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Protein

LanC-like protein 1

Gene

LANCL1

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

May play a role in EPS8 signaling. Binds glutathione.1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi276 – 2761Zinc
Binding sitei317 – 3171Glutathione1 Publication
Metal bindingi322 – 3221Zinc
Metal bindingi323 – 3231Zinc

GO - Molecular functioni

  1. catalytic activity Source: InterPro
  2. glutathione binding Source: UniProtKB
  3. G-protein coupled receptor activity Source: ProtInc
  4. low-density lipoprotein particle receptor binding Source: MGI
  5. SH3 domain binding Source: UniProtKB
  6. zinc ion binding Source: UniProtKB

GO - Biological processi

  1. G-protein coupled receptor signaling pathway Source: ProtInc
Complete GO annotation...

Keywords - Ligandi

Metal-binding, Zinc

Names & Taxonomyi

Protein namesi
Recommended name:
LanC-like protein 1
Alternative name(s):
40 kDa erythrocyte membrane protein
Short name:
p40
Gene namesi
Name:LANCL1
Synonyms:GPR69A
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 2

Organism-specific databases

HGNCiHGNC:6508. LANCL1.

Subcellular locationi

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.

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB-SubCell
  2. extracellular vesicular exosome Source: UniProtKB
  3. integral component of plasma membrane Source: ProtInc
  4. nucleus Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Membrane, Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi4 – 41R → A: Loss of glutathione binding. 1 Publication
Mutagenesisi317 – 3171K → A: Loss of glutathione binding. 1 Publication
Mutagenesisi322 – 3221C → A: Loss of glutathione binding. 1 Publication
Mutagenesisi364 – 3641R → A or E: Loss of glutathione binding. 1 Publication

Organism-specific databases

PharmGKBiPA30293.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed1 Publication
Chaini2 – 399398LanC-like protein 1PRO_0000191268Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanine1 Publication
Modified residuei142 – 1421N6-acetyllysine1 Publication

Keywords - PTMi

Acetylation

Proteomic databases

MaxQBiO43813.
PaxDbiO43813.
PeptideAtlasiO43813.
PRIDEiO43813.

PTM databases

PhosphoSiteiO43813.

Expressioni

Tissue specificityi

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.3 Publications

Gene expression databases

BgeeiO43813.
CleanExiHS_LANCL1.
ExpressionAtlasiO43813. baseline and differential.
GenevestigatoriO43813.

Organism-specific databases

HPAiHPA034994.

Interactioni

Subunit structurei

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 SBP1.3 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
Eps8Q085092EBI-3046631,EBI-375596From a different organism.

Protein-protein interaction databases

BioGridi115599. 15 interactions.
IntActiO43813. 4 interactions.
MINTiMINT-3308405.
STRINGi9606.ENSP00000233714.

Structurei

Secondary structure

1
399
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi2 – 43Combined sources
Helixi15 – 195Combined sources
Helixi30 – 5021Combined sources
Turni51 – 533Combined sources
Beta strandi61 – 644Combined sources
Helixi65 – 7915Combined sources
Helixi82 – 9615Combined sources
Beta strandi106 – 1094Combined sources
Helixi111 – 12313Combined sources
Helixi127 – 13812Combined sources
Helixi139 – 1435Combined sources
Turni151 – 1533Combined sources
Helixi155 – 16915Combined sources
Helixi176 – 19621Combined sources
Turni197 – 2026Combined sources
Turni217 – 2193Combined sources
Helixi221 – 2288Combined sources
Helixi231 – 2333Combined sources
Helixi237 – 2426Combined sources
Helixi244 – 25310Combined sources
Beta strandi274 – 2785Combined sources
Helixi279 – 29315Combined sources
Helixi296 – 31217Combined sources
Turni321 – 3233Combined sources
Helixi325 – 33915Combined sources
Helixi342 – 35514Combined sources
Turni356 – 3594Combined sources
Turni372 – 3743Combined sources
Helixi376 – 38611Combined sources
Helixi389 – 3913Combined sources
Turni395 – 3973Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3E6UX-ray2.60A/B/C/D1-399[»]
3E73X-ray2.80A/B1-399[»]
ProteinModelPortaliO43813.
SMRiO43813. Positions 1-399.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiO43813.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni364 – 3674Glutathione binding

Sequence similaritiesi

Belongs to the LanC-like protein family.Curated

Phylogenomic databases

eggNOGiNOG245101.
HOGENOMiHOG000240926.
HOVERGENiHBG065387.
InParanoidiO43813.
OMAiNPYADFN.
OrthoDBiEOG71VSTN.
PhylomeDBiO43813.
TreeFamiTF300068.

Family and domain databases

Gene3Di1.50.10.10. 1 hit.
InterProiIPR012341. 6hp_glycosidase.
IPR007822. LANC-like.
IPR020464. LanC-like_prot_euk.
[Graphical view]
PfamiPF05147. LANC_like. 1 hit.
[Graphical view]
PRINTSiPR01951. LANCEUKARYTE.
PR01950. LANCSUPER.

