Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Entry version 142 (07 Apr 2021)
Sequence version 1 (01 Oct 1996)
Previous versions | rss
Add a publicationFeedback
Protein

Acyl-coenzyme A diphosphatase SCS3

Gene

SCS3

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
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

Fatty acyl-coenzyme A (CoA) diphosphatase that hydrolyzes fatty acyl-CoA to yield acyl-4'-phosphopantetheine and adenosine 3',5'-bisphosphate. Preferentially hydrolyzes unsaturated long-chain acyl-CoA substrates in the endoplasmic reticulum (ER) lumen (By similarity). This catalytic activity is required for maintaining ER structure and for lipid droplets (LDs) biogenesis, which are lipid storage organelles involved in maintaining lipid and energy homeostasis (PubMed:26504167, PubMed:29526591, PubMed:32915949) (By similarity). May directly bind to diacylglycerol (DAGs) and triacylglycerol, which is also important for LD biogenesis (By similarity). May support directional budding of nacent LDs from the ER into the cytosol by reducing DAG levels at sites of LD formation (PubMed:29526591) (By similarity). May play a role in the regulation of cell morphology and cytoskeletal organization (By similarity). Involved in phospholipid biosynthesis (PubMed:7706223, PubMed:29417057, PubMed:32915949) (By similarity).UniRule annotationBy similarity5 Publications

Miscellaneous

Present with 538 molecules/cell in log phase SD medium.1 Publication

<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 sitei235UniRule annotation1
Active sitei350UniRule annotation1

<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 functionHydrolase
Biological processLipid biosynthesis, Lipid metabolism, Phospholipid biosynthesis, Phospholipid metabolism

Enzyme and pathway databases

Reactome - a knowledgebase of biological pathways and processes

More...
Reactomei
R-SCE-8964572, Lipid particle organization

<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:
Acyl-coenzyme A diphosphatase SCS3UniRule annotation (EC:3.6.1.-UniRule annotation)
Alternative name(s):
FIT family protein SCS31 PublicationUniRule annotation
<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:SCS31 PublicationUniRule annotation
Synonyms:FIT2B
Ordered Locus Names:YGL126WImported
ORF Names:G2868
<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>OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
<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 identifieri559292 [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 lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
<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
  • UP000002311 <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: Chromosome VII

Organism-specific databases

Saccharomyces Genome Database

More...
SGDi
S000003094, SCS3

Eukaryotic Pathogen, Vector and Host Database Resources

More...
VEuPathDBi
FungiDB:YGL126W

<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

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/subcellular%5Flocation%5Fsection">'Subcellular location'</a> section describes the subcellular compartment where each non-membrane region of a membrane-spanning protein is found.<p><a href='/help/topo_dom' target='_top'>More...</a></p>Topological domaini1 – 7CytoplasmicCurated7
<p>This subsection of the <a href="http://www.uniprot.org/help/subcellular%5Flocation%5Fsection">'Subcellular location'</a> section describes the extent of a membrane-spanning region of the protein. It denotes the presence of both alpha-helical transmembrane regions and the membrane spanning regions of beta-barrel transmembrane proteins.<p><a href='/help/transmem' target='_top'>More...</a></p>Transmembranei8 – 28HelicalSequence analysisAdd BLAST21
Topological domaini29 – 43LumenalCuratedAdd BLAST15
Transmembranei44 – 64HelicalSequence analysisAdd BLAST21
Topological domaini65 – 88CytoplasmicCuratedAdd BLAST24
Transmembranei89 – 109HelicalSequence analysisAdd BLAST21
Topological domaini110 – 233LumenalCuratedAdd BLAST124
Transmembranei234 – 254HelicalSequence analysisAdd BLAST21
Topological domaini255 – 325CytoplasmicCuratedAdd BLAST71
Transmembranei326 – 346HelicalSequence analysisAdd BLAST21
Topological domaini347 – 356LumenalCurated10
Transmembranei357 – 377HelicalSequence analysisAdd BLAST21
Topological domaini378 – 380CytoplasmicCurated3

Keywords - Cellular componenti

Endoplasmic reticulum, Membrane

<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>Mutagenesisi235H → A: Inositol auxotrophy. Impaired ER morphology with the apparition of clumps of ER membrane. 1 Publication1
Mutagenesisi350H → A: Inositol auxotrophy. Impaired ER morphology with the apparition of clumps of ER membrane. 1 Publication1
Mutagenesisi354E → A: Temperature sensitive. Inositol auxotroph at 37 degrees Celsius, but partially supports growth on inositol at 25 degrees Celsius. Impaired ER morphology and aberrant lipid droplet (LD) budding. 1 Publication1
Mutagenesisi354E → K or V: Inositol auxotrophy. Impaired ER morphology and aberrant lipid droplet (LD) budding. 1 Publication1
Mutagenesisi354E → Q or D: No defect in inositol biosynthesis. Aberrant lipid droplet (LD) budding. 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 polypeptide chain in the mature protein following processing or proteolytic cleavage.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00000976351 – 380Acyl-coenzyme A diphosphatase SCS3Add BLAST380

Proteomic databases

PaxDb, a database of protein abundance averages across all three domains of life

More...
PaxDbi
P53012

PRoteomics IDEntifications database

More...
PRIDEi
P53012

<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

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGRID)

More...
BioGRIDi
33125, 207 interactors

Database of interacting proteins

More...
DIPi
DIP-1209N

Protein interaction database and analysis system

More...
IntActi
P53012, 7 interactors

Molecular INTeraction database

More...
MINTi
P53012

STRING: functional protein association networks

More...
STRINGi
4932.YGL126W

Miscellaneous databases

RNAct, Protein-RNA interaction predictions for model organisms.

