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O43813

- LANC1_HUMAN

UniProt

O43813 - LANC1_HUMAN

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Protein
LanC-like protein 1
Gene
LANCL1, GPR69A
Organism
Homo sapiens (Human)
Status
Reviewed - 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 – 3171Glutathione
Metal bindingi322 – 3221Zinc
Metal bindingi323 – 3231Zinc

GO - Molecular functioni

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

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.3 Publications

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB-SubCell
  2. extracellular vesicular exosome Source: UniProt
  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 1
PRO_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

ArrayExpressiO43813.
BgeeiO43813.
CleanExiHS_LANCL1.
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. 6 interactions.
IntActiO43813. 4 interactions.
MINTiMINT-3308405.
STRINGi9606.ENSP00000233714.

Structurei

Secondary structure

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

3D structure databases

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

Miscellaneous databases

EvolutionaryTraceiO43813.

Family & Domainsi

Region

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

Sequence similaritiesi

Belongs to the LanC-like protein family.

Phylogenomic databases

eggNOGiNOG245101.
HOGENOMiHOG000240926.
HOVERGENiHBG065387.
InParanoidiO43813.
OMAiPGVIYML.
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

MAQRAFPNPY ADYNKSLAEG YFDAAGRLTP EFSQRLTNKI RELLQQMERG    50
LKSADPRDGT GYTGWAGIAV LYLHLYDVFG DPAYLQLAHG YVKQSLNCLT 100
KRSITFLCGD AGPLAVAAVL YHKMNNEKQA EDCITRLIHL NKIDPHAPNE 150
MLYGRIGYIY ALLFVNKNFG VEKIPQSHIQ QICETILTSG ENLARKRNFT 200
AKSPLMYEWY QEYYVGAAHG LAGIYYYLMQ PSLQVSQGKL HSLVKPSVDY 250
VCQLKFPSGN YPPCIGDNRD LLVHWCHGAP GVIYMLIQAY KVFREEKYLC 300
DAYQCADVIW QYGLLKKGYG LCHGSAGNAY AFLTLYNLTQ DMKYLYRACK 350
FAEWCLEYGE HGCRTPDTPF SLFEGMAGTI YFLADLLVPT KARFPAFEL 399
Length:399
Mass (Da):45,283
Last modified:June 1, 1998 - v1
Checksum:i2664F275F9281AF2
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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:
EMBL
GenBank
DDBJ
Links Updated
Y11395 mRNA. Translation: CAA72205.1 .
AJ289236
, AJ289237 , AJ289238 , AJ289239 Genomic DNA. Translation: CAC21950.1 .
BC028685 mRNA. Translation: AAH28685.1 .
CCDSi CCDS2392.1.
RefSeqi NP_001130046.1. NM_001136574.1.
NP_001130047.1. NM_001136575.1.
NP_006046.1. NM_006055.2.
UniGenei Hs.13351.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
3E6U X-ray 2.60 A/B/C/D 1-399 [» ]
3E73 X-ray 2.80 A/B 1-399 [» ]
ProteinModelPortali O43813.
SMRi O43813. Positions 1-399.
ModBasei Search...

Protein-protein interaction databases

BioGridi 115599. 6 interactions.
IntActi O43813. 4 interactions.
MINTi MINT-3308405.
STRINGi 9606.ENSP00000233714.

PTM databases

PhosphoSitei O43813.

Proteomic databases

MaxQBi O43813.
PaxDbi O43813.
PeptideAtlasi O43813.
PRIDEi O43813.

Protocols and materials databases

DNASUi 10314.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000233714 ; ENSP00000233714 ; ENSG00000115365 .
ENST00000431941 ; ENSP00000397646 ; ENSG00000115365 .
ENST00000441020 ; ENSP00000393323 ; ENSG00000115365 .
ENST00000443314 ; ENSP00000388713 ; ENSG00000115365 .
ENST00000450366 ; ENSP00000393597 ; ENSG00000115365 .
GeneIDi 10314.
KEGGi hsa:10314.
UCSCi uc002ved.3. human.

Organism-specific databases

CTDi 10314.
GeneCardsi GC02M211259.
HGNCi HGNC:6508. LANCL1.
HPAi HPA034994.
MIMi 604155. gene.
neXtProti NX_O43813.
PharmGKBi PA30293.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG245101.
HOGENOMi HOG000240926.
HOVERGENi HBG065387.
InParanoidi O43813.
OMAi PGVIYML.
OrthoDBi EOG71VSTN.
PhylomeDBi O43813.
TreeFami TF300068.

Miscellaneous databases

ChiTaRSi LANCL1. human.
EvolutionaryTracei O43813.
GenomeRNAii 10314.
NextBioi 39095.
PROi O43813.
SOURCEi Search...

Gene expression databases

ArrayExpressi O43813.
Bgeei O43813.
CleanExi HS_LANCL1.
Genevestigatori O43813.

Family and domain databases

Gene3Di 1.50.10.10. 1 hit.
InterProi IPR012341. 6hp_glycosidase.
IPR007822. LANC-like.
IPR020464. LanC-like_prot_euk.
[Graphical view ]
Pfami PF05147. LANC_like. 1 hit.
[Graphical view ]
PRINTSi PR01951. LANCEUKARYTE.
PR01950. LANCSUPER.
ProtoNeti Search...

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: September 3, 2014
This is version 113 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 (1 Publication) thought to be a G-protein coupled receptor.

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

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