Full text data of LANCL1
LANCL1
(GPR69A)
[Confidence: medium (present in either hRBCD or BSc_CH or PM22954596)]
LanC-like protein 1 (40 kDa erythrocyte membrane protein; p40)
LanC-like protein 1 (40 kDa erythrocyte membrane protein; p40)
hRBCD
IPI00005724
IPI00005724 LanC-like protein 1 LanC-like protein 1 membrane n/a n/a n/a n/a n/a n/a n/a n/a 5 n/a n/a n/a n/a n/a n/a n/a n/a 1 2 2 integral membrane protein n/a found at its expected molecular weight found at molecular weight
IPI00005724 LanC-like protein 1 LanC-like protein 1 membrane n/a n/a n/a n/a n/a n/a n/a n/a 5 n/a n/a n/a n/a n/a n/a n/a n/a 1 2 2 integral membrane protein n/a found at its expected molecular weight found at molecular weight
UniProt
O43813
ID LANC1_HUMAN Reviewed; 399 AA.
AC O43813;
DT 10-MAY-2004, integrated into UniProtKB/Swiss-Prot.
read moreDT 01-JUN-1998, sequence version 1.
DT 22-JAN-2014, entry version 106.
DE RecName: Full=LanC-like protein 1;
DE AltName: Full=40 kDa erythrocyte membrane protein;
DE Short=p40;
GN Name=LANCL1; Synonyms=GPR69A;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 5-24; 28-35; 40-50;
RP 198-201 AND 392-399, TISSUE SPECIFICITY, AND INTERACTION WITH STOM.
RC TISSUE=Bone marrow, Erythrocyte, and Fetal brain;
RX PubMed=9512664; DOI=10.1016/S0167-4781(97)00178-4;
RA Mayer H., Salzer U., Breuss J., Ziegler S., Marchler-Bauer A.,
RA Prohaska R.;
RT "Isolation, molecular characterization, and tissue-specific expression
RT of a novel putative G protein-coupled receptor.";
RL Biochim. Biophys. Acta 1395:301-308(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
RC TISSUE=Brain, and Testis;
RX PubMed=11474189;
RA Mayer H., Bauer H., Prohaska R.;
RT "Organization and chromosomal localization of the human and mouse
RT genes coding for LanC-like protein 1 (LANCL1).";
RL Cytogenet. Cell Genet. 93:100-104(2001).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Testis;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [4]
RP SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=10944443; DOI=10.1006/bbrc.2000.3260;
RA Bauer H., Mayer H., Marchler-Bauer A., Salzer U., Prohaska R.;
RT "Characterization of p40/GPR69A as a peripheral membrane protein
RT related to the lantibiotic synthetase component C.";
RL Biochem. Biophys. Res. Commun. 275:69-74(2000).
RN [5]
RP TISSUE SPECIFICITY, INTERACTION WITH P.FALCIPARUM SBP1, MASS
RP SPECTROMETRY, AND SUBCELLULAR LOCATION.
RX PubMed=15811525; DOI=10.1016/j.molbiopara.2005.01.013;
RA Blisnick T., Vincensini L., Barale J.C., Namane A., Braun Breton C.;
RT "LANCL1, an erythrocyte protein recruited to the Maurer's clefts
RT during Plasmodium falciparum development.";
RL Mol. Biochem. Parasitol. 141:39-47(2005).
RN [6]
RP SUBCELLULAR LOCATION.
RX PubMed=16979580; DOI=10.1016/j.bbamem.2006.07.018;
RA Landlinger C., Salzer U., Prohaska R.;
RT "Myristoylation of human LanC-like protein 2 (LANCL2) is essential for
RT the interaction with the plasma membrane and the increase in cellular
RT sensitivity to adriamycin.";
RL Biochim. Biophys. Acta 1758:1759-1767(2006).
RN [7]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, MASS SPECTROMETRY, AND
RP CLEAVAGE OF INITIATOR METHIONINE.
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
RA Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in
RT a refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [8]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-142, AND MASS SPECTROMETRY.
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M.,
RA Walther T.C., Olsen J.V., Mann M.;
RT "Lysine acetylation targets protein complexes and co-regulates major
RT cellular functions.";
RL Science 325:834-840(2009).
RN [9]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
RA Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [10]
RP X-RAY CRYSTALLOGRAPHY (2.60 ANGSTROMS) IN COMPLEX WITH GLUTATHIONE AND
RP ZINC IONS, MUTAGENESIS OF ARG-4; LYS-317; CYS-322 AND ARG-364,
RP INTERACTION WITH EPS8, AND FUNCTION.
