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Protein

Seed linoleate 13S-lipoxygenase-1

Gene

LOX1.1

Organism
Glycine max (Soybean) (Glycine hispida)
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

Plant lipoxygenase may be involved in a number of diverse aspects of plant physiology including growth and development, pest resistance, and senescence or responses to wounding. With linoleate as substrate, L-1 shows a preference for carbon 13 as the site for hydroperoxidation (in contrast to L-2 and L-3, which utilize either carbon 9 or 13). At pH above 8.5, only (9Z,11E,13S)-13-hydroperoxyoctadeca-9,11-dienoate is produced, but as the pH decreases, the proportion of (9S)-hydroperoxide increases linearly until at pH 6.0 it represents about 25 % of the products.1 Publication

Miscellaneous

Soybean contains at least 4 distinct isoenzymes, L-1, L-2, L-3a and L-3b in dry seeds, and at least two distinct isozymes in the hypocotyl/radicle region of the seedling stem.

<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">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

<p>This subsection of the ‘Function’ section provides information relevant to cofactors. A cofactor is any non-protein substance required for a protein to be catalytically active. Some cofactors are inorganic, such as the metal atoms zinc, iron, and copper in various oxidation states. Others, such as most vitamins, are organic.<p><a href='/help/cofactor' target='_top'>More...</a></p>Cofactori

Fe cationPROSITE-ProRule annotation1 PublicationNote: Binds 1 Fe cation per subunit. Iron is tightly bound.PROSITE-ProRule annotation1 Publication

<p>This subsection of the ‘Function’ section describes biophysical and chemical properties, such as maximal absorption, kinetic parameters, pH dependence, redox potentials and temperature dependence.<p><a href='/help/biophysicochemical_properties' target='_top'>More...</a></p>pH dependencei

Inactive below pH 6.0.1 Publication

<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">'Function'</a> section describes the metabolic pathway(s) associated with a protein.<p><a href='/help/pathway' target='_top'>More...</a></p>Pathwayi: oxylipin biosynthesis

This protein is involved in the pathway oxylipin biosynthesis, which is part of Lipid metabolism.PROSITE-ProRule annotation
View all proteins of this organism that are known to be involved in the pathway oxylipin biosynthesis and in Lipid metabolism.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Function’ section indicates at which position the protein binds a given metal ion. The nature of the metal is indicated in the ‘Description’ field.<p><a href='/help/metal' target='_top'>More...</a></p>Metal bindingi499Iron; catalyticPROSITE-ProRule annotation1 Publication1
Metal bindingi504Iron; catalyticPROSITE-ProRule annotation1 Publication1
Metal bindingi690Iron; catalyticPROSITE-ProRule annotation1 Publication1
Metal bindingi694Iron; catalytic1
Metal bindingi839Iron; via carboxylate; catalytic1

<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 functionDioxygenase, Oxidoreductase
Biological processFatty acid biosynthesis, Fatty acid metabolism, Lipid biosynthesis, Lipid metabolism, Oxylipin biosynthesis
LigandIron, Metal-binding

Enzyme and pathway databases

SABIO-RK: Biochemical Reaction Kinetics Database

More...
SABIO-RKi
P08170

UniPathway: a resource for the exploration and annotation of metabolic pathways

More...
UniPathwayi
UPA00382

Chemistry databases

SwissLipids knowledge resource for lipid biology

More...
SwissLipidsi
SLP:000001639

<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_and_taxonomy_section">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:
Seed linoleate 13S-lipoxygenase-1 (EC:1.13.11.122 Publications)
Alternative name(s):
Lipoxygenase-1
Short name:
L-1
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">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:LOX1.1
Synonyms:LOX1
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">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>OrganismiGlycine max (Soybean) (Glycine hispida)
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">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 identifieri3847 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">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 lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsfabidsFabalesFabaceaePapilionoideae50 kb inversion cladeNPAAA cladeindigoferoid/millettioid cladePhaseoleaeGlycineSoja
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">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
  • UP000008827 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes_manual">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

