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Entry version 172 (17 Jun 2020)
Sequence version 3 (21 Mar 2012)
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Protein

Cytosolic 10-formyltetrahydrofolate dehydrogenase

Gene

Aldh1l1

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score:

Annotation score:5 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the 'correct annotation' for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the 'protein existence' evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functioni

Caution

The phosphoserine observed at Ser-354 in PubMed:16396499 undoubtedly results from the secondary neutral loss of pantetheine from the phosphodiester linked cofactor.Curated

<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes the catalytic activity of an enzyme, i.e. a chemical reaction that the enzyme catalyzes.<p><a href='/help/catalytic_activity' target='_top'>More...</a></p>Catalytic activityi

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section is used for enzymes and indicates the residues directly involved in catalysis.<p><a href='/help/act_site' target='_top'>More...</a></p>Active sitei106Proton donorBy similarity1
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes the interaction between a single amino acid and another chemical entity. Priority is given to the annotation of physiological ligands.<p><a href='/help/binding' target='_top'>More...</a></p>Binding sitei142SubstrateBy similarity1
<p>This subsection describes interesting single amino acid sites on the sequence that are not defined in any other subsection. This subsection can be displayed in different sections ('Function', 'PTM / Processing', 'Pathology and Biotech') according to its content.<p><a href='/help/site' target='_top'>More...</a></p>Sitei142Essential for catalytic activity1
Active sitei673Proton acceptorCurated1
Active sitei707Proton donorCurated1
Binding sitei757NADP2 Publications1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes a region in the protein which binds nucleotide phosphates. It always involves more than one amino acid and includes all residues involved in nucleotide-binding.<p><a href='/help/np_bind' target='_top'>More...</a></p>Nucleotide bindingi571 – 573NADP2 Publications3
Nucleotide bindingi597 – 600NADP2 Publications4
Nucleotide bindingi630 – 635NADP2 Publications6
Nucleotide bindingi650 – 651NADP2 Publications2
Nucleotide bindingi804 – 806NADP2 Publications3

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

GO - Biological processi

<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi

Molecular functionOxidoreductase
Biological processOne-carbon metabolism
LigandNADP

Enzyme and pathway databases

BRENDA Comprehensive Enzyme Information System

More...
BRENDAi
1.5.1.6 5301

Reactome - a knowledgebase of biological pathways and processes

More...
Reactomei
R-RNO-196757 Metabolism of folate and pterines

SABIO-RK: Biochemical Reaction Kinetics Database

More...
SABIO-RKi
P28037

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>Protein namesi
Recommended name:
Cytosolic 10-formyltetrahydrofolate dehydrogenase (EC:1.5.1.6)
Short name:
10-FTHFDH
Short name:
FDH
Alternative name(s):
Aldehyde dehydrogenase family 1 member L1
FBP-CI
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: 'Name', 'Synonyms', 'Ordered locus names' and 'ORF names'.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi
Name:Aldh1l1
Synonyms:Fthfd
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiRattus norvegicus (Rat)
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the 'taxonomic identifier' or 'taxid'.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri10116 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaMyomorphaMuroideaMuridaeMurinaeRattus
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi
  • UP000002494 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes%5Fmanual">proteome</a> can consist of several components.<br></br>The component name refers to the genomic component encoding a set of proteins.<p><a href='/help/proteome_component' target='_top'>More...</a></p> Componenti: Unplaced

Organism-specific databases

Rat genome database

More...
RGDi
621294 Aldh1l1

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte & Seán O’Donoghue; Source: COMPARTMENTS

Keywords - Cellular componenti

Cytoplasm

<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/manual/pathology%5Fand%5Fbiotech%5Fsection">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi142D → A, N, E or Q: Loss of hydrolase activity. 1 Publication1
Mutagenesisi673E → A: Loss of aldehyde dehydrogenase activity. 1 Publication1
Mutagenesisi707C → A: Loss of dehydrogenase activity. No effect on hydrolase activity and NADP binding. 1 Publication1

Chemistry databases

ChEMBL database of bioactive drug-like small molecules

More...
ChEMBLi
CHEMBL3414419

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'PTM / Processing' section describes the extent of a polypeptide chain in the mature protein following processing or proteolytic cleavage.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00001994221 – 902Cytosolic 10-formyltetrahydrofolate dehydrogenaseAdd BLAST902