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

O43813-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MAQRAFPNPY ADYNKSLAEG YFDAAGRLTP EFSQRLTNKI RELLQQMERG
60 70 80 90 100
LKSADPRDGT GYTGWAGIAV LYLHLYDVFG DPAYLQLAHG YVKQSLNCLT
110 120 130 140 150
KRSITFLCGD AGPLAVAAVL YHKMNNEKQA EDCITRLIHL NKIDPHAPNE
160 170 180 190 200
MLYGRIGYIY ALLFVNKNFG VEKIPQSHIQ QICETILTSG ENLARKRNFT
210 220 230 240 250
AKSPLMYEWY QEYYVGAAHG LAGIYYYLMQ PSLQVSQGKL HSLVKPSVDY
260 270 280 290 300
VCQLKFPSGN YPPCIGDNRD LLVHWCHGAP GVIYMLIQAY KVFREEKYLC
310 320 330 340 350
DAYQCADVIW QYGLLKKGYG LCHGSAGNAY AFLTLYNLTQ DMKYLYRACK
360 370 380 390
FAEWCLEYGE HGCRTPDTPF SLFEGMAGTI YFLADLLVPT KARFPAFEL
Length:399
Mass (Da):45,283
Last modified:June 1, 1998 - v1
Checksum:i2664F275F9281AF2
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Y11395 mRNA. Translation: CAA72205.1.
AJ289236
, AJ289237, AJ289238, AJ289239 Genomic DNA. Translation: CAC21950.1.
BC028685 mRNA. Translation: AAH28685.1.
CCDSiCCDS2392.1.
RefSeqiNP_001130046.1. NM_001136574.1.
NP_001130047.1. NM_001136575.1.
NP_006046.1. NM_006055.2.
UniGeneiHs.13351.

Genome annotation databases

EnsembliENST00000233714; ENSP00000233714; ENSG00000115365.
ENST00000431941; ENSP00000397646; ENSG00000115365.
ENST00000441020; ENSP00000393323; ENSG00000115365.
ENST00000443314; ENSP00000388713; ENSG00000115365.
ENST00000450366; ENSP00000393597; ENSG00000115365.
GeneIDi10314.
KEGGihsa:10314.
UCSCiuc002ved.3. human.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Y11395 mRNA. Translation: CAA72205.1.
AJ289236
, AJ289237, AJ289238, AJ289239 Genomic DNA. Translation: CAC21950.1.
BC028685 mRNA. Translation: AAH28685.1.
CCDSiCCDS2392.1.
RefSeqiNP_001130046.1. NM_001136574.1.
NP_001130047.1. NM_001136575.1.
NP_006046.1. NM_006055.2.
UniGeneiHs.13351.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3E6UX-ray2.60A/B/C/D1-399[»]
3E73X-ray2.80A/B1-399[»]
ProteinModelPortaliO43813.
SMRiO43813. Positions 1-399.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi115599. 15 interactions.
IntActiO43813. 4 interactions.
MINTiMINT-3308405.
STRINGi9606.ENSP00000233714.

PTM databases

PhosphoSiteiO43813.

Proteomic databases

MaxQBiO43813.
PaxDbiO43813.
PeptideAtlasiO43813.
PRIDEiO43813.

Protocols and materials databases

DNASUi10314.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000233714; ENSP00000233714; ENSG00000115365.
ENST00000431941; ENSP00000397646; ENSG00000115365.
ENST00000441020; ENSP00000393323; ENSG00000115365.
ENST00000443314; ENSP00000388713; ENSG00000115365.
ENST00000450366; ENSP00000393597; ENSG00000115365.
GeneIDi10314.
KEGGihsa:10314.
UCSCiuc002ved.3. human.

Organism-specific databases

CTDi10314.
GeneCardsiGC02M211259.
HGNCiHGNC:6508. LANCL1.
HPAiHPA034994.
MIMi604155. gene.
neXtProtiNX_O43813.
PharmGKBiPA30293.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiNOG245101.
HOGENOMiHOG000240926.
HOVERGENiHBG065387.
InParanoidiO43813.
OMAiNPYADFN.
OrthoDBiEOG71VSTN.
PhylomeDBiO43813.
TreeFamiTF300068.

Miscellaneous databases

ChiTaRSiLANCL1. human.
EvolutionaryTraceiO43813.
GenomeRNAii10314.
NextBioi39095.
PROiO43813.
SOURCEiSearch...

Gene expression databases

BgeeiO43813.
CleanExiHS_LANCL1.
ExpressionAtlasiO43813. baseline and differential.
GenevestigatoriO43813.

Family and domain databases

Gene3Di1.50.10.10. 1 hit.
InterProiIPR012341. 6hp_glycosidase.
IPR007822. LANC-like.
IPR020464. LanC-like_prot_euk.
[Graphical view]
PfamiPF05147. LANC_like. 1 hit.
[Graphical view]
PRINTSiPR01951. LANCEUKARYTE.
PR01950. LANCSUPER.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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. 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.

Entry informationi

Entry nameiLANC1_HUMAN
AccessioniPrimary (citable) accession number: O43813
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 10, 2004
Last sequence update: June 1, 1998
Last modified: January 7, 2015
This is version 117 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (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.

Miscellaneousi

Caution

Was originally thought to be a G-protein coupled receptor.1 Publication

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 2
    Human chromosome 2: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. 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.