LYPD1_MOUSE
ID LYPD1_MOUSE Reviewed; 141 AA.
AC Q8BLC3; Q3V2X5; Q3V447; Q9JJ96;
DT 07-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 125.
DE RecName: Full=Ly6/PLAUR domain-containing protein 1;
DE AltName: Full=Ly-6/neurotoxin-like protein 2;
DE Short=Lynx2;
DE Flags: Precursor;
GN Name=Lypd1; Synonyms=Lypdc1; ORFNames=MNCb-0671;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Brain;
RA Osada N., Kusuda J., Tanuma R., Ito A., Hirata M., Sugano S., Hashimoto K.;
RT "Isolation of full-length cDNA clones from mouse brain cDNA library made by
RT oligo-capping method.";
RL Submitted (APR-2000) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Corpora quadrigemina;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Olfactory epithelium;
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 [4]
RP TISSUE SPECIFICITY.
RX PubMed=16236524; DOI=10.1016/j.mcn.2005.09.010;
RA Dessaud E., Salauen D., Gayet O., Chabbert M., deLapeyriere O.;
RT "Identification of lynx2, a novel member of the ly-6/neurotoxin
RT superfamily, expressed in neuronal subpopulations during mouse
RT development.";
RL Mol. Cell. Neurosci. 31:232-242(2006).
RN [5]
RP FUNCTION, INTERACTION WITH CHRNA4; CHRNA7 AND CHRNB2, TISSUE SPECIFICITY,
RP AND DISRUPTION PHENOTYPE.
RX PubMed=19246390; DOI=10.1073/pnas.0813109106;
RA Tekinay A.B., Nong Y., Miwa J.M., Lieberam I., Ibanez-Tallon I.,
RA Greengard P., Heintz N.;
RT "A role for LYNX2 in anxiety-related behavior.";
RL Proc. Natl. Acad. Sci. U.S.A. 106:4477-4482(2009).
RN [6]
RP FUNCTION, AND INTERACTION WITH CHRNA4.
RX PubMed=26276394; DOI=10.1074/jbc.m115.647248;
RA Wu M., Puddifoot C.A., Taylor P., Joiner W.J.;
RT "Mechanisms of inhibition and potentiation of alpha4beta2 nicotinic
RT acetylcholine receptors by members of the Ly6 protein family.";
RL J. Biol. Chem. 290:24509-24518(2015).
RN [7]
RP FUNCTION, AND INTERACTION WITH CHRNA7.
RX PubMed=25716842; DOI=10.1523/jneurosci.3630-14.2015;
RA Puddifoot C.A., Wu M., Sung R.J., Joiner W.J.;
RT "Ly6h regulates trafficking of alpha7 nicotinic acetylcholine receptors and
RT nicotine-induced potentiation of glutamatergic signaling.";
RL J. Neurosci. 35:3420-3430(2015).
CC -!- FUNCTION: Believed to act as a modulator of nicotinic acetylcholine
CC receptors (nAChRs) activity. In vitro increases receptor
CC desensitization and decreases affinity for ACh of alpha-4:beta-2-
CC containing nAChRs (PubMed:19246390). May play a role in the
CC intracellular trafficking of alpha-4:beta-2 and alpha-7-containing
CC nAChRs and may inhibit their expression at the cell surface
CC (PubMed:26276394, PubMed:25716842). May be involved in the control of
CC anxiety (PubMed:19246390). {ECO:0000269|PubMed:19246390,
CC ECO:0000269|PubMed:25716842, ECO:0000269|PubMed:26276394}.
CC -!- SUBUNIT: Interacts with CHRNA4 and nAChRs containing alpha-4:beta-2
CC (CHRNA4:CHRNB2) and alpha-7 (CHRNA7) subunits.
CC {ECO:0000269|PubMed:19246390, ECO:0000269|PubMed:25716842,
CC ECO:0000269|PubMed:26276394}.
CC -!- INTERACTION:
CC Q8BLC3; O70174: Chrna4; NbExp=3; IntAct=EBI-14035010, EBI-10916203;
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Lipid-anchor, GPI-
CC anchor {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Preferentially expressed in the nervous system.
CC Expressed in embryonic and postnatal postmitotic central and peripheral
CC neurons including subpopulations of motor neurons, sensory neurons,
CC interneurons and neurons of the autonomous nervous system. Expressed
CC around the growing nerves in the limb bud (PubMed:16236524). Expressed
CC at high levels in specific brain regions such as the prefrontal cortex,
CC amygdala, hippocampus, mediodorsal thalamus, dentate gyrus and specific
CC brainstem nuclei (at protein level) (PubMed:19246390).
CC {ECO:0000269|PubMed:16236524, ECO:0000269|PubMed:19246390}.
CC -!- DISRUPTION PHENOTYPE: Increased anxiety-like behaviors. Increased
CC glutamatergic activity in response to nicotine in layer V neurons of
CC the medial prefrontal cortex. {ECO:0000269|PubMed:19246390}.
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DR EMBL; AB041649; BAA95101.1; -; mRNA.
DR EMBL; AK012406; BAE43232.1; -; mRNA.
DR EMBL; AK045592; BAC32428.1; -; mRNA.
DR EMBL; AK082941; BAE43380.1; -; mRNA.
DR EMBL; BC058599; AAH58599.1; -; mRNA.
