LYVE1_HUMAN
ID LYVE1_HUMAN Reviewed; 322 AA.
AC Q9Y5Y7; Q8TC18; Q9UNF4;
DT 03-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 03-OCT-2006, sequence version 2.
DT 03-AUG-2022, entry version 153.
DE RecName: Full=Lymphatic vessel endothelial hyaluronic acid receptor 1;
DE Short=LYVE-1;
DE AltName: Full=Cell surface retention sequence-binding protein 1;
DE Short=CRSBP-1;
DE AltName: Full=Extracellular link domain-containing protein 1;
DE AltName: Full=Hyaluronic acid receptor;
DE Flags: Precursor;
GN Name=LYVE1; Synonyms=CRSBP1, HAR, XLKD1; ORFNames=UNQ230/PRO263;
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 [MRNA], FUNCTION, SUBCELLULAR LOCATION, AND TISSUE
RP SPECIFICITY.
RX PubMed=10037799; DOI=10.1083/jcb.144.4.789;
RA Banerji S., Ni J., Wang S.-X., Clasper S., Su J., Tammi R., Jones M.,
RA Jackson D.G.;
RT "LYVE-1, a new homologue of the CD44 glycoprotein is a lymph-specific
RT receptor for hyaluronan.";
RL J. Cell Biol. 144:789-801(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Winkelmann J.C., Basu S., Ozdemir E., Blough R.I.;
RT "HAR: a novel homolog of CD44 and putative hyaluronic acid receptor encoded
RT by a gene on human chromosome 11p15.";
RL Submitted (OCT-1999) to the EMBL/GenBank/DDBJ databases.
RN [3]
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT ARG-116.
RC TISSUE=Liver;
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).
RN [5]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-53.
RC TISSUE=Plasma;
RX PubMed=16335952; DOI=10.1021/pr0502065;
RA Liu T., Qian W.-J., Gritsenko M.A., Camp D.G. II, Monroe M.E., Moore R.J.,
RA Smith R.D.;
RT "Human plasma N-glycoproteome analysis by immunoaffinity subtraction,
RT hydrazide chemistry, and mass spectrometry.";
RL J. Proteome Res. 4:2070-2080(2005).
RN [6]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-53.
RC TISSUE=Liver;
RX PubMed=19159218; DOI=10.1021/pr8008012;
RA Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.;
RT "Glycoproteomics analysis of human liver tissue by combination of multiple
RT enzyme digestion and hydrazide chemistry.";
RL J. Proteome Res. 8:651-661(2009).
RN [7]
RP FUNCTION, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=26823460; DOI=10.1074/jbc.m115.708305;
RA Lawrance W., Banerji S., Day A.J., Bhattacharjee S., Jackson D.G.;
RT "Binding of Hyaluronan to the Native Lymphatic Vessel Endothelial Receptor
RT LYVE-1 Is Critically Dependent on Receptor Clustering and Hyaluronan
RT Organization.";
RL J. Biol. Chem. 291:8014-8030(2016).
CC -!- FUNCTION: Ligand-specific transporter trafficking between intracellular
CC organelles (TGN) and the plasma membrane. Plays a role in autocrine
CC regulation of cell growth mediated by growth regulators containing cell
CC surface retention sequence binding (CRS). May act as a hyaluronan (HA)
CC transporter, either mediating its uptake for catabolism within
CC lymphatic endothelial cells themselves, or its transport into the lumen
CC of afferent lymphatic vessels for subsequent re-uptake and degradation
CC in lymph nodes (PubMed:10037799). Binds to pericelluar hyaluronan
CC matrices deposited on the surface of leukocytes and facilitates cell
CC adhesion and migration through lymphatic endothelium (PubMed:26823460).
CC {ECO:0000269|PubMed:10037799, ECO:0000269|PubMed:26823460}.
CC -!- SUBUNIT: Homodimer; disulfide-linked. Interacts with PDGFB and IGFBP3.