More...
RNActi
P53012, protein

<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

3D structure databases

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

More...
SMRi
P53012

Database of comparative protein structure models

More...
ModBasei
Search...

<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

Belongs to the FIT family. Fungal FIT2B/SCS3 subfamily.UniRule annotation

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...
eggNOGi
KOG3750, Eukaryota

Ensembl GeneTree

More...
GeneTreei
ENSGT00530000063693

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...
HOGENOMi
CLU_048143_2_1_1

InParanoid: Eukaryotic Ortholog Groups

More...
InParanoidi
P53012

Identification of Orthologs from Complete Genome Data

More...
OMAi
HDPSGHI

Family and domain databases

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
IPR019388, FIT

The PANTHER Classification System

More...
PANTHERi
PTHR23129, PTHR23129, 1 hit

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF10261, Scs3p, 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>Sequencei

<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.

P53012-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MSSKWFNAIH LLVCPLTVLV GYLMNAYGYG AALQATLNKD GLVNAMLVKK
60 70 80 90 100
GWFWTSLVGW WCIIRYRAVP GATGRDRRHI VQSFKRYAIL TVWWYVFTQG
110 120 130 140 150
IWFGVGPIMD LVFVYTGGHC HYDVFDDAGH VNEDFQGSVT RTNRALALIH
160 170 180 190 200
NVLTLHGHHQ EHRQQQLWDR SIGSIQGALQ ATQPKTPKNV TASAAAAINT
210 220 230 240 250
FIHDQMHRWQ GPLTTSAQCR RFGGHWAGGH DPSGHVFLAT LMCMFLLGEL
260 270 280 290 300
RVFGRRALAH LYAQKWQLVR LVTRLFDTGP LWTWRRCGGG SMTCGARLWR
310 320 330 340 350
AIVEPPVTCA AALLRLTRCI ACDHPVIILL TLLVTWLWQL LLTAVASRFH
360 370 380
TVREHMSGLL AAYIVTGLVY ARDAAALRPV
Length:380
Mass (Da):42,735
Last modified:October 1, 1996 - 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:iE0A7A890C780ACD3
GO

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 conflicti240T → A in AAS56825 (PubMed:17322287).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
D21200 Genomic DNA Translation: BAA04742.1
Z72648 Genomic DNA Translation: CAA96835.1
Z72647 Genomic DNA Translation: CAA96834.1
AY558499 Genomic DNA Translation: AAS56825.1
BK006941 Genomic DNA Translation: DAA07983.1

Protein sequence database of the Protein Information Resource

More...
PIRi
S53293

NCBI Reference Sequences

More...
RefSeqi
NP_011389.3, NM_001180991.3

Genome annotation databases

Ensembl fungal genome annotation project

More...
EnsemblFungii
YGL126W_mRNA; YGL126W; YGL126W

Database of genes from NCBI RefSeq genomes

More...
GeneIDi
852751

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
sce:YGL126W

<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
D21200 Genomic DNA Translation: BAA04742.1
Z72648 Genomic DNA Translation: CAA96835.1
Z72647 Genomic DNA Translation: CAA96834.1
AY558499 Genomic DNA Translation: AAS56825.1
BK006941 Genomic DNA Translation: DAA07983.1
PIRiS53293
RefSeqiNP_011389.3, NM_001180991.3

3D structure databases

SMRiP53012
ModBaseiSearch...

Protein-protein interaction databases

BioGRIDi33125, 207 interactors
DIPiDIP-1209N
IntActiP53012, 7 interactors
MINTiP53012
STRINGi4932.YGL126W

Proteomic databases

PaxDbiP53012
PRIDEiP53012

Genome annotation databases

EnsemblFungiiYGL126W_mRNA; YGL126W; YGL126W
GeneIDi852751
KEGGisce:YGL126W

Organism-specific databases

SGDiS000003094, SCS3
VEuPathDBiFungiDB:YGL126W

Phylogenomic databases

eggNOGiKOG3750, Eukaryota
GeneTreeiENSGT00530000063693
HOGENOMiCLU_048143_2_1_1
InParanoidiP53012
OMAiHDPSGHI

Enzyme and pathway databases

ReactomeiR-SCE-8964572, Lipid particle organization

Miscellaneous databases

Protein Ontology

More...
PROi
PR:P53012
RNActiP53012, protein

Family and domain databases

InterProiView protein in InterPro
IPR019388, FIT
PANTHERiPTHR23129, PTHR23129, 1 hit
PfamiView protein in Pfam
PF10261, Scs3p, 1 hit

ProtoNet; Automatic hierarchical classification of proteins

More...
ProtoNeti
Search...

MobiDB: a database of protein disorder and mobility annotations

More...
MobiDBi
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 nameiSCS3_YEAST
<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: P53012
Secondary accession number(s): D6VU22, E9P8W2
<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: October 1, 1996
Last sequence update: October 1, 1996
Last modified: April 7, 2021
This is version 142 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 programFungal 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

Reference proteome

Documents

  1. Yeast
    Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
  2. Yeast chromosome VII
    Yeast (Saccharomyces cerevisiae) chromosome VII: entries and gene names
  3. SIMILARITY comments
    Index of protein domains and families
UniProt is an ELIXIR core data resource
Main funding by: National Institutes of Health

We'd like to inform you that we have updated our Privacy Notice to comply with Europe’s new General Data Protection Regulation (GDPR) that applies since 25 May 2018.

Do not show this banner again