RX PubMed=19528316; DOI=10.1101/gad.1789209;
RA Zhang W., Wang L., Liu Y., Xu J., Zhu G., Cang H., Li X., Bartlam M.,
RA Hensley K., Li G., Rao Z., Zhang X.C.;
RT "Structure of human lanthionine synthetase C-like protein 1 and its
RT interaction with Eps8 and glutathione.";
RL Genes Dev. 23:1387-1392(2009).
CC -!- FUNCTION: May play a role in EPS8 signaling. Binds glutathione.
CC -!- SUBUNIT: Interacts with the C-terminal of STOM. Interacts with the
CC EPS8 SH3 domain. Interaction with EPS8 is inhibited by glutathione
CC binding. Interacts with P.falciparum SBP1.
CC -!- INTERACTION:
CC Q08509:Eps8 (xeno); NbExp=2; IntAct=EBI-3046631, EBI-375596;
CC -!- SUBCELLULAR LOCATION: Cytoplasm. Membrane; Peripheral membrane
CC protein. Nucleus. Note=Detected at the surface of Maurer's clefts
CC in malaria-infected erythrocytes at late stages of parasite
CC development.
CC -!- TISSUE SPECIFICITY: Detected in erythrocytes, brain, kidney,
CC testis, ovary, heart, lung, placenta and spleen (at protein
CC level). Ubiquitous. Strongly expressed in brain, spinal cord,
CC pituitary gland, kidney, heart, skeletal muscle, pancreas, ovary
CC and testis.
CC -!- SIMILARITY: Belongs to the LanC-like protein family.
CC -!- CAUTION: Was originally (PubMed:9512664) thought to be a G-protein
CC coupled receptor.
CC -----------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution-NoDerivs License
CC -----------------------------------------------------------------------
DR EMBL; Y11395; CAA72205.1; -; mRNA.
DR EMBL; AJ289236; CAC21950.1; -; Genomic_DNA.
DR EMBL; AJ289237; CAC21950.1; JOINED; Genomic_DNA.
DR EMBL; AJ289238; CAC21950.1; JOINED; Genomic_DNA.
DR EMBL; AJ289239; CAC21950.1; JOINED; Genomic_DNA.
DR EMBL; BC028685; AAH28685.1; -; mRNA.
DR RefSeq; NP_001130046.1; NM_001136574.1.
DR RefSeq; NP_001130047.1; NM_001136575.1.
DR RefSeq; NP_006046.1; NM_006055.2.
DR UniGene; Hs.13351; -.
DR PDB; 3E6U; X-ray; 2.60 A; A/B/C/D=1-399.
DR PDB; 3E73; X-ray; 2.80 A; A/B=1-399.
DR PDBsum; 3E6U; -.
DR PDBsum; 3E73; -.
DR ProteinModelPortal; O43813; -.
DR SMR; O43813; 1-399.
DR IntAct; O43813; 3.
DR MINT; MINT-3308405; -.
DR STRING; 9606.ENSP00000233714; -.
DR PhosphoSite; O43813; -.
DR PaxDb; O43813; -.
DR PeptideAtlas; O43813; -.
DR PRIDE; O43813; -.
DR DNASU; 10314; -.
DR Ensembl; ENST00000233714; ENSP00000233714; ENSG00000115365.
DR Ensembl; ENST00000431941; ENSP00000397646; ENSG00000115365.
DR Ensembl; ENST00000441020; ENSP00000393323; ENSG00000115365.
DR Ensembl; ENST00000443314; ENSP00000388713; ENSG00000115365.
DR Ensembl; ENST00000450366; ENSP00000393597; ENSG00000115365.
DR GeneID; 10314; -.
DR KEGG; hsa:10314; -.
DR UCSC; uc002ved.3; human.
DR CTD; 10314; -.
DR GeneCards; GC02M211259; -.
DR HGNC; HGNC:6508; LANCL1.
DR HPA; HPA034994; -.
DR MIM; 604155; gene.
DR neXtProt; NX_O43813; -.
DR PharmGKB; PA30293; -.
DR eggNOG; NOG245101; -.
DR HOGENOM; HOG000240926; -.
DR HOVERGEN; HBG065387; -.
DR InParanoid; O43813; -.
DR OMA; PGVIYML; -.
