LYPD8_HUMAN
ID LYPD8_HUMAN Reviewed; 237 AA.
AC Q6UX82; A0A075B722; K7ELG6;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 08-JUN-2016, sequence version 2.
DT 03-AUG-2022, entry version 89.
DE RecName: Full=Ly6/PLAUR domain-containing protein 8 {ECO:0000305};
DE Flags: Precursor;
GN Name=LYPD8 {ECO:0000312|HGNC:HGNC:44208};
GN ORFNames=UNQ511/PRO1026 {ECO:0000303|PubMed:12975309};
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX PubMed=12975309; DOI=10.1101/gr.1293003;
RA Clark H.F., Gurney A.L., Abaya E., Baker K., Baldwin D.T., Brush J.,
RA Chen J., Chow B., Chui C., Crowley C., Currell B., Deuel B., Dowd P.,
RA Eaton D., Foster J.S., Grimaldi C., Gu Q., Hass P.E., Heldens S., Huang A.,
RA Kim H.S., Klimowski L., Jin Y., Johnson S., Lee J., Lewis L., Liao D.,
RA Mark M.R., Robbie E., Sanchez C., Schoenfeld J., Seshagiri S., Simmons L.,
RA Singh J., Smith V., Stinson J., Vagts A., Vandlen R.L., Watanabe C.,
RA Wieand D., Woods K., Xie M.-H., Yansura D.G., Yi S., Yu G., Yuan J.,
RA Zhang M., Zhang Z., Goddard A.D., Wood W.I., Godowski P.J., Gray A.M.;
RT "The secreted protein discovery initiative (SPDI), a large-scale effort to
RT identify novel human secreted and transmembrane proteins: a bioinformatics
RT assessment.";
RL Genome Res. 13:2265-2270(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16710414; DOI=10.1038/nature04727;
RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A.,
RA Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C.,
RA Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.,
RA Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C.,
RA Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W.,
RA Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J.,
RA Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J.,
RA Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y.,
RA Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J.,
RA Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
RA Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
RA Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
RA Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S.,
RA Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K.,
RA Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R.,
RA Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M.,
RA Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S.,
RA Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J.,
RA Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W.,
RA McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
RA Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
RA Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
RA Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
RA Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S.,
RA Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M.,
RA White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H.,
RA Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E.,
RA Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G.,
RA Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.;
RT "The DNA sequence and biological annotation of human chromosome 1.";
RL Nature 441:315-321(2006).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP TISSUE SPECIFICITY.
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: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 -!- TISSUE SPECIFICITY: Expressed in the large intestine. Preferentially
CC expressed on the epithelial layer exposed to the lumen (at protein
CC level). {ECO:0000269|PubMed:27027293}.
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}.
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DR EMBL; AY358469; AAQ88833.1; -; mRNA.
DR EMBL; AEKP01210869; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CR589904; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; FP476111; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; FP885904; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471257; EAW57531.1; -; Genomic_DNA.
DR CCDS; CCDS73059.1; -.
DR RefSeq; NP_001078943.1; NM_001085474.1.
DR RefSeq; NP_001278212.1; NM_001291283.1.
DR AlphaFoldDB; Q6UX82; -.
DR STRING; 9606.ENSP00000466070; -.
DR GlyGen; Q6UX82; 8 sites.
DR iPTMnet; Q6UX82; -.
DR PhosphoSitePlus; Q6UX82; -.
DR BioMuta; LYPD8; -.
DR DMDM; 74738190; -.
DR jPOST; Q6UX82; -.
DR MassIVE; Q6UX82; -.
DR PaxDb; Q6UX82; -.
DR PeptideAtlas; Q6UX82; -.
DR PRIDE; Q6UX82; -.
DR ProteomicsDB; 67577; -.
DR Antibodypedia; 75553; 19 antibodies from 4 providers.
DR DNASU; 646627; -.
DR Ensembl; ENST00000590317.4; ENSP00000466070.2; ENSG00000259823.6.
DR GeneID; 646627; -.
DR KEGG; hsa:646627; -.
DR MANE-Select; ENST00000590317.4; ENSP00000466070.2; NM_001085474.2; NP_001078943.2.
DR UCSC; uc031vuv.2; human.
DR CTD; 646627; -.
DR DisGeNET; 646627; -.
DR GeneCards; LYPD8; -.
DR HGNC; HGNC:44208; LYPD8.
DR HPA; ENSG00000259823; Tissue enriched (intestine).
DR neXtProt; NX_Q6UX82; -.
DR OpenTargets; ENSG00000259823; -.
DR VEuPathDB; HostDB:ENSG00000259823; -.
DR eggNOG; ENOG502TBDM; Eukaryota.
DR GeneTree; ENSGT00570000079564; -.
DR InParanoid; Q6UX82; -.
DR OMA; FRFVSRC; -.
DR OrthoDB; 1288934at2759; -.
DR PhylomeDB; Q6UX82; -.
DR PathwayCommons; Q6UX82; -.
DR Reactome; R-HSA-163125; Post-translational modification: synthesis of GPI-anchored proteins.
DR BioGRID-ORCS; 646627; 5 hits in 222 CRISPR screens.
DR ChiTaRS; LYPD8; human.
DR GenomeRNAi; 646627; -.
DR Pharos; Q6UX82; Tdark.
DR PRO; PR:Q6UX82; -.
DR Proteomes; UP000005640; Chromosome 1.
DR RNAct; Q6UX82; protein.
DR Bgee; ENSG00000259823; Expressed in rectum and 69 other tissues.
DR GO; GO:0031225; C:anchored component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005576; C:extracellular region; TAS:Reactome.
DR GO; GO:0005615; C:extracellular space; ISS:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; TAS:Reactome.
DR GO; GO:0050829; P:defense response to Gram-negative bacterium; ISS:UniProtKB.
DR InterPro; IPR016054; LY6_UPA_recep-like.
DR Pfam; PF00021; UPAR_LY6; 1.
PE 1: Evidence at protein level;
KW Cell membrane; Glycoprotein; GPI-anchor; Lipoprotein; Membrane;
KW Reference proteome; Secreted; Signal.
FT SIGNAL 1..19
FT /evidence="ECO:0000255"
FT CHAIN 20..215
FT /note="Ly6/PLAUR domain-containing protein 8"
FT /id="PRO_0000317739"
FT PROPEP 216..237
FT /note="Removed in mature form"
FT /evidence="ECO:0000255"
FT /id="PRO_0000317740"
FT DOMAIN 125..176
FT /note="UPAR/Ly6"
FT LIPID 215
FT /note="GPI-anchor amidated asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 45
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 73
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 107
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 118
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 172
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 175
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 185
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CONFLICT 137
FT /note="H -> R (in Ref. 1; AAQ88833 and 3; EAW57531)"
SQ SEQUENCE 237 AA; 25265 MW; AB3EFE9E31274A3A CRC64;
MKGILVAGIT AVLVAAVESL SCVQCNSWEK SCVNSIASEC PSHANTSCIS SSASSSLETP
VRLYQNMFCS AENCSEETHI TAFTVHVSAE EHFHFVSQCC QGKECSNTSD ALDPPLKNVS
SNAECPACYE SNGTSCHGKP WKCYEEEQCV FLVAELKNDI ESKSLVLKGC SNVSNATCQF
LSGENKTLGG VIFRKFECAN VNSLTPTSAP TTSHNVGSKA SLYLLALASL LLRGLLP
