LYPD8_MOUSE
ID LYPD8_MOUSE Reviewed; 255 AA.
AC Q9D7S0;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 109.
DE RecName: Full=Ly6/PLAUR domain-containing protein 8 {ECO:0000305};
DE Flags: Precursor;
GN Name=Lypd8 {ECO:0000312|MGI:MGI:1917413};
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 [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Stomach;
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 [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 FUNCTION, SUBCELLULAR LOCATION, GLYCOSYLATION, GPI-ANCHOR, TISSUE
RP SPECIFICITY, DISRUPTION PHENOTYPE, AND MUTAGENESIS OF ASN-22; ASN-30;
RP ASN-53; ASN-72; ASN-76; ASN-105; ASN-115; ASN-128; ASN-154; ASN-169;
RP ASN-179; ASN-200 AND ASN-210.
RX PubMed=27027293; DOI=10.1038/nature17406;
RA Okumura R., Kurakawa T., Nakano T., Kayama H., Kinoshita M., Motooka D.,
RA Gotoh K., Kimura T., Kamiyama N., Kusu T., Ueda Y., Wu H., Iijima H.,
RA Barman S., Osawa H., Matsuno H., Nishimura J., Ohba Y., Nakamura S.,
RA Iida T., Yamamoto M., Umemoto E., Sano K., Takeda K.;
RT "Lypd8 promotes the segregation of flagellated microbiota and colonic
RT epithelia.";
RL Nature 532:117-121(2016).
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:0000269|PubMed:27027293}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Lipid-anchor, GPI-
CC anchor {ECO:0000269|PubMed:27027293}. Secreted
CC {ECO:0000269|PubMed:27027293}. Note=Secreted into the lumen of the
CC colon following cleavage of the GPI-anchor.
CC {ECO:0000269|PubMed:27027293}.
CC -!- TISSUE SPECIFICITY: Specifically present in enterocytes located at the
CC uppermost epithelial layer of the colon (at protein level). Exclusively
CC expressed in the large intestine: specifically expressed on the apical
CC surface of epithelial cells located at the uppermost layer of the
CC colonic gland. {ECO:0000269|PubMed:27027293}.
CC -!- PTM: Highly N-glycosylated. Not O-glycosylated.
CC {ECO:0000269|PubMed:27027293}.
CC -!- PTM: GPI-anchored. The GPI-anchor is cleaved, leading to secretion into
CC the colonic lumen. {ECO:0000269|PubMed:27027293}.
CC -!- DISRUPTION PHENOTYPE: Mice are highly sensitive to intestinal
CC inflammation induced by dextran sulfate sodium (DSS), due to the
CC presence of bacteria in the inner mucus layer. Mice are healthy when
CC raised in a specific-pathogen-free environment, in which bacterial
CC contamination was strictly controlled. {ECO:0000269|PubMed:27027293}.
CC -!- SIMILARITY: Belongs to the CNF-like-inhibitor family. {ECO:0000305}.
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DR EMBL; AK008940; BAB25981.1; -; mRNA.
DR EMBL; AL663107; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR CCDS; CCDS36163.1; -.
DR RefSeq; NP_001077353.1; NM_001083884.1.
DR RefSeq; NP_001317126.1; NM_001330197.1.
DR RefSeq; NP_081615.2; NM_027339.2.
DR AlphaFoldDB; Q9D7S0; -.
DR STRING; 10090.ENSMUSP00000104454; -.
DR GlyGen; Q9D7S0; 13 sites.
DR PhosphoSitePlus; Q9D7S0; -.
DR PaxDb; Q9D7S0; -.
DR PRIDE; Q9D7S0; -.
DR ProteomicsDB; 287279; -.
DR Ensembl; ENSMUST00000013787; ENSMUSP00000013787; ENSMUSG00000013643.
DR Ensembl; ENSMUST00000108826; ENSMUSP00000104454; ENSMUSG00000013643.
DR GeneID; 70163; -.
DR KEGG; mmu:70163; -.
DR UCSC; uc007jbj.1; mouse.
DR CTD; 646627; -.
DR MGI; MGI:1917413; Lypd8.
DR VEuPathDB; HostDB:ENSMUSG00000013643; -.
DR eggNOG; ENOG502TBDM; Eukaryota.
DR GeneTree; ENSGT00570000079564; -.
DR HOGENOM; CLU_107635_0_0_1; -.
DR InParanoid; Q9D7S0; -.
DR OMA; FRFVSRC; -.
DR OrthoDB; 1288934at2759; -.
DR PhylomeDB; Q9D7S0; -.
DR TreeFam; TF339495; -.
DR Reactome; R-MMU-163125; Post-translational modification: synthesis of GPI-anchored proteins.
DR BioGRID-ORCS; 70163; 2 hits in 71 CRISPR screens.
DR PRO; PR:Q9D7S0; -.
DR Proteomes; UP000000589; Chromosome 11.
DR RNAct; Q9D7S0; protein.
DR Bgee; ENSMUSG00000013643; Expressed in left colon and 50 other tissues.
DR Genevisible; Q9D7S0; MM.
DR GO; GO:0031225; C:anchored component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005615; C:extracellular space; IDA:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0050829; P:defense response to Gram-negative bacterium; IMP:UniProtKB.
DR InterPro; IPR016054; LY6_UPA_recep-like.
DR InterPro; IPR045860; Snake_toxin-like_sf.
DR Pfam; PF00021; UPAR_LY6; 2.
DR SUPFAM; SSF57302; SSF57302; 1.
