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O24371

- LOX31_SOLTU

UniProt

O24371 - LOX31_SOLTU

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Protein

Linoleate 13S-lipoxygenase 3-1, chloroplastic

Gene
LOX3.1, LOX-H3
Organism
Solanum tuberosum (Potato)
Status
Reviewed - Annotation score: 4 out of 5 - Experimental evidence at protein leveli

Functioni

Plant lipoxygenases may be involved in a number of diverse aspects of plant physiology including growth and development, pest resistance, and senescence or responses to wounding. Required for the regulation of wound-induced gene expression, but is not involved in the bulk production of jasmonate upon wounding. Catalyzes the hydroperoxidation of lipids containing a cis,cis-1,4-pentadiene structure. Linolenic acid is the preferred substrate, before linoleic and arachidonic acids.2 Publications

Catalytic activityi

Linoleate + O2 = (9Z,11E,13S)-13-hydroperoxyoctadeca-9,11-dienoate.1 Publication
Alpha-linolenate + O2 = (9Z,11E,13S,15Z)-13-hydroperoxyoctadeca-9,11,15-trienoate.1 Publication

Cofactori

Binds 1 iron ion per subunit By similarity.

pH dependencei

Optimum pH is 6.0.1 Publication

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi574 – 5741Iron; catalytic By similarity
Metal bindingi579 – 5791Iron; catalytic By similarity
Metal bindingi765 – 7651Iron; catalytic By similarity
Metal bindingi769 – 7691Iron; catalytic By similarity
Metal bindingi914 – 9141Iron; via carboxylate; catalytic By similarity

GO - Molecular functioni

  1. iron ion binding Source: InterPro
  2. linoleate 13S-lipoxygenase activity Source: UniProtKB-EC

GO - Biological processi

  1. oxylipin biosynthetic process Source: UniProtKB-UniPathway
Complete GO annotation...

Keywords - Molecular functioni

Dioxygenase, Oxidoreductase

Keywords - Biological processi

Fatty acid biosynthesis, Fatty acid metabolism, Lipid biosynthesis, Lipid metabolism, Oxylipin biosynthesis

Keywords - Ligandi

Iron, Metal-binding

Enzyme and pathway databases

UniPathwayiUPA00382.

Names & Taxonomyi

Protein namesi
Recommended name:
Linoleate 13S-lipoxygenase 3-1, chloroplastic (EC:1.13.11.12)
Gene namesi
Name:LOX3.1
Synonyms:LOX-H3
OrganismiSolanum tuberosum (Potato)
Taxonomic identifieri4113 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaeasteridslamiidsSolanalesSolanaceaeSolanoideaeSolaneaeSolanum
ProteomesiUP000011115: Unplaced

Subcellular locationi

Plastidchloroplast stroma. Plastidchloroplast thylakoid 2 Publications

GO - Cellular componenti

  1. chloroplast stroma Source: UniProtKB-SubCell
  2. chloroplast thylakoid Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Chloroplast, Plastid, Thylakoid

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transit peptidei1 – 8383Chloroplast Reviewed predictionAdd
BLAST
Chaini84 – 914831Linoleate 13S-lipoxygenase 3-1, chloroplasticPRO_0000412928Add
BLAST

Expressioni

Tissue specificityi

Expressed in roots and leaves. Detected in tubers and flower buds.1 Publication

Inductioni

Up-regulated localy and systemically 30 minutes after wounding. Up-regulated by jasmonate and abscisic acid treatment. Not induced by pathogen infection.3 Publications

Interactioni

Subunit structurei

Monomer By similarity.

Structurei

3D structure databases

ProteinModelPortaliO24371.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini96 – 218123PLATAdd
BLAST
Domaini221 – 914694LipoxygenaseAdd
BLAST

Sequence similaritiesi

Belongs to the lipoxygenase family.
Contains 1 PLAT domain.

Keywords - Domaini

Transit peptide

Phylogenomic databases

KOiK00454.