<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

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_and_biotech_section">'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>Mutagenesisi494H → Q: 37% of wild-type activity. 1
Mutagenesisi494H → S: 8% of wild-type activity. 1
Mutagenesisi495Q → A: Reduces catalytic activity. 1 Publication1
Mutagenesisi495Q → E: No effect on catalytic activity. 1 Publication1
Mutagenesisi499H → Q: Inactive. 1
Mutagenesisi504H → Q or S: Inactive. 1
Mutagenesisi517H → Q: 33% of wild-type activity. 1
Mutagenesisi522H → Q: 1% of wild-type activity. 1
Mutagenesisi531H → Q: 20% of wild-type activity. 1
Mutagenesisi542A → G: Changes reaction profile to produce almost equal amounts of 13S- and 9R-hydroperoxyoctadecadienoate. 1 Publication1
Mutagenesisi542A → S: Little effect on reaction profile. 1 Publication1
Mutagenesisi542A → T or V: Complete loss of activity. 1 Publication1
Mutagenesisi690H → Q: Inactive. 1
Mutagenesisi697Q → N or E: Reduces catalytic activity. 1 Publication1

Chemistry databases

ChEMBL database of bioactive drug-like small molecules

More...
ChEMBLi
CHEMBL4586

<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.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00002207171 – 839Seed linoleate 13S-lipoxygenase-1Add BLAST839

<p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni

<p>This subsection of the ‘Expression’ section reports the experimentally proven effects of inducers and repressors (usually chemical compounds or environmental factors) on the level of protein (or mRNA) expression (up-regulation, down-regulation, constitutive expression).<p><a href='/help/induction' target='_top'>More...</a></p>Inductioni

The hydroperoxide product serves to activate the resting enzyme. The activation is accompanied by the oxidation of Fe2+entadiene structure. L-1 prefers anionic substrate.

<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_section">'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_section">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

Monomer.3 Publications

Protein-protein interaction databases

STRING: functional protein association networks

More...
STRINGi
3847.GLYMA13G42320.1

Chemistry databases

BindingDB database of measured binding affinities

More...
BindingDBi
P08170

<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

1839
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase

More...
ProteinModelPortali
P08170

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

More...
SMRi
P08170

Database of comparative protein structure models

More...
ModBasei
Search...

MobiDB: a database of protein disorder and mobility annotations

More...
MobiDBi
Search...

Miscellaneous databases

Relative evolutionary importance of amino acids within a protein sequence

More...
EvolutionaryTracei
P08170

<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_and_domains_section">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>Domaini16 – 145PLATPROSITE-ProRule annotationAdd BLAST130
Domaini148 – 839LipoxygenasePROSITE-ProRule annotationAdd BLAST692

<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

Belongs to the lipoxygenase family.Curated

Phylogenomic databases

InParanoid: Eukaryotic Ortholog Groups

More...
InParanoidi
P08170

KEGG Orthology (KO)

More...
KOi
K15718

Family and domain databases

Gene3D Structural and Functional Annotation of Protein Families

More...
Gene3Di
4.10.372.10, 1 hit

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
IPR000907 LipOase
IPR013819 LipOase_C
IPR036226 LipOase_C_sf
IPR020834 LipOase_CS
IPR020833 LipOase_Fe_BS
IPR001246 LipOase_plant
IPR027433 Lipoxygenase_dom_3
IPR001024 PLAT/LH2_dom
IPR036392 PLAT/LH2_dom_sf

The PANTHER Classification System

More...
PANTHERi
PTHR11771 PTHR11771, 1 hit

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF00305 Lipoxygenase, 1 hit
PF01477 PLAT, 1 hit

Protein Motif fingerprint database; a protein domain database

More...
PRINTSi
PR00087 LIPOXYGENASE
PR00468 PLTLPOXGNASE

Simple Modular Architecture Research Tool; a protein domain database

More...
SMARTi
View protein in SMART
SM00308 LH2, 1 hit

Superfamily database of structural and functional annotation

More...
SUPFAMi
SSF48484 SSF48484, 1 hit
SSF49723 SSF49723, 1 hit

PROSITE; a protein domain and family database

More...
PROSITEi
View protein in PROSITE
PS00711 LIPOXYGENASE_1, 1 hit
PS00081 LIPOXYGENASE_2, 1 hit
PS51393 LIPOXYGENASE_3, 1 hit
PS50095 PLAT, 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_length">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>.<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequencei

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">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.

