Full text data of PYCRL
PYCRL
[Confidence: low (only semi-automatic identification from reviews)]
Pyrroline-5-carboxylate reductase 3; P5C reductase 3; P5CR 3; 1.5.1.2 (Pyrroline-5-carboxylate reductase-like protein)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
Pyrroline-5-carboxylate reductase 3; P5C reductase 3; P5CR 3; 1.5.1.2 (Pyrroline-5-carboxylate reductase-like protein)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
UniProt
Q53H96
ID P5CR3_HUMAN Reviewed; 274 AA.
AC Q53H96; B3KMB5; Q8N3N9; Q96HX4; Q9H896;
DT 18-MAR-2008, integrated into UniProtKB/Swiss-Prot.
read moreDT 18-MAR-2008, sequence version 2.
DT 22-JAN-2014, entry version 78.
DE RecName: Full=Pyrroline-5-carboxylate reductase 3;
DE Short=P5C reductase 3;
DE Short=P5CR 3;
DE EC=1.5.1.2;
DE AltName: Full=Pyrroline-5-carboxylate reductase-like protein;
GN Name=PYCRL;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT LYS-150.
RC TISSUE=Thyroid;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Lung;
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
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-264.
RC TISSUE=Brain;
RA Suzuki Y., Sugano S., Totoki Y., Toyoda A., Takeda T., Sakaki Y.,
RA Tanaka A., Yokoyama S.;
RL Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 31-274.
RC TISSUE=Amygdala;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H.,
RA Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K.,
RA Ottenwaelder B., Poustka A., Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
RA Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [6]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, MASS SPECTROMETRY, AND
RP CLEAVAGE OF INITIATOR METHIONINE.
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E.,
RA Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K.,
RA Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-
RT terminal acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
CC -!- CATALYTIC ACTIVITY: L-proline + NAD(P)(+) = 1-pyrroline-5-
CC carboxylate + NAD(P)H.
CC -!- PATHWAY: Amino-acid biosynthesis; L-proline biosynthesis; L-
CC proline from L-glutamate 5-semialdehyde: step 1/1.
CC -!- SUBUNIT: Homodecamer; composed of 5 homodimers (By similarity).
CC -!- SIMILARITY: Belongs to the pyrroline-5-carboxylate reductase
CC family.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAD96405.1; Type=Erroneous initiation; Note=Translation N-terminally shortened;
CC Sequence=BAD96405.1; Type=Miscellaneous discrepancy; Note=Chimeric cDNA;
CC -----------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution-NoDerivs License
CC -----------------------------------------------------------------------
DR EMBL; AK001500; BAG50927.1; -; mRNA.
DR EMBL; AK023914; BAB14721.1; -; mRNA.
DR EMBL; BC007993; AAH07993.1; -; mRNA.
DR EMBL; AK222685; BAD96405.1; ALT_SEQ; mRNA.
DR EMBL; AL833857; CAD38716.1; -; mRNA.
DR RefSeq; NP_075566.2; NM_023078.3.
DR UniGene; Hs.165186; -.
DR ProteinModelPortal; Q53H96; -.
DR SMR; Q53H96; 11-271.
DR IntAct; Q53H96; 4.
DR STRING; 9606.ENSP00000220966; -.
DR PhosphoSite; Q53H96; -.
DR DMDM; 172046829; -.
DR PaxDb; Q53H96; -.
DR PeptideAtlas; Q53H96; -.
DR PRIDE; Q53H96; -.
DR DNASU; 65263; -.
DR Ensembl; ENST00000220966; ENSP00000220966; ENSG00000104524.
DR GeneID; 65263; -.
DR KEGG; hsa:65263; -.
DR CTD; 65263; -.
DR GeneCards; GC08M144686; -.
DR H-InvDB; HIX0007842; -.
DR HGNC; HGNC:25846; PYCRL.
DR neXtProt; NX_Q53H96; -.
DR PharmGKB; PA134889043; -.
DR eggNOG; COG0345; -.
DR HOGENOM; HOG000230247; -.
DR HOVERGEN; HBG053399; -.
DR KO; K00286; -.
DR OrthoDB; EOG7N0C5N; -.
DR UniPathway; UPA00098; UER00361.
DR GenomeRNAi; 65263; -.
DR NextBio; 67386; -.
DR PRO; PR:Q53H96; -.
DR ArrayExpress; Q53H96; -.
DR Bgee; Q53H96; -.
DR CleanEx; HS_PYCRL; -.
DR Genevestigator; Q53H96; -.
DR GO; GO:0004735; F:pyrroline-5-carboxylate reductase activity; IEA:UniProtKB-EC.
DR GO; GO:0055129; P:L-proline biosynthetic process; IEA:UniProtKB-UniPathway.
DR Gene3D; 3.40.50.720; -; 1.
DR InterPro; IPR008927; 6-PGluconate_DH_C-like.
DR InterPro; IPR016040; NAD(P)-bd_dom.
DR InterPro; IPR000304; Pyrroline-COOH_reductase.
DR PANTHER; PTHR11645; PTHR11645; 1.
DR PIRSF; PIRSF000193; Pyrrol-5-carb_rd; 1.
DR SUPFAM; SSF48179; SSF48179; 1.
DR TIGRFAMs; TIGR00112; proC; 1.
DR PROSITE; PS00521; P5CR; 1.
PE 1: Evidence at protein level;
KW Acetylation; Amino-acid biosynthesis; Complete proteome; NADP;
KW Oxidoreductase; Polymorphism; Proline biosynthesis;
KW Reference proteome.
FT INIT_MET 1 1 Removed.
FT CHAIN 2 274 Pyrroline-5-carboxylate reductase 3.
FT /FTId=PRO_0000324561.
FT MOD_RES 2 2 N-acetylalanine.
FT VARIANT 57 57 R -> Q (in dbSNP:rs11549789).
FT /FTId=VAR_039828.
FT VARIANT 105 105 V -> M (in dbSNP:rs2242089).
FT /FTId=VAR_039829.
FT VARIANT 150 150 N -> K (in dbSNP:rs2242090).
FT /FTId=VAR_039830.
SQ SEQUENCE 274 AA; 28649 MW; 846FD9B60183B048 CRC64;
MAAAEPSPRR VGFVGAGRMA GAIAQGLIRA GKVEAQHILA SAPTDRNLCH FQALGCRTTH
SNQEVLQSCL LVIFATKPHV LPAVLAEVAP VVTTEHILVS VAAGVSLSTL EELLPPNTRV
LRVLPNLPCV VQEGAIVMAR GRHVGSSETN LLQHLLEACG RCEEVPEAYV DIHTGLSGSG
VAFVCAFSEA LAEGAVKMGM PSSLAHRIAA QTLLGTAKML LHEGQHPAQL RSDVCTPGGT
TIYGLHALEQ GGLRAATMSA VEAATCRAKE LSRK
//
ID P5CR3_HUMAN Reviewed; 274 AA.
AC Q53H96; B3KMB5; Q8N3N9; Q96HX4; Q9H896;
DT 18-MAR-2008, integrated into UniProtKB/Swiss-Prot.
read moreDT 18-MAR-2008, sequence version 2.
DT 22-JAN-2014, entry version 78.
DE RecName: Full=Pyrroline-5-carboxylate reductase 3;
DE Short=P5C reductase 3;
DE Short=P5CR 3;
DE EC=1.5.1.2;
DE AltName: Full=Pyrroline-5-carboxylate reductase-like protein;
GN Name=PYCRL;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT LYS-150.
RC TISSUE=Thyroid;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Lung;
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
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-264.
RC TISSUE=Brain;
RA Suzuki Y., Sugano S., Totoki Y., Toyoda A., Takeda T., Sakaki Y.,
RA Tanaka A., Yokoyama S.;
RL Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 31-274.
RC TISSUE=Amygdala;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H.,
RA Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K.,
RA Ottenwaelder B., Poustka A., Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
RA Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [6]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, MASS SPECTROMETRY, AND
RP CLEAVAGE OF INITIATOR METHIONINE.
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E.,
RA Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K.,
RA Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-
RT terminal acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
CC -!- CATALYTIC ACTIVITY: L-proline + NAD(P)(+) = 1-pyrroline-5-
CC carboxylate + NAD(P)H.
CC -!- PATHWAY: Amino-acid biosynthesis; L-proline biosynthesis; L-
CC proline from L-glutamate 5-semialdehyde: step 1/1.
CC -!- SUBUNIT: Homodecamer; composed of 5 homodimers (By similarity).
CC -!- SIMILARITY: Belongs to the pyrroline-5-carboxylate reductase
CC family.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAD96405.1; Type=Erroneous initiation; Note=Translation N-terminally shortened;
CC Sequence=BAD96405.1; Type=Miscellaneous discrepancy; Note=Chimeric cDNA;
CC -----------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution-NoDerivs License
CC -----------------------------------------------------------------------
DR EMBL; AK001500; BAG50927.1; -; mRNA.
