LY66E_MOUSE
ID LY66E_MOUSE Reviewed; 166 AA.
AC Q8K1T6; Q9D7E5;
DT 05-JUL-2017, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 1.
DT 03-AUG-2022, entry version 104.
DE RecName: Full=Lymphocyte antigen 6G6e;
DE AltName: Full=Lymphocyte antigen 6 complex locus protein G6e;
DE Flags: Precursor;
GN Name=Ly6g6e;
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 [MRNA] (ISOFORM 1).
RC STRAIN=129;
RX PubMed=12079290; DOI=10.1006/geno.2002.6794;
RA Mallya M., Campbell R.D., Aguado B.;
RT "Transcriptional analysis of a novel cluster of LY-6 family members in the
RT human and mouse major histocompatibility complex: five genes with many
RT splice forms.";
RL Genomics 80:113-123(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
RA Lopez-Diez R., Rastrojo A., Hernandez-Torres F., Aguado B.;
RT "Alternative splicing and transcription induced chimerism in G6F and Ly6G6D
RT among mammals.";
RL Submitted (DEC-2015) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC STRAIN=C57BL/6J; TISSUE=Tongue;
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Lung;
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 [7]
RP SUBCELLULAR LOCATION, AND GLYCOSYLATION.
RX PubMed=17008713; DOI=10.1110/ps.062242606;
RA Mallya M., Campbell R.D., Aguado B.;
RT "Characterization of the five novel Ly-6 superfamily members encoded in the
RT MHC, and detection of cells expressing their potential ligands.";
RL Protein Sci. 15:2244-2256(2006).
RN [8]
RP FUNCTION, INTERACTION WITH CHRNA4, AND SUBCELLULAR LOCATION.
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).
CC -!- FUNCTION: Believed to act as a modulator of nicotinic acetylcholine
CC receptors (nAChRs) activity. In vitro potentiates alpha-3:beta-4-
CC containing nAChRs maximum response by increasing peak current and
CC slowing down receptor desensitization; the activity is dependent on its
CC cell surface localization. {ECO:0000269|PubMed:26276394}.
CC -!- SUBUNIT: Interacts with CHRNA4. {ECO:0000269|PubMed:26276394}.
CC -!- SUBCELLULAR LOCATION: Cell surface {ECO:0000305|PubMed:26276394}. Cell
CC membrane {ECO:0000269|PubMed:17008713, ECO:0000305|PubMed:26276394}.
CC Cell projection {ECO:0000269|PubMed:17008713}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q8K1T6-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8K1T6-2; Sequence=VSP_059015;
CC -!- PTM: O-glycosylated. Contains sialic acid residues.
CC {ECO:0000269|PubMed:17008713}.
CC -!- MISCELLANEOUS: LY6G6E is a pseudogene in humans. {ECO:0000305}.
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DR EMBL; AJ315550; CAC85546.1; -; mRNA.
DR EMBL; KU253700; APT43293.1; -; mRNA.
DR EMBL; AK009303; BAB26204.1; -; mRNA.
DR EMBL; AC087117; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH466666; EDL26668.1; -; Genomic_DNA.
DR EMBL; AJ315551; CAC85547.1; -; mRNA.
DR EMBL; BC132420; AAI32421.1; -; mRNA.
DR EMBL; BC138777; AAI38778.1; -; mRNA.
DR CCDS; CCDS28679.1; -. [Q8K1T6-2]
DR RefSeq; NP_081642.1; NM_027366.1. [Q8K1T6-2]
DR RefSeq; XP_006524949.1; XM_006524886.3. [Q8K1T6-1]
DR RefSeq; XP_006524950.1; XM_006524887.3. [Q8K1T6-1]
DR AlphaFoldDB; Q8K1T6; -.
DR IntAct; Q8K1T6; 1.
DR PRIDE; Q8K1T6; -.
