNOG00000003267; Expressed in pancreas and 20 other tissues.
DR Genevisible; Q6AY23; RN.
DR GO; GO:0005739; C:mitochondrion; ISS:UniProtKB.
DR GO; GO:0004735; F:pyrroline-5-carboxylate reductase activity; IBA:GO_Central.
DR GO; GO:0034599; P:cellular response to oxidative stress; ISS:UniProtKB.
DR GO; GO:0055129; P:L-proline biosynthetic process; IBA:GO_Central.
DR GO; GO:0006561; P: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.
DR PROSITE; PS00521; P5CR; 1.
PE 2: Evidence at transcript level;
KW Acetylation; Amino-acid biosynthesis; Cytoplasm; Mitochondrion; NADP;
KW Oxidoreductase; Phosphoprotein; Proline biosynthesis; Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:Q96C36"
FT CHAIN 2..320
FT /note="Pyrroline-5-carboxylate reductase 2"
FT /id="PRO_0000187320"
FT REGION 293..320
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 297..312
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 6..11
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
FT BINDING 34
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
FT BINDING 56
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
FT BINDING 69..72
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
FT BINDING 95..97
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0000250|UniProtKB:Q96C36"
FT MOD_RES 304
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q96C36"
SQ SEQUENCE 320 AA; 33673 MW; 6434E5A7CBC739A9 CRC64;
MSVGFIGAGQ LACALARGFT AAGVLSAHKI IASSPEMDLP TVSALRKMGV NLTRSNKDTV
RHSDVLFLAV KPHIIPFILD EIGADVQERH IVVSCAAGVT ISSVEKKLMA FQPAPKVIRC
MTNTPVVVRE GATVYATGTH ALVEDGKLLE QLMSSVGFCT EVEEDLIDAI TGLSGSGPAY
AFMALDALAD GGVKMGVPRR LAVRLGAQAL LGAAKMLLDS EDHPGQLKDN VCSPGGATIH
ALHFLESGGF RSLLINAVEA SCIRTRELQS MADQEKVSPA ALKKTLLDRV KLESPTVSTL
APPSSGKLLT RNPAQGSKRE
