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UniProtKB/Swiss-Prot entry P0C2X9

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

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Entry information
Entry name AL4A1_RAT
Primary accession number P0C2X9
Secondary accession numbers None
Integrated into Swiss-Prot on May 15, 2007
Sequence was last modified on May 15, 2007 (Sequence version 1)
Annotations were last modified on    November 25, 2008 (Entry version 15)
Name and origin of the protein
Protein name Delta-1-pyrroline-5-carboxylate dehydrogenase, mitochondrial [Precursor]
Synonyms P5C dehydrogenase
EC 1.5.1.12
Aldehyde dehydrogenase family 4 member A1
Gene name
Name: Aldh4a1
From
Rattus norvegicus (Rat) [TaxID: 10116] 
Taxonomy Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; Muroidea; Muridae; Murinae; Rattus.
Protein existence 1: Evidence at protein level;
References
[1]
 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=Brown Norway;
DOI=10.1038/nature02426; PubMed=15057822 [NCBI, ExPASy, EBI, Israel, Japan]
Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J., Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G., Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G., Morgan M., Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G., Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S., Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T., Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T., Smith D., Lee H.-M., Gustafson E., Cahill P., Kana A., Doucette-Stamm L., Weinstock K., Fechtel K., Weiss R.B., Dunn D.M., Green E.D., Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K., Zhu B., Marra M., Schein J., Bosdet I., Fjell C., Jones S., Krzywinski M., Mathewson C., Siddiqui A., Wye N., McPherson J., Zhao S., Fraser C.M., Shetty J., Shatsman S., Geer K., Chen Y., Abramzon S., Nierman W.C., Havlak P.H., Chen R., Durbin K.J., Egan A., Ren Y., Song X.-Z., Li B., Liu Y., Qin X., Cawley S., Cooney A.J., D'Souza L.M., Martin K., Wu J.Q., Gonzalez-Garay M.L., Jackson A.R., Kalafus K.J., McLeod M.P., Milosavljevic A., Virk D., Volkov A., Wheeler D.A., Zhang Z., Bailey J.A., Eichler E.E., Tuzun E., Birney E., Mongin E., Ureta-Vidal A., Woodwark C., Zdobnov E., Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J., Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D., Schmidt J., Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M., Abril J.F., Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O., Poliakov A., Huebner N., Ganten D., Goesele C., Hummel O., Kreitler T., Lee Y.-A., Monti J., Schulz H., Zimdahl H., Himmelbauer H., Lehrach H., Jacob H.J., Bromberg S., Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E., Lazar J., Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M., Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E., Webber C., Brandt P., Nyakatura G., Adetobi M., Chiaromonte F., Elnitski L., Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K., Miller W., Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S., Zhang Y., Lindpaintner K., Andrews T.D., Caccamo M., Clamp M., Clarke L., Curwen V., Durbin R.M., Eyras E., Searle S.M., Cooper G.M., Batzoglou S., Brudno M., Sidow A., Stone E.A., Payseur B.A., Bourque G., Lopez-Otin C., Puente X.S., Chakrabarti K., Chatterji S., Dewey C., Pachter L., Bray N., Yap V.B., Caspi A., Tesler G., Pevzner P.A., Haussler D., Roskin K.M., Baertsch R., Clawson H., Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J., Rosenbloom K.R., Trumbower H., Weirauch M., Cooper D.N., Stenson P.D., Ma B., Brent M., Arumugam M., Shteynberg D., Copley R.R., Taylor M.S., Riethman H., Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S., Mockrin S., Collins F.S.;
"Genome sequence of the Brown Norway rat yields insights into mammalian evolution.";
Nature 428:493-521(2004).
[2]
 PROTEIN SEQUENCE OF 79-89 AND 318-337, AND MASS SPECTROMETRY.
STRAIN=Sprague-Dawley;
TISSUE=Hippocampus;
Lubec G., Chen W.-Q.;
Submitted (APR-2007) to UniProtKB.
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
AABR03107656; -; NOT_ANNOTATED_CDS; Genomic_DNA.[EMBL / GenBank / DDBJ]
UniGene Rn.203359
3D structure databases
ModBase P0C2X9.
Gene expression databases
ArrayExpress P0C2X9; -.
Ontologies
GO
GO:0005759; Cellular component: mitochondrial matrix (inferred from electronic annotation from InterPro).
GO:0003842; Molecular function: 1-pyrroline-5-carboxylate dehydrogenase activity (inferred from electronic annotation from InterPro).
GO:0055114; Biological process: oxidation reduction (inferred from electronic annotation from UniProtKB-KW).
GO:0006561; Biological process: proline biosynthetic process (inferred from electronic annotation from InterPro).
QuickGo view.
Family and domain databases
InterPro IPR016160; Ald_DHase_CS.
IPR016162; Ald_DHase_N.
IPR015590; Aldehyde_DHase.
IPR005931; d-1-pyrroline-5-COlate_DHase-1.
Graphical view of domain structure.
Gene3D G3DSA:3.40.605.10; Aldehyde_dehydrogenase_N; 1.
PANTHER PTHR11699; Aldehyde_dehyd; 1.
Pfam PF00171; Aldedh; 1.
Pfam graphical view of domain structure.
TIGRFAMs TIGR01236; D1pyr5carbox1; 1.
PROSITE PS00070; ALDEHYDE_DEHYDR_CYS; 1.
PS00687; ALDEHYDE_DEHYDR_GLU; 1.
Genome annotation databases
Ensembl ENSRNOG00000018608; Rattus norvegicus. [Contig view]
Other
ProtoNet P0C2X9.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
Acetylation; Direct protein sequencing; Mitochondrion; NAD; Oxidoreductase; Phosphoprotein; Proline metabolism; Transit peptide.
Features
SEVIEWER logo Feature table viewer
KeyFrom   To Length Description FTId
TRANSIT   1    23  23     Mitochondrion (By similarity). 
CHAIN   24   563  540     Delta-1-pyrroline-5-carboxylate dehydrogenase, mitochondrial. PRO_0000287827
NP_BIND   295   300  6     NAD (By similarity). 
ACT_SITE   313   313        By similarity. 
ACT_SITE   347   347        By similarity. 
MOD_RES   98    98        N6-acetyllysine (By similarity). 
MOD_RES   113   113        N6-acetyllysine (By similarity). 
MOD_RES   401   401        N6-acetyllysine (By similarity). 
MOD_RES   504   504        Phosphotyrosine (By similarity). 
Sequence information
Length: 563 AA [This is the length of the unprocessed precursor] Molecular weight: 61869 Da [This is the MW of the unprocessed precursor] CRC64: AF19417D93825EA5 [This is a checksum on the sequence] 
        10         20         30         40         50         60 
MLPPALLRRS LLSYAWRGSG LRWKHASSLK VANEPILAFT QGSPERDALQ KALNDLKDQT 