DR OrthoDB; EOG71VSTN; -.
DR PhylomeDB; O43813; -.
DR ChiTaRS; LANCL1; human.
DR EvolutionaryTrace; O43813; -.
DR GenomeRNAi; 10314; -.
DR NextBio; 39095; -.
DR PRO; PR:O43813; -.
DR ArrayExpress; O43813; -.
DR Bgee; O43813; -.
DR CleanEx; HS_LANCL1; -.
DR Genevestigator; O43813; -.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005887; C:integral to plasma membrane; TAS:ProtInc.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA:HPA.
DR GO; GO:0015630; C:microtubule cytoskeleton; IDA:HPA.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0003824; F:catalytic activity; IEA:InterPro.
DR GO; GO:0004930; F:G-protein coupled receptor activity; TAS:ProtInc.
DR GO; GO:0043295; F:glutathione binding; IDA:UniProtKB.
DR GO; GO:0050750; F:low-density lipoprotein particle receptor binding; IDA:MGI.
DR GO; GO:0008270; F:zinc ion binding; IDA:UniProtKB.
DR GO; GO:0008152; P:metabolic process; IEA:GOC.
DR Gene3D; 1.50.10.10; -; 1.
DR InterPro; IPR012341; 6hp_glycosidase.
DR InterPro; IPR007822; LANC-like.
DR InterPro; IPR020464; LanC-like_prot_euk.
DR Pfam; PF05147; LANC_like; 1.
DR PRINTS; PR01951; LANCEUKARYTE.
DR PRINTS; PR01950; LANCSUPER.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Complete proteome; Cytoplasm;
KW Direct protein sequencing; Membrane; Metal-binding; Nucleus;
KW Reference proteome; Zinc.
FT INIT_MET 1 1 Removed.
FT CHAIN 2 399 LanC-like protein 1.
FT /FTId=PRO_0000191268.
FT REGION 364 367 Glutathione binding.
FT METAL 276 276 Zinc.
FT METAL 322 322 Zinc.
FT METAL 323 323 Zinc.
FT BINDING 317 317 Glutathione.
FT MOD_RES 2 2 N-acetylalanine.
FT MOD_RES 142 142 N6-acetyllysine.
FT MUTAGEN 4 4 R->A: Loss of glutathione binding.
FT MUTAGEN 317 317 K->A: Loss of glutathione binding.
FT MUTAGEN 322 322 C->A: Loss of glutathione binding.
FT MUTAGEN 364 364 R->A,E: Loss of glutathione binding.
FT HELIX 2 4
FT HELIX 15 19
FT HELIX 30 50
FT TURN 51 53
FT STRAND 61 64
FT HELIX 65 79
FT HELIX 82 96
FT STRAND 106 109
FT HELIX 111 123
FT HELIX 127 138
FT HELIX 139 143
FT TURN 151 153
FT HELIX 155 169
FT HELIX 176 196
FT TURN 197 202
FT TURN 217 219
FT HELIX 221 228
FT HELIX 231 233
FT HELIX 237 242
FT HELIX 244 253
FT STRAND 274 278
FT HELIX 279 293
FT HELIX 296 312
FT TURN 321 323
FT HELIX 325 339
FT HELIX 342 355
FT TURN 356 359
FT TURN 372 374
FT HELIX 376 386
FT HELIX 389 391
FT TURN 395 397
SQ SEQUENCE 399 AA; 45283 MW; 2664F275F9281AF2 CRC64;
MAQRAFPNPY ADYNKSLAEG YFDAAGRLTP EFSQRLTNKI RELLQQMERG LKSADPRDGT
GYTGWAGIAV LYLHLYDVFG DPAYLQLAHG YVKQSLNCLT KRSITFLCGD AGPLAVAAVL
YHKMNNEKQA EDCITRLIHL NKIDPHAPNE MLYGRIGYIY ALLFVNKNFG VEKIPQSHIQ
QICETILTSG ENLARKRNFT AKSPLMYEWY QEYYVGAAHG LAGIYYYLMQ PSLQVSQGKL
HSLVKPSVDY VCQLKFPSGN YPPCIGDNRD LLVHWCHGAP GVIYMLIQAY KVFREEKYLC
DAYQCADVIW QYGLLKKGYG LCHGSAGNAY AFLTLYNLTQ DMKYLYRACK FAEWCLEYGE
HGCRTPDTPF SLFEGMAGTI YFLADLLVPT KARFPAFEL
//
ID LANC1_HUMAN Reviewed; 399 AA.
