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P30038

- AL4A1_HUMAN

UniProt

P30038 - AL4A1_HUMAN

Protein

Delta-1-pyrroline-5-carboxylate dehydrogenase, mitochondrial

Gene

ALDH4A1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 156 (01 Oct 2014)
      Sequence version 3 (01 Feb 2005)
      Previous versions | rss
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    Functioni

    Irreversible conversion of delta-1-pyrroline-5-carboxylate (P5C), derived either from proline or ornithine, to glutamate. This is a necessary step in the pathway interconnecting the urea and tricarboxylic acid cycles. The preferred substrate is glutamic gamma-semialdehyde, other substrates include succinic, glutaric and adipic semialdehydes.1 Publication

    Catalytic activityi

    L-glutamate 5-semialdehyde + NAD+ + H2O = L-glutamate + NADH.1 Publication

    Kineticsi

    1. KM=100 µM for NAD1 Publication
    2. KM=32 µM for L-pyrroline-5-carboxylate1 Publication

    Pathwayi

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei208 – 2081NADBy similarity
    Sitei211 – 2111Transition state stabilizerBy similarity
    Binding sitei233 – 2331NADBy similarity
    Active sitei314 – 3141Proton acceptorPROSITE-ProRule annotation
    Active sitei348 – 3481Nucleophile1 PublicationPROSITE-ProRule annotation
    Binding sitei447 – 4471NADBy similarity
    Binding sitei513 – 5131SubstrateBy similarity

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi286 – 2905NADBy similarity

    GO - Molecular functioni

    1. 1-pyrroline-5-carboxylate dehydrogenase activity Source: Reactome
    2. aldehyde dehydrogenase (NAD) activity Source: ProtInc
    3. electron carrier activity Source: UniProtKB
    4. identical protein binding Source: IntAct

    GO - Biological processi

    1. 4-hydroxyproline catabolic process Source: BHF-UCL
    2. cellular nitrogen compound metabolic process Source: Reactome
    3. proline biosynthetic process Source: InterPro
    4. proline catabolic process Source: Reactome
    5. proline catabolic process to glutamate Source: UniProtKB-UniPathway
    6. proline metabolic process Source: ProtInc
    7. small molecule metabolic process Source: Reactome

    Keywords - Molecular functioni

    Oxidoreductase

    Keywords - Biological processi

    Proline metabolism

    Keywords - Ligandi

    NAD

    Enzyme and pathway databases

    BioCyciMetaCyc:HS14757-MONOMER.
    ReactomeiREACT_1002. Proline catabolism.
    SABIO-RKP30038.
    UniPathwayiUPA00261; UER00374.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Delta-1-pyrroline-5-carboxylate dehydrogenase, mitochondrial (EC:1.2.1.88)
    Short name:
    P5C dehydrogenase
    Alternative name(s):
    Aldehyde dehydrogenase family 4 member A1
    L-glutamate gamma-semialdehyde dehydrogenase
    Gene namesi
    Name:ALDH4A1
    Synonyms:ALDH4, P5CDH
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 1

    Organism-specific databases

    HGNCiHGNC:406. ALDH4A1.

    Subcellular locationi

    GO - Cellular componenti

    1. mitochondrial matrix Source: Reactome

    Keywords - Cellular componenti

    Mitochondrion

    Pathology & Biotechi

    Involvement in diseasei

    Hyperprolinemia 2 (HP-2) [MIM:239510]: Characterized by the accumulation of delta-1-pyrroline-5-carboxylate (P5C) and proline. The disorder may be causally related to neurologic manifestations, including seizures and mental retardation.1 Publication
    Note: The disease is caused by mutations affecting the gene represented in this entry.
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti352 – 3521S → L in HP-2; allele ALDH4A1*3; loss of enzyme activity. 1 Publication
    VAR_002260

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi352 – 3521S → A: Reduced affinity for NAD. No effect on enzyme activity. 1 Publication