        70         80         90        100        110        120 
EAIPCVVGDE EVWTSDVRYQ LSPFNHGHKV AKFCYADKAL LNKAIEAAVL ARKEWDLKPV 

       130        140        150        160        170        180 
ADRAQIFLKA ADMLSGPRRA EILAKTMVGQ GKTVIQAEID AAAELIDFFR FNAKFAVELE 

       190        200        210        220        230        240 
GEQPISVPPS TNHVVYRGLE GFVAAISPFN FTAIGGNLAG APALMGNVVL WKPSDTAMLA 

       250        260        270        280        290        300 
SYAVYRILRE AGLPPNVIQF VPADGPTFGD TVTSSEHLCG INFTGSVPTF KHLWKQVAQN 

       310        320        330        340        350        360 
LDRFRTFPRL AGECGGKNFH FVHSSADVDS VVSGTLRSAF EYGGQKCSAC SRLYVPQSLW 

       370        380        390        400        410        420 
PQIKGRLLEE HSRIKVGNPA EDFGTFFSAV IDAKAFARIK KWLEHARSSP SLSILAGGQC 

       430        440        450        460        470        480 
NESVGYFVEP CIIESKDPQE PIMKEEIFGP VLTVYVYPDE KYRETLQLVD STTSYGLTGA 

       490        500        510        520        530        540 
VFAQDKTIVQ EATRMLRNAA GNFYINDKST GSVVGQQPFG GARASGERDI PGQPRLVQLW 

       550        560 
TEPPFTPLAV SPPLGDWRYS YMQ
P0C2X9 in FASTA format

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