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Protein

Phosphatidylcholine:ceramide cholinephosphotransferase 2

Gene

sms-2

Organism
Caenorhabditis elegans
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

Sphingomyelin synthases synthesize the sphingolipid, sphingomyelin, through transfer of the phosphatidyl head group, phosphatidylcholine, on to the primary hydroxyl of ceramide. The reaction is bidirectional depending on the respective levels of the sphingolipid and ceramide.1 Publication

Catalytic activityi

A ceramide + a phosphatidylcholine = a sphingomyelin + a 1,2-diacyl-sn-glycerol.1 Publication

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei210 – 2101By similarity
Active sitei253 – 2531By similarity
Active sitei257 – 2571By similarity

GO - Molecular functioni

  1. ceramide cholinephosphotransferase activity Source: UniProtKB
  2. sphingomyelin synthase activity Source: UniProtKB

GO - Biological processi

  1. sphingomyelin biosynthetic process Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Transferase

Keywords - Biological processi

Lipid metabolism, Sphingolipid metabolism

Enzyme and pathway databases

BRENDAi2.7.8.27. 1045.
ReactomeiREACT_183003. Sphingolipid de novo biosynthesis.
UniPathwayiUPA00222.

Names & Taxonomyi

Protein namesi
Recommended name:
Phosphatidylcholine:ceramide cholinephosphotransferase 2 (EC:2.7.8.27)
Alternative name(s):
Sphingomyelin synthase 2
Gene namesi
Name:sms-2
ORF Names:F53H8.4
OrganismiCaenorhabditis elegans
Taxonomic identifieri6239 [NCBI]
Taxonomic lineageiEukaryotaMetazoaEcdysozoaNematodaChromadoreaRhabditidaRhabditoideaRhabditidaePeloderinaeCaenorhabditis
ProteomesiUP000001940: Chromosome X

Organism-specific databases

WormBaseiF53H8.4; CE04657; WBGene00004893; sms-2.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transmembranei60 – 8021HelicalSequence AnalysisAdd
BLAST
Transmembranei104 – 12421HelicalSequence AnalysisAdd
BLAST
Transmembranei136 – 15621HelicalSequence AnalysisAdd
BLAST
Transmembranei200 – 22021HelicalSequence AnalysisAdd
BLAST
Transmembranei229 – 24921HelicalSequence AnalysisAdd
BLAST
Transmembranei258 – 27821HelicalSequence AnalysisAdd
BLAST
Topological domaini279 – 33557CytoplasmicSequence AnalysisAdd
BLAST

GO - Cellular componenti

  1. integral component of membrane Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 335335Phosphatidylcholine:ceramide cholinephosphotransferase 2PRO_0000221075Add
BLAST

Proteomic databases

PaxDbiQ20735.
PRIDEiQ20735.

Interactioni

Protein-protein interaction databases

STRINGi6239.F53H8.4.

Structurei

3D structure databases

ProteinModelPortaliQ20735.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the sphingomyelin synthase family.Curated

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiNOG259509.
GeneTreeiENSGT00390000001630.
HOGENOMiHOG000018457.
InParanoidiQ20735.
KOiK04714.
OMAiNRDEICQ.
OrthoDBiEOG7KWSNC.
PhylomeDBiQ20735.

Family and domain databases

InterProiIPR025749. Sphingomyelin_synth-like_dom.
[Graphical view]
PfamiPF14360. PAP2_C. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q20735-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MTNSSEFTDV LQSRDPCVSN GIVINIDPID PEPTPIRKEF TCEDTFHHEH
60 70 80 90 100
HGNSEGFKTL TAFLCLMLSA FLNFFLLTVI HDVVPRQPLP DLTFMIIPQQ
110 120 130 140 150
RWAWSVGDVL STVSSVVAFT IIFLHHQRWI VLRRTFLLGA IMYGLRAVIL
160 170 180 190 200
GVTFLPPSFH NRDEICQPQV NRTAMYGMEI ATRFLTYVIT LGLTSGQDKI
210 220 230 240 250
LCGDLMFSGH TVVLTIMYFV QLQYTPRGLV ILRYIAAPIT FLGIAALVVS
260 270 280 290 300
GGHYTMDVLI AYWLTSHVFW SYHQIFEMRK DDRPQAPLSR LWWFWLCYWF
310 320 330
ESDVADGKLV NKWNWPLEGP QRMHTIMNRI NYKLQ
Length:335
Mass (Da):38,737
Last modified:November 1, 1996 - v1
Checksum:i7FCA39B7B849A4A4
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
FO080855 Genomic DNA. Translation: CCD67244.1.
PIRiT34296.
RefSeqiNP_508182.1. NM_075781.3.
UniGeneiCel.38936.

Genome annotation databases

EnsemblMetazoaiF53H8.4; F53H8.4; WBGene00004893.
GeneIDi180445.
KEGGicel:CELE_F53H8.4.
UCSCiF53H8.4. c. elegans.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
FO080855 Genomic DNA. Translation: CCD67244.1.
PIRiT34296.
RefSeqiNP_508182.1. NM_075781.3.
UniGeneiCel.38936.

3D structure databases

ProteinModelPortaliQ20735.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi6239.F53H8.4.

Proteomic databases

PaxDbiQ20735.
PRIDEiQ20735.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblMetazoaiF53H8.4; F53H8.4; WBGene00004893.
GeneIDi180445.
KEGGicel:CELE_F53H8.4.
UCSCiF53H8.4. c. elegans.

Organism-specific databases

CTDi180445.
WormBaseiF53H8.4; CE04657; WBGene00004893; sms-2.

Phylogenomic databases

eggNOGiNOG259509.
GeneTreeiENSGT00390000001630.
HOGENOMiHOG000018457.
InParanoidiQ20735.
KOiK04714.
OMAiNRDEICQ.
OrthoDBiEOG7KWSNC.
PhylomeDBiQ20735.

Enzyme and pathway databases

UniPathwayiUPA00222.
BRENDAi2.7.8.27. 1045.
ReactomeiREACT_183003. Sphingolipid de novo biosynthesis.

Miscellaneous databases

NextBioi909408.

Family and domain databases

InterProiIPR025749. Sphingomyelin_synth-like_dom.
[Graphical view]
PfamiPF14360. PAP2_C. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Genome sequence of the nematode C. elegans: a platform for investigating biology."
    The C. elegans sequencing consortium
    Science 282:2012-2018(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: Bristol N2.
  2. "Identification of a family of animal sphingomyelin synthases."
    Huitema K., Van Den Dikkenberg J., Brouwers J.F.H.M., Holthuis J.C.
    EMBO J. 23:33-44(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, CATALYTIC ACTIVITY, PATHWAY.

Entry informationi

Entry nameiSMS2_CAEEL
AccessioniPrimary (citable) accession number: Q20735
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 1, 2004
Last sequence update: November 1, 1996
Last modified: January 7, 2015
This is version 86 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programCaenorhabditis annotation project

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Caenorhabditis elegans
    Caenorhabditis elegans: entries, gene names and cross-references to WormBase
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.