DR CCDS; CCDS15243.1; -.
DR RefSeq; NP_001298018.1; NM_001311089.1.
DR RefSeq; NP_001298019.1; NM_001311090.1.
DR RefSeq; NP_659568.2; NM_145100.4.
DR AlphaFoldDB; Q8BLC3; -.
DR SMR; Q8BLC3; -.
DR DIP; DIP-48729N; -.
DR IntAct; Q8BLC3; 2.
DR STRING; 10090.ENSMUSP00000125149; -.
DR GlyGen; Q8BLC3; 1 site.
DR PhosphoSitePlus; Q8BLC3; -.
DR PaxDb; Q8BLC3; -.
DR PRIDE; Q8BLC3; -.
DR ProteomicsDB; 295738; -.
DR Antibodypedia; 56153; 81 antibodies from 19 providers.
DR DNASU; 72585; -.
DR Ensembl; ENSMUST00000159417; ENSMUSP00000125149; ENSMUSG00000026344.
DR GeneID; 72585; -.
DR KEGG; mmu:72585; -.
DR UCSC; uc007cki.1; mouse.
DR CTD; 116372; -.
DR MGI; MGI:1919835; Lypd1.
DR VEuPathDB; HostDB:ENSMUSG00000026344; -.
DR eggNOG; ENOG502S22T; Eukaryota.
DR GeneTree; ENSGT00390000002215; -.
DR HOGENOM; CLU_152037_0_0_1; -.
DR InParanoid; Q8BLC3; -.
DR OMA; TFCGLFW; -.
DR OrthoDB; 1377473at2759; -.
DR TreeFam; TF332325; -.
DR Reactome; R-MMU-163125; Post-translational modification: synthesis of GPI-anchored proteins.
DR BioGRID-ORCS; 72585; 4 hits in 74 CRISPR screens.
DR PRO; PR:Q8BLC3; -.
DR Proteomes; UP000000589; Chromosome 1.
DR RNAct; Q8BLC3; protein.
DR Bgee; ENSMUSG00000026344; Expressed in epibranchial ganglion and 181 other tissues.
DR ExpressionAtlas; Q8BLC3; baseline and differential.
DR Genevisible; Q8BLC3; MM.
DR GO; GO:0031225; C:anchored component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0016020; C:membrane; IDA:MGI.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0045202; C:synapse; IEA:GOC.
DR GO; GO:0033130; F:acetylcholine receptor binding; IDA:MGI.
DR GO; GO:0030550; F:acetylcholine receptor inhibitor activity; IDA:MGI.
DR GO; GO:0095500; P:acetylcholine receptor signaling pathway; IDA:MGI.
DR GO; GO:0001662; P:behavioral fear response; IMP:MGI.
DR GO; GO:1903077; P:negative regulation of protein localization to plasma membrane; IDA:MGI.
DR GO; GO:0072659; P:protein localization to plasma membrane; IDA:MGI.
DR GO; GO:0035094; P:response to nicotine; IMP:MGI.
DR GO; GO:0007271; P:synaptic transmission, cholinergic; IDA:MGI.
DR InterPro; IPR045860; Snake_toxin-like_sf.
DR SUPFAM; SSF57302; SSF57302; 1.
PE 1: Evidence at protein level;
KW Cell membrane; Disulfide bond; Glycoprotein; GPI-anchor; Lipoprotein;
KW Membrane; Reference proteome; Signal.
FT SIGNAL 1..20
FT /evidence="ECO:0000255"
FT CHAIN 21..115
FT /note="Ly6/PLAUR domain-containing protein 1"
FT /id="PRO_0000226743"
FT PROPEP 116..141
FT /note="Removed in mature form"
FT /evidence="ECO:0000255"
FT /id="PRO_0000226744"
FT DOMAIN 25..107
FT /note="UPAR/Ly6"
FT LIPID 115
FT /note="GPI-anchor amidated glycine"
FT /evidence="ECO:0000255"
FT CARBOHYD 45
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 25..54
FT /evidence="ECO:0000250|UniProtKB:P0DP57,
FT ECO:0000250|UniProtKB:P0DP58"
FT DISULFID 28..37
FT /evidence="ECO:0000250|UniProtKB:P0DP57,
FT ECO:0000250|UniProtKB:P0DP58"
FT DISULFID 46..77
FT /evidence="ECO:0000250|UniProtKB:P0DP57,
FT ECO:0000250|UniProtKB:P0DP58"
FT DISULFID 88..100
FT /evidence="ECO:0000250|UniProtKB:P0DP57,
FT ECO:0000250|UniProtKB:P0DP58"
FT DISULFID 101..106
FT /evidence="ECO:0000250|UniProtKB:P0DP57,
FT ECO:0000250|UniProtKB:P0DP58"
FT CONFLICT 59
FT /note="M -> T (in Ref. 1; BAA95101)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 141 AA; 15261 MW; 51717F7922C02DAA CRC64;
MWVLGIAATF CGLFWLPGLA LQIQCYQCEE FQLNNDCSSP EFIVNCTVNV QDMCQKEVME
QSAGIMYRKS CASSAACLIA SAGYQSFCSP GKLNSVCISC CNTPLCNGPR PKKRGSSASA
IRPGLLTTLL FFHLALCLAH C