DR EMBL; AK023914; BAB14721.1; -; mRNA.
DR EMBL; BC007993; AAH07993.1; -; mRNA.
DR EMBL; AK222685; BAD96405.1; ALT_SEQ; mRNA.
DR EMBL; AL833857; CAD38716.1; -; mRNA.
DR RefSeq; NP_075566.2; NM_023078.3.
DR UniGene; Hs.165186; -.
DR ProteinModelPortal; Q53H96; -.
DR SMR; Q53H96; 11-271.
DR IntAct; Q53H96; 4.
DR STRING; 9606.ENSP00000220966; -.
DR PhosphoSite; Q53H96; -.
DR DMDM; 172046829; -.
DR PaxDb; Q53H96; -.
DR PeptideAtlas; Q53H96; -.
DR PRIDE; Q53H96; -.
DR DNASU; 65263; -.
DR Ensembl; ENST00000220966; ENSP00000220966; ENSG00000104524.
DR GeneID; 65263; -.
DR KEGG; hsa:65263; -.
DR CTD; 65263; -.
DR GeneCards; GC08M144686; -.
DR H-InvDB; HIX0007842; -.
DR HGNC; HGNC:25846; PYCRL.
DR neXtProt; NX_Q53H96; -.
DR PharmGKB; PA134889043; -.
DR eggNOG; COG0345; -.
DR HOGENOM; HOG000230247; -.
DR HOVERGEN; HBG053399; -.
DR KO; K00286; -.
DR OrthoDB; EOG7N0C5N; -.
DR UniPathway; UPA00098; UER00361.
DR GenomeRNAi; 65263; -.
DR NextBio; 67386; -.
DR PRO; PR:Q53H96; -.
DR ArrayExpress; Q53H96; -.
DR Bgee; Q53H96; -.
DR CleanEx; HS_PYCRL; -.
DR Genevestigator; Q53H96; -.
DR GO; GO:0004735; F:pyrroline-5-carboxylate reductase activity; IEA:UniProtKB-EC.
DR GO; GO:0055129; P:L-proline biosynthetic process; IEA:UniProtKB-UniPathway.
DR Gene3D; 3.40.50.720; -; 1.
DR InterPro; IPR008927; 6-PGluconate_DH_C-like.
DR InterPro; IPR016040; NAD(P)-bd_dom.
DR InterPro; IPR000304; Pyrroline-COOH_reductase.
DR PANTHER; PTHR11645; PTHR11645; 1.
DR PIRSF; PIRSF000193; Pyrrol-5-carb_rd; 1.
DR SUPFAM; SSF48179; SSF48179; 1.
DR TIGRFAMs; TIGR00112; proC; 1.
DR PROSITE; PS00521; P5CR; 1.
PE 1: Evidence at protein level;
KW Acetylation; Amino-acid biosynthesis; Complete proteome; NADP;
KW Oxidoreductase; Polymorphism; Proline biosynthesis;
KW Reference proteome.
FT INIT_MET 1 1 Removed.
FT CHAIN 2 274 Pyrroline-5-carboxylate reductase 3.
FT /FTId=PRO_0000324561.
FT MOD_RES 2 2 N-acetylalanine.
FT VARIANT 57 57 R -> Q (in dbSNP:rs11549789).
FT /FTId=VAR_039828.
FT VARIANT 105 105 V -> M (in dbSNP:rs2242089).
FT /FTId=VAR_039829.
FT VARIANT 150 150 N -> K (in dbSNP:rs2242090).
FT /FTId=VAR_039830.
SQ SEQUENCE 274 AA; 28649 MW; 846FD9B60183B048 CRC64;
MAAAEPSPRR VGFVGAGRMA GAIAQGLIRA GKVEAQHILA SAPTDRNLCH FQALGCRTTH
SNQEVLQSCL LVIFATKPHV LPAVLAEVAP VVTTEHILVS VAAGVSLSTL EELLPPNTRV
LRVLPNLPCV VQEGAIVMAR GRHVGSSETN LLQHLLEACG RCEEVPEAYV DIHTGLSGSG
VAFVCAFSEA LAEGAVKMGM PSSLAHRIAA QTLLGTAKML LHEGQHPAQL RSDVCTPGGT
TIYGLHALEQ GGLRAATMSA VEAATCRAKE LSRK
//