P08170-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MFSAGHKIKG TVVLMPKNEL EVNPDGSAVD NLNAFLGRSV SLQLISATKA
60 70 80 90 100
DAHGKGKVGK DTFLEGINTS LPTLGAGESA FNIHFEWDGS MGIPGAFYIK
110 120 130 140 150
NYMQVEFFLK SLTLEAISNQ GTIRFVCNSW VYNTKLYKSV RIFFANHTYV
160 170 180 190 200
PSETPAPLVS YREEELKSLR GNGTGERKEY DRIYDYDVYN DLGNPDKSEK
210 220 230 240 250
LARPVLGGSS TFPYPRRGRT GRGPTVTDPN TEKQGEVFYV PRDENLGHLK
260 270 280 290 300
SKDALEIGTK SLSQIVQPAF ESAFDLKSTP IEFHSFQDVH DLYEGGIKLP
310 320 330 340 350
RDVISTIIPL PVIKELYRTD GQHILKFPQP HVVQVSQSAW MTDEEFAREM
360 370 380 390 400
IAGVNPCVIR GLEEFPPKSN LDPAIYGDQS SKITADSLDL DGYTMDEALG
410 420 430 440 450
SRRLFMLDYH DIFMPYVRQI NQLNSAKTYA TRTILFLRED GTLKPVAIEL
460 470 480 490 500
SLPHSAGDLS AAVSQVVLPA KEGVESTIWL LAKAYVIVND SCYHQLMSHW
510 520 530 540 550
LNTHAAMEPF VIATHRHLSV LHPIYKLLTP HYRNNMNINA LARQSLINAN
560 570 580 590 600
GIIETTFLPS KYSVEMSSAV YKNWVFTDQA LPADLIKRGV AIKDPSTPHG
610 620 630 640 650
VRLLIEDYPY AADGLEIWAA IKTWVQEYVP LYYARDDDVK NDSELQHWWK
660 670 680 690 700
EAVEKGHGDL KDKPWWPKLQ TLEDLVEVCL IIIWIASALH AAVNFGQYPY
710 720 730 740 750
GGLIMNRPTA SRRLLPEKGT PEYEEMINNH EKAYLRTITS KLPTLISLSV
760 770 780 790 800
IEILSTHASD EVYLGQRDNP HWTSDSKALQ AFQKFGNKLK EIEEKLVRRN
810 820 830
NDPSLQGNRL GPVQLPYTLL YPSSEEGLTF RGIPNSISI
Length:839
Mass (Da):94,369
Last modified:August 1, 1992 - v2
<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:i1586250ACD3E34A4
GO

<p>This subsection of the ‘Sequence’ section reports difference(s) between the protein sequence shown in the UniProtKB entry and other available protein sequences derived from the same gene.<p><a href='/help/sequence_caution' target='_top'>More...</a></p>Sequence cautioni

The sequence CAA47717 differs from that shown. Reason: Frameshift at positions 663 and 697.Curated

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 conflicti426 – 427AK → RN (Ref. 3) Curated2
Sequence conflicti558 – 560LPS → AL (Ref. 3) Curated3
Sequence conflicti572 – 574KNW → EL (Ref. 3) Curated3
Sequence conflicti641N → P (Ref. 3) Curated1
Sequence conflicti741 – 748KLPTLISL → SCRLSLAV (Ref. 3) Curated8

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
J02795 mRNA Translation: AAA33986.1
X67304 mRNA Translation: CAA47717.1 Frameshift.