CC Forms a transient ternary complex with PDGFB and PDGFRB in TGN (By
CC similarity). {ECO:0000250}.
CC -!- INTERACTION:
CC Q9Y5Y7; Q9NVV5-2: AIG1; NbExp=3; IntAct=EBI-10329546, EBI-11957045;
CC Q9Y5Y7; Q96PS8: AQP10; NbExp=3; IntAct=EBI-10329546, EBI-12820279;
CC Q9Y5Y7; P51798: CLCN7; NbExp=3; IntAct=EBI-10329546, EBI-4402346;
CC Q9Y5Y7; A8MQ03: CYSRT1; NbExp=3; IntAct=EBI-10329546, EBI-3867333;
CC Q9Y5Y7; P54852: EMP3; NbExp=3; IntAct=EBI-10329546, EBI-3907816;
CC Q9Y5Y7; O76011: KRT34; NbExp=3; IntAct=EBI-10329546, EBI-1047093;
CC Q9Y5Y7; P60410: KRTAP10-8; NbExp=3; IntAct=EBI-10329546, EBI-10171774;
CC Q9Y5Y7; P60328: KRTAP12-3; NbExp=3; IntAct=EBI-10329546, EBI-11953334;
CC Q9Y5Y7; Q3LI66: KRTAP6-2; NbExp=3; IntAct=EBI-10329546, EBI-11962084;
CC Q9Y5Y7; Q9BYQ4: KRTAP9-2; NbExp=3; IntAct=EBI-10329546, EBI-1044640;
CC Q9Y5Y7; Q9NZG7: NINJ2; NbExp=3; IntAct=EBI-10329546, EBI-10317425;
CC Q9Y5Y7; P0DPK4: NOTCH2NLC; NbExp=3; IntAct=EBI-10329546, EBI-22310682;
CC Q9Y5Y7; Q8IZ57: NRSN1; NbExp=3; IntAct=EBI-10329546, EBI-10264528;
CC Q9Y5Y7; Q07326: PIGF; NbExp=3; IntAct=EBI-10329546, EBI-17180304;
CC Q9Y5Y7; Q8N6R1: SERP2; NbExp=3; IntAct=EBI-10329546, EBI-749270;
CC Q9Y5Y7; Q9BRI3: SLC30A2; NbExp=3; IntAct=EBI-10329546, EBI-8644112;
CC Q9Y5Y7; Q9NVC3: SLC38A7; NbExp=3; IntAct=EBI-10329546, EBI-10314552;
CC Q9Y5Y7; Q96JW4: SLC41A2; NbExp=3; IntAct=EBI-10329546, EBI-10290130;
CC Q9Y5Y7; Q9UPZ6: THSD7A; NbExp=3; IntAct=EBI-10329546, EBI-310962;
CC Q9Y5Y7; C9JKN6: THSD7B; NbExp=3; IntAct=EBI-10329546, EBI-17192156;
CC Q9Y5Y7; Q9Y385: UBE2J1; NbExp=3; IntAct=EBI-10329546, EBI-988826;
CC Q9Y5Y7; Q96EC8: YIPF6; NbExp=3; IntAct=EBI-10329546, EBI-751210;
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:10037799,
CC ECO:0000269|PubMed:26823460}; Single-pass type I membrane protein
CC {ECO:0000269|PubMed:10037799}. Note=Localized to the plasma membrane
CC and in vesicles near extranuclear membranes which may represent trans-
CC Golgi network (TGN) and endosomes/prelysosomeal compartments. Undergoes
CC ligand-dependent internalization and recycling at the cell surface.
CC Localizes at cell-cell junctions.
CC -!- TISSUE SPECIFICITY: Mainly expressed in endothelial cells lining
CC lymphatic vessels. {ECO:0000269|PubMed:10037799,
CC ECO:0000269|PubMed:26823460}.
CC -!- PTM: O-glycosylated. {ECO:0000250}.