AC O43813;
DT 10-MAY-2004, integrated into UniProtKB/Swiss-Prot.
read moreDT 01-JUN-1998, sequence version 1.
DT 22-JAN-2014, entry version 106.
DE RecName: Full=LanC-like protein 1;
DE AltName: Full=40 kDa erythrocyte membrane protein;
DE Short=p40;
GN Name=LANCL1; Synonyms=GPR69A;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 5-24; 28-35; 40-50;
RP 198-201 AND 392-399, TISSUE SPECIFICITY, AND INTERACTION WITH STOM.
RC TISSUE=Bone marrow, Erythrocyte, and Fetal brain;
RX PubMed=9512664; DOI=10.1016/S0167-4781(97)00178-4;
RA Mayer H., Salzer U., Breuss J., Ziegler S., Marchler-Bauer A.,
RA Prohaska R.;
RT "Isolation, molecular characterization, and tissue-specific expression
RT of a novel putative G protein-coupled receptor.";
RL Biochim. Biophys. Acta 1395:301-308(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
RC TISSUE=Brain, and Testis;
RX PubMed=11474189;
RA Mayer H., Bauer H., Prohaska R.;
RT "Organization and chromosomal localization of the human and mouse
RT genes coding for LanC-like protein 1 (LANCL1).";
RL Cytogenet. Cell Genet. 93:100-104(2001).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Testis;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [4]
RP SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=10944443; DOI=10.1006/bbrc.2000.3260;
RA Bauer H., Mayer H., Marchler-Bauer A., Salzer U., Prohaska R.;
RT "Characterization of p40/GPR69A as a peripheral membrane protein
RT related to the lantibiotic synthetase component C.";
RL Biochem. Biophys. Res. Commun. 275:69-74(2000).
RN [5]
RP TISSUE SPECIFICITY, INTERACTION WITH P.FALCIPARUM SBP1, MASS
RP SPECTROMETRY, AND SUBCELLULAR LOCATION.
RX PubMed=15811525; DOI=10.1016/j.molbiopara.2005.01.013;
RA Blisnick T., Vincensini L., Barale J.C., Namane A., Braun Breton C.;
RT "LANCL1, an erythrocyte protein recruited to the Maurer's clefts
RT during Plasmodium falciparum development.";
RL Mol. Biochem. Parasitol. 141:39-47(2005).
RN [6]
RP SUBCELLULAR LOCATION.
RX PubMed=16979580; DOI=10.1016/j.bbamem.2006.07.018;
RA Landlinger C., Salzer U., Prohaska R.;
RT "Myristoylation of human LanC-like protein 2 (LANCL2) is essential for
RT the interaction with the plasma membrane and the increase in cellular
RT sensitivity to adriamycin.";
RL Biochim. Biophys. Acta 1758:1759-1767(2006).
RN [7]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, MASS SPECTROMETRY, AND
RP CLEAVAGE OF INITIATOR METHIONINE.
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
RA Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in
RT a refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [8]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-142, AND MASS SPECTROMETRY.
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M.,
RA Walther T.C., Olsen J.V., Mann M.;
RT "Lysine acetylation targets protein complexes and co-regulates major
RT cellular functions.";
RL Science 325:834-840(2009).
RN [9]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
RA Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [10]
RP X-RAY CRYSTALLOGRAPHY (2.60 ANGSTROMS) IN COMPLEX WITH GLUTATHIONE AND
RP ZINC IONS, MUTAGENESIS OF ARG-4; LYS-317; CYS-322 AND ARG-364,
RP INTERACTION WITH EPS8, AND FUNCTION.
RX PubMed=19528316; DOI=10.1101/gad.1789209;
RA Zhang W., Wang L., Liu Y., Xu J., Zhu G., Cang H., Li X., Bartlam M.,
RA Hensley K., Li G., Rao Z., Zhang X.C.;
RT "Structure of human lanthionine synthetase C-like protein 1 and its
RT interaction with Eps8 and glutathione.";
RL Genes Dev. 23:1387-1392(2009).
CC -!- FUNCTION: May play a role in EPS8 signaling. Binds glutathione.
CC -!- SUBUNIT: Interacts with the C-terminal of STOM. Interacts with the
CC EPS8 SH3 domain. Interaction with EPS8 is inhibited by glutathione
CC binding. Interacts with P.falciparum SBP1.