Family and domain databases

Gene3Di2.60.60.20. 1 hit.
4.10.372.10. 1 hit.
InterProiIPR008976. Lipase_LipOase.
IPR000907. LipOase.
IPR013819. LipOase_C.
IPR020834. LipOase_CS.
IPR020833. LipOase_Fe_BS.
IPR001246. LipOase_pln.
IPR027433. Lipoxygenase_domain_3.
IPR001024. PLAT/LH2_dom.
[Graphical view]
PANTHERiPTHR11771. PTHR11771. 1 hit.
PfamiPF00305. Lipoxygenase. 1 hit.
PF01477. PLAT. 1 hit.
[Graphical view]
PRINTSiPR00087. LIPOXYGENASE.
PR00468. PLTLPOXGNASE.
SMARTiSM00308. LH2. 1 hit.
[Graphical view]
SUPFAMiSSF48484. SSF48484. 1 hit.
SSF49723. SSF49723. 1 hit.
PROSITEiPS00711. LIPOXYGENASE_1. 1 hit.
PS00081. LIPOXYGENASE_2. 1 hit.
PS51393. LIPOXYGENASE_3. 1 hit.
PS50095. PLAT. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

O24371-1 [UniParc]FASTAAdd to Basket

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MALAKEIMGI SLLEKSSSFM NSSSMALFNP NNYHKENHLW FNQQFQGRRN    50
LSRRKAFRQS TMAAISENLI KVVPEKAVRF KVRAVVTVRN KNKEDLKETI 100
VKHLDAFTDK IGRNVTLELI STDMDPNTKG PKKSNQAVLK DWSKKSNLKT 150
ERVNYTAEFI VDSNFGNPGA ITVTNKHQQE FFLESITIEG FACGPVHFPC 200
NSWVQPKKDH PGKRIFFSNQ PYLPDETPAG LKSLRERELR DLRGDGKGVR 250
KLSDRIYDYD IYNDLGNPDK GIDFARPKLG GDDNVPYPRR CRSGRVPTDT 300
DISAESRVEK PNPTYVPRDE QFEESKMNTF STSRLKAVLH NLIPSLMASI 350
SSNNHDFKGF SDIDNLYSKG LLLKLGLQDE VLKKLPLPKV VSSIKEGDLL 400
KYDTPKILSK DKFAWLRDDE FARQAIAGVN PVSIEKLQFF PPVSKLDPEI 450
YGPQESALKE EHILGHLNGM TVQEALDANK LFIVDHHDVY LPFLDRINAL 500
DGRKAYATRT IFFLSDVGTL KPIAIELSLP QTGPSSRSKR VVTPPVCATG 550
NWTWQIAKAH VCANDAGVHQ LVNHWLRTHA SLEPFILAAH RQLSAMHPIY 600
KLLDPHMRYT LEINGLARQS LINADGVIEA CFTPGRYCME ISAAAYKNWR 650
FDLEGLPADL IRRGMAVPDS TQPHGLKLLI EDYPYAADGL MIWGAIESWV 700
RDYVNHYYPS SAQVCSDREL QAWYAETINV GHVDLRNEEW WPTLATPEDL 750
ISILTTLIWL ASAQHAALNF GQYPYGGYVP NRPPLMRRLI PDENDPEYAV 800
FLADPQKYFF SALPSLLQAT KFMAVVDTLS THSPDEEYLG ERHQPSTWTG 850
DAEIVEAFYK FSAEIGRIEK EIDERNANTK LKNRCGAGVL PYELLAPSSG 900
PGVTCRGVPN SVSI 914
Length:914
Mass (Da):103,089
Last modified:January 1, 1998 - v1
Checksum:i45BBC7D7180390E4
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X96406 mRNA. Translation: CAA65269.1.
PIRiT07065.
RefSeqiNP_001275115.1. NM_001288186.1.
UniGeneiStu.213.

Genome annotation databases

GeneIDi102597498.
KEGGisot:102597498.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X96406 mRNA. Translation: CAA65269.1 .
PIRi T07065.
RefSeqi NP_001275115.1. NM_001288186.1.
UniGenei Stu.213.

3D structure databases

ProteinModelPortali O24371.
ModBasei Search...
MobiDBi Search...

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

GeneIDi 102597498.
KEGGi sot:102597498.

Phylogenomic databases

KOi K00454.

Enzyme and pathway databases

UniPathwayi UPA00382 .

Family and domain databases

Gene3Di 2.60.60.20. 1 hit.
4.10.372.10. 1 hit.
InterProi IPR008976. Lipase_LipOase.
IPR000907. LipOase.
IPR013819. LipOase_C.
IPR020834. LipOase_CS.
IPR020833. LipOase_Fe_BS.
IPR001246. LipOase_pln.
IPR027433. Lipoxygenase_domain_3.
IPR001024. PLAT/LH2_dom.
[Graphical view ]
PANTHERi PTHR11771. PTHR11771. 1 hit.
Pfami PF00305. Lipoxygenase. 1 hit.
PF01477. PLAT. 1 hit.
[Graphical view ]
PRINTSi PR00087. LIPOXYGENASE.
PR00468. PLTLPOXGNASE.
SMARTi SM00308. LH2. 1 hit.
[Graphical view ]
SUPFAMi SSF48484. SSF48484. 1 hit.
SSF49723. SSF49723. 1 hit.
PROSITEi PS00711. LIPOXYGENASE_1. 1 hit.
PS00081. LIPOXYGENASE_2. 1 hit.
PS51393. LIPOXYGENASE_3. 1 hit.
PS50095. PLAT. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  1. "Characterization of three potato lipoxygenases with distinct enzymatic activities and different organ-specific and wound-regulated expression patterns."
    Royo J., Vancanneyt G., Perez A.G., Sanz C., Stormann K., Rosahl S., Sanchez-Serrano J.J.
    J. Biol. Chem. 271:21012-21019(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY, TISSUE SPECIFICITY, INDUCTION BY WOUNDING; JASMONATE AND ABSCISIC ACID, BIOPHYSICOCHEMICAL PROPERTIES.
    Tissue: Leaf.
  2. "Antisense-mediated depletion of a potato lipoxygenase reduces wound induction of proteinase inhibitors and increases weight gain of insect pests."
    Royo J., Leon J., Vancanneyt G., Albar J.P., Rosahl S., Ortego F., Castanera P., Sanchez-Serrano J.J.
    Proc. Natl. Acad. Sci. U.S.A. 96:1146-1151(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  3. "A leaf lipoxygenase of potato induced specifically by pathogen infection."
    Kolomiets M.V., Chen H., Gladon R.J., Braun E.J., Hannapel D.J.
    Plant Physiol. 124:1121-1130(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: INDUCTION BY PATHOGEN.
  4. "Lipoxygenase H1 gene silencing reveals a specific role in supplying fatty acid hydroperoxides for aliphatic aldehyde production."
    Leon J., Royo J., Vancanneyt G., Sanz C., Silkowski H., Griffiths G., Sanchez-Serrano J.J.
    J. Biol. Chem. 277:416-423(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION.
  5. "Differential distribution of the lipoxygenase pathway enzymes within potato chloroplasts."
    Farmaki T., Sanmartin M., Jimenez P., Paneque M., Sanz C., Vancanneyt G., Leon J., Sanchez-Serrano J.J.
    J. Exp. Bot. 58:555-568(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION, INDUCTION BY WOUNDING.

Entry informationi

Entry nameiLOX31_SOLTU
AccessioniPrimary (citable) accession number: O24371
Entry historyi
Integrated into UniProtKB/Swiss-Prot: September 21, 2011
Last sequence update: January 1, 1998
Last modified: June 11, 2014
This is version 91 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Miscellaneousi

Miscellaneous

Depletion of LOX-H3 by co-suppression-mediated gene silencing leads to higher tuber yield, but has no effect on the number of tubers per plant.

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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