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O43813 (LANC1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 112. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
LanC-like protein 1
Alternative name(s):
40 kDa erythrocyte membrane protein
Short name=p40
Gene names
Name:LANCL1
Synonyms:GPR69A
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length399 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

May play a role in EPS8 signaling. Binds glutathione. Ref.10

Subunit structure

Interacts with the C-terminal of STOM. Interacts with the EPS8 SH3 domain. Interaction with EPS8 is inhibited by glutathione binding. Interacts with P.falciparum SBP1. Ref.1 Ref.5 Ref.10

Subcellular location

Cytoplasm. Membrane; Peripheral membrane protein. Nucleus. Note: Detected at the surface of Maurer's clefts in malaria-infected erythrocytes at late stages of parasite development. Ref.4 Ref.5 Ref.6

Tissue specificity

Detected in erythrocytes, brain, kidney, testis, ovary, heart, lung, placenta and spleen (at protein level). Ubiquitous. Strongly expressed in brain, spinal cord, pituitary gland, kidney, heart, skeletal muscle, pancreas, ovary and testis. Ref.1 Ref.4 Ref.5

Sequence similarities

Belongs to the LanC-like protein family.

Caution

Was originally (Ref.1) thought to be a G-protein coupled receptor.

Binary interactions

With

Entry

#Exp.

IntAct

Notes

Eps8Q085092EBI-3046631,EBI-375596From a different organism.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.7
Chain2 – 399398LanC-like protein 1
PRO_0000191268

Regions

Region364 – 3674Glutathione binding

Sites

Metal binding2761Zinc
Metal binding3221Zinc
Metal binding3231Zinc
Binding site3171Glutathione

Amino acid modifications

Modified residue21N-acetylalanine Ref.7
Modified residue1421N6-acetyllysine Ref.8

Experimental info

Mutagenesis41R → A: Loss of glutathione binding. Ref.10
Mutagenesis3171K → A: Loss of glutathione binding. Ref.10
Mutagenesis3221C → A: Loss of glutathione binding. Ref.10
Mutagenesis3641R → A or E: Loss of glutathione binding. Ref.10

Secondary structure

......................................................... 399
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
O43813 [UniParc].

Last modified June 1, 1998. Version 1.
Checksum: 2664F275F9281AF2

FASTA39945,283
        10         20         30         40         50         60 
MAQRAFPNPY ADYNKSLAEG YFDAAGRLTP EFSQRLTNKI RELLQQMERG LKSADPRDGT 

        70         80         90        100        110        120 
GYTGWAGIAV LYLHLYDVFG DPAYLQLAHG YVKQSLNCLT KRSITFLCGD AGPLAVAAVL 

       130        140        150        160        170        180 
YHKMNNEKQA EDCITRLIHL NKIDPHAPNE MLYGRIGYIY ALLFVNKNFG VEKIPQSHIQ 

       190        200        210        220        230        240 
QICETILTSG ENLARKRNFT AKSPLMYEWY QEYYVGAAHG LAGIYYYLMQ PSLQVSQGKL 

       250        260        270        280        290        300 
HSLVKPSVDY VCQLKFPSGN YPPCIGDNRD LLVHWCHGAP GVIYMLIQAY KVFREEKYLC 

       310        320        330        340        350        360 
DAYQCADVIW QYGLLKKGYG LCHGSAGNAY AFLTLYNLTQ DMKYLYRACK FAEWCLEYGE 