    Keywords - Diseasei

    Disease mutation

    Organism-specific databases

    MIMi239510. phenotype.
    Orphaneti79101. Hyperprolinemia type 2.
    PharmGKBiPA24701.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transit peptidei1 – 2424Mitochondrion1 PublicationAdd
    BLAST
    Chaini25 – 563539Delta-1-pyrroline-5-carboxylate dehydrogenase, mitochondrialPRO_0000007173Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei31 – 311N6-succinyllysineBy similarity
    Modified residuei52 – 521N6-acetyllysineBy similarity
    Modified residuei93 – 931N6-acetyllysine; alternateBy similarity
    Modified residuei93 – 931N6-succinyllysine; alternateBy similarity
    Modified residuei99 – 991N6-acetyllysine; alternateBy similarity
    Modified residuei99 – 991N6-succinyllysine; alternateBy similarity
    Modified residuei114 – 1141N6-acetyllysine; alternateBy similarity
    Modified residuei114 – 1141N6-succinyllysine; alternateBy similarity
    Modified residuei130 – 1301N6-acetyllysine; alternateBy similarity
    Modified residuei130 – 1301N6-succinyllysine; alternateBy similarity
    Modified residuei175 – 1751N6-acetyllysine; alternateBy similarity
    Modified residuei175 – 1751N6-succinyllysine; alternateBy similarity
    Modified residuei318 – 3181N6-acetyllysineBy similarity
    Modified residuei347 – 3471N6-succinyllysineBy similarity
    Modified residuei365 – 3651N6-acetyllysineBy similarity
    Modified residuei376 – 3761N6-acetyllysineBy similarity
    Modified residuei395 – 3951N6-succinyllysineBy similarity
    Modified residuei462 – 4621N6-acetyllysineBy similarity
    Modified residuei509 – 5091N6-acetyllysine; alternateBy similarity
    Modified residuei509 – 5091N6-succinyllysine; alternateBy similarity
    Modified residuei531 – 5311N6-acetyllysineBy similarity
    Modified residuei552 – 5521N6-acetyllysineBy similarity

    Keywords - PTMi

    Acetylation

    Proteomic databases

    MaxQBiP30038.
    PaxDbiP30038.
    PRIDEiP30038.

    2D gel databases

    OGPiP30038.
    SWISS-2DPAGEP30038.

    PTM databases

    PhosphoSiteiP30038.

    Expressioni

    Tissue specificityi

    Highest expression is found in liver followed by skeletal muscle, kidney, heart, brain, placenta, lung and pancreas.

    Gene expression databases

    ArrayExpressiP30038.
    BgeeiP30038.
    CleanExiHS_ALDH4A1.
    GenevestigatoriP30038.

    Organism-specific databases

    HPAiCAB004645.
    HPA006401.

    Interactioni

    Subunit structurei

    Homodimer.1 Publication

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    itself2EBI-3926971,EBI-3926971

    Protein-protein interaction databases

    BioGridi114208. 5 interactions.
    IntActiP30038. 1 interaction.
    STRINGi9606.ENSP00000290597.

    Structurei

    Secondary structure

    1
    563
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi24 – 307
    Helixi45 – 5713
    Beta strandi62 – 643
    Beta strandi66 – 683
    Beta strandi71 – 733
    Beta strandi78 – 836
    Beta strandi86 – 9510
    Helixi99 – 11820
    Helixi121 – 13616
    Turni137 – 1393
    Helixi140 – 15112
    Helixi155 – 16511
    Helixi167 – 18014
    Beta strandi192 – 1998
    Beta strandi201 – 2077
    Helixi217 – 2259
    Beta strandi229 – 2335
    Helixi236 – 2383
    Helixi239 – 25113
    Beta strandi258 – 2614
    Helixi266 – 2749
    Beta strandi279 – 2868
    Helixi288 – 30013
    Helixi301 – 3044
    Beta strandi310 – 3156
    Beta strandi319 – 3235
    Helixi329 – 34113
    Helixi342 – 3454
    Beta strandi351 – 3577
    Turni358 – 3603
    Helixi361 – 37212
    Turni380 – 3823
    Helixi394 – 40916
    Beta strandi413 – 4175
    Beta strandi424 – 4263
    Beta strandi432 – 4376
    Helixi442 – 4454
    Beta strandi450 – 4589
    Helixi460 – 4623
    Helixi463 – 47210
    Beta strandi475 – 4773
    Beta strandi479 – 4835
    Helixi487 – 49610
    Turni497 – 5004
    Beta strandi502 – 5087
    Turni515 – 5173
    Beta strandi534 – 5363
    Helixi537 – 5415
    Beta strandi542 – 5498
    Helixi560 – 5623