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DR EMBL; AF118108; AAD42764.1; -; mRNA.
DR EMBL; AF127670; AAD49220.2; -; mRNA.
DR EMBL; AY358925; AAQ89284.1; -; mRNA.
DR EMBL; BC026231; AAH26231.1; -; mRNA.
DR CCDS; CCDS7804.1; -.
DR RefSeq; NP_006682.2; NM_006691.3.
DR AlphaFoldDB; Q9Y5Y7; -.
DR SMR; Q9Y5Y7; -.
DR BioGRID; 116100; 26.
DR IntAct; Q9Y5Y7; 22.
DR STRING; 9606.ENSP00000256178; -.
DR DrugBank; DB08818; Hyaluronic acid.
DR TCDB; 9.B.87.1.26; the selenoprotein p receptor (selp-receptor) family.
DR GlyConnect; 734; 12 N-Linked glycans (2 sites).
DR GlyGen; Q9Y5Y7; 4 sites, 13 N-linked glycans (2 sites), 1 O-linked glycan (1 site).
DR iPTMnet; Q9Y5Y7; -.
DR PhosphoSitePlus; Q9Y5Y7; -.
DR SwissPalm; Q9Y5Y7; -.
DR BioMuta; LYVE1; -.
DR DMDM; 115502898; -.
DR CPTAC; CPTAC-679; -.
DR jPOST; Q9Y5Y7; -.
DR MassIVE; Q9Y5Y7; -.
DR PaxDb; Q9Y5Y7; -.
DR PeptideAtlas; Q9Y5Y7; -.
DR PRIDE; Q9Y5Y7; -.
DR ProteomicsDB; 86544; -.
DR Antibodypedia; 24364; 867 antibodies from 38 providers.
DR DNASU; 10894; -.
DR Ensembl; ENST00000256178.8; ENSP00000256178.3; ENSG00000133800.9.
DR GeneID; 10894; -.
DR KEGG; hsa:10894; -.
DR MANE-Select; ENST00000256178.8; ENSP00000256178.3; NM_006691.4; NP_006682.2.
DR UCSC; uc001miv.3; human.
DR CTD; 10894; -.
DR DisGeNET; 10894; -.
DR GeneCards; LYVE1; -.
DR HGNC; HGNC:14687; LYVE1.
DR HPA; ENSG00000133800; Tissue enhanced (adipose tissue, placenta).
DR MIM; 605702; gene.
DR neXtProt; NX_Q9Y5Y7; -.
DR OpenTargets; ENSG00000133800; -.
DR PharmGKB; PA162394799; -.
DR VEuPathDB; HostDB:ENSG00000133800; -.
DR eggNOG; ENOG502RY70; Eukaryota.
DR GeneTree; ENSGT00530000063822; -.
DR HOGENOM; CLU_074364_1_0_1; -.
DR InParanoid; Q9Y5Y7; -.
DR OMA; ILPNPKC; -.
DR OrthoDB; 1524801at2759; -.
DR PhylomeDB; Q9Y5Y7; -.
DR TreeFam; TF334173; -.
DR PathwayCommons; Q9Y5Y7; -.
DR Reactome; R-HSA-2160916; Hyaluronan uptake and degradation.
DR SignaLink; Q9Y5Y7; -.
DR BioGRID-ORCS; 10894; 9 hits in 1066 CRISPR screens.
DR ChiTaRS; LYVE1; human.
DR GeneWiki; LYVE1; -.
DR GenomeRNAi; 10894; -.
DR Pharos; Q9Y5Y7; Tbio.
DR PRO; PR:Q9Y5Y7; -.
DR Proteomes; UP000005640; Chromosome 11.
DR RNAct; Q9Y5Y7; protein.
DR Bgee; ENSG00000133800; Expressed in pericardium and 168 other tissues.
DR ExpressionAtlas; Q9Y5Y7; baseline and differential.
DR Genevisible; Q9Y5Y7; HS.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0005887; C:integral component of plasma membrane; TAS:ProtInc.
