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Q9HDD0 (HRSL1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 86. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | 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

Names and origin

Protein namesRecommended name:
Phospholipid-metabolizing enzyme A-C1

EC=2.3.1.-
EC=3.1.1.-
Alternative name(s):
HRAS-like suppressor 1
Short name=HRSL1
Gene names
Name:HRASLS
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length168 AA.
Sequence statusComplete.
Protein existenceEvidence at transcript level

General annotation (Comments)

Function

Exhibits calcium-independent phospholipase activity towards phosphatidylcholine (PC) and phosphatidylethanolamine (PE). Also shows acyltransferase activities, transferring an acyl group of PCs to the amino group of PEs and the hydroxyl group of lyso PCs. Ref.2

Subcellular location

Membrane; Single-pass membrane protein By similarity.

Tissue specificity

Abundantly expressed in testis, skeletal muscle, brain, and heart. Ref.2

Sequence similarities

Belongs to the H-rev107 family.

Ontologies

Keywords
   Biological processLipid degradation
Lipid metabolism
   Cellular componentMembrane
   DomainTransmembrane
Transmembrane helix
   Molecular functionHydrolase
Transferase
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processlipid catabolic process

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentintegral component of membrane

Inferred from electronic annotation. Source: UniProtKB-KW

   Molecular_functionhydrolase activity

Inferred from electronic annotation. Source: UniProtKB-KW

transferase activity

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 168168Phospholipid-metabolizing enzyme A-C1
PRO_0000152481

Regions

Topological domain1 – 139139Cytoplasmic Potential
Transmembrane140 – 16324Helical; Potential
Topological domain164 – 1685Lumenal Potential

Sites

Active site301 By similarity
Active site1191Acyl-thioester intermediate By similarity

Sequences

Sequence LengthMass (Da)Tools
Q9HDD0 [UniParc].

Last modified March 1, 2001. Version 1.
Checksum: 11844F8B5963D39B

FASTA16818,750
        10         20         30         40         50         60 
MAFNDCFSLN YPGNPCPGDL IEVFRPGYQH WALYLGDGYV INIAPVDGIP ASFTSAKSVF 

        70         80         90        100        110        120 
SSKALVKMQL LKDVVGNDTY RINNKYDETY PPLPVEEIIK RSEFVIGQEV AYNLLVNNCE 

       130        140        150        160 
HFVTLLRYGE GVSEQANRAI STVEFVTAAV GVFSFLGLFP KGQRAKYY 

« Hide

References

« Hide 'large scale' references
[1]Kato S.
Submitted (AUG-1999) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]"Enzymological analysis of the tumor suppressor A-C1 reveals a novel group of phospholipid-metabolizing enzymes."
Shinohara N., Uyama T., Jin X.H., Tsuboi K., Tonai T., Houchi H., Ueda N.
J. Lipid Res. 52:1927-1935(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, TISSUE SPECIFICITY.
[3]Mural R.J., Istrail S., Sutton G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AB030816 mRNA. Translation: BAB08110.1.
AB510981 mRNA. Translation: BAI63210.1.
CH471052 Genomic DNA. Translation: EAW78078.1.
UniGeneHs.36761.

3D structure databases

ProteinModelPortalQ9HDD0.
SMRQ9HDD0. Positions 15-129.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid121376. 1 interaction.
STRING9606.ENSP00000264735.

Polymorphism databases

DMDM20138344.

Proteomic databases

PaxDbQ9HDD0.
PRIDEQ9HDD0.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000602513; ENSP00000473258; ENSG00000127252.
UCSCuc003fta.4. human.

Organism-specific databases

GeneCardsGC03P192958.
HGNCHGNC:14922. HRASLS.
HPAHPA051179.
MIM606487. gene.
neXtProtNX_Q9HDD0.
PharmGKBPA29445.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG43478.
HOGENOMHOG000293227.
HOVERGENHBG028837.
InParanoidQ9HDD0.
OrthoDBEOG7B8S59.
PhylomeDBQ9HDD0.
TreeFamTF330836.

Gene expression databases

ArrayExpressQ9HDD0.
BgeeQ9HDD0.
CleanExHS_HRASLS.
GenevestigatorQ9HDD0.

Family and domain databases

InterProIPR007053. LRAT-like_dom.
[Graphical view]
PfamPF04970. LRAT. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio13651577.
PROQ9HDD0.
SOURCESearch...

Entry information

Entry nameHRSL1_HUMAN
AccessionPrimary (citable) accession number: Q9HDD0
Secondary accession number(s): D2KX19
Entry history
Integrated into UniProtKB/Swiss-Prot: January 31, 2002
Last sequence update: March 1, 2001
Last modified: May 14, 2014
This is version 86 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human chromosome 3

Human chromosome 3: entries, gene names and cross-references to MIM