CC -!- INTERACTION:
CC Q08509:Eps8 (xeno); NbExp=2; IntAct=EBI-3046631, EBI-375596;
CC -!- SUBCELLULAR LOCATION: Cytoplasm. Membrane; Peripheral membrane
CC protein. Nucleus. Note=Detected at the surface of Maurer's clefts
CC in malaria-infected erythrocytes at late stages of parasite
CC development.
CC -!- TISSUE SPECIFICITY: Detected in erythrocytes, brain, kidney,
CC testis, ovary, heart, lung, placenta and spleen (at protein
CC level). Ubiquitous. Strongly expressed in brain, spinal cord,
CC pituitary gland, kidney, heart, skeletal muscle, pancreas, ovary
CC and testis.
CC -!- SIMILARITY: Belongs to the LanC-like protein family.
CC -!- CAUTION: Was originally (PubMed:9512664) thought to be a G-protein
CC coupled receptor.
CC -----------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution-NoDerivs License
CC -----------------------------------------------------------------------
DR EMBL; Y11395; CAA72205.1; -; mRNA.
DR EMBL; AJ289236; CAC21950.1; -; Genomic_DNA.
DR EMBL; AJ289237; CAC21950.1; JOINED; Genomic_DNA.
DR EMBL; AJ289238; CAC21950.1; JOINED; Genomic_DNA.
DR EMBL; AJ289239; CAC21950.1; JOINED; Genomic_DNA.
DR EMBL; BC028685; AAH28685.1; -; mRNA.
DR RefSeq; NP_001130046.1; NM_001136574.1.
DR RefSeq; NP_001130047.1; NM_001136575.1.
DR RefSeq; NP_006046.1; NM_006055.2.
DR UniGene; Hs.13351; -.
DR PDB; 3E6U; X-ray; 2.60 A; A/B/C/D=1-399.
DR PDB; 3E73; X-ray; 2.80 A; A/B=1-399.
DR PDBsum; 3E6U; -.
DR PDBsum; 3E73; -.
DR ProteinModelPortal; O43813; -.
DR SMR; O43813; 1-399.
DR IntAct; O43813; 3.
DR MINT; MINT-3308405; -.
DR STRING; 9606.ENSP00000233714; -.
DR PhosphoSite; O43813; -.
DR PaxDb; O43813; -.
DR PeptideAtlas; O43813; -.
DR PRIDE; O43813; -.
DR DNASU; 10314; -.
DR Ensembl; ENST00000233714; ENSP00000233714; ENSG00000115365.
DR Ensembl; ENST00000431941; ENSP00000397646; ENSG00000115365.
DR Ensembl; ENST00000441020; ENSP00000393323; ENSG00000115365.
DR Ensembl; ENST00000443314; ENSP00000388713; ENSG00000115365.
DR Ensembl; ENST00000450366; ENSP00000393597; ENSG00000115365.
DR GeneID; 10314; -.
DR KEGG; hsa:10314; -.
DR UCSC; uc002ved.3; human.
DR CTD; 10314; -.
DR GeneCards; GC02M211259; -.
DR HGNC; HGNC:6508; LANCL1.
DR HPA; HPA034994; -.
DR MIM; 604155; gene.
DR neXtProt; NX_O43813; -.
DR PharmGKB; PA30293; -.
DR eggNOG; NOG245101; -.
DR HOGENOM; HOG000240926; -.
DR HOVERGEN; HBG065387; -.
DR InParanoid; O43813; -.
DR OMA; PGVIYML; -.
DR OrthoDB; EOG71VSTN; -.
DR PhylomeDB; O43813; -.
DR ChiTaRS; LANCL1; human.
DR EvolutionaryTrace; O43813; -.
DR GenomeRNAi; 10314; -.
DR NextBio; 39095; -.
DR PRO; PR:O43813; -.
DR ArrayExpress; O43813; -.
DR Bgee; O43813; -.
DR CleanEx; HS_LANCL1; -.
DR Genevestigator; O43813; -.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005887; C:integral to plasma membrane; TAS:ProtInc.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA:HPA.
DR GO; GO:0015630; C:microtubule cytoskeleton; IDA:HPA.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0003824; F:catalytic activity; IEA:InterPro.
DR GO; GO:0004930; F:G-protein coupled receptor activity; TAS:ProtInc.
DR GO; GO:0043295; F:glutathione binding; IDA:UniProtKB.
DR GO; GO:0050750; F:low-density lipoprotein particle receptor binding; IDA:MGI.
