LPD6B_HUMAN
ID LPD6B_HUMAN Reviewed; 183 AA.
AC Q8NI32; D3DP90; Q53TK0; Q7Z747; Q8IXK7;
DT 26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 1.
DT 03-AUG-2022, entry version 120.
DE RecName: Full=Ly6/PLAUR domain-containing protein 6B;
DE Flags: Precursor;
GN Name=LYPD6B;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RA Guo J.H., Yu L.;
RL Submitted (OCT-2001) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15815621; DOI=10.1038/nature03466;
RA Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P.,
RA Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C.,
RA Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L.,
RA Du H., Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A.,
RA Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J.,
RA Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M.,
RA Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T.,
RA Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S.,
RA Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K.,
RA McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C.,
RA Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S.,
RA Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C.,
RA Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M.,
RA Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C.,
RA Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J.,
RA Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E.,
RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X.,
RA Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M.,
RA Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C.,
RA Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S.,
RA Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H.,
RA Wilson R.K.;
RT "Generation and annotation of the DNA sequences of human chromosomes 2 and
RT 4.";
RL Nature 434:724-731(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Brain, and Ovary;
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 project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [5]
RP FUNCTION.
RX PubMed=26586467; DOI=10.1096/fj.15-274548;
RA Ochoa V., George A.A., Nishi R., Whiteaker P.;
RT "The prototoxin LYPD6B modulates heteromeric alpha3beta4-containing
RT nicotinic acetylcholine receptors, but not alpha7 homomers.";
RL FASEB J. 30:1109-1119(2016).
CC -!- FUNCTION: Believed to act as a modulator of nicotinic acetylcholine
CC receptors (nAChRs) activity. In vitro acts on nAChRs in a subtype- and
CC stoichiometry-dependent manner. Modulates specifically alpha-3(3):beta-
CC 4(2) nAChRs by enhancing the sensitivity to ACh, decreasing ACh-induced
CC maximal current response and increasing the rate of desensitization to
CC ACh; has no effect on alpha-7 homomeric nAChRs; modulates alpha-
CC 3(2):alpha-5:beta-4(2) nAChRs in the context of CHRNA5/alpha-5 variant
CC Asn-398 but not its wild-type sequence. {ECO:0000269|PubMed:26586467}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Lipid-anchor, GPI-
CC anchor {ECO:0000305}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q8NI32-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8NI32-2; Sequence=VSP_031842;
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH18203.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=AAH18203.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AF435957; AAM20908.1; -; mRNA.
DR EMBL; AC009230; AAY14974.1; -; Genomic_DNA.
DR EMBL; AC073271; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471058; EAX11541.1; -; Genomic_DNA.
DR EMBL; CH471058; EAX11542.1; -; Genomic_DNA.
DR EMBL; CH471058; EAX11543.1; -; Genomic_DNA.
DR EMBL; BC018203; AAH18203.1; ALT_SEQ; mRNA.
DR EMBL; BC040176; AAH40176.2; -; mRNA.
DR CCDS; CCDS46423.1; -. [Q8NI32-2]
DR CCDS; CCDS82519.1; -. [Q8NI32-1]
DR RefSeq; NP_001303931.1; NM_001317002.1. [Q8NI32-2]
DR RefSeq; NP_001303932.1; NM_001317003.1. [Q8NI32-1]
DR RefSeq; NP_001303933.1; NM_001317004.1. [Q8NI32-1]
DR RefSeq; NP_001303934.1; NM_001317005.1. [Q8NI32-1]
DR RefSeq; NP_001303935.1; NM_001317006.1.
DR RefSeq; NP_808879.2; NM_177964.4. [Q8NI32-2]
DR RefSeq; XP_006712344.1; XM_006712281.3. [Q8NI32-1]
DR RefSeq; XP_011508925.1; XM_011510623.2. [Q8NI32-1]
DR RefSeq; XP_016858853.1; XM_017003364.1. [Q8NI32-2]
DR RefSeq; XP_016858854.1; XM_017003365.1. [Q8NI32-1]
DR RefSeq; XP_016858855.1; XM_017003366.1. [Q8NI32-1]
DR PDB; 6ZSO; NMR; -; A=60-154.
DR PDBsum; 6ZSO; -.
DR AlphaFoldDB; Q8NI32; -.
DR SMR; Q8NI32; -.
DR BioGRID; 126243; 50.
DR IntAct; Q8NI32; 1.
DR STRING; 9606.ENSP00000387077; -.
DR TCDB; 8.A.31.1.2; the ly-6 neurotoxin-like protein1 precursor (lynx1) family.
DR GlyGen; Q8NI32; 4 sites.
DR BioMuta; LYPD6B; -.
DR DMDM; 74715711; -.
DR MassIVE; Q8NI32; -.
DR PaxDb; Q8NI32; -.
DR PeptideAtlas; Q8NI32; -.
DR PRIDE; Q8NI32; -.
DR ProteomicsDB; 73820; -. [Q8NI32-1]
DR ProteomicsDB; 73821; -. [Q8NI32-2]
DR Antibodypedia; 62112; 27 antibodies from 12 providers.
DR DNASU; 130576; -.
