ID   LYPD1_RAT               Reviewed;         141 AA.
AC   Q66H42;
DT   07-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT   11-OCT-2004, sequence version 1.
DT   03-AUG-2022, entry version 100.
DE   RecName: Full=Ly6/PLAUR domain-containing protein 1;
DE   Flags: Precursor;
GN   Name=Lypd1; Synonyms=Lypdc1;
OS   Rattus norvegicus (Rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Rattus.
OX   NCBI_TaxID=10116;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Kidney;
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: 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. May play a role in the intracellular trafficking of
CC       alpha-4:beta-2 and alpha-7-containing nAChRs and may inhibit their
CC       expression at the cell surface. May be involved in the control of
CC       anxiety. {ECO:0000250|UniProtKB:Q8BLC3}.
CC   -!- SUBUNIT: Interacts with CHRNA4 and nAChRs containing alpha-4:beta-2
CC       (CHRNA4:CHRNB2) and alpha-7 (CHRNA7) subunits.
CC       {ECO:0000250|UniProtKB:Q8BLC3}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Lipid-anchor, GPI-
CC       anchor {ECO:0000305}.
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DR   EMBL; BC082032; AAH82032.1; -; mRNA.
DR   RefSeq; NP_001007728.1; NM_001007727.1.
DR   AlphaFoldDB; Q66H42; -.
DR   SMR; Q66H42; -.
DR   STRING; 10116.ENSRNOP00000004741; -.
DR   GlyGen; Q66H42; 1 site.
DR   PaxDb; Q66H42; -.
DR   Ensembl; ENSRNOT00000004741; ENSRNOP00000004741; ENSRNOG00000003453.
DR   GeneID; 360838; -.
DR   KEGG; rno:360838; -.
DR   UCSC; RGD:1549754; rat.
DR   CTD; 116372; -.
DR   RGD; 1549754; Lypd1.
DR   eggNOG; ENOG502S22T; Eukaryota.
DR   GeneTree; ENSGT00390000002215; -.
DR   HOGENOM; CLU_152037_0_0_1; -.
DR   InParanoid; Q66H42; -.
DR   OMA; TFCGLFW; -.
DR   OrthoDB; 1377473at2759; -.
DR   PhylomeDB; Q66H42; -.
DR   TreeFam; TF332325; -.
DR   Reactome; R-RNO-163125; Post-translational modification: synthesis of GPI-anchored proteins.
DR   PRO; PR:Q66H42; -.
DR   Proteomes; UP000002494; Chromosome 13.
DR   Bgee; ENSRNOG00000003453; Expressed in brain and 20 other tissues.
DR   GO; GO:0031225; C:anchored component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0016020; C:membrane; ISO:RGD.
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; ISO:RGD.
DR   GO; GO:0030550; F:acetylcholine receptor inhibitor activity; ISO:RGD.
DR   GO; GO:0095500; P:acetylcholine receptor signaling pathway; ISO:RGD.
DR   GO; GO:0001662; P:behavioral fear response; ISO:RGD.
DR   GO; GO:1903077; P:negative regulation of protein localization to plasma membrane; ISO:RGD.
DR   GO; GO:0072659; P:protein localization to plasma membrane; IEA:Ensembl.
DR   GO; GO:0035094; P:response to nicotine; ISO:RGD.
DR   GO; GO:0007271; P:synaptic transmission, cholinergic; ISO:RGD.
DR   InterPro; IPR045860; Snake_toxin-like_sf.
DR   SUPFAM; SSF57302; SSF57302; 1.
PE   2: Evidence at transcript 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_0000226745"
FT   PROPEP          116..141
FT                   /note="Removed in mature form"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000226746"
FT   DOMAIN          25..108
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"
SQ   SEQUENCE   141 AA;  15330 MW;  BB8CC9993E322DA2 CRC64;
     MWVLGIAATF CGLFWLPGLA LQIQCYQCEE FQLNNDCSSP EFIVNCTVNV QDMCQKEVME
     QSAGIMYRKS CASSAACLIA SAGYQSFCSP GKLNSVCISC CNTPLCNGPR PKKRGSSASA
     IRPELFTTVL FFNLALCLAH C