DR GO; GO:0016020; C:membrane; TAS:ProtInc.
DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR GO; GO:0005540; F:hyaluronic acid binding; IDA:UniProtKB.
DR GO; GO:0038023; F:signaling receptor activity; TAS:ProtInc.
DR GO; GO:0004888; F:transmembrane signaling receptor activity; IBA:GO_Central.
DR GO; GO:0009653; P:anatomical structure morphogenesis; TAS:ProtInc.
DR GO; GO:0007160; P:cell-matrix adhesion; TAS:ProtInc.
DR GO; GO:0006027; P:glycosaminoglycan catabolic process; IEA:Ensembl.
DR GO; GO:0002693; P:positive regulation of cellular extravasation; IDA:UniProtKB.
DR GO; GO:0009611; P:response to wounding; TAS:ProtInc.
DR Gene3D; 3.10.100.10; -; 1.
DR InterPro; IPR016186; C-type_lectin-like/link_sf.
DR InterPro; IPR043210; CD44_antigen-like.
DR InterPro; IPR016187; CTDL_fold.
DR InterPro; IPR000538; Link_dom.
DR PANTHER; PTHR10225; PTHR10225; 1.
DR Pfam; PF00193; Xlink; 1.
DR PRINTS; PR01265; LINKMODULE.
DR SMART; SM00445; LINK; 1.
DR SUPFAM; SSF56436; SSF56436; 1.
DR PROSITE; PS50963; LINK_2; 1.
PE 1: Evidence at protein level;
KW Cell membrane; Disulfide bond; Glycoprotein; Membrane; Receptor;
KW Reference proteome; Signal; Transmembrane; Transmembrane helix; Transport.
FT SIGNAL 1..19
FT /evidence="ECO:0000255"
FT CHAIN 20..322
FT /note="Lymphatic vessel endothelial hyaluronic acid
FT receptor 1"
FT /id="PRO_0000252133"
FT TOPO_DOM 20..238
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 239..259
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 260..322
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 40..130
FT /note="Link"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00323"
FT REGION 279..322
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 279..309
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 53
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:16335952,
FT ECO:0000269|PubMed:19159218"
FT CARBOHYD 130
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 61..128
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00323"
FT DISULFID 85..106
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00323"
FT VARIANT 116
FT /note="W -> R (in dbSNP:rs17852369)"
FT /evidence="ECO:0000269|PubMed:15489334"
FT /id="VAR_027763"
FT VARIANT 214
FT /note="T -> I (in dbSNP:rs16907980)"
FT /id="VAR_027764"
FT VARIANT 315
FT /note="V -> M (in dbSNP:rs7948666)"
FT /id="VAR_027765"
FT CONFLICT 75
FT /note="E -> D (in Ref. 1; AAD42764)"
FT /evidence="ECO:0000305"
FT CONFLICT 125
FT /note="A -> G (in Ref. 1; AAD42764)"
FT /evidence="ECO:0000305"
FT CONFLICT 139
FT /note="C -> R (in Ref. 1; AAD42764)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 322 AA; 35213 MW; 8B4D6D623F52D559 CRC64;
MARCFSLVLL LTSIWTTRLL VQGSLRAEEL SIQVSCRIMG ITLVSKKANQ QLNFTEAKEA
CRLLGLSLAG KDQVETALKA SFETCSYGWV GDGFVVISRI SPNPKCGKNG VGVLIWKVPV
SRQFAAYCYN SSDTWTNSCI PEIITTKDPI FNTQTATQTT EFIVSDSTYS VASPYSTIPA
PTTTPPAPAS TSIPRRKKLI CVTEVFMETS TMSTETEPFV ENKAAFKNEA AGFGGVPTAL
LVLALLFFGA AAGLGFCYVK RYVKAFPFTN KNQQKEMIET KVVKEEKAND SNPNEESKKT
DKNPEESKSP SKTTVRCLEA EV