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'PTM / Processing' section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei9PhosphoserineBy similarity1
Modified residuei38N6-succinyllysineBy similarity1
Modified residuei354O-(pantetheine 4'-phosphoryl)serine; alternatePROSITE-ProRule annotation1
Modified residuei354Phosphoserine; alternateCombined sources1
Modified residuei629PhosphoserineBy similarity1
Modified residuei631PhosphoserineBy similarity1
Modified residuei660N6-succinyllysineBy similarity1
Modified residuei767N6-succinyllysineBy similarity1
Modified residuei825PhosphoserineBy similarity1
Modified residuei882N6-acetyllysineBy similarity1

Keywords - PTMi

Acetylation, Phosphopantetheine, Phosphoprotein

Proteomic databases

PeptideAtlas

More...
PeptideAtlasi
P28037

PRoteomics IDEntifications database

More...
PRIDEi
P28037

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

More...
iPTMneti
P28037

Comprehensive resource for the study of protein post-translational modifications (PTMs) in human, mouse and rat.

More...
PhosphoSitePlusi
P28037

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

<p>This subsection of the <a href="http://www.uniprot.org/help/interaction%5Fsection">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function%5Fsection">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

Homotetramer.

3 Publications

Protein-protein interaction databases

STRING: functional protein association networks

More...
STRINGi
10116.ENSRNOP00000065882

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

Secondary structure

1902
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

SWISS-MODEL Repository - a database of annotated 3D protein structure models

More...
SMRi
P28037

Database of comparative protein structure models

More...
ModBasei
Search...

Protein Data Bank in Europe - Knowledge Base

More...
PDBe-KBi
Search...

Miscellaneous databases

Relative evolutionary importance of amino acids within a protein sequence

More...
EvolutionaryTracei
P28037

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/family%5Fand%5Fdomains%5Fsection">Family and Domains</a> section describes the position and type of a domain, which is defined as a specific combination of secondary structures organized into a characteristic three-dimensional structure or fold.<p><a href='/help/domain' target='_top'>More...</a></p>Domaini318 – 395CarrierPROSITE-ProRule annotationAdd BLAST78

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Family and Domains' section describes a region of interest that cannot be described in other subsections.<p><a href='/help/region' target='_top'>More...</a></p>Regioni1 – 203GARTAdd BLAST203
Regioni88 – 90Substrate bindingBy similarity3
Regioni417 – 902Aldehyde dehydrogenaseAdd BLAST486

<p>This subsection of the 'Family and domains' section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

In the N-terminal section; belongs to the GART family.Curated
In the C-terminal section; belongs to the aldehyde dehydrogenase family. ALDH1L subfamily.Curated

Phylogenomic databases

InParanoid: Eukaryotic Ortholog Groups

More...
InParanoidi
P28037

KEGG Orthology (KO)

More...
KOi
K00289

Database of Orthologous Groups

More...
OrthoDBi
153834at2759

Family and domain databases

Gene3D Structural and Functional Annotation of Protein Families

More...
Gene3Di
1.10.1200.10, 1 hit
3.10.25.10, 1 hit
3.40.309.10, 1 hit
3.40.605.10, 1 hit

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
IPR011407 10_FTHF_DH
IPR036736 ACP-like_sf
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
IPR005793 Formyl_trans_C
IPR037022 Formyl_trans_C_sf
IPR002376 Formyl_transf_N
IPR036477 Formyl_transf_N_sf
IPR011034 Formyl_transferase-like_C_sf
IPR001555 GART_AS
IPR009081 PP-bd_ACP

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF00171 Aldedh, 1 hit
PF02911 Formyl_trans_C, 1 hit
PF00551 Formyl_trans_N, 1 hit

PIRSF; a whole-protein classification database

More...
PIRSFi
PIRSF036489 10-FTHFDH, 1 hit

Superfamily database of structural and functional annotation

More...
SUPFAMi
SSF47336 SSF47336, 1 hit
SSF50486 SSF50486, 1 hit
SSF53328 SSF53328, 1 hit
SSF53720 SSF53720, 1 hit

PROSITE; a protein domain and family database

More...
PROSITEi
View protein in PROSITE
PS00070 ALDEHYDE_DEHYDR_CYS, 1 hit
PS00687 ALDEHYDE_DEHYDR_GLU, 1 hit
PS50075 CARRIER, 1 hit
PS00373 GART, 1 hit

<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence%5Flength">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>. The information is filed in different subsections. The current subsections and their content are listed below:<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequence (1+)i

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.