DR ProteomicsDB; 292058; -. [Q8K1T6-1]
DR ProteomicsDB; 292059; -. [Q8K1T6-2]
DR Ensembl; ENSMUST00000013910; ENSMUSP00000013910; ENSMUSG00000013766. [Q8K1T6-2]
DR Ensembl; ENSMUST00000172678; ENSMUSP00000134073; ENSMUSG00000013766. [Q8K1T6-2]
DR Ensembl; ENSMUST00000172959; ENSMUSP00000133753; ENSMUSG00000013766. [Q8K1T6-1]
DR GeneID; 70274; -.
DR KEGG; mmu:70274; -.
DR UCSC; uc008cfo.1; mouse. [Q8K1T6-1]
DR UCSC; uc008cfp.1; mouse.
DR CTD; 79136; -.
DR MGI; MGI:1917524; Ly6g6e.
DR VEuPathDB; HostDB:ENSMUSG00000013766; -.
DR GeneTree; ENSGT00390000007175; -.
DR HOGENOM; CLU_136280_0_0_1; -.
DR InParanoid; Q8K1T6; -.
DR OMA; TYWLRSY; -.
DR OrthoDB; 1536888at2759; -.
DR PhylomeDB; Q8K1T6; -.
DR TreeFam; TF338408; -.
DR BioGRID-ORCS; 70274; 2 hits in 71 CRISPR screens.
DR PRO; PR:Q8K1T6; -.
DR Proteomes; UP000000589; Chromosome 17.
DR RNAct; Q8K1T6; protein.
DR Bgee; ENSMUSG00000013766; Expressed in esophagus and 76 other tissues.
DR ExpressionAtlas; Q8K1T6; baseline and differential.
DR GO; GO:0042995; C:cell projection; IEA:UniProtKB-SubCell.
DR GO; GO:0009986; C:cell surface; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; IDA:MGI.
DR GO; GO:0045202; C:synapse; IEA:GOC.
DR GO; GO:0030549; F:acetylcholine receptor activator activity; IDA:MGI.
DR GO; GO:0033130; F:acetylcholine receptor binding; IDA:MGI.
DR GO; GO:0004675; F:transmembrane receptor protein serine/threonine kinase activity; IEA:InterPro.
DR GO; GO:0095500; P:acetylcholine receptor signaling pathway; IDA:MGI.
DR GO; GO:0002029; P:desensitization of G protein-coupled receptor signaling pathway; IDA:MGI.
DR Gene3D; 2.10.60.10; -; 1.
DR InterPro; IPR000472; Activin_recp.
DR InterPro; IPR039700; Ly6g6e.
DR InterPro; IPR045860; Snake_toxin-like_sf.
DR PANTHER; PTHR14569; PTHR14569; 1.
DR Pfam; PF01064; Activin_recp; 1.
DR SUPFAM; SSF57302; SSF57302; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Cell membrane; Cell projection; Disulfide bond;
KW Membrane; Reference proteome; Signal.
FT SIGNAL 1..18
FT /evidence="ECO:0000255"
FT CHAIN 19..166
FT /note="Lymphocyte antigen 6G6e"
FT /evidence="ECO:0000255"
FT /id="PRO_5010146328"
FT DOMAIN 28..151
FT /note="UPAR/Ly6"
FT DISULFID 30..52
FT /evidence="ECO:0000250|UniProtKB:P0DP57"
FT DISULFID 33..39
FT /evidence="ECO:0000250|UniProtKB:P0DP57"
FT DISULFID 110..129
FT /evidence="ECO:0000250|UniProtKB:P0DP57"
FT DISULFID 130..135
FT /evidence="ECO:0000250|UniProtKB:P0DP57"
FT VAR_SEQ 60..91
FT /note="Missing (in isoform 2)"
FT /id="VSP_059015"
SQ SEQUENCE 166 AA; 18197 MW; DF4318A83864D808 CRC64;
MGPSSAFLGV LFLSGTLGLT TSPARGRLRC YTCSFAKPCD PVPRECREDE VCGVSVGTSG
RTLVRWPFSR WLLSFLPMAA AATSAFLFCP TEQKEEEVIE RKGCLPRAQC PLLGHATYWS
RSYSLRHQCC EQDLCNAAAS QPPPNLPLMT LLPLAAMIGW GVHDFL
