SLUR2_MOUSE
ID SLUR2_MOUSE Reviewed; 97 AA.
AC P0DP59; Q08EF7; Q3TRB5; Q9WVC2;
DT 05-JUL-2017, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2017, sequence version 1.
DT 03-AUG-2022, entry version 28.
DE RecName: Full=Secreted Ly-6/uPAR domain-containing protein 2 {ECO:0000305};
DE Short=SLURP-2 {ECO:0000303|PubMed:17286989};
DE Flags: Precursor;
GN Name=Slurp2 {ECO:0000312|MGI:MGI:1916712};
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], AND TISSUE SPECIFICITY.
RC STRAIN=C57BL/6J;
RX PubMed=17286989; DOI=10.1016/j.lfs.2006.12.028;
RA Moriwaki Y., Yoshikawa K., Fukuda H., Fujii Y.X., Misawa H., Kawashima K.;
RT "Immune system expression of SLURP-1 and SLURP-2, two endogenous nicotinic
RT acetylcholine receptor ligands.";
RL Life Sci. 80:2365-2368(2007).
RN [2]
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=FVB/N;
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).
CC -!- FUNCTION: Binds and may modulate the functional properties of nicotinic
CC and muscarinic acetylcholine receptors. May regulate keratinocytes
CC proliferation, differentiation and apoptosis. In vitro moderately
CC inhibits ACh-evoked currents of alpha-3:beta-2-containing nAChRs,
CC strongly these of alpha-4:beta-2-containing nAChRs, modulates alpha-7-
CC containing nAChRs, and inhibits nicotine-induced signaling probably
CC implicating alpha-3:beta-4-containing nAChRs. Proposed to act on alpha-
CC 3:beta-2 and alpha-7 nAChRs in an orthosteric, and on mAChRs, such as
CC CHRM1 and CHRM3, in an allosteric manner.
CC {ECO:0000250|UniProtKB:P0DP57}.
CC -!- SUBUNIT: Interacts with CHRNA3, CHRNA4, CHRNA5, CHRNA7, CHRNB2 and
CC CHRNB4. Interacts with CHRM1 and CHRM3 probably in an allosteric manner
CC (By similarity). {ECO:0000250|UniProtKB:P0DP57}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:P0DP57}.
CC -!- TISSUE SPECIFICITY: Widely expressed, including in dendritic cells,
CC macrophages, B- and T-lymphocytes. {ECO:0000269|PubMed:17286989}.
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DR EMBL; AB272582; BAF48397.1; -; mRNA.
DR EMBL; AC118022; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC115610; AAI15611.1; -; mRNA.
DR EMBL; BC115611; AAI15612.1; -; mRNA.
DR CCDS; CCDS37103.1; -.
DR RefSeq; NP_001075430.1; NM_001081961.1.
DR AlphaFoldDB; P0DP59; -.
DR SMR; P0DP59; -.
DR STRING; 10090.ENSMUSP00000051457; -.
DR PRIDE; P0DP59; -.
DR ProteomicsDB; 261084; -.
DR Ensembl; ENSMUST00000057932; ENSMUSP00000051457; ENSMUSG00000075605.
DR GeneID; 69462; -.
DR KEGG; mmu:69462; -.
DR CTD; 432355; -.
DR MGI; MGI:1916712; Slurp2.
DR VEuPathDB; HostDB:ENSMUSG00000075605; -.
DR eggNOG; ENOG502T3MN; Eukaryota.
DR GeneTree; ENSGT00730000111571; -.
DR OMA; LMCHQCK; -.
DR OrthoDB; 1544318at2759; -.
DR PRO; PR:P0DP59; -.
DR Proteomes; UP000000589; Chromosome 15.
DR RNAct; P0DP59; protein.
DR Bgee; ENSMUSG00000075605; Expressed in lip and 13 other tissues.
DR Genevisible; Q9WVC2; MM.
DR GO; GO:0031225; C:anchored component of membrane; IBA:GO_Central.
DR GO; GO:0005615; C:extracellular space; ISS:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0045202; C:synapse; IEA:GOC.
DR GO; GO:0033130; F:acetylcholine receptor binding; ISS:UniProtKB.
DR GO; GO:0030550; F:acetylcholine receptor inhibitor activity; IBA:GO_Central.
DR GO; GO:0030548; F:acetylcholine receptor regulator activity; ISS:UniProtKB.
DR GO; GO:0095500; P:acetylcholine receptor signaling pathway; ISS:UniProtKB.
DR GO; GO:0043616; P:keratinocyte proliferation; IMP:MGI.
DR GO; GO:0099601; P:regulation of neurotransmitter receptor activity; ISS:UniProtKB.
DR CDD; cd00117; LU; 1.
DR Gene3D; 2.10.60.10; -; 1.
DR InterPro; IPR018363; CD59_antigen_CS.
DR InterPro; IPR016054; LY6_UPA_recep-like.
DR InterPro; IPR045860; Snake_toxin-like_sf.
DR Pfam; PF00021; UPAR_LY6; 1.
DR SUPFAM; SSF57302; SSF57302; 1.
PE 2: Evidence at transcript level;
KW Disulfide bond; Reference proteome; Secreted; Signal.
FT SIGNAL 1..22
FT /evidence="ECO:0000255"
FT CHAIN 23..97
FT /note="Secreted Ly-6/uPAR domain-containing protein 2"
FT /evidence="ECO:0000255"
FT /id="PRO_0000440647"
FT DOMAIN 24..72
FT /note="UPAR/Ly6"
FT DISULFID 25..47
FT /evidence="ECO:0000250|UniProtKB:P0DP57"
FT DISULFID 28..34
FT /evidence="ECO:0000250|UniProtKB:P0DP57"
FT DISULFID 40..68
FT /evidence="ECO:0000250|UniProtKB:P0DP57"
FT DISULFID 72..88
FT /evidence="ECO:0000250|UniProtKB:P0DP57"
FT DISULFID 89..94
FT /evidence="ECO:0000250|UniProtKB:P0DP57"
SQ SEQUENCE 97 AA; 10452 MW; 8F6D8EA15E951E8F CRC64;
MRLPFWFLLA VVLSMELAVT QGLQCHLCKG FGGCSRPSSC PWSSTHCVII ATRSPISFTD
LPLVTKMCYS GCPDVSSLGL GPHVSIACCQ SNLCNRD