DR GO; GO:0008270; F:zinc ion binding; IDA:UniProtKB.
DR GO; GO:0008152; P:metabolic process; IEA:GOC.
DR Gene3D; 1.50.10.10; -; 1.
DR InterPro; IPR012341; 6hp_glycosidase.
DR InterPro; IPR007822; LANC-like.
DR InterPro; IPR020464; LanC-like_prot_euk.
DR Pfam; PF05147; LANC_like; 1.
DR PRINTS; PR01951; LANCEUKARYTE.
DR PRINTS; PR01950; LANCSUPER.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Complete proteome; Cytoplasm;
KW Direct protein sequencing; Membrane; Metal-binding; Nucleus;
KW Reference proteome; Zinc.
FT INIT_MET 1 1 Removed.
FT CHAIN 2 399 LanC-like protein 1.
FT /FTId=PRO_0000191268.
FT REGION 364 367 Glutathione binding.
FT METAL 276 276 Zinc.
FT METAL 322 322 Zinc.
FT METAL 323 323 Zinc.
FT BINDING 317 317 Glutathione.
FT MOD_RES 2 2 N-acetylalanine.
FT MOD_RES 142 142 N6-acetyllysine.
FT MUTAGEN 4 4 R->A: Loss of glutathione binding.
FT MUTAGEN 317 317 K->A: Loss of glutathione binding.
FT MUTAGEN 322 322 C->A: Loss of glutathione binding.
FT MUTAGEN 364 364 R->A,E: Loss of glutathione binding.
FT HELIX 2 4
FT HELIX 15 19
FT HELIX 30 50
FT TURN 51 53
FT STRAND 61 64
FT HELIX 65 79
FT HELIX 82 96
FT STRAND 106 109
FT HELIX 111 123
FT HELIX 127 138
FT HELIX 139 143
FT TURN 151 153
FT HELIX 155 169
FT HELIX 176 196
FT TURN 197 202
FT TURN 217 219
FT HELIX 221 228
FT HELIX 231 233
FT HELIX 237 242
FT HELIX 244 253
FT STRAND 274 278
FT HELIX 279 293
FT HELIX 296 312
FT TURN 321 323
FT HELIX 325 339
FT HELIX 342 355
FT TURN 356 359
FT TURN 372 374
FT HELIX 376 386
FT HELIX 389 391
FT TURN 395 397
SQ SEQUENCE 399 AA; 45283 MW; 2664F275F9281AF2 CRC64;
MAQRAFPNPY ADYNKSLAEG YFDAAGRLTP EFSQRLTNKI RELLQQMERG LKSADPRDGT
GYTGWAGIAV LYLHLYDVFG DPAYLQLAHG YVKQSLNCLT KRSITFLCGD AGPLAVAAVL
YHKMNNEKQA EDCITRLIHL NKIDPHAPNE MLYGRIGYIY ALLFVNKNFG VEKIPQSHIQ
QICETILTSG ENLARKRNFT AKSPLMYEWY QEYYVGAAHG LAGIYYYLMQ PSLQVSQGKL
HSLVKPSVDY VCQLKFPSGN YPPCIGDNRD LLVHWCHGAP GVIYMLIQAY KVFREEKYLC
DAYQCADVIW QYGLLKKGYG LCHGSAGNAY AFLTLYNLTQ DMKYLYRACK FAEWCLEYGE
HGCRTPDTPF SLFEGMAGTI YFLADLLVPT KARFPAFEL
//
MIM
604155
*RECORD*
*FIELD* NO
604155
*FIELD* TI
*604155 LanC-LIKE 1; LANCL1
;;LANTHIONINE-SYNTHETASE COMPONENT C-LIKE 1 G PROTEIN-COUPLED RECEPTOR;;
read moreG PROTEIN-COUPLED RECEPTOR 69A; GPR69A
*FIELD* TX
CLONING
By affinity chromatography of solubilized human erythrocyte membrane
proteins, Mayer et al. (1998) identified p40, a 40-kD protein that
interacts with the C-terminus of the membrane protein stomatin (133090).