This entry has 1 described isoform and 2 potential isoforms that are computationally mapped.Show allAlign All

P28037-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MKIAVIGQSL FGQEVYCQLR KEGHEVVGVF TIPDKDGKAD PLGLEAEKDG
60 70 80 90 100
VPVFKFPRWR ARGQALPEVV AKYQALGAEL NVLPFCSQFI PMEVINAPRH
110 120 130 140 150
GSIIYHPSLL PRHRGASAIN WTLIHGDKKG GFTIFWADDG LDTGDLLLQK
160 170 180 190 200
ECEVLPDDTV STLYNRFLFP EGIKGMVQAV RLIAEGTAPR CPQSEEGATY
210 220 230 240 250
EGIQKKETAK INWDQPAEAI HNWIRGNDKV PGAWTEACGQ KLTFFNSTLN
260 270 280 290 300
TSGLSTQGEA LPIPGAHRPG VVTKAGLILF GNDDRMLLVK NIQLEDGKMM
310 320 330 340 350
PASQFFKGSA SSDLELTEAE LATAEAVRSS WMRILPNVPE VEDSTDFFKS
360 370 380 390 400
GAASVDVVRL VEEVKELCDG LELENEDVYM ATTFRGFIQL LVRKLRGEDD
410 420 430 440 450
ESECVINYVE KAVNKLTLQM PYQLFIGGEF VDAEGSKTYN TINPTDGSVI
460 470 480 490 500
CQVSLAQVSD VDKAVAAAKE AFENGLWGKI NARDRGRLLY RLADVMEQHQ
510 520 530 540 550
EELATIEALD AGAVYTLALK THVGMSIQTF RYFAGWCDKI QGATIPINQA
560 570 580 590 600
RPNRNLTLTK KEPVGVCGIV IPWNYPLMML SWKTAACLAA GNTVVIKPAQ
610 620 630 640 650
VTPLTALKFA ELTLKAGIPK GVVNILPGSG SLVGQRLSDH PDVRKIGFTG
660 670 680 690 700
STEVGKHIMK SCALSNVKKV SLELGGKSPL IIFADCDLNK AVQMGMSSVF
710 720 730 740 750
FNKGENCIAA GRLFVEESIH NQFVQKVVEE VEKMKIGNPL ERDTNHGPQN
760 770 780 790 800
HEAHLRKLVE YCQRGVKEGA TLVCGGNQVP RPGFFFQPTV FTDVEDHMYI
810 820 830 840 850
AKEESFGPIM IISRFADGDV DAVLSRANAT EFGLASGVFT RDINKALYVS
860 870 880 890 900
DKLQAGTVFI NTYNKTDVAA PFGGFKQSGF GKDLGEAALN EYLRIKTVTF

EY
Length:902
Mass (Da):98,874
Last modified:March 21, 2012 - v3
<p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> Checksum:i562A8CBD73D6474A
GO

<p>In eukaryotic reference proteomes, unreviewed entries that are likely to belong to the same gene are computationally mapped, based on gene identifiers from Ensembl, EnsemblGenomes and model organism databases.<p><a href='/help/gene_centric_isoform_mapping' target='_top'>More...</a></p>Computationally mapped potential isoform sequencesi

There are 2 potential isoforms mapped to this entry.BLASTAlignShow allAdd to basket
EntryEntry nameProtein names
Gene namesLengthAnnotation
M0R8T2M0R8T2_RAT
10-formyltetrahydrofolate dehydroge...
Aldh1l1
907Annotation score:

Annotation score:3 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the 'correct annotation' for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
A0A0G2K0D8A0A0G2K0D8_RAT
10-formyltetrahydrofolate dehydroge...
Aldh1l1
902Annotation score:

Annotation score:3 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the 'correct annotation' for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Sequence' section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti51 – 52VP → RA in AAA70429 (PubMed:1848231).Curated2
Sequence conflicti283 – 284DD → EH in AAA70429 (PubMed:1848231).Curated2
Sequence conflicti386G → E in AAA70429 (PubMed:1848231).Curated1
Sequence conflicti411K → R in AAA70429 (PubMed:1848231).Curated1
Sequence conflicti511A → R in AAA70429 (PubMed:1848231).Curated1

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

More...
EMBLi

GenBank nucleotide sequence database

More...
GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...
DDBJi
Links Updated
M59861 mRNA Translation: AAA70429.1
BC089101 mRNA Translation: AAH89101.1

Protein sequence database of the Protein Information Resource

More...
PIRi
A23709 A60560

NCBI Reference Sequences

More...
RefSeqi
NP_071992.1, NM_022547.1

Genome annotation databases

Database of genes from NCBI RefSeq genomes

More...
GeneIDi
64392

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
rno:64392

<p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsi

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M59861 mRNA Translation: AAA70429.1
BC089101 mRNA Translation: AAH89101.1
PIRiA23709 A60560
RefSeqiNP_071992.1, NM_022547.1

