O43813 (LANC1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
LanC-like protein 1

Alternative name(s):
40 kDa erythrocyte membrane protein
Short name=p40

Gene names

Name:	LANCL1
Synonyms:	GPR69A

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	399 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	May play a role in EPS8 signaling. Binds glutathion. Ref.9
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.9
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.

Ontologies

Keywords
Cellular component	Cytoplasm Membrane Nucleus
Ligand	Metal-binding Zinc
PTM	Acetylation
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	metabolic process Inferred from electronic annotation. Source: GOC
Cellular_component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell integral to plasma membrane Traceable author statement Ref.1. Source: ProtInc intracellular membrane-bounded organelle Inferred from direct assay. Source: HPA microtubule cytoskeleton Inferred from direct assay. Source: HPA nucleus Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	G-protein coupled receptor activity Traceable author statement Ref.1. Source: ProtInc catalytic activity Inferred from electronic annotation. Source: InterPro glutathione binding Inferred from direct assay Ref.9. Source: UniProtKB low-density lipoprotein particle receptor binding Inferred from direct assay PubMed 15082773. Source: MGI zinc ion binding Inferred from direct assay Ref.9. Source: UniProtKB
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 399

399

LanC-like protein 1

PRO_0000191268

Regions

Region

364 – 367

4

Glutathione binding

Sites

Metal binding

276

1

Zinc

Metal binding

322

1

Zinc

Metal binding

323

1

Zinc

Binding site

317

1

Glutathione

Amino acid modifications

Modified residue

142

1

N6-acetyllysine Ref.7

Experimental info

Mutagenesis

4

1

R → A: Loss of glutathione binding. Ref.9

Mutagenesis

317

1

K → A: Loss of glutathione binding. Ref.9

Mutagenesis

322

1

C → A: Loss of glutathione binding. Ref.9

Mutagenesis

364

1

R → A or E: Loss of glutathione binding. Ref.9

Secondary structure

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399

Helix Strand Turn

Details...

Helix

1 – 4

4

Helix

15 – 19

5

Helix

30 – 50

21

Turn

51 – 53

3

Beta strand

61 – 64

4

Helix

65 – 79

15

Helix

82 – 96

15

Beta strand

106 – 109

4

Helix

111 – 123

13

Helix

127 – 138

12

Helix

139 – 143

5

Turn

151 – 153

3

Helix

155 – 169

15

Helix

176 – 196

21

Turn

197 – 202

6

Turn

217 – 219

3

Helix

221 – 228

8

Helix

231 – 233

3

Helix

237 – 242

6

Helix

244 – 253

10

Beta strand

274 – 278

5

Helix

279 – 293

15

Helix

296 – 312

17

Turn

321 – 323

3

Helix

325 – 339

15

Helix

342 – 355

14

Turn

356 – 359

4

Turn

372 – 374

3

Helix

376 – 386

11

Helix

389 – 391

3

Turn

395 – 397

3

Sequences

	Sequence		Length	Mass (Da)
	O43813 [UniParc]. Last modified June 1, 1998. Version 1. Checksum: 2664F275F9281AF2	FASTA	399	45,283
	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

References

	« Hide 'large scale' referencesShow '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, 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]	"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, MASS SPECTROMETRY.
[8]	"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].
[9]	"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 , AJ289237, AJ289238, AJ289239 Genomic DNA. Translation: CAC21950.1.
BC028685 mRNA. Translation: AAH28685.1.

IPI

IPI00005724.

RefSeq

NP_001130046.1. NM_001136574.1.
NP_001130047.1. NM_001136575.1.
NP_006046.1. NM_006055.2.

UniGene

Hs.13351.

3D structure databases

PDBe
RCSB PDB
PDBj

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	[»]

ProteinModelPortal

O43813.

ModBase

Search...

Protein-protein interaction databases

IntAct

O43813. 1 interaction.

MINT

MINT-3308405.

STRING

9606.ENSP00000233714.

PTM databases

PhosphoSite

O43813.

Proteomic databases

PaxDb

O43813.

PeptideAtlas

O43813.

PRIDE

O43813.

Protocols and materials databases

DNASU

10314.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000233714; ENSP00000233714; ENSG00000115365.
ENST00000431941; ENSP00000397646; ENSG00000115365.
ENST00000441020; ENSP00000393323; ENSG00000115365.
ENST00000443314; ENSP00000388713; ENSG00000115365.
ENST00000450366; ENSP00000393597; ENSG00000115365.

GeneID

10314.

KEGG

hsa:10314.

UCSC

uc002ved.3. human.

Organism-specific databases

CTD

10314.

GeneCards

GC02M211259.

HGNC

HGNC:6508. LANCL1.

HPA

HPA034994.

MIM

604155. gene.

neXtProt

NX_O43813.

PharmGKB

PA30293.

GenAtlas

Search...

Phylogenomic databases

eggNOG

NOG245101.

HOGENOM

HOG000240926.

HOVERGEN

HBG065387.

InParanoid

O43813.

OMA

APGVIYM.

OrthoDB

EOG4NZTT7.

PhylomeDB

O43813.

Gene expression databases

ArrayExpress

O43813.

Bgee

O43813.

CleanEx

HS_LANCL1.

Genevestigator

O43813.

GermOnline

ENSG00000115365. Homo sapiens.

Family and domain databases

Gene3D

1.50.10.10. 1 hit.

InterPro

IPR008928. 6-hairpin_glycosidase-like.
IPR012341. 6hp_glycosidase.
IPR007822. LANC-like.
IPR020464. LanC-like_prot_euk.
[Graphical view]

Pfam

PF05147. LANC_like. 1 hit.
[Graphical view]

PRINTS

PR01951. LANCEUKARYTE.
PR01950. LANCSUPER.

SUPFAM

SSF48208. Glyco_trans_6hp. 1 hit.

ProtoNet

Search...

Other

ChiTaRS

LANCL1. human.

EvolutionaryTrace

O43813.

GenomeRNAi

10314.

NextBio

39095.

SOURCE

Search...

Entry information

Entry name

LANC1_HUMAN

Accession

Primary (citable) accession number: O43813

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 10, 2004
Last sequence update:	June 1, 1998
Last modified:	May 1, 2013
This is version 101 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.