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Protein

Stearoyl-[acyl-carrier-protein] 9-desaturase, chloroplastic

Gene
N/A
Organism
Ricinus communis (Castor bean)
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

Converts stearoyl-ACP to oleoyl-ACP by introduction of a cis double bond between carbons 9 and 10 of the acyl chain.2 Publications

<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

Fe2+3 PublicationsNote: Binds 2 Fe2+ ions per subunit.3 Publications

<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: fatty acid metabolism

This protein is involved in the pathway fatty acid metabolism, which is part of Lipid metabolism.
View all proteins of this organism that are known to be involved in the pathway fatty acid metabolism 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 bindingi138Iron 13 Publications1
Metal bindingi176Iron 13 Publications1
Metal bindingi176Iron 23 Publications1
Metal bindingi179Iron 1; via pros nitrogen3 Publications1
Metal bindingi229Iron 23 Publications1
Metal bindingi262Iron 13 Publications1
Metal bindingi262Iron 23 Publications1
Metal bindingi265Iron 2; via pros nitrogen3 Publications1

<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 processFatty acid biosynthesis, Fatty acid metabolism, Lipid biosynthesis, Lipid metabolism
LigandIron, Metal-binding

Enzyme and pathway databases

BRENDA Comprehensive Enzyme Information System

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BRENDAi
1.14.19.2 1204

SABIO-RK: Biochemical Reaction Kinetics Database

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SABIO-RKi
P22337

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

More...
UniPathwayi
UPA00199

<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:
Stearoyl-[acyl-carrier-protein] 9-desaturase, chloroplastic (EC:1.14.19.22 Publications)
Short name:
Stearoyl-ACP desaturase
Alternative name(s):
Acyl-[acyl-carrier-protein] desaturase
Delta(9) stearoyl-acyl carrier protein desaturase
<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>OrganismiRicinus communis (Castor bean)
<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 identifieri3988 [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 lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsfabidsMalpighialesEuphorbiaceaeAcalyphoideaeAcalypheaeRicinus

<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 Cell wall Cytoskeleton Vacuole Chloroplast Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertion Graphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

Chloroplast, Plastid

<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>Mutagenesisi232T → D or E: Decreases desaturase activity and increases oxidase activity. 1 Publication1
Mutagenesisi313D → K or R: Decreases Delta(9) desaturase activity and increases Delta(4) desaturase activity. 1 Publication1

<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 transit peptide.<p><a href='/help/transit' target='_top'>More...</a></p>Transit peptidei1 – 33ChloroplastAdd BLAST33
<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_000000713734 – 396Stearoyl-[acyl-carrier-protein] 9-desaturase, chloroplasticAdd BLAST363

Proteomic databases

PRoteomics IDEntifications database

More...
PRIDEi
P22337

<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 provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms. By default, the information is derived from experiments at the mRNA level, unless specified ‘at protein level’. <br></br>Examples: <a href="http://www.uniprot.org/uniprot/P92958#expression">P92958</a>, <a href="http://www.uniprot.org/uniprot/Q8TDN4#expression">Q8TDN4</a>, <a href="http://www.uniprot.org/uniprot/O14734#expression">O14734</a><p><a href='/help/tissue_specificity' target='_top'>More...</a></p>Tissue specificityi

Higher levels in developing seeds than in leaf and root tissues.

<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

Homodimer.3 Publications

<p>This subsection of the '<a href="http://www.uniprot.org/help/interaction_section%27">Interaction</a> section provides information about binary protein-protein interactions. The data presented in this section are a quality-filtered subset of binary interactions automatically derived from the <a href="http://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated on a monthly basis. Each binary interaction is displayed on a separate line.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsi

WithEntry#Exp.IntActNotes
ACL1.1P078542EBI-15944981,EBI-15944962From Spinacia oleracea.

Protein-protein interaction databases

Database of interacting proteins

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DIPi
DIP-60379N

Protein interaction database and analysis system

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IntActi
P22337, 1 interactor

<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

1396
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase

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ProteinModelPortali
P22337

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

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SMRi
P22337

Database of comparative protein structure models

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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
P22337

<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

<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

Keywords - Domaini

Transit peptide

Phylogenomic databases

KEGG Orthology (KO)

More...
KOi
K03921

Family and domain databases

Conserved Domains Database

More...
CDDi
cd01050 Acyl_ACP_Desat, 1 hit

Gene3D Structural and Functional Annotation of Protein Families

More...
Gene3Di
1.10.620.20, 1 hit

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
IPR005803 FADS-2_CS
IPR005067 Fatty_acid_desaturase-2
IPR009078 Ferritin-like_SF
IPR012348 RNR-like

The PANTHER Classification System

More...
PANTHERi
PTHR31155 PTHR31155, 1 hit

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF03405 FA_desaturase_2, 1 hit

PIRSF; a whole-protein classification database

More...
PIRSFi
PIRSF000346 Dlt9_acylACP_des, 1 hit

Superfamily database of structural and functional annotation

More...
SUPFAMi
SSF47240 SSF47240, 1 hit

PROSITE; a protein domain and family database

More...
PROSITEi
View protein in PROSITE
PS00574 FATTY_ACID_DESATUR_2, 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.