They used the sequence of p40 peptides to identify partial cDNAs in an
EST database, and then cloned cDNAs corresponding to the entire coding
region using a PCR strategy. The predicted 399-amino acid protein
contains the characteristic features of G protein-coupled receptors
(GPCRs), including 7 transmembrane domains. Northern blot analysis
revealed that p40 is expressed as a major 4.8-kb mRNA and as a minor
1.9-kb mRNA in all tissues. Dot blot experiments indicated that the
highest levels of expression were in brain, spinal cord, testis,
pituitary gland, and kidney. Using in situ hybridization to monkey
tissues, Mayer et al. (1998) determined that p40 is expressed at high
levels in neurons of the brain and spinal cord, in thymocytes,
megakaryocytes, and macrophages.
Bauer et al. (2000) determined that LANCL1 is not an integral membrane
protein, but rather a weakly associated peripheral membrane protein, and
is not a GPCR. They found that LANCL1 contains 7 highly conserved
hydrophobic repeats and may play a role in peptide modification. Western
blot analysis showed that LANCL1 is mainly expressed in brain, testis,
ovary, and kidney.
GENE FUNCTION
Zhang et al. (2009) showed that LANCL1 exhibited Zn(2+)-dependent
glutathione binding. LANCL1 also bound the SH3 domain of mouse Eps8
(600206), but not other SH3-containing proteins. The interaction between
LANCL1 and Eps8 did not require either of the PxxP motifs of LANCL1, but
it was inhibited by glutathione. Overexpression of LANCL1 in rat PC12
cells had no effect on NGF (see 162030)-induced neurite outgrowth, but
overexpression of an LANCL1 mutant defective in Eps8 binding inhibited
NGF-induced neurite outgrowth by 50%.
BIOCHEMICAL FEATURES
Zhang et al. (2009) reported the crystal structure of LANCL1, which
consists of 2 concentric alpha-helical barrels made up of 7 helices
each. A GxxG-containing bulge that mediates Zn(2+) binding is located at
the N terminus of each of the 7 inner helices. LANCL1 had a similar
structure when cocrystalized with glutathione. In addition to
Zn(2+)-mediated binding, there were extensive interactions between
LANCL1 and glutathione.
GENE STRUCTURE
Mayer et al. (2001) determined that the human and mouse LANCL1 genes
span 45 kb and 38 kb, respectively, each comprising 10 exons.
MAPPING
The International Radiation Hybrid Mapping Consortium mapped the LANCL1
gene to 2q33-q35 (TMAP WI-13674). By FISH, Mayer et al. (2001) mapped
the LANCL1 gene to 2q34 and the mouse homolog to a region of conserved
synteny at chromosome 1C2-C5.
*FIELD* RF
1. Bauer, H.; Mayer, H.; Marchler-Bauer, A.; Salzer, U.; Prohaska,
R.: Characterization of p40/GPR69A as a peripheral membrane protein
related to the lantibiotic synthetase component C. Biochem. Biophys.
Res. Commun. 275: 69-74, 2000.
2. Mayer, H.; Bauer, H.; Prohaska, R.: Organization and chromosomal
localization of the human and mouse genes coding for LanC-like protein
1 (LANCL1). Cytogenet. Cell Genet. 93: 100-104, 2001.
3. Mayer, H.; Salzer, U.; Breuss, J.; Ziegler, S.; Marchler-Bauer,
A.; Prohaska, R.: Isolation, molecular characterization, and tissue-specific
expression of a novel putative G protein-coupled receptor. Biochim.
Biophys. Acta 1395: 301-308, 1998.
4. 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.: Structure
of human lanthionine synthetase C-like protein 1 and its interaction
with Eps8 and glutathione. Genes Dev. 23: 1387-1392, 2009.
*FIELD* CN
Patricia A. Hartz - updated: 7/17/2009
Carol A. Bocchini - updated: 8/28/2001
Paul J. Converse - updated: 12/7/2000
*FIELD* CD
Rebekah S. Rasooly: 9/3/1999
*FIELD* ED
mgross: 07/17/2009
mgross: 7/17/2009
terry: 7/17/2009
carol: 11/6/2003
carol: 9/10/2001
mcapotos: 8/28/2001
mgross: 12/8/2000
terry: 12/7/2000
carol: 10/2/2000
alopez: 9/3/1999
*RECORD*
*FIELD* NO
604155
*FIELD* TI
*604155 LanC-LIKE 1; LANCL1
;;LANTHIONINE-SYNTHETASE COMPONENT C-LIKE 1 G PROTEIN-COUPLED RECEPTOR;;
read moreG PROTEIN-COUPLED RECEPTOR 69A; GPR69A
*FIELD* TX
CLONING
By affinity chromatography of solubilized human erythrocyte membrane
proteins, Mayer et al. (1998) identified p40, a 40-kD protein that
interacts with the C-terminus of the membrane protein stomatin (133090).