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    3V9GX-ray2.50A/B/C/D18-563[»]
    3V9HX-ray2.40A/B/C/D18-563[»]
    3V9IX-ray2.85A/B/C/D18-563[»]
    4OE5X-ray1.95A/B/C/D18-563[»]
    ProteinModelPortaliP30038.
    SMRiP30038. Positions 23-563.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the aldehyde dehydrogenase family.Curated

    Keywords - Domaini

    Transit peptide

    Phylogenomic databases

    eggNOGiCOG1012.
    HOVERGENiHBG050484.
    InParanoidiP30038.
    KOiK00294.
    OMAiLRWKHTS.
    OrthoDBiEOG7T1R9D.
    PhylomeDBiP30038.
    TreeFamiTF300481.

    Family and domain databases

    Gene3Di3.40.309.10. 1 hit.
    3.40.605.10. 1 hit.
    InterProiIPR016161. Ald_DH/histidinol_DH.
    IPR016163. Ald_DH_C.
    IPR016160. Ald_DH_CS_CYS.
    IPR029510. Ald_DH_CS_GLU.
    IPR016162. Ald_DH_N.
    IPR015590. Aldehyde_DH_dom.
    IPR005931. P5CDH/ALDH4A1.
    [Graphical view]
    PfamiPF00171. Aldedh. 1 hit.
    [Graphical view]
    SUPFAMiSSF53720. SSF53720. 1 hit.
    TIGRFAMsiTIGR01236. D1pyr5carbox1. 1 hit.
    PROSITEiPS00070. ALDEHYDE_DEHYDR_CYS. 1 hit.
    PS00687. ALDEHYDE_DEHYDR_GLU. 1 hit.
    [Graphical view]

    Sequences (3)i

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    This entry describes 3 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: P30038-1) [UniParc]FASTAAdd to Basket

    This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

    « Hide

    MLLPAPALRR ALLSRPWTGA GLRWKHTSSL KVANEPVLAF TQGSPERDAL    50
    QKALKDLKGR MEAIPCVVGD EEVWTSDVQY QVSPFNHGHK VAKFCYADKS 100
    LLNKAIEAAL AARKEWDLKP IADRAQIFLK AADMLSGPRR AEILAKTMVG 150
    QGKTVIQAEI DAAAELIDFF RFNAKYAVEL EGQQPISVPP STNSTVYRGL 200
    EGFVAAISPF NFTAIGGNLA GAPALMGNVV LWKPSDTAML ASYAVYRILR 250
    EAGLPPNIIQ FVPADGPLFG DTVTSSEHLC GINFTGSVPT FKHLWKQVAQ 300
    NLDRFHTFPR LAGECGGKNF HFVHRSADVE SVVSGTLRSA FEYGGQKCSA 350
    CSRLYVPHSL WPQIKGRLLE EHSRIKVGDP AEDFGTFFSA VIDAKSFARI 400
    KKWLEHARSS PSLTILAGGK CDDSVGYFVE PCIVESKDPQ EPIMKEEIFG 450
    PVLSVYVYPD DKYKETLQLV DSTTSYGLTG AVFSQDKDVV QEATKVLRNA 500
    AGNFYINDKS TGSIVGQQPF GGARASGTND KPGGPHYILR WTSPQVIKET 550
    HKPLGDWSYA YMQ 563
    Length:563
    Mass (Da):61,719
    Last modified:February 1, 2005 - v3
    Checksum:i4D964771B7DB5FFD
    GO
    Isoform 2 (identifier: P30038-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-60: Missing.

