Q96C36 (P5CR2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Pyrroline-5-carboxylate reductase 2
Short name=P5C reductase 2
Short name=P5CR 2
EC=1.5.1.2

Gene names

Name:

PYCR2

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	320 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Housekeeping enzyme that catalyzes the last step in proline biosynthesis. In some cell types, such as erythrocytes, its primary function may be the generation of NADP+. Can utilize both NAD and NADP. Has higher affinity for NADP, but higher catalytic efficiency with NADH. Ref.7 Ref.8
Catalytic activity	L-proline + NAD(P)+ = 1-pyrroline-5-carboxylate + NAD(P)H. Ref.7 Ref.8
Enzyme regulation	Subject to competitive inhibition by NADP. Not inhibited by proline. Ref.7 Ref.8
Pathway	Amino-acid biosynthesis; L-proline biosynthesis; L-proline from L-glutamate 5-semialdehyde: step 1/1.
Subunit structure	Homodecamer; composed of 5 homodimers Probable. Ref.8
Subcellular location	Cytoplasm Ref.8.
Tissue specificity	Detected in erythrocytes (at protein level). Ref.7 Ref.8
Sequence similarities	Belongs to the pyrroline-5-carboxylate reductase family.
Biophysicochemical properties	Kinetic parameters: KM=0.64 mM for NADH Ref.8 KM=0.04 mM for NADPH KM=1.49 mM for pyrroline-5-carboxylate (in the presence of NADH) KM=0.23 mM for pyrroline-5-carboxylate (in the presence of NADPH) Vmax=28.5 µmol/min/µg enzyme (in the presence of NADH) Vmax=3.7 µmol/min/µg enzyme (in the presence of NADPH)

Ontologies

Keywords
Biological process	Amino-acid biosynthesis Proline biosynthesis
Cellular component	Cytoplasm
Ligand	NADP
Molecular function	Oxidoreductase
PTM	Acetylation Phosphoprotein
Technical term	Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	L-proline biosynthetic process Inferred from electronic annotation. Source: UniProtKB-UniPathway
Cellular_component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	nucleotide binding Inferred from electronic annotation. Source: InterPro pyrroline-5-carboxylate reductase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Initiator methionine	1	1	Removed Ref.6
	Chain	2 – 320	319	Pyrroline-5-carboxylate reductase 2		PRO_0000187317
Regions
	Nucleotide binding	6 – 11	6	NADP By similarity
	Nucleotide binding	69 – 72	4	NADP By similarity
	Nucleotide binding	95 – 97	3	NADP By similarity
Sites
	Binding site	34	1	NADP; via carbonyl oxygen By similarity
	Binding site	56	1	NADP By similarity
Amino acid modifications
	Modified residue	2	1	N-acetylserine Ref.6
	Modified residue	304	1	Phosphoserine Ref.10 Ref.11 Ref.13
Experimental info
	Sequence conflict	13	1	Y → N in AAP97169. Ref.1
	Sequence conflict	23 – 24	2	GI → AF in AAP97169. Ref.1
	Sequence conflict	72 – 73	2	PH → HI in AAP97169. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	Q96C36 [UniParc]. Last modified December 1, 2001. Version 1. Checksum: 9348455A64CCE722	FASTA	320	33,637
	10 20 30 40 50 60 MSVGFIGAGQ LAYALARGFT AAGILSAHKI IASSPEMNLP TVSALRKMGV NLTRSNKETV 70 80 90 100 110 120 KHSDVLFLAV KPHIIPFILD EIGADVQARH IVVSCAAGVT ISSVEKKLMA FQPAPKVIRC 130 140 150 160 170 180 MTNTPVVVQE GATVYATGTH ALVEDGQLLE QLMSSVGFCT EVEEDLIDAV TGLSGSGPAY 190 200 210 220 230 240 AFMALDALAD GGVKMGLPRR LAIQLGAQAL LGAAKMLLDS EQHPCQLKDN VCSPGGATIH 250 260 270 280 290 300 ALHFLESGGF RSLLINAVEA SCIRTRELQS MADQEKISPA ALKKTLLDRV KLESPTVSTL 310 320 TPSSPGKLLT RSLALGGKKD

