SLUR2_MACMU
ID SLUR2_MACMU Reviewed; 97 AA.
AC P0DP61; F6VEA7; F6VEB6; F6VED0; P61050;
DT 05-JUL-2017, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2017, sequence version 1.
DT 03-AUG-2022, entry version 24.
DE RecName: Full=Secreted Ly-6/uPAR domain-containing protein 2 {ECO:0000305};
DE Flags: Precursor;
GN Name=SLURP2 {ECO:0000250|UniProtKB:P0DP58};
OS Macaca mulatta (Rhesus macaque).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Cercopithecinae; Macaca.
OX NCBI_TaxID=9544;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Testis;
RA Pandey S., Maudhoo M.D., Guda C., Ferguson B., Fox H., Norgren R.B.;
RT "De novo assembly of the rhesus macaque transcriptome from NextGen mRNA
RT sequences.";
RL Submitted (APR-2012) to the EMBL/GenBank/DDBJ databases.
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}.
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DR EMBL; JV045600; AFI35671.1; -; mRNA.
DR RefSeq; NP_001253551.1; NM_001266622.2.
DR AlphaFoldDB; P0DP61; -.
DR SMR; P0DP61; -.
DR Ensembl; ENSMMUT00000021016; ENSMMUP00000019652; ENSMMUG00000041404.
DR GeneID; 100428508; -.
DR KEGG; mcc:100428508; -.
DR CTD; 432355; -.
DR VEuPathDB; HostDB:ENSMMUG00000041404; -.
DR GeneTree; ENSGT00940000153378; -.
DR OrthoDB; 1544318at2759; -.
DR Proteomes; UP000006718; Chromosome 8.
DR Bgee; ENSMMUG00000041404; Expressed in dorsolateral prefrontal cortex and 22 other tissues.
DR ExpressionAtlas; P0DP61; baseline.
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:0099601; P:regulation of neurotransmitter receptor activity; ISS:UniProtKB.
DR CDD; cd00117; LU; 1.
DR Gene3D; 2.10.60.10; -; 1.
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 3: Inferred from homology;
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 /id="PRO_0000036156"
FT DOMAIN 23..95
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; 10275 MW; 67347EAB23A4F00F CRC64;
MQFHTGLLLA AVLSLQLAAA QALWCHQCTG FGGCSRGSRC PRDSTHCVTT ATRVLSNIEN
LPLVTKMCHT GCPDIPSLGL GPYVSIACCQ TSLCNHD