LYVE1_BOVIN
ID LYVE1_BOVIN Reviewed; 322 AA.
AC Q6UC88;
DT 03-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 106.
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 Flags: Precursor;
GN Name=LYVE1; Synonyms=CRSBP1, XLKD1;
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 [MRNA], FUNCTION, INTERACTION WITH PDGFB AND IGFBP3,
RP GLYCOSYLATION, AND SUBUNIT.
RX PubMed=12912978; DOI=10.1074/jbc.m306411200;
RA Huang S.S., Tang F.-M., Huang Y.-H., Liu I.-H., Hsu S.-C., Chen S.-T.,
RA Huang J.S.;
RT "Cloning, expression, characterization and role in autocrine cell growth of
RT cell surface retention sequence binding protein-1.";
RL J. Biol. Chem. 278:43855-43869(2003).
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:12912978). Binds to pericelluar hyaluronan
CC matrices deposited on the surface of leukocytes and facilitates cell
CC adhesion and migration through lymphatic endothelium (By similarity).
CC {ECO:0000250|UniProtKB:Q9Y5Y7, ECO:0000269|PubMed:12912978}.
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 -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass membrane
CC protein {ECO:0000305}. Note=Localized to the plasma membrane and in
CC vesicles near extranuclear membranes which may represent trans-Golgi
CC network (TGN) and endosomes/prelysosomeal compartments. Undergoes
CC ligand-dependent internalization and recycling at the cell surface (By
CC similarity). {ECO:0000250}.
CC -!- PTM: N-glycosylated. {ECO:0000269|PubMed:12912978}.
CC -!- PTM: O-glycosylated. {ECO:0000269|PubMed:12912978}.
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; AY372937; AAQ85130.1; -; mRNA.
DR AlphaFoldDB; Q6UC88; -.
DR SMR; Q6UC88; -.
DR STRING; 9913.ENSBTAP00000001061; -.
DR PaxDb; Q6UC88; -.
DR PRIDE; Q6UC88; -.
DR Ensembl; ENSBTAT00000001061; ENSBTAP00000001061; ENSBTAG00000000802.
DR VEuPathDB; HostDB:ENSBTAG00000000802; -.
DR VGNC; VGNC:31116; LYVE1.
DR eggNOG; ENOG502RY70; Eukaryota.
DR GeneTree; ENSGT00530000063822; -.
DR HOGENOM; CLU_074364_1_0_1; -.
DR InParanoid; Q6UC88; -.
DR OMA; ILPNPKC; -.
DR TreeFam; TF334173; -.
DR Reactome; R-BTA-2160916; Hyaluronan uptake and degradation.
DR Proteomes; UP000009136; Chromosome 15.
DR Bgee; ENSBTAG00000000802; Expressed in lung and 98 other tissues.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
DR GO; GO:0005540; F:hyaluronic acid binding; ISS:UniProtKB.
DR GO; GO:0004888; F:transmembrane signaling receptor activity; IBA:GO_Central.
DR GO; GO:0007155; P:cell adhesion; IEA:InterPro.
DR GO; GO:0006027; P:glycosaminoglycan catabolic process; IEA:Ensembl.
DR GO; GO:0002693; P:positive regulation of cellular extravasation; IEA:Ensembl.
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 SMART; SM00445; LINK; 1.
DR SUPFAM; SSF56436; SSF56436; 1.
DR PROSITE; PS01241; LINK_1; 1.
DR PROSITE; PS50963; LINK_2; 1.
PE 1: Evidence at protein level;
KW Disulfide bond; Glycoprotein; Membrane; Receptor; Reference proteome;
KW Signal; Transmembrane; Transmembrane helix; Transport.
FT SIGNAL 1..16
FT /evidence="ECO:0000255"
FT CHAIN 17..322
FT /note="Lymphatic vessel endothelial hyaluronic acid
FT receptor 1"
FT /id="PRO_0000252132"
FT TOPO_DOM 17..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..306
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:0000255"
FT DISULFID 61..128
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00323"
FT DISULFID 85..106
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00323"
SQ SEQUENCE 322 AA; 35561 MW; 4901DA1BF92648AE CRC64;
MAKFFSLGLL LASIWTTRLL VQGSLRSEEI SILGPCRIMG VTLVTKKTQP LLNFTEAQEA
CRLVGLTLAS QDQVEEARKF GFETCSYGWV KNQFVVIPRI ISNPKCGKSG VGVVIWRSSL
SSRHRSYCHN SSDIWINSCL PEIITTDDPL FNTETATYTT KLMVSDSTHS ELSTDGPDYV
TTTVAPPLAS TSTPRKRKLI CITEAFMDTS AVATERESDI QNRPAFKNEA VGFGGVPTAL
LVLALLFFAA AAGLAVCYVK RYVKAFPFTN KNQQKEMIET KVVKEEKADD SNPNEESKKM
NKTPEEPKSP PKTTVRCLEA EV
