Skip Header

Contribute Send feedback
Read comments (?) or add your own

Q7ZYQ3 (CEPT1_XENLA) Reviewed, UniProtKB/Swiss-Prot

Last modified April 3, 2013. Version 54. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Choline/ethanolaminephosphotransferase 1
EC=2.7.8.1
EC=2.7.8.2
Gene names
Name:cept1
OrganismXenopus laevis (African clawed frog)
Taxonomic identifier8355 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Amphibia › Batrachia › Anura › Pipoidea › Pipidae › Xenopodinae › Xenopus › Xenopus

Protein attributes

Sequence length416 AA.
Sequence statusComplete.
Protein existenceEvidence at transcript level

General annotation (Comments)

Function

Catalyzes both phosphatidylcholine and phosphatidylethanolamine biosynthesis from CDP-choline and CDP-ethanolamine, respectively. Involved in protein-dependent process of phospholipid transport to distribute phosphatidyl choline to the lumenal surface By similarity.

Catalytic activity

CDP-ethanolamine + 1,2-diacylglycerol = CMP + a phosphatidylethanolamine.

CDP-choline + 1,2-diacylglycerol = CMP + a phosphatidylcholine.

Cofactor

Magnesium or manganese By similarity.

Pathway

Phospholipid metabolism; phosphatidylethanolamine biosynthesis; phosphatidylethanolamine from ethanolamine: step 3/3.

Phospholipid metabolism; phosphatidylcholine biosynthesis; phosphatidylcholine from phosphocholine: step 2/2.

Subcellular location

Endoplasmic reticulum membrane; Multi-pass membrane protein By similarity. Nucleus membrane; Multi-pass membrane protein By similarity.

Sequence similarities

Belongs to the CDP-alcohol phosphatidyltransferase class-I family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 416416Choline/ethanolaminephosphotransferase 1
PRO_0000289249

Regions

Transmembrane87 – 10721Helical; Potential
Transmembrane115 – 13521Helical; Potential
Transmembrane156 – 17621Helical; Potential
Transmembrane182 – 20221Helical; Potential
Transmembrane218 – 23821Helical; Potential
Transmembrane249 – 27123Helical; Potential
Transmembrane283 – 30321Helical; Potential
Transmembrane317 – 33721Helical; Potential
Transmembrane365 – 38521Helical; Potential

Amino acid modifications

Glycosylation1441N-linked (GlcNAc...) Potential

Sequences

Sequence LengthMass (Da)Tools
Q7ZYQ3 [UniParc].

Last modified June 1, 2003. Version 1.
Checksum: 79CE7F5989D0C5AF

FASTA41646,637
        10         20         30         40         50         60 
MSAQRAAKRR TGDFHSEFPS SCGNPYQTAC LLSKFIELPN PPLSRHQLKR LEEHRYQSCG 

        70         80         90        100        110        120 
KSLLEPLMQG FWEWLVIQVP QWIAPNLITI IGLLINIVTT VVLIYYCPTA TEKAPTWTYL 

       130        140        150        160        170        180 
SCAIGLFMYQ SLDAIDGKQA RRTNSSTPLG ELFDHGCDSL STVFVVLGTC IAVQLGTNPD 

       190        200        210        220        230        240 
WMFFCCFAGM FMFYCAHWQT YVSGTLRFGI IDVTEVQIFI IIMHLLAAIG GPTLWLSMIP 

       250        260        270        280        290        300 
VLNVPMKLFP ALCTVAGTVF SCTNYFRVIF TGGVGKNGST IAGTSVLSPM LHIGSVIVLA 

       310        320        330        340        350        360 
TMIYKKSSVQ LFEKHPCLYI LTFGFVSAKV TNKLVVAHMT KSEMHLHDSA FIGPALLFLN 

       370        380        390        400        410 
QYFNSFIDEY LVLWIALVLS LIDLIRYSVS VCNQIASHLH IEVFRIKTKM ARFNHH

« Hide

References

[1]NIH - Xenopus Gene Collection (XGC) project
Submitted (JAN-2003) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Embryo.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		BC042267 mRNA. Translation: AAH42267.1.
RefSeqNP_001080113.1. NM_001086644.1.
UniGeneXl.8741.

3D structure databases

ProteinModelPortalQ7ZYQ3.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID379805.
KEGGxla:379805.

Organism-specific databases

CTD10390.
XenbaseXB-GENE-6254692. cept1.

Phylogenomic databases

HOVERGENHBG107647.
KOK13644.

Enzyme and pathway databases

UniPathwayUPA00558; UER00743.
UPA00753; UER00740.

Family and domain databases

InterProIPR000462. CDP-OH_P_trans.
IPR014472. CHOPT.
[Graphical view]
PfamPF01066. CDP-OH_P_transf. 1 hit.
[Graphical view]
PIRSFPIRSF015665. CHOPT. 1 hit.
PROSITEPS00379. CDP_ALCOHOL_P_TRANSF. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameCEPT1_XENLA
AccessionPrimary (citable) accession number: Q7ZYQ3
Entry history
Integrated into UniProtKB/Swiss-Prot: May 29, 2007
Last sequence update: June 1, 2003
Last modified: April 3, 2013
This is version 54 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents