LYPD8_BOVIN
ID LYPD8_BOVIN Reviewed; 230 AA.
AC A2VE33; F1N1X9;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 08-JUN-2016, sequence version 2.
DT 03-AUG-2022, entry version 75.
DE RecName: Full=Ly6/PLAUR domain-containing protein 8 {ECO:0000305};
DE Flags: Precursor;
GN Name=LYPD8;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Hereford;
RX PubMed=19393038; DOI=10.1186/gb-2009-10-4-r42;
RA Zimin A.V., Delcher A.L., Florea L., Kelley D.R., Schatz M.C., Puiu D.,
RA Hanrahan F., Pertea G., Van Tassell C.P., Sonstegard T.S., Marcais G.,
RA Roberts M., Subramanian P., Yorke J.A., Salzberg S.L.;
RT "A whole-genome assembly of the domestic cow, Bos taurus.";
RL Genome Biol. 10:R42.01-R42.10(2009).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Crossbred X Angus; TISSUE=Ileum;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (FEB-2007) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Secreted protein specifically required to prevent invasion of
CC Gram-negative bacteria in the inner mucus layer of the colon
CC epithelium, a portion of the large intestine which is free of commensal
CC microbiota. Prevents invasion of flagellated microbiota by binding to
CC the flagellum of bacteria, such as P.mirabilis, thereby inhibiting
CC bacterial motility in the intestinal lumen. Segregation of intestinal
CC bacteria and epithelial cells in the colon is required to preserve
CC intestinal homeostasis. {ECO:0000250|UniProtKB:Q9D7S0}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q9D7S0};
CC Lipid-anchor, GPI-anchor {ECO:0000250|UniProtKB:Q9D7S0}. Secreted
CC {ECO:0000250|UniProtKB:Q9D7S0}. Note=Secreted into the lumen of the
CC colon following cleavage of the GPI-anchor.
CC {ECO:0000250|UniProtKB:Q9D7S0}.
CC -!- PTM: Highly N-glycosylated. Not O-glycosylated.
CC {ECO:0000250|UniProtKB:Q9D7S0}.
CC -!- PTM: GPI-anchored. The GPI-anchor is cleaved, leading to secretion into
CC the colonic lumen. {ECO:0000250|UniProtKB:Q9D7S0}.
CC -!- SIMILARITY: Belongs to the CNF-like-inhibitor family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; DAAA02020187; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC133550; AAI33551.1; -; mRNA.
DR RefSeq; NP_001075931.1; NM_001082462.2.
DR AlphaFoldDB; A2VE33; -.
DR STRING; 9913.ENSBTAP00000040995; -.
DR PaxDb; A2VE33; -.
DR GeneID; 617425; -.
DR KEGG; bta:617425; -.
DR CTD; 646627; -.
DR eggNOG; ENOG502TBDM; Eukaryota.
DR InParanoid; A2VE33; -.
DR OrthoDB; 1288934at2759; -.
DR TreeFam; TF339495; -.
DR Proteomes; UP000009136; Unplaced.
DR GO; GO:0031225; C:anchored component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005615; C:extracellular space; ISS:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0050829; P:defense response to Gram-negative bacterium; ISS:UniProtKB.
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.
PE 2: Evidence at transcript level;
KW Cell membrane; Glycoprotein; GPI-anchor; Lipoprotein; Membrane;
KW Reference proteome; Secreted; Signal.
FT SIGNAL 1..20
FT /evidence="ECO:0000255"
FT CHAIN 21..211
FT /note="Ly6/PLAUR domain-containing protein 8"
FT /id="PRO_0000317737"
FT PROPEP 212..230
FT /note="Removed in mature form"
FT /evidence="ECO:0000255"
FT /id="PRO_0000317738"
FT DOMAIN 125..172
FT /note="UPAR/Ly6"
FT LIPID 211
FT /note="GPI-anchor amidated serine"
FT /evidence="ECO:0000255"
FT CARBOHYD 37
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 44
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 74
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 77
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 90
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 106
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 110
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 132
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 137
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 156
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 168
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 181
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 197
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CONFLICT 154
FT /note="F -> L (in Ref. 2; AAI33551)"
SQ SEQUENCE 230 AA; 24724 MW; 95AB70731F649A86 CRC64;
MKSFLFAGIV VVLTVAAVDT LRCIQCNSLK DSCVAKNATE CPSNATTSCT SFSTNFYHGE
HPTWYEDHAC SEENCSNTTV ESFTVSVSEN ETFHFESQCC LGEPCNQTSN TTASPHQVGS
GNMECPACYG NNETSCNETR KCYGERCVSI IAEFTNETKT LVLKGCSNVS ISTCESLGAG
NQTFRGVTFR KFECGDNFST TTPLATTDTG SQASFTPLAL ASILLLSLLL