PE 1: Evidence at protein 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..233
FT /note="Ly6/PLAUR domain-containing protein 8"
FT /id="PRO_0000317741"
FT PROPEP 234..255
FT /note="Removed in mature form"
FT /evidence="ECO:0000255"
FT /id="PRO_0000317742"
FT DOMAIN 121..170
FT /note="UPAR/Ly6"
FT LIPID 233
FT /note="GPI-anchor amidated serine"
FT /evidence="ECO:0000255"
FT CARBOHYD 22
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 30
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 53
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 72
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 76
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 105
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 115
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 128
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 154
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 169
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 179
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 200
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 210
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT MUTAGEN 22
FT /note="N->D: In mutant N-D: Abolished N-glycosylation; when
FT associated with D-30; D-53; D-72; D-76; D-105; D-115; D-
FT 128; D-154; D-169; D-179; D-200 and D-210."
FT /evidence="ECO:0000269|PubMed:27027293"
FT MUTAGEN 30
FT /note="N->D: In mutant N-D: Abolished N-glycosylation; when
FT associated with D-22; D-53; D-72; D-76; D-105; D-115; D-
FT 128; D-154; D-169; D-179; D-200 and D-210."
FT /evidence="ECO:0000269|PubMed:27027293"
FT MUTAGEN 53
FT /note="N->D: In mutant N-D: Abolished N-glycosylation; when
FT associated with D-22; D-30; D-72; D-76; D-105; D-115; D-
FT 128; D-154; D-169; D-179; D-200 and D-210."
FT /evidence="ECO:0000269|PubMed:27027293"
FT MUTAGEN 72
FT /note="N->D: In mutant N-D: Abolished N-glycosylation; when
FT associated with D-22; D-30; D-53; D-76; D-105; D-115; D-
FT 128; D-154; D-169; D-179; D-200 and D-210."
FT /evidence="ECO:0000269|PubMed:27027293"
FT MUTAGEN 76
FT /note="N->D: In mutant N-D: Abolished N-glycosylation; when
FT associated with D-22; D-30; D-53; D-72; D-105; D-115; D-
FT 128; D-154; D-169; D-179; D-200 and D-210."
FT /evidence="ECO:0000269|PubMed:27027293"
FT MUTAGEN 105
FT /note="N->D: In mutant N-D: Abolished N-glycosylation; when
FT associated with D-22; D-30; D-53; D-72; D-76; D-115; D-128;
FT D-154; D-169; D-179; D-200 and D-210."
FT /evidence="ECO:0000269|PubMed:27027293"
FT MUTAGEN 115
FT /note="N->D: In mutant N-D: Abolished N-glycosylation; when
FT associated with D-22; D-30; D-53; D-72; D-76; D-105; D-128;
FT D-154; D-169; D-179; D-200 and D-210."
FT /evidence="ECO:0000269|PubMed:27027293"
FT MUTAGEN 128
FT /note="N->D: In mutant N-D: Abolished N-glycosylation; when
FT associated with D-22; D-30; D-53; D-72; D-76; D-105; D-115;
FT D-154; D-169; D-179; D-200 and D-210."
FT /evidence="ECO:0000269|PubMed:27027293"
FT MUTAGEN 154
FT /note="N->D: In mutant N-D: Abolished N-glycosylation; when
FT associated with D-22; D-30; D-53; D-72; D-76; D-105; D-115;
FT D-128; D-169; D-179; D-200 and D-210."
FT /evidence="ECO:0000269|PubMed:27027293"
FT MUTAGEN 169
FT /note="N->D: In mutant N-D: Abolished N-glycosylation; when
FT associated with D-22; D-30; D-53; D-72; D-76; D-105; D-115;
FT D-128; D-154; D-179; D-200 and D-210."
FT /evidence="ECO:0000269|PubMed:27027293"
FT MUTAGEN 179
FT /note="N->D: In mutant N-D: Abolished N-glycosylation; when
FT associated with D-22; D-30; D-53; D-72; D-76; D-105; D-115;
FT D-128; D-154; D-169; D-200 and D-210."
FT /evidence="ECO:0000269|PubMed:27027293"
FT MUTAGEN 200
FT /note="N->D: In mutant N-D: Abolished N-glycosylation; when
FT associated with D-22; D-30; D-53; D-72; D-76; D-105; D-115;
FT D-128; D-154; D-169; D-179 and D-210."
FT /evidence="ECO:0000269|PubMed:27027293"
FT MUTAGEN 210
FT /note="N->D: In mutant N-D: Abolished N-glycosylation; when
FT associated with D-22; D-30; D-53; D-72; D-76; D-105; D-115;
FT D-128; D-154; D-169; D-179 and D-200."
FT /evidence="ECO:0000269|PubMed:27027293"
SQ SEQUENCE 255 AA; 27524 MW; 6D699A3BF5DAE5DD CRC64;
MRGVFIAGVI AAFAITVVDS LNCTQCYTYN STCDGQATEC NEQSFSCVES SINSTLGGFL
HVYQNKFCSA SNCTENSTEV AFTVHLFDDQ RYHFASQCCQ GESCNATHSE SGTQNVTDMQ
CMSCYGHNKT LCEEKPQKCY EGEQCVFIIA EMVNGSGRVE LKGCSDISNS TCQFLSPGNT
TVGEFVFKSV ECTQPTEYTN STTTIPPITN TSLTSVTRPG IKTSPASVTP QASMGTKASF
TSSIFGSLLL LKLLF