DR Ensembl; ENST00000409029.5; ENSP00000386650.1; ENSG00000150556.17. [Q8NI32-1]
DR Ensembl; ENST00000409642.8; ENSP00000387077.3; ENSG00000150556.17. [Q8NI32-2]
DR Ensembl; ENST00000409876.5; ENSP00000386479.1; ENSG00000150556.17. [Q8NI32-1]
DR GeneID; 130576; -.
DR KEGG; hsa:130576; -.
DR MANE-Select; ENST00000409642.8; ENSP00000387077.3; NM_177964.5; NP_808879.2. [Q8NI32-2]
DR UCSC; uc002twv.2; human. [Q8NI32-1]
DR CTD; 130576; -.
DR GeneCards; LYPD6B; -.
DR HGNC; HGNC:27018; LYPD6B.
DR HPA; ENSG00000150556; Tissue enhanced (skin, stomach).
DR neXtProt; NX_Q8NI32; -.
DR OpenTargets; ENSG00000150556; -.
DR PharmGKB; PA162394734; -.
DR VEuPathDB; HostDB:ENSG00000150556; -.
DR eggNOG; ENOG502RXMG; Eukaryota.
DR GeneTree; ENSGT00390000000220; -.
DR InParanoid; Q8NI32; -.
DR OMA; DCNRWAE; -.
DR PhylomeDB; Q8NI32; -.
DR TreeFam; TF332443; -.
DR PathwayCommons; Q8NI32; -.
DR Reactome; R-HSA-163125; Post-translational modification: synthesis of GPI-anchored proteins.
DR SignaLink; Q8NI32; -.
DR BioGRID-ORCS; 130576; 9 hits in 1059 CRISPR screens.
DR ChiTaRS; LYPD6B; human.
DR GenomeRNAi; 130576; -.
DR Pharos; Q8NI32; Tdark.
DR PRO; PR:Q8NI32; -.
DR Proteomes; UP000005640; Chromosome 2.
DR RNAct; Q8NI32; protein.
DR Bgee; ENSG00000150556; Expressed in skin of abdomen and 115 other tissues.
DR ExpressionAtlas; Q8NI32; baseline and differential.
DR Genevisible; Q8NI32; HS.
DR GO; GO:0031225; C:anchored component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005576; C:extracellular region; TAS:Reactome.
DR GO; GO:0005886; C:plasma membrane; TAS:Reactome.
DR GO; GO:0030548; F:acetylcholine receptor regulator activity; IDA:UniProtKB.
DR Gene3D; 2.10.60.10; -; 1.
DR InterPro; IPR039457; LYPD6-like.
DR InterPro; IPR045860; Snake_toxin-like_sf.
DR PANTHER; PTHR31171; PTHR31171; 1.
DR SUPFAM; SSF57302; SSF57302; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Cell membrane; Disulfide bond;
KW Glycoprotein; GPI-anchor; Lipoprotein; Membrane; Reference proteome;
KW Signal.
FT SIGNAL 1..39
FT /evidence="ECO:0000255"
FT CHAIN 40..164
FT /note="Ly6/PLAUR domain-containing protein 6B"
FT /id="PRO_0000321950"
FT PROPEP 165..183
FT /note="Removed in mature form"
FT /evidence="ECO:0000255"
FT /id="PRO_0000321951"
FT DOMAIN 60..151
FT /note="UPAR/Ly6"
FT LIPID 164
FT /note="GPI-anchor amidated serine"
FT /evidence="ECO:0000255"
FT DISULFID 62..90
FT /evidence="ECO:0000250|UniProtKB:P0DP57,
FT ECO:0000250|UniProtKB:P0DP58"
FT DISULFID 65..74
FT /evidence="ECO:0000250|UniProtKB:P0DP57,
FT ECO:0000250|UniProtKB:P0DP58"
FT DISULFID 83..109
FT /evidence="ECO:0000250|UniProtKB:P0DP57,
FT ECO:0000250|UniProtKB:P0DP58"
FT DISULFID 115..134
FT /evidence="ECO:0000250|UniProtKB:P0DP57,
FT ECO:0000250|UniProtKB:P0DP58"
FT DISULFID 135..140
FT /evidence="ECO:0000250|UniProtKB:P0DP57,
FT ECO:0000250|UniProtKB:P0DP58"
FT VAR_SEQ 2
FT /note="L -> LLITLSANLFTVPERSLTTTFSFSR (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_031842"
FT HELIX 71..77
FT /evidence="ECO:0007829|PDB:6ZSO"
FT STRAND 89..99
FT /evidence="ECO:0007829|PDB:6ZSO"
FT STRAND 105..110
FT /evidence="ECO:0007829|PDB:6ZSO"
FT TURN 112..117
FT /evidence="ECO:0007829|PDB:6ZSO"
FT STRAND 119..122
FT /evidence="ECO:0007829|PDB:6ZSO"
FT STRAND 124..135
FT /evidence="ECO:0007829|PDB:6ZSO"
SQ SEQUENCE 183 AA; 20656 MW; 817D3D181568C5A2 CRC64;
MLYKSSDRPA HKVSMLLLCH ALAIAVVQIV IFSESWAFAK NINFYNVRPP LDPTPFPNSF
KCFTCENAGD NYNCNRWAED KWCPQNTQYC LTVHHFTSHG RSTSITKKCA SRSECHFVGC
HHSRDSEHTE CRSCCEGMIC NVELPTNHTN AVFAVMHAQR TSGSSAPTLY LPVLAWVFVL
PLL
