ExPASy logo ExPASy Home page Site Map Search ExPASy Contact us Swiss-Prot
Notice: This page will be replaced with www.uniprot.org. Please send us your feedback!
Search for

UniProtKB/Swiss-Prot entry Q9DCC4


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

Note: most headings are clickable, even if they don't appear as links. They link to the user manual or other documents.
Entry information
Entry name P5CR3_MOUSE
Primary accession number Q9DCC4
Secondary accession numbers Q8R0P9 Q9D0X2
Integrated into Swiss-Prot on March 18, 2008
Sequence was last modified on March 18, 2008 (Sequence version 2)
Annotations were last modified on    July 22, 2008 (Entry version 39)
Name and origin of the protein
Protein name Pyrroline-5-carboxylate reductase 3
Synonyms P5C reductase 3
P5CR 3
EC 1.5.1.2
Pyrroline-5-carboxylate reductase-like protein
Gene name
Name: Pycrl
From
Mus musculus (Mouse) [TaxID: 10090] 
Taxonomy Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; Muroidea; Muridae; Murinae; Mus.
Protein existence 2: Evidence at transcript level;
References
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=C57BL/6J;
TISSUE=Kidney;
DOI=10.1126/science.1112014; PubMed=16141072 [NCBI, ExPASy, EBI, Israel, Japan]
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J., Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
"The transcriptional landscape of the mammalian genome.";
Science 309:1559-1563(2005).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=FVB/N;
TISSUE=Colon;
DOI=10.1101/gr.2596504; PubMed=15489334 [NCBI, ExPASy, EBI, Israel, Japan]
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
Comments
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
AK002912; BAB22451.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AK004291; BAB23252.1; ALT_FRAME; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC026536; AAH26536.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
RefSeq NP_079688.2; -.
UniGene Mm.250599
3D structure databases
ModBase Q9DCC4.
Organism-specific databases
MGI MGI:1913444; Pycrl.
Gene expression databases
ArrayExpress Q9DCC4; -.
CleanEx MM_PYCRL; -.
Ontologies
GO
GO:0042802; Molecular function: identical protein binding (inferred from physical interaction from MGI).
QuickGo view.
Family and domain databases
InterPro IPR016040; NAD(P)-bd.
IPR004455; NADP_OxRdtase_F420.
IPR000304; P5CR.
Graphical view of domain structure.
Gene3D G3DSA:3.40.50.720; NAD(P)-bd; 1.
PANTHER PTHR11645; P5CR; 1.
Pfam PF03807; F420_oxidored; 1.
Pfam graphical view of domain structure.
PIRSF PIRSF000193; Pyrrol-5-carb_rd; 1.
TIGRFAMs TIGR00112; proC; 1.
PROSITE PS00521; P5CR; FALSE_NEG.
BLOCKS Q9DCC4.
Genome annotation databases
Ensembl ENSMUSG00000022571; Mus musculus. [Contig view]
GeneID 66194; -.
KEGG mmu:66194; -.
Phylogenomic databases
HOVERGEN Q9DCC4; -.
Other
SOURCE Pycrl; Mus musculus.
ProtoNet Q9DCC4.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
Amino-acid biosynthesis; NADP; Oxidoreductase; Proline biosynthesis.
Features
SEVIEWER logo Feature table viewer
KeyFrom   To Length Description FTId
CHAIN   1   274  274     Pyrroline-5-carboxylate reductase 3. PRO_0000324563
CONFLICT   59    59        T -> N (in Ref. 1; BAB23252). 
CONFLICT   68    68        N -> S (in Ref. 1; BAB22451). 
CONFLICT   92    93        VT -> IN (in Ref. 1; BAB23252). 
CONFLICT   107   110        LSTM -> HGTK (in Ref. 1; BAB23252). 
CONFLICT   120   120        V -> A (in Ref. 1; BAB23252). 
CONFLICT   128   128        P -> T (in Ref. 1; BAB23252). 
CONFLICT   152   152        L -> I (in Ref. 1; BAB23252). 
CONFLICT   164   164        E -> K (in Ref. 1; BAB23252). 
CONFLICT   190   190        A -> G (in Ref. 1; BAB23252). 
CONFLICT   198   198        M -> I (in Ref. 1; BAB23252). 
CONFLICT   268   268        A -> V (in Ref. 1; BAB23252). 
Sequence information
Length: 274 AA [This is the length of the unprocessed precursor] Molecular weight: 28721 Da [This is the MW of the unprocessed precursor] CRC64: E01FB7133B45BD7C [This is a checksum on the sequence]
        10         20         30         40         50         60 
MAATMSEPRR VGFVGAGRMA EAIARGLIQA GKVEAKQVLA SAPTDNNLCH FRALGCQTTH 

        70         80         90        100        110        120 
SNHEVLQNCP LVIFATKPQV LPTVLAEVAP IVTTEHIIVS VAAGISLSTM EGLLPPNTRV 

       130        140        150        160        170        180 
LRVSPNLPCV VQEGAMVMAR GHHAGNDDAE LLQNLLEACG QCIEVPESYV DIHTGLSGSG 

       190        200        210        220        230        240 
VAFVCTFSEA LAEGAIKMGM PSGLAHRIAA QTLLGTAKML QQEGKHPAQL RTDVLTPAGT 

       250        260        270 
TIHGLHALER GGFRAATMSA VEAATCRAKE LSKK 

Q9DCC4 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

BLAST logo BLAST submission on ExPASy/SIB
or at NCBI (USA)
Tools Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
PROSITE logo ScanProsite, MotifScan SWISS-MODEL Submit a homology modeling request to SWISS-MODEL
NPSA logo NPSA Sequence analysis tools

ExPASy logo ExPASy Home page Site Map Search ExPASy Contact us Swiss-Prot
 Hosted by ca flag CBR Canada Mirror sites: Australia  Brazil  China  Korea  Switzerland
Notice: This page will be replaced with www.uniprot.org. Please send us your feedback!