    Show »
    Length:503
    Mass (Da):55,118
    Checksum:i51F7786045941395
    GO
    Isoform 3 (identifier: P30038-3) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         396-446: Missing.

    Show »
    Length:512
    Mass (Da):56,043
    Checksum:i1AA9C976895301FE
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti68 – 681V → M in AAC50501. (PubMed:8621661)Curated
    Sequence conflicti68 – 681V → M in AAC50500. (PubMed:8621661)Curated
    Sequence conflicti189 – 1913PPS → LPY AA sequence (PubMed:8493898)Curated
    Sequence conflicti189 – 1891P → L AA sequence (PubMed:1395511)Curated
    Sequence conflicti226 – 2261M → I in BAD96206. 1 PublicationCurated
    Sequence conflicti271 – 2711D → E AA sequence (PubMed:1395511)Curated
    Sequence conflicti271 – 2711D → E AA sequence (PubMed:8493898)Curated
    Sequence conflicti354 – 3541L → K AA sequence (PubMed:8493898)Curated
    Sequence conflicti376 – 3761K → R in BAD96206. 1 PublicationCurated
    Sequence conflicti524 – 5263RAS → GSA AA sequence (PubMed:8493898)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti16 – 161P → L in allele ALDH4A1*4. 1 Publication
    Corresponds to variant rs146450609 [ dbSNP | Ensembl ].
    VAR_002259
    Natural varianti352 – 3521S → L in HP-2; allele ALDH4A1*3; loss of enzyme activity. 1 Publication
    VAR_002260
    Natural varianti470 – 4701V → I.2 Publications
    Corresponds to variant rs2230709 [ dbSNP | Ensembl ].
    VAR_029337
    Natural varianti473 – 4731T → A.
    Corresponds to variant rs6695033 [ dbSNP | Ensembl ].
    VAR_048903

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 6060Missing in isoform 2. 1 PublicationVSP_043785Add
    BLAST
    Alternative sequencei396 – 44651Missing in isoform 3. 1 PublicationVSP_047732Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U24267 mRNA. Translation: AAC50501.1.
    U24266 mRNA. Translation: AAC50500.1.
    FJ462711 mRNA. Translation: ACN89883.1.
    AK289972 mRNA. Translation: BAF82661.1.
    AK294552 mRNA. Translation: BAG57755.1.
    AK222486 mRNA. Translation: BAD96206.1.
    AL080251, AL954340 Genomic DNA. Translation: CAI23417.1.
    AL954340, AL080251 Genomic DNA. Translation: CAI39493.1.
    BX537160 Genomic DNA. No translation available.
    CH471134 Genomic DNA. Translation: EAW94858.1.
    BC007581 mRNA. Translation: AAH07581.1.
    BC023600 mRNA. Translation: AAH23600.1.
    CCDSiCCDS188.1. [P30038-1]
    CCDS53272.1. [P30038-2]
    RefSeqiNP_001154976.1. NM_001161504.1. [P30038-2]
    NP_003739.2. NM_003748.3. [P30038-1]
    NP_733844.1. NM_170726.2. [P30038-1]
    UniGeneiHs.77448.

    Genome annotation databases

    EnsembliENST00000290597; ENSP00000290597; ENSG00000159423. [P30038-1]
    ENST00000375341; ENSP00000364490; ENSG00000159423. [P30038-1]
    ENST00000538309; ENSP00000442988; ENSG00000159423. [P30038-2]
    ENST00000538839; ENSP00000446071; ENSG00000159423. [P30038-3]
    GeneIDi8659.
    KEGGihsa:8659.
    UCSCiuc001bbb.3. human. [P30038-1]

