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O24370

- LOX21_SOLTU

UniProt

O24370 - LOX21_SOLTU

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Protein

Linoleate 13S-lipoxygenase 2-1, chloroplastic

Gene

LOX2.1

Organism
Solanum tuberosum (Potato)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli

Functioni

Plant lipoxygenase involved in a number of diverse aspects of plant physiology including growth and development, pest resistance, and senescence. May not be 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. Has also some activity with phosphatidylglycerol, but not with galactolipids.2 Publications

Catalytic activityi

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

Cofactori

Binds 1 iron ion per subunit.PROSITE-ProRule annotation

pH dependencei

Optimum pH is 7.0.1 Publication

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi557 – 5571Iron; catalyticPROSITE-ProRule annotation
Metal bindingi562 – 5621Iron; catalyticPROSITE-ProRule annotation
Metal bindingi749 – 7491Iron; catalyticPROSITE-ProRule annotation
Metal bindingi753 – 7531Iron; catalyticPROSITE-ProRule annotation
Metal bindingi899 – 8991Iron; via carboxylate; catalyticPROSITE-ProRule annotation

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 2-1, chloroplastic (EC:1.13.11.12)
Alternative name(s):
Lipoxygenase 2-1
Gene namesi
Name:LOX2.1
Synonyms:LOX-H1
OrganismiSolanum tuberosum (Potato)
Taxonomic identifieri4113 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaeasteridslamiidsSolanalesSolanaceaeSolanoideaeSolaneaeSolanum
ProteomesiUP000011115: Unplaced

Subcellular locationi

Plastidchloroplast stroma. Plastidchloroplast thylakoid
Note: Associated with the non-appressed part of the thylakoid membrane.

GO - Cellular componenti

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

Keywords - Cellular componenti

Chloroplast, Plastid, Thylakoid

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transit peptidei1 – 4040ChloroplastSequence AnalysisAdd
BLAST
Chaini41 – 899859Linoleate 13S-lipoxygenase 2-1, chloroplasticPRO_0000412927Add
BLAST

Expressioni

Tissue specificityi

Expressed in leaves and floral buds.1 Publication

Inductioni

Up-regulated by jasmonate and abscisic acid treatment. Up-regulated localy and systemically at the transcript levels 6 hours after wounding, but the protein levels remain constant. Not induced by pathogen infection.3 Publications

Interactioni

Subunit structurei

Monomer.By similarity

Structurei

3D structure databases

ProteinModelPortaliO24370.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini78 – 200123PLATPROSITE-ProRule annotationAdd
BLAST
Domaini203 – 899697LipoxygenasePROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Belongs to the lipoxygenase family.Curated
Contains 1 lipoxygenase domain.PROSITE-ProRule annotation
Contains 1 PLAT domain.PROSITE-ProRule annotation

Keywords - Domaini

Transit peptide

Phylogenomic databases

InParanoidiO24370.
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.

O24370-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MLKPQLQQSS QSTKALIPSW NTNPLFLASF PINILNKNFR LKKKNNFRVH
60 70 80 90 100
HNYNGASTTK AVLSSTEKAT GVKAVVTVQK QVNLNLSRGL DDIGDLLGKS
110 120 130 140 150
LLLWIVAAEL DHKTGIEKPG IRAYAHRGRD VDGDTHYEAD FVIPQDFGEV
160 170 180 190 200
GAILIENEHH KEMYVKNIVI DGFVHGKVEI TCNSWVHSKF DNPDKRIFFT
210 220 230 240 250
NKSYLPSQTP SGVSRLREEE LVTLRGDGIG ERKVFERIYD YDVYNDLGEA
260 270 280 290 300
DSNNDDAKRP VLGGKELPYP RRCKTGRPRS KKDPLSETRS TFVYVPRDEA
310 320 330 340 350
FSEVKSVAFS GNTVYSVLHA VVPALESVVT DPNLGFPHFP AIDSLFNVGV
360 370 380 390 400
DLPGLGDKKS GLFNVVPRLI KAISDTRKDV LLFESPQLVQ RDKFSWFRDV
410 420 430 440 450
EFARQTLAGL NPYSIRLVTE WPLRSKLDPK VYGPPESEIT KELIEKEIGN
460 470 480 490 500
YMTVEQAVQQ KKLFILDYHD LLLPYVNKVN ELKGSMLYGS RTIFFLTPQG
510 520 530 540 550
TLKPLAIELT RPPVDDKPQW KEVYSPNDWN ATGAWLWKLA KAHVLSHDSG
560 570 580 590 600
YHQLVSHWLR THCCTEPYII ASNRQLSAMH PIYRLLHPHF RYTMEINALA
610 620 630 640 650
REALINANGV IESSFFPGKY AIELSSIAYG AEWRFDQEAL PQNLISRGLA
660 670 680 690 700
VEDPNEPHGL KLAIEDYPFA NDGLVLWDIL KQWVTNYVNH YYPQTNLIES
710 720 730 740 750
DKELQAWWSE IKNVGHGDKR DEPWWPELKT PNDLIGIITT IVWVTSGHHA
760 770 780 790 800
AVNFGQYSYA GYFPNRPTVA RSKMPTEDPT AEEWEWFMNK PEEALLRCFP
810 820 830 840 850
SQIQATKVMA ILDVLSNHSP DEEYIGEKIE PYWAEDPVIN AAFEVFSGKL
860 870 880 890
KELEGIIDAR NNDSKLSNRN GAGVMPYELL KPYSEPGVTG KGVPYSISI
Length:899
Mass (Da):101,937
Last modified:January 1, 1998 - v1
Checksum:i43E9D512C0E808FF
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X96405 mRNA. Translation: CAA65268.1.
PIRiT07062.
RefSeqiNP_001274843.1. NM_001287914.1.
UniGeneiStu.18313.

Genome annotation databases

GeneIDi102596122.
KEGGisot:102596122.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X96405 mRNA. Translation: CAA65268.1 .
PIRi T07062.
RefSeqi NP_001274843.1. NM_001287914.1.
UniGenei Stu.18313.

3D structure databases

ProteinModelPortali O24370.
ModBasei Search...
MobiDBi Search...

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

GeneIDi 102596122.
KEGGi sot:102596122.

Phylogenomic databases

InParanoidi O24370.
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.
  2. "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.
  3. "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: FUNCTION, SUBCELLULAR LOCATION, CATALYTIC ACTIVITY.
  4. "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 nameiLOX21_SOLTU
AccessioniPrimary (citable) accession number: O24370
Entry historyi
Integrated into UniProtKB/Swiss-Prot: September 21, 2011
Last sequence update: January 1, 1998
Last modified: October 29, 2014
This is version 94 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Miscellaneousi

Miscellaneous

99% depletion of LOX-H1 by co-suppression-mediated gene silencing has no effect on the basal or wound-induced levels of jasmonates but results in a marked reduction in the production of volatile aliphatic C6 aldehydes.

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