       370        380        390 
HGCRTPDTPF SLFEGMAGTI YFLADLLVPT KARFPAFEL 

« Hide

References

« Hide 'large scale' references
[1]"Isolation, molecular characterization, and tissue-specific expression of a novel putative G protein-coupled receptor."
Mayer H., Salzer U., Breuss J., Ziegler S., Marchler-Bauer A., Prohaska R.
Biochim. Biophys. Acta 1395:301-308(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 5-24; 28-35; 40-50; 198-201 AND 392-399, TISSUE SPECIFICITY, INTERACTION WITH STOM.
Tissue: Bone marrow, Erythrocyte and Fetal brain.
[2]"Organization and chromosomal localization of the human and mouse genes coding for LanC-like protein 1 (LANCL1)."
Mayer H., Bauer H., Prohaska R.
Cytogenet. Cell Genet. 93:100-104(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
Tissue: Brain and Testis.
[3]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Testis.
[4]"Characterization of p40/GPR69A as a peripheral membrane protein related to the lantibiotic synthetase component C."
Bauer H., Mayer H., Marchler-Bauer A., Salzer U., Prohaska R.
Biochem. Biophys. Res. Commun. 275:69-74(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
[5]"LANCL1, an erythrocyte protein recruited to the Maurer's clefts during Plasmodium falciparum development."
Blisnick T., Vincensini L., Barale J.C., Namane A., Braun Breton C.
Mol. Biochem. Parasitol. 141:39-47(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: TISSUE SPECIFICITY, INTERACTION WITH P.FALCIPARUM SBP1, IDENTIFICATION BY MASS SPECTROMETRY, SUBCELLULAR LOCATION.
[6]"Myristoylation of human LanC-like protein 2 (LANCL2) is essential for the interaction with the plasma membrane and the increase in cellular sensitivity to adriamycin."
Landlinger C., Salzer U., Prohaska R.
Biochim. Biophys. Acta 1758:1759-1767(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION.
[7]"Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
[8]"Lysine acetylation targets protein complexes and co-regulates major cellular functions."
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-142, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[9]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[10]"Structure of human lanthionine synthetase C-like protein 1 and its interaction with Eps8 and glutathione."
Zhang W., Wang L., Liu Y., Xu J., Zhu G., Cang H., Li X., Bartlam M., Hensley K., Li G., Rao Z., Zhang X.C.
Genes Dev. 23:1387-1392(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.60 ANGSTROMS) IN COMPLEX WITH GLUTATHIONE AND ZINC IONS, MUTAGENESIS OF ARG-4; LYS-317; CYS-322 AND ARG-364, INTERACTION WITH EPS8, FUNCTION.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
Y11395 mRNA. Translation: CAA72205.1.
AJ289236 expand/collapse EMBL AC list , AJ289237, AJ289238, AJ289239 Genomic DNA. Translation: CAC21950.1.
BC028685 mRNA. Translation: AAH28685.1.
CCDSCCDS2392.1.
RefSeqNP_001130046.1. NM_001136574.1.
NP_001130047.1. NM_001136575.1.
NP_006046.1. NM_006055.2.
UniGeneHs.13351.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
3E6UX-ray2.60A/B/C/D1-399[»]
3E73X-ray2.80A/B1-399[»]
ProteinModelPortalO43813.
SMRO43813. Positions 1-399.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid115599. 6 interactions.
IntActO43813. 4 interactions.
MINTMINT-3308405.
STRING9606.ENSP00000233714.

PTM databases

PhosphoSiteO43813.

Proteomic databases

MaxQBO43813.
PaxDbO43813.
PeptideAtlasO43813.
PRIDEO43813.

Protocols and materials databases

DNASU10314.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000233714; ENSP00000233714; ENSG00000115365.
ENST00000431941; ENSP00000397646; ENSG00000115365.
ENST00000441020; ENSP00000393323; ENSG00000115365.
ENST00000443314; ENSP00000388713; ENSG00000115365.
ENST00000450366; ENSP00000393597; ENSG00000115365.
GeneID10314.
KEGGhsa:10314.
UCSCuc002ved.3. human.

Organism-specific databases

CTD10314.
GeneCardsGC02M211259.
HGNCHGNC:6508. LANCL1.
HPAHPA034994.
MIM604155. gene.
neXtProtNX_O43813.
PharmGKBPA30293.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG245101.
HOGENOMHOG000240926.
HOVERGENHBG065387.
InParanoidO43813.
OMAPGVIYML.
OrthoDBEOG71VSTN.
PhylomeDBO43813.
TreeFamTF300068.

Gene expression databases

ArrayExpressO43813.
BgeeO43813.
CleanExHS_LANCL1.
GenevestigatorO43813.

Family and domain databases

Gene3D1.50.10.10. 1 hit.
InterProIPR012341. 6hp_glycosidase.
IPR007822. LANC-like.
IPR020464. LanC-like_prot_euk.
[Graphical view]
PfamPF05147. LANC_like. 1 hit.
[Graphical view]
PRINTSPR01951. LANCEUKARYTE.
PR01950. LANCSUPER.
ProtoNetSearch...

Other

ChiTaRSLANCL1. human.
EvolutionaryTraceO43813.
GenomeRNAi10314.
NextBio39095.
PROO43813.
SOURCESearch...

Entry information

Entry nameLANC1_HUMAN
AccessionPrimary (citable) accession number: O43813
Entry history
Integrated into UniProtKB/Swiss-Prot: May 10, 2004
Last sequence update: June 1, 1998
Last modified: July 9, 2014
This is version 112 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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

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

Human chromosome 2

Human chromosome 2: entries, gene names and cross-references to MIM