    Polymorphism databases

    DMDMi62511241.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U24267 mRNA. Translation: AAC50501.1 .
    U24266 mRNA. Translation: AAC50500.1 .
    FJ462711 mRNA. Translation: ACN89883.1 .
    AK289972 mRNA. Translation: BAF82661.1 .
    AK294552 mRNA. Translation: BAG57755.1 .
    AK222486 mRNA. Translation: BAD96206.1 .
    AL080251 , AL954340 Genomic DNA. Translation: CAI23417.1 .
    AL954340 , AL080251 Genomic DNA. Translation: CAI39493.1 .
    BX537160 Genomic DNA. No translation available.
    CH471134 Genomic DNA. Translation: EAW94858.1 .
    BC007581 mRNA. Translation: AAH07581.1 .
    BC023600 mRNA. Translation: AAH23600.1 .
    CCDSi CCDS188.1. [P30038-1 ]
    CCDS53272.1. [P30038-2 ]
    RefSeqi NP_001154976.1. NM_001161504.1. [P30038-2 ]
    NP_003739.2. NM_003748.3. [P30038-1 ]
    NP_733844.1. NM_170726.2. [P30038-1 ]
    UniGenei Hs.77448.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    3V9G X-ray 2.50 A/B/C/D 18-563 [» ]
    3V9H X-ray 2.40 A/B/C/D 18-563 [» ]
    3V9I X-ray 2.85 A/B/C/D 18-563 [» ]
    4OE5 X-ray 1.95 A/B/C/D 18-563 [» ]
    ProteinModelPortali P30038.
    SMRi P30038. Positions 23-563.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 114208. 5 interactions.
    IntActi P30038. 1 interaction.
    STRINGi 9606.ENSP00000290597.

    Chemistry

    DrugBanki DB00157. NADH.

    PTM databases

    PhosphoSitei P30038.

    Polymorphism databases

    DMDMi 62511241.

    2D gel databases

    OGPi P30038.
    SWISS-2DPAGE P30038.

    Proteomic databases

    MaxQBi P30038.
    PaxDbi P30038.
    PRIDEi P30038.

    Protocols and materials databases

    DNASUi 8659.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000290597 ; ENSP00000290597 ; ENSG00000159423 . [P30038-1 ]
    ENST00000375341 ; ENSP00000364490 ; ENSG00000159423 . [P30038-1 ]
    ENST00000538309 ; ENSP00000442988 ; ENSG00000159423 . [P30038-2 ]
    ENST00000538839 ; ENSP00000446071 ; ENSG00000159423 . [P30038-3 ]
    GeneIDi 8659.
    KEGGi hsa:8659.
    UCSCi uc001bbb.3. human. [P30038-1 ]

    Organism-specific databases

    CTDi 8659.
    GeneCardsi GC01M019197.
    HGNCi HGNC:406. ALDH4A1.
    HPAi CAB004645.
    HPA006401.
    MIMi 239510. phenotype.
    606811. gene.
    neXtProti NX_P30038.
    Orphaneti 79101. Hyperprolinemia type 2.
    PharmGKBi PA24701.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG1012.
    HOVERGENi HBG050484.
    InParanoidi P30038.
    KOi K00294.
    OMAi LRWKHTS.
    OrthoDBi EOG7T1R9D.
    PhylomeDBi P30038.
    TreeFami TF300481.

    Enzyme and pathway databases

    UniPathwayi UPA00261 ; UER00374 .
    BioCyci MetaCyc:HS14757-MONOMER.
    Reactomei REACT_1002. Proline catabolism.
    SABIO-RK P30038.

    Miscellaneous databases

    GeneWikii Aldehyde_dehydrogenase_4_family,_member_A1.
    GenomeRNAii 8659.
    NextBioi 32473.
    PROi P30038.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P30038.
    Bgeei P30038.
    CleanExi HS_ALDH4A1.
    Genevestigatori P30038.