<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 in its mature form or if it represents the precursor.<p><a href='/help/sequence_processing' target='_top'>More...</a></p>Sequence processingi: The displayed sequence is further processed into a mature form.

P22337-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MALKLNPFLS QTQKLPSFAL PPMASTRSPK FYMASTLKSG SKEVENLKKP
60 70 80 90 100
FMPPREVHVQ VTHSMPPQKI EIFKSLDNWA EENILVHLKP VEKCWQPQDF
110 120 130 140 150
LPDPASDGFD EQVRELRERA KEIPDDYFVV LVGDMITEEA LPTYQTMLNT
160 170 180 190 200
LDGVRDETGA SPTSWAIWTR AWTAEENRHG DLLNKYLYLS GRVDMRQIEK
210 220 230 240 250
TIQYLIGSGM DPRTENSPYL GFIYTSFQER ATFISHGNTA RQAKEHGDIK
260 270 280 290 300
LAQICGTIAA DEKRHETAYT KIVEKLFEID PDGTVLAFAD MMRKKISMPA
310 320 330 340 350
HLMYDGRDDN LFDHFSAVAQ RLGVYTAKDY ADILEFLVGR WKVDKLTGLS
360 370 380 390
AEGQKAQDYV CRLPPRIRRL EERAQGRAKE APTMPFSWIF DRQVKL
Length:396
Mass (Da):45,371
Last modified:August 1, 1991 - v1
<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:iE50D4725996392AF
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 AAA74692 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

More...
EMBLi

GenBank nucleotide sequence database

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GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...
DDBJi
Links Updated
M59857 mRNA Translation: AAA74692.1 Different initiation.
X56508 mRNA Translation: CAA39859.1

Protein sequence database of the Protein Information Resource

More...
PIRi
S16463 OHCSAD

NCBI Reference Sequences

More...
RefSeqi
NP_001310659.1, NM_001323730.1

Genome annotation databases

Database of genes from NCBI RefSeq genomes

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GeneIDi
8271760

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
rcu:8271760

<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
M59857 mRNA Translation: AAA74692.1 Different initiation.
X56508 mRNA Translation: CAA39859.1
PIRiS16463 OHCSAD
RefSeqiNP_001310659.1, NM_001323730.1

3D structure databases

Select the link destinations:

Protein Data Bank Europe

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PDBei

Protein Data Bank RCSB

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RCSB PDBi

Protein Data Bank Japan

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PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1AFRX-ray2.40A/B/C/D/E/F52-396[»]
1OQ4X-ray2.40A/B/C/D/E/F34-396[»]
1OQ7X-ray3.20A/B/C/D/E/F34-396[»]
1OQ9X-ray2.40A34-396[»]
1OQBX-ray2.80A/B/C/D/E/F34-396[»]
2J2FX-ray2.65A/B/C/D/E/F34-396[»]
2XZ0X-ray3.00A/B/C34-396[»]
2XZ1X-ray3.35A/B34-396[»]
4V0JX-ray2.80A/B/C/D/E/F66-396[»]
ProteinModelPortaliP22337
SMRiP22337
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

DIPiDIP-60379N
IntActiP22337, 1 interactor

Proteomic databases

PRIDEiP22337

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi8271760
KEGGircu:8271760

Phylogenomic databases

KOiK03921

Enzyme and pathway databases

UniPathwayi
UPA00199

BRENDAi1.14.19.2 1204
SABIO-RKiP22337

Miscellaneous databases

EvolutionaryTraceiP22337

Family and domain databases

CDDicd01050 Acyl_ACP_Desat, 1 hit
Gene3Di1.10.620.20, 1 hit
InterProiView protein in InterPro
IPR005803 FADS-2_CS
IPR005067 Fatty_acid_desaturase-2
IPR009078 Ferritin-like_SF
IPR012348 RNR-like
PANTHERiPTHR31155 PTHR31155, 1 hit
PfamiView protein in Pfam
PF03405 FA_desaturase_2, 1 hit
PIRSFiPIRSF000346 Dlt9_acylACP_des, 1 hit
SUPFAMiSSF47240 SSF47240, 1 hit
PROSITEiView protein in PROSITE
PS00574 FATTY_ACID_DESATUR_2, 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 nameiSTAD_RICCO
<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: P22337
<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, 1991
Last sequence update: August 1, 1991
Last modified: December 5, 2018
This is version 130 of the entry and version 1 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

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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