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Cloning of a new human cDNA homologous to human pyrroline 5-carboxylate reductase mRNA." Yue P., Yu L., Zhao S.Y. Submitted (AUG-1998) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]	"Complete sequencing and characterization of 21,243 full-length human cDNAs." Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S. Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[3]	"The DNA sequence and biological annotation of human chromosome 1." Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K. , Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R. Nature 441:315-321(2006) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[4]	Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C. Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[5]	"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Cervix and Skin.
[6]	Bienvenut W.V., Heiserich L., Gottlieb E., Zebisch A., Kolch W. Submitted (OCT-2008) to UniProtKB Cited for: PROTEIN SEQUENCE OF 2-17, CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT SER-2, MASS SPECTROMETRY. Tissue: Colon carcinoma.
[7]	"Pyrroline-5-carboxylate reductase in human erythrocytes." Yeh G.C., Harris S.C., Phang J.M. J. Clin. Invest. 67:1042-1046(1981) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, CATALYTIC ACTIVITY, ENZYME REGULATION, TISSUE SPECIFICITY.
[8]	"Purified human erythrocyte pyrroline-5-carboxylate reductase. Preferential oxidation of NADPH." Merrill M.J., Yeh G.C., Phang J.M. J. Biol. Chem. 264:9352-9358(1989) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, CATALYTIC ACTIVITY, SUBUNIT, SUBCELLULAR LOCATION, ENZYME REGULATION, BIOPHYSICOCHEMICAL PROPERTIES, TISSUE SPECIFICITY.
[9]	"A probability-based approach for high-throughput protein phosphorylation analysis and site localization." Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P. Nat. Biotechnol. 24:1285-1292(2006) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. Tissue: Cervix carcinoma.
[10]	"A quantitative atlas of mitotic phosphorylation." Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P. Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-304, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[11]	"Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis." Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M. Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-304, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[12]	"Initial characterization of the human central proteome." Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J. BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[13]	"System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation." Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B. Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-304, MASS SPECTROMETRY.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AF087859 mRNA. Translation: AAP97169.1. AK291913 mRNA. Translation: BAF84602.1. AL117348 Genomic DNA. Translation: CAI21802.1. CH471098 Genomic DNA. Translation: EAW69762.1. BC014868 mRNA. Translation: AAH14868.1. BC020553 mRNA. Translation: AAH20553.1.
IPI	IPI00470610.
RefSeq	NP_001258610.1. NM_001271681.1. NP_037460.2. NM_013328.3.
UniGene	Hs.654718.
3D structure databases
ProteinModelPortal	Q96C36.
ModBase	Search...
Protein-protein interaction databases
IntAct	Q96C36. 3 interactions.
MINT	MINT-1150827.
STRING	9606.ENSP00000342502.
PTM databases
PhosphoSite	Q96C36.
Polymorphism databases
DMDM	60390642.
Proteomic databases
PaxDb	Q96C36.
PRIDE	Q96C36.
Protocols and materials databases
DNASU	29920.
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000343818; ENSP00000342502; ENSG00000143811.
GeneID	29920.
KEGG	hsa:29920.
UCSC	uc001hpq.3. human.
Organism-specific databases
CTD	29920.
GeneCards	GC01M226107.
H-InvDB	HIX0200217.
HGNC	HGNC:30262. PYCR2.
HPA	HPA056873.
neXtProt	NX_Q96C36.
PharmGKB	PA134881955.
GenAtlas	Search...
Phylogenomic databases
eggNOG	COG0345.
HOGENOM	HOG000230247.
HOVERGEN	HBG053399.
InParanoid	Q96C36.
KO	K00286.
OMA	EQNAFRH.
Enzyme and pathway databases
UniPathway	UPA00098; UER00361.
Gene expression databases
ArrayExpress	Q96C36.
Bgee	Q96C36.
CleanEx	HS_PYCR2.
Genevestigator	Q96C36.
GermOnline	ENSG00000143811. Homo sapiens.
Family and domain databases
Gene3D	3.40.50.720. 1 hit.
InterPro	IPR008927. 6-PGluconate_DH_C-like. IPR016040. NAD(P)-bd_dom. IPR004455. NADP_OxRdtase_F420. IPR000304. Pyrroline-COOH_reductase. [Graphical view]
PANTHER	PTHR11645. PTHR11645. 1 hit.
Pfam	PF03807. F420_oxidored. 1 hit. [Graphical view]
PIRSF	PIRSF000193. Pyrrol-5-carb_rd. 1 hit.
SUPFAM	SSF48179. 6DGDH_C_like. 1 hit.
TIGRFAMs	TIGR00112. proC. 1 hit.
PROSITE	PS00521. P5CR. 1 hit. [Graphical view]
ProtoNet	Search...
Other
DrugBank	DB00172. L-Proline. DB00157. NADH.
GenomeRNAi	29920.
NextBio	52520.

Entry information

Entry name

P5CR2_HUMAN

Accession

Primary (citable) accession number: Q96C36
Secondary accession number(s): A8K798, Q7Z515, Q9Y5J4

Entry history

Integrated into UniProtKB/Swiss-Prot:	March 1, 2005
Last sequence update:	December 1, 2001
Last modified:	May 1, 2013
This is version 98 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.