    Family and domain databases

    Gene3Di 3.40.309.10. 1 hit.
    3.40.605.10. 1 hit.
    InterProi IPR016161. Ald_DH/histidinol_DH.
    IPR016163. Ald_DH_C.
    IPR016160. Ald_DH_CS_CYS.
    IPR029510. Ald_DH_CS_GLU.
    IPR016162. Ald_DH_N.
    IPR015590. Aldehyde_DH_dom.
    IPR005931. P5CDH/ALDH4A1.
    [Graphical view ]
    Pfami PF00171. Aldedh. 1 hit.
    [Graphical view ]
    SUPFAMi SSF53720. SSF53720. 1 hit.
    TIGRFAMsi TIGR01236. D1pyr5carbox1. 1 hit.
    PROSITEi PS00070. ALDEHYDE_DEHYDR_CYS. 1 hit.
    PS00687. ALDEHYDE_DEHYDR_GLU. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Cloning, characterization, and expression of cDNAs encoding human delta 1-pyrroline-5-carboxylate dehydrogenase."
      Hu C.-A., Lin W.-W., Valle D.
      J. Biol. Chem. 271:9795-9800(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
      Tissue: Kidney and Retina.
    2. "A novel transcript variant of human ALDH4A1 gene."
      Stagos D., Vasiliou V.
      Submitted (NOV-2008) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3).
    3. "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] (ISOFORMS 1 AND 2), VARIANT ILE-470.
      Tissue: Amygdala and Hippocampus.
    4. 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
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
      Tissue: Adipose tissue.
    5. "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].
    6. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    7. "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], VARIANT ILE-470.
      Tissue: Lung and Placenta.
    8. "Human liver glutamic gamma-semialdehyde dehydrogenase: structural relationship to the yeast enzyme."
      Hempel J., Eckey R., Berie D., Romovacek H., Agarwal D.P., Goedde H.W.
      Comp. Biochem. Physiol. 102B:791-793(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: PARTIAL PROTEIN SEQUENCE.
      Tissue: Liver.
    9. "Human liver protein map: a reference database established by microsequencing and gel comparison."
      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.
      Electrophoresis 13:992-1001(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 25-35.
      Tissue: Liver.
    10. "Human liver high Km aldehyde dehydrogenase (ALDH4): properties and structural relationship to the glutamic gamma-semialdehyde dehydrogenase."
      Agarwal D.P., Eckey R., Hempel J., Goedde H.W.
      Adv. Exp. Med. Biol. 328:191-197(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 94-99; 105-113; 125-139; 176-191; 251-273; 339-347; 354-365 AND 510-526.
      Tissue: Liver.
    11. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    12. "The three-dimensional structural basis of type II hyperprolinemia."
      Srivastava D., Singh R.K., Moxley M.A., Henzl M.T., Becker D.F., Tanner J.J.
      J. Mol. Biol. 420:176-189(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.40 ANGSTROMS) OF 18-563 OF WILD-TYPE; MUTANT ALA-352 AND VARIANT HP-2 LEU-352, CATALYTIC ACTIVITY, FUNCTION, PATHWAY, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, ACTIVE SITE, CHARACTERIZATION OF VARIANT HP-2 LEU-352, MUTAGENESIS OF SER-352.
    13. "Mutations in the Delta1-pyrroline 5-carboxylate dehydrogenase gene cause type II hyperprolinemia."
      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.
      Hum. Mol. Genet. 7:1411-1415(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT HP-2 LEU-352, VARIANT LEU-16.

    Entry informationi

    Entry nameiAL4A1_HUMAN
    AccessioniPrimary (citable) accession number: P30038
    Secondary accession number(s): A8K1Q7
    , B4DGE4, D2D4A3, Q16882, Q53HU4, Q5JNV6, Q8IZ38, Q96IF0, Q9UDI6
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: April 1, 1993
    Last sequence update: February 1, 2005
    Last modified: October 1, 2014
    This is version 156 of the entry and version 3 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program
    DisclaimerAny 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.

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. Human chromosome 1
      Human chromosome 1: entries, gene names and cross-references to MIM
    2. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    3. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    4. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    5. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    6. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    7. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3