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UniProtKB/Swiss-Prot entry P30038


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

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Entry information
Entry name AL4A1_HUMAN
Primary accession number P30038
Secondary accession numbers A8K1Q7 Q16882 Q53HU4 Q5JNV6 Q8IZ38 Q96IF0
Integrated into Swiss-Prot on April 1, 1993
Sequence was last modified on February 1, 2005 (Sequence version 3)
Annotations were last modified on    November 25, 2008 (Entry version 95)
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
Synonyms: ALDH4, P5CDH
From
Homo sapiens (Human) [TaxID: 9606] 
Taxonomy Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; Homo.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Kidney, and Retina;
DOI=10.1074/jbc.271.16.9795; PubMed=8621661 [NCBI, ExPASy, EBI, Israel, Japan]
Hu C.-A., Lin W.-W., Valle D.;
"Cloning, characterization, and expression of cDNAs encoding human delta 1-pyrroline-5-carboxylate dehydrogenase.";
J. Biol. Chem. 271:9795-9800(1996).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT ILE-470.
TISSUE=Hippocampus;
DOI=10.1038/ng1285; PubMed=14702039 [NCBI, ExPASy, EBI, Israel, Japan]
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.;
"Complete sequencing and characterization of 21,243 full-length human cDNAs.";
Nat. Genet. 36:40-45(2004).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Adipose tissue;
Suzuki Y., Sugano S., Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S.;
Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
DOI=10.1038/nature04727; PubMed=16710414 [NCBI, ExPASy, EBI, Israel, Japan]
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.;
"The DNA sequence and biological annotation of human chromosome 1.";
Nature 441:315-321(2006).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
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.
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT ILE-470.
TISSUE=Lung, and Placenta;
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).
[7]
PARTIAL PROTEIN SEQUENCE.
TISSUE=Liver;
PubMed=1395511 [NCBI, ExPASy, EBI, Israel, Japan]
Hempel J., Eckey R., Berie D., Romovacek H., Agarwal D.P., Goedde H.W.;
"Human liver glutamic gamma-semialdehyde dehydrogenase: structural relationship to the yeast enzyme.";
Comp. Biochem. Physiol. 102B:791-793(1992).
[8]
PROTEIN SEQUENCE OF 25-35.
TISSUE=Liver;
DOI=10.1002/elps.11501301201; PubMed=1286669 [NCBI, ExPASy, EBI, Israel, Japan]
Hochstrasser D.F., Frutiger S., Paquet N., Bairoch A., Ravier F., Pasquali C., Sanchez J.-C., Tissot J.-D., Bjellqvist B., Vargas R., Appel R.D., Hughes G.J.;
"Human liver protein map: a reference database established by microsequencing and gel comparison.";
Electrophoresis 13:992-1001(1992).
[9]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-505, AND MASS SPECTROMETRY.
DOI=10.1016/j.cell.2007.11.025; PubMed=18083107 [NCBI, ExPASy, EBI, Israel, Japan]
Rikova K., Guo A., Zeng Q., Possemato A., Yu J., Haack H., Nardone J., Lee K., Reeves C., Li Y., Hu Y., Tan Z., Stokes M., Sullivan L., Mitchell J., Wetzel R., Macneill J., Ren J.M., Yuan J., Bakalarski C.E., Villen J., Kornhauser J.M., Smith B., Li D., Zhou X., Gygi S.P., Gu T.-L., Polakiewicz R.D., Rush J., Comb M.J.;
"Global survey of phosphotyrosine signaling identifies oncogenic kinases in lung cancer.";
Cell 131:1190-1203(2007).
[10]
VARIANT HPII LEU-352, AND VARIANT LEU-16.
DOI=10.1093/hmg/7.9.1411; PubMed=9700195 [NCBI, ExPASy, EBI, Israel, Japan]
Geraghty M.T., Vaughn D., Nicholson A.J., Lin W.-W., Jimenez-Sanchez G., Obie C., Flynn M.P., Valle D., Hu C.-A.A.;
"Mutations in the Delta1-pyrroline 5-carboxylate dehydrogenase gene cause type II hyperprolinemia.";
Hum. Mol. Genet. 7:1411-1415(1998).
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
U24267; AAC50501.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
U24266; AAC50500.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AK289972; BAF82661.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AK222486; BAD96206.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AL080251; CAI23417.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AL954340; CAI23417.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AL954340; CAI39493.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AL080251; CAI39493.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
CH471134; EAW94858.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC007581; AAH07581.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC023600; AAH23600.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
RefSeq NP_003739.2; -.
NP_733844.1; -.
UniGene Hs.77448
3D structure databases
ModBase P30038.
PTM databases
PhosphoSite P30038; -.
Enzyme and pathway databases
BioCyc MetaCyc:MON-11403; -.
Reactome REACT_13; Metabolism of amino acids.
2D gel databases
SWISS-2DPAGE P30038; -.
OGP P30038; -.
Organism-specific databases
H-InvDB HIX0022349; -.
HGNC HGNC:406; ALDH4A1.
GenAtlas ALDH4A1.
HPA CAB004645; -.
HPA006401; -.
MIM 239510; phenotype. [NCBI / EBI]
606811; gene. [NCBI / EBI]
Orphanet 79101; Hyperprolinaemia type II.
PharmGKB PA24701; -.
GeneCards P30038.
Gene expression databases
ArrayExpress P30038; -.
CleanEx HS_ALDH4A1; -.
GermOnline ENSG00000159423; Homo sapiens.
Ontologies
GO
GO:0005759; Cellular component: mitochondrial matrix (traceable author statement from ProtInc).
GO:0003842; Molecular function: 1-pyrroline-5-carboxylate dehydrogenase activity (traceable author statement from ProtInc).
GO:0004029; Molecular function: aldehyde dehydrogenase (NAD) activity (traceable author statement from ProtInc).
GO:0009055; Molecular function: electron carrier activity (traceable author statement from UniProtKB).
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).
GO:0006562; Biological process: proline catabolic process (traceable author statement from ProtInc).
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.
BLOCKS P30038.
ProtoNet P30038.
Genome annotation databases
Ensembl ENSG00000159423; Homo sapiens. [Contig view]
GeneID 8659; -.
KEGG hsa:8659; -.
Phylogenomic databases
HOGENOM P30038; -.
HOVERGEN P30038; -.
Other
DrugBank DB00157; NADH.
NextBio 32473; -.
SOURCE ALDH4A1; Homo sapiens.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
Acetylation; Direct protein sequencing; Disease mutation; Mitochondrion; NAD; Oxidoreductase; Phosphoprotein; Polymorphism; Proline metabolism; Transit peptide.
Features
SEVIEWER logo Feature table viewer
KeyFrom   To Length Description FTId
TRANSIT   1    24  24     Mitochondrion. 
CHAIN   25   563  539     Delta-1-pyrroline-5-carboxylate dehydrogenase, mitochondrial. PRO_0000007173
NP_BIND   296   301  6     NAD (By similarity). 
ACT_SITE   314   314        Proton acceptor (By similarity). 
ACT_SITE   348   348        Nucleophile (By similarity). 
SITE   211   211  1     Transition state stabilizer (By similarity). 
MOD_RES   99    99        N6-acetyllysine (By similarity). 
MOD_RES   114   114        N6-acetyllysine (By similarity). 
MOD_RES   402   402        N6-acetyllysine (By similarity). 
MOD_RES   505   505        Phosphotyrosine. 
VARIANT   16    16  1     P -> L (in allele ALDH4A1*4). VAR_002259 
VARIANT   352   352  1     S -> L (in HPII; allele ALDH4A1*3). VAR_002260 
VARIANT   470   470  1     V -> I (in dbSNP:rs2230709 [NCBI]). VAR_029337 
CONFLICT   68    68        V -> M (in Ref. 1; AAC50501/AAC50500). 
CONFLICT   189   189        P -> L (in Ref. 7; AA sequence). 
CONFLICT   226   226        M -> I (in Ref. 3; BAD96206). 
CONFLICT   271   271        D -> E (in Ref. 7; AA sequence). 
CONFLICT   376   376        K -> R (in Ref. 3; BAD96206). 
Sequence information
Length: 563 AA [This is the length of the unprocessed precursor] Molecular weight: 61719 Da [This is the MW of the unprocessed precursor] CRC64: 4D964771B7DB5FFD [This is a checksum on the sequence]
        10         20         30         40         50         60 
MLLPAPALRR ALLSRPWTGA GLRWKHTSSL KVANEPVLAF TQGSPERDAL QKALKDLKGR 

