LYVE1_MOUSE
ID LYVE1_MOUSE Reviewed; 318 AA.
AC Q8BHC0; Q3TUC1; Q99NE4;
DT 03-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 135.
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 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 [MRNA].
RC STRAIN=BALB/cJ; TISSUE=Gastrointestinal tract;
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 [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Brain, and Lung;
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Czech II; TISSUE=Lung, and Mammary gland;
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 [4]
RP FUNCTION, INTERACTION WITH PDGFB, AND SUBCELLULAR LOCATION.
RX PubMed=10187853; DOI=10.1074/jbc.274.15.10582;
RA Boensch C., Huang S.S., Connolly D.T., Huang J.S.;
RT "Cell surface retention sequence binding protein-1 interacts with the v-sis
RT gene product and platelet-derived growth factor beta-type receptor in
RT simian sarcoma virus-transformed cells.";
RL J. Biol. Chem. 274:10582-10589(1999).
RN [5]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-52.
RC STRAIN=C57BL/6J; TISSUE=Plasma;
RX PubMed=17330941; DOI=10.1021/pr0604559;
RA Bernhard O.K., Kapp E.A., Simpson R.J.;
RT "Enhanced analysis of the mouse plasma proteome using cysteine-containing
RT tryptic glycopeptides.";
RL J. Proteome Res. 6:987-995(2007).
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Lung;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
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:10187853). 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:10187853}.
CC -!- SUBUNIT: Homodimer; disulfide-linked. Interacts with PDGFB and IGFBP3.
CC Forms a transient ternary complex with PDGFB and PDGFRB in TGN.
CC {ECO:0000269|PubMed:10187853}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000269|PubMed:10187853}; Single-
CC pass type I membrane protein {ECO:0000269|PubMed:10187853}.
CC Note=Localized to the plasma membrane and in vesicles near extranuclear
CC membranes which may represent trans-Golgi network (TGN) and
CC endosomes/prelysosomeal compartments. Undergoes ligand-dependent
CC internalization and recycling at the cell surface.
CC -!- PTM: O-glycosylated. {ECO:0000250}.
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DR EMBL; AJ311501; CAC33082.1; -; mRNA.
DR EMBL; AK004726; BAC25094.1; -; mRNA.
DR EMBL; AK160857; BAE36050.1; -; mRNA.
DR EMBL; BC038653; AAH38653.1; -; mRNA.
DR EMBL; BC038892; AAH38892.1; -; mRNA.
DR CCDS; CCDS21748.1; -.
DR RefSeq; NP_444477.2; NM_053247.4.
DR AlphaFoldDB; Q8BHC0; -.
DR SMR; Q8BHC0; -.
DR STRING; 10090.ENSMUSP00000033050; -.
DR GlyGen; Q8BHC0; 2 sites.
DR iPTMnet; Q8BHC0; -.
DR PhosphoSitePlus; Q8BHC0; -.
DR MaxQB; Q8BHC0; -.
DR PaxDb; Q8BHC0; -.
DR PeptideAtlas; Q8BHC0; -.
DR PRIDE; Q8BHC0; -.
DR ProteomicsDB; 290205; -.
DR Antibodypedia; 24364; 867 antibodies from 38 providers.
DR DNASU; 114332; -.
DR Ensembl; ENSMUST00000033050; ENSMUSP00000033050; ENSMUSG00000030787.
DR GeneID; 114332; -.
DR KEGG; mmu:114332; -.
DR UCSC; uc009jfr.1; mouse.
DR CTD; 10894; -.
DR MGI; MGI:2136348; Lyve1.
DR VEuPathDB; HostDB:ENSMUSG00000030787; -.
DR eggNOG; ENOG502RY70; Eukaryota.
DR GeneTree; ENSGT00530000063822; -.
DR HOGENOM; CLU_074364_1_0_1; -.
DR InParanoid; Q8BHC0; -.
DR OMA; ILPNPKC; -.
DR OrthoDB; 1524801at2759; -.
DR PhylomeDB; Q8BHC0; -.
DR TreeFam; TF334173; -.
DR Reactome; R-MMU-2160916; Hyaluronan uptake and degradation.
DR BioGRID-ORCS; 114332; 3 hits in 72 CRISPR screens.
DR ChiTaRS; Lyve1; mouse.
DR PRO; PR:Q8BHC0; -.
DR Proteomes; UP000000589; Chromosome 7.
DR RNAct; Q8BHC0; protein.
DR Bgee; ENSMUSG00000030787; Expressed in endothelial cell of lymphatic vessel and 157 other tissues.
DR Genevisible; Q8BHC0; MM.
DR GO; GO:0071944; C:cell periphery; IDA:MGI.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IDA:MGI.
DR GO; GO:0038024; F:cargo receptor activity; IDA:MGI.
DR GO; GO:0005540; F:hyaluronic acid binding; IDA:MGI.
DR GO; GO:0004888; F:transmembrane signaling receptor activity; IDA:MGI.
DR GO; GO:0007155; P:cell adhesion; IEA:InterPro.
DR GO; GO:0006027; P:glycosaminoglycan catabolic process; IDA:MGI.
DR GO; GO:0030214; P:hyaluronan catabolic process; IDA:MGI.
DR GO; GO:0002693; P:positive regulation of cellular extravasation; ISO:MGI.
DR GO; GO:0006898; P:receptor-mediated endocytosis; IDA:MGI.
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..23
FT /evidence="ECO:0000255"
FT CHAIN 24..318
FT /note="Lymphatic vessel endothelial hyaluronic acid
FT receptor 1"
FT /id="PRO_0000252134"
FT TOPO_DOM 24..234
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 235..255
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 256..318
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 39..129
FT /note="Link"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00323"
FT REGION 284..318
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 284..302
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 52
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:17330941"
FT CARBOHYD 129
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 60..127
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00323"
FT DISULFID 84..105
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00323"
FT CONFLICT 9..10
FT /note="LL -> FF (in Ref. 1; CAC33082)"
FT /evidence="ECO:0000305"
FT CONFLICT 60
FT /note="C -> G (in Ref. 2; BAE36050)"
FT /evidence="ECO:0000305"
FT CONFLICT 124
FT /note="K -> E (in Ref. 2; BAE36050)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 318 AA; 34574 MW; 34AA31AEF5430B08 CRC64;
MLQHTSLVLL LASIWTTRHP VQGADLVQDL SISTCRIMGV ALVGRNKNPQ MNFTEANEAC
KMLGLTLASR DQVESAQKSG FETCSYGWVG EQFSVIPRIF SNPRCGKNGK GVLIWNAPSS
QKFKAYCHNS SDTWVNSCIP EIVTTFYPVL DTQTPATEFS VSSSAYLASS PDSTTPVSAT
TRAPPLTSMA RKTKKICITE VYTEPITMAT ETEAFVASGA AFKNEAAGFG GVPTALLVLA
LLFFGAAAVL AVCYVKRYVK AFPFTTKNQQ KEMIETKVVK EEKADDVNAN EESKKTIKNP
EEAKSPPKTT VRCLEAEV