Protein sequence database of the Protein Information Resource

More...
PIRi
S25064 DASYL2

NCBI Reference Sequences

More...
RefSeqi
NP_001236153.1, NM_001249224.1

UniGene gene-oriented nucleotide sequence clusters

More...
UniGenei
Gma.947

Genome annotation databases

Database of genes from NCBI RefSeq genomes

More...
GeneIDi
547923

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
gmx:547923

<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
J02795 mRNA Translation: AAA33986.1
X67304 mRNA Translation: CAA47717.1 Frameshift.
PIRiS25064 DASYL2
RefSeqiNP_001236153.1, NM_001249224.1
UniGeneiGma.947

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
1F8NX-ray1.40A1-839[»]
1FGMX-ray1.90A1-839[»]
1FGOX-ray1.62A1-839[»]
1FGQX-ray1.85A1-839[»]
1FGRX-ray1.60A1-839[»]
1FGTX-ray1.62A1-839[»]
1Y4KX-ray1.95A1-839[»]
1YGEX-ray1.40A1-839[»]
2SBLX-ray2.60A/B1-839[»]
3BNBX-ray1.45A1-839[»]
3BNCX-ray1.65A1-839[»]
3BNDX-ray1.60A1-839[»]
3BNEX-ray1.40A1-839[»]
3PZWX-ray1.40A1-839[»]
4WFOX-ray1.14A1-839[»]
4WHAX-ray1.70A1-839[»]
5EEOX-ray2.10A1-839[»]
5T5VX-ray1.80A/B1-839[»]
5TQNX-ray1.80A/B1-839[»]
5TQOX-ray1.70A/B1-839[»]
5TQPX-ray1.70A/B1-839[»]
5TR0X-ray1.85A/B1-839[»]
ProteinModelPortaliP08170
SMRiP08170
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi3847.GLYMA13G42320.1

Chemistry databases

BindingDBiP08170
ChEMBLiCHEMBL4586
SwissLipidsiSLP:000001639

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi547923
KEGGigmx:547923

Phylogenomic databases

InParanoidiP08170
KOiK15718

Enzyme and pathway databases

UniPathwayi
UPA00382

SABIO-RKiP08170

Miscellaneous databases

EvolutionaryTraceiP08170

Protein Ontology

More...
PROi
PR:P08170

Family and domain databases

Gene3Di4.10.372.10, 1 hit
InterProiView protein in InterPro
IPR000907 LipOase
IPR013819 LipOase_C
IPR036226 LipOase_C_sf
IPR020834 LipOase_CS
IPR020833 LipOase_Fe_BS
IPR001246 LipOase_plant
IPR027433 Lipoxygenase_dom_3
IPR001024 PLAT/LH2_dom
IPR036392 PLAT/LH2_dom_sf
PANTHERiPTHR11771 PTHR11771, 1 hit
PfamiView protein in Pfam
PF00305 Lipoxygenase, 1 hit
PF01477 PLAT, 1 hit
PRINTSiPR00087 LIPOXYGENASE
PR00468 PLTLPOXGNASE
SMARTiView protein in SMART
SM00308 LH2, 1 hit
SUPFAMiSSF48484 SSF48484, 1 hit
SSF49723 SSF49723, 1 hit
PROSITEiView protein in PROSITE
PS00711 LIPOXYGENASE_1, 1 hit
PS00081 LIPOXYGENASE_2, 1 hit
PS51393 LIPOXYGENASE_3, 1 hit
PS50095 PLAT, 1 hit

ProtoNet; Automatic hierarchical classification of proteins

More...
ProtoNeti
Search...

<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 nameiLOX1_SOYBN
<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: P08170
<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_and_isoforms">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, 1988
Last sequence update: August 1, 1992
Last modified: December 5, 2018
This is version 168 of the entry and version 2 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 programPlant 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, Complete proteome, 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
  3. PATHWAY comments
    Index of metabolic and biosynthesis pathways
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