They used the sequence of p40 peptides to identify partial cDNAs in an
EST database, and then cloned cDNAs corresponding to the entire coding
region using a PCR strategy. The predicted 399-amino acid protein
contains the characteristic features of G protein-coupled receptors
(GPCRs), including 7 transmembrane domains. Northern blot analysis
revealed that p40 is expressed as a major 4.8-kb mRNA and as a minor
1.9-kb mRNA in all tissues. Dot blot experiments indicated that the
highest levels of expression were in brain, spinal cord, testis,
pituitary gland, and kidney. Using in situ hybridization to monkey
tissues, Mayer et al. (1998) determined that p40 is expressed at high
levels in neurons of the brain and spinal cord, in thymocytes,
megakaryocytes, and macrophages.
Bauer et al. (2000) determined that LANCL1 is not an integral membrane
protein, but rather a weakly associated peripheral membrane protein, and
is not a GPCR. They found that LANCL1 contains 7 highly conserved
hydrophobic repeats and may play a role in peptide modification. Western
blot analysis showed that LANCL1 is mainly expressed in brain, testis,
ovary, and kidney.
GENE FUNCTION
Zhang et al. (2009) showed that LANCL1 exhibited Zn(2+)-dependent
glutathione binding. LANCL1 also bound the SH3 domain of mouse Eps8
(600206), but not other SH3-containing proteins. The interaction between
LANCL1 and Eps8 did not require either of the PxxP motifs of LANCL1, but
it was inhibited by glutathione. Overexpression of LANCL1 in rat PC12
cells had no effect on NGF (see 162030)-induced neurite outgrowth, but
overexpression of an LANCL1 mutant defective in Eps8 binding inhibited
NGF-induced neurite outgrowth by 50%.
BIOCHEMICAL FEATURES
Zhang et al. (2009) reported the crystal structure of LANCL1, which
consists of 2 concentric alpha-helical barrels made up of 7 helices
each. A GxxG-containing bulge that mediates Zn(2+) binding is located at
the N terminus of each of the 7 inner helices. LANCL1 had a similar
structure when cocrystalized with glutathione. In addition to
Zn(2+)-mediated binding, there were extensive interactions between
LANCL1 and glutathione.
GENE STRUCTURE
Mayer et al. (2001) determined that the human and mouse LANCL1 genes
span 45 kb and 38 kb, respectively, each comprising 10 exons.
MAPPING
The International Radiation Hybrid Mapping Consortium mapped the LANCL1
gene to 2q33-q35 (TMAP WI-13674). By FISH, Mayer et al. (2001) mapped
the LANCL1 gene to 2q34 and the mouse homolog to a region of conserved
synteny at chromosome 1C2-C5.
*FIELD* RF
1. Bauer, H.; Mayer, H.; Marchler-Bauer, A.; Salzer, U.; Prohaska,
R.: Characterization of p40/GPR69A as a peripheral membrane protein
related to the lantibiotic synthetase component C. Biochem. Biophys.
Res. Commun. 275: 69-74, 2000.
2. Mayer, H.; Bauer, H.; Prohaska, R.: Organization and chromosomal
localization of the human and mouse genes coding for LanC-like protein
1 (LANCL1). Cytogenet. Cell Genet. 93: 100-104, 2001.
3. Mayer, H.; Salzer, U.; Breuss, J.; Ziegler, S.; Marchler-Bauer,
A.; Prohaska, R.: Isolation, molecular characterization, and tissue-specific
expression of a novel putative G protein-coupled receptor. Biochim.
Biophys. Acta 1395: 301-308, 1998.
4. 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.: Structure
of human lanthionine synthetase C-like protein 1 and its interaction
with Eps8 and glutathione. Genes Dev. 23: 1387-1392, 2009.
*FIELD* CN
Patricia A. Hartz - updated: 7/17/2009
Carol A. Bocchini - updated: 8/28/2001
Paul J. Converse - updated: 12/7/2000
*FIELD* CD
Rebekah S. Rasooly: 9/3/1999
*FIELD* ED
mgross: 07/17/2009
mgross: 7/17/2009
terry: 7/17/2009
carol: 11/6/2003
carol: 9/10/2001
mcapotos: 8/28/2001
mgross: 12/8/2000
terry: 12/7/2000
carol: 10/2/2000
alopez: 9/3/1999