3D structure databases

Select the link destinations:

Protein Data Bank Europe

More...
PDBei

Protein Data Bank RCSB

More...
RCSB PDBi

Protein Data Bank Japan

More...
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1S3IX-ray2.30A1-310[»]
2O2PX-ray1.70A/B/C/D397-902[»]
2O2QX-ray2.00A/B/C/D397-902[»]
2O2RX-ray2.20A/B/C/D397-902[»]
3RHJX-ray1.89A/B/C/D397-902[»]
3RHLX-ray2.00A/B/C/D397-902[»]
3RHMX-ray2.38A/B/C/D397-902[»]
3RHOX-ray2.26A/B/C/D397-902[»]
3RHPX-ray2.50A/B/C/D397-902[»]
3RHQX-ray2.10A/B/C/D397-902[»]
3RHRX-ray2.30A/B/C/D397-902[»]
4GNZX-ray2.30A/B/C/D397-902[»]
4GO0X-ray3.38A/B/C/D397-902[»]
4GO2X-ray2.28A/B/C/D397-902[»]
SMRiP28037
ModBaseiSearch...
PDBe-KBiSearch...

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000065882

Chemistry databases

ChEMBLiCHEMBL3414419

PTM databases

iPTMnetiP28037
PhosphoSitePlusiP28037

Proteomic databases

PeptideAtlasiP28037
PRIDEiP28037

Genome annotation databases

GeneIDi64392
KEGGirno:64392

Organism-specific databases

Comparative Toxicogenomics Database

More...
CTDi
10840
RGDi621294 Aldh1l1

Phylogenomic databases

InParanoidiP28037
KOiK00289
OrthoDBi153834at2759

Enzyme and pathway databases

BRENDAi1.5.1.6 5301
ReactomeiR-RNO-196757 Metabolism of folate and pterines
SABIO-RKiP28037

Miscellaneous databases

EvolutionaryTraceiP28037

Protein Ontology

More...
PROi
PR:P28037

Family and domain databases

Gene3Di1.10.1200.10, 1 hit
3.10.25.10, 1 hit
3.40.309.10, 1 hit
3.40.605.10, 1 hit
InterProiView protein in InterPro
IPR011407 10_FTHF_DH
IPR036736 ACP-like_sf
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
IPR005793 Formyl_trans_C
IPR037022 Formyl_trans_C_sf
IPR002376 Formyl_transf_N
IPR036477 Formyl_transf_N_sf
IPR011034 Formyl_transferase-like_C_sf
IPR001555 GART_AS
IPR009081 PP-bd_ACP
PfamiView protein in Pfam
PF00171 Aldedh, 1 hit
PF02911 Formyl_trans_C, 1 hit
PF00551 Formyl_trans_N, 1 hit
PIRSFiPIRSF036489 10-FTHFDH, 1 hit
SUPFAMiSSF47336 SSF47336, 1 hit
SSF50486 SSF50486, 1 hit
SSF53328 SSF53328, 1 hit
SSF53720 SSF53720, 1 hit
PROSITEiView protein in PROSITE
PS00070 ALDEHYDE_DEHYDR_CYS, 1 hit
PS00687 ALDEHYDE_DEHYDR_GLU, 1 hit
PS50075 CARRIER, 1 hit
PS00373 GART, 1 hit

ProtoNet; Automatic hierarchical classification of proteins

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ProtoNeti
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MobiDB: a database of protein disorder and mobility annotations

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MobiDBi
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<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>This subsection of the 'Entry information' section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiAL1L1_RAT
<p>This subsection of the 'Entry information' section provides one or more accession number(s). These are stable identifiers and should be used to cite UniProtKB entries. Upon integration into UniProtKB, each entry is assigned a unique accession number, which is called 'Primary (citable) accession number'.<p><a href='/help/accession_numbers' target='_top'>More...</a></p>AccessioniPrimary (citable) accession number: P28037
Secondary accession number(s): Q5HZB2
<p>This subsection of the 'Entry information' section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification ('Last modified'). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: August 1, 1992
Last sequence update: March 21, 2012
Last modified: June 17, 2020
This is version 172 of the entry and version 3 of the sequence. See complete history.
<p>This subsection of the 'Entry information' section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

<p>This section contains any relevant information that doesn't fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

Keywords - Technical termi

3D-structure, Direct protein sequencing, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families
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