        70         80         90        100        110        120 
MEAIPCVVGD EEVWTSDVQY QVSPFNHGHK VAKFCYADKS LLNKAIEAAL AARKEWDLKP 

       130        140        150        160        170        180 
IADRAQIFLK AADMLSGPRR AEILAKTMVG QGKTVIQAEI DAAAELIDFF RFNAKYAVEL 

       190        200        210        220        230        240 
EGQQPISVPP STNSTVYRGL EGFVAAISPF NFTAIGGNLA GAPALMGNVV LWKPSDTAML 

       250        260        270        280        290        300 
ASYAVYRILR EAGLPPNIIQ FVPADGPLFG DTVTSSEHLC GINFTGSVPT FKHLWKQVAQ 

       310        320        330        340        350        360 
NLDRFHTFPR LAGECGGKNF HFVHRSADVE SVVSGTLRSA FEYGGQKCSA CSRLYVPHSL 

       370        380        390        400        410        420 
WPQIKGRLLE EHSRIKVGDP AEDFGTFFSA VIDAKSFARI KKWLEHARSS PSLTILAGGK 

       430        440        450        460        470        480 
CDDSVGYFVE PCIVESKDPQ EPIMKEEIFG PVLSVYVYPD DKYKETLQLV DSTTSYGLTG 

       490        500        510        520        530        540 
AVFSQDKDVV QEATKVLRNA AGNFYINDKS TGSIVGQQPF GGARASGTND KPGGPHYILR 

       550        560 
WTSPQVIKET HKPLGDWSYA YMQ 

P30038 in FASTA format

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