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Lymphatic vessel endothelial hyaluronic acid receptor 1 (LYVE-1) (Cell surface retention sequence-binding protein 1) (CRSBP-1) (Extracellular link domain-containing protein 1)

 LYVE1_MOUSE             Reviewed;         318 AA.
Q8BHC0; Q3TUC1; Q99NE4;
03-OCT-2006, integrated into UniProtKB/Swiss-Prot.
01-MAR-2003, sequence version 1.
10-MAY-2017, entry version 116.
RecName: Full=Lymphatic vessel endothelial hyaluronic acid receptor 1;
Short=LYVE-1;
AltName: Full=Cell surface retention sequence-binding protein 1;
Short=CRSBP-1;
AltName: Full=Extracellular link domain-containing protein 1;
Flags: Precursor;
Name=Lyve1; Synonyms=Crsbp1, Xlkd1;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
STRAIN=BALB/cJ; TISSUE=Gastrointestinal tract;
PubMed=10037799; DOI=10.1083/jcb.144.4.789;
Banerji S., Ni J., Wang S.-X., Clasper S., Su J., Tammi R., Jones M.,
Jackson D.G.;
"LYVE-1, a new homologue of the CD44 glycoprotein is a lymph-specific
receptor for hyaluronan.";
J. Cell Biol. 144:789-801(1999).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=C57BL/6J; TISSUE=Brain, and Lung;
PubMed=16141072; DOI=10.1126/science.1112014;
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
Hayashizaki Y.;
"The transcriptional landscape of the mammalian genome.";
Science 309:1559-1563(2005).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=Czech II; TISSUE=Lung, and Mammary gland;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[4]
FUNCTION, INTERACTION WITH PDGFB, AND SUBCELLULAR LOCATION.
PubMed=10187853; DOI=10.1074/jbc.274.15.10582;
Boensch C., Huang S.S., Connolly D.T., Huang J.S.;
"Cell surface retention sequence binding protein-1 interacts with the
v-sis gene product and platelet-derived growth factor beta-type
receptor in simian sarcoma virus-transformed cells.";
J. Biol. Chem. 274:10582-10589(1999).
[5]
GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-52.
STRAIN=C57BL/6J; TISSUE=Plasma;
PubMed=17330941; DOI=10.1021/pr0604559;
Bernhard O.K., Kapp E.A., Simpson R.J.;
"Enhanced analysis of the mouse plasma proteome using cysteine-
containing tryptic glycopeptides.";
J. Proteome Res. 6:987-995(2007).
[6]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Lung;
PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
"A tissue-specific atlas of mouse protein phosphorylation and
expression.";
Cell 143:1174-1189(2010).
-!- FUNCTION: Ligand-specific transporter trafficking between
intracellular organelles (TGN) and the plasma membrane. Plays a
role in autocrine regulation of cell growth mediated by growth
regulators containing cell surface retention sequence binding
(CRS). May act as a hyaluronan (HA) transporter, either mediating
its uptake for catabolism within lymphatic endothelial cells
themselves, or its transport into the lumen of afferent lymphatic
vessels for subsequent re-uptake and degradation in lymph nodes.
{ECO:0000269|PubMed:10187853}.
-!- SUBUNIT: Homodimer; disulfide-linked. Interacts with PDGFB and
IGFBP3. Forms a transient ternary complex with PDGFB and PDGFRB in
TGN. {ECO:0000269|PubMed:10187853}.
-!- SUBCELLULAR LOCATION: Membrane {ECO:0000269|PubMed:10187853};
Single-pass type I membrane protein {ECO:0000269|PubMed:10187853}.
Note=Localized to the plasma membrane and in vesicles near
extranuclear membranes which may represent trans-Golgi network
(TGN) and endosomes/prelysosomeal compartments. Undergoes ligand-
dependent internalization and recycling at the cell surface.
-!- PTM: O-glycosylated. {ECO:0000250}.
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EMBL; AJ311501; CAC33082.1; -; mRNA.
EMBL; AK004726; BAC25094.1; -; mRNA.
EMBL; AK160857; BAE36050.1; -; mRNA.
EMBL; BC038653; AAH38653.1; -; mRNA.
EMBL; BC038892; AAH38892.1; -; mRNA.
CCDS; CCDS21748.1; -.
RefSeq; NP_444477.2; NM_053247.4.
UniGene; Mm.396078; -.
ProteinModelPortal; Q8BHC0; -.
SMR; Q8BHC0; -.
STRING; 10090.ENSMUSP00000033050; -.
iPTMnet; Q8BHC0; -.
PhosphoSitePlus; Q8BHC0; -.
MaxQB; Q8BHC0; -.
PaxDb; Q8BHC0; -.
PeptideAtlas; Q8BHC0; -.
PRIDE; Q8BHC0; -.
Ensembl; ENSMUST00000033050; ENSMUSP00000033050; ENSMUSG00000030787.
GeneID; 114332; -.
KEGG; mmu:114332; -.
UCSC; uc009jfr.1; mouse.
CTD; 10894; -.
MGI; MGI:2136348; Lyve1.
eggNOG; ENOG410IHIF; Eukaryota.
eggNOG; ENOG41127CQ; LUCA.
GeneTree; ENSGT00530000063822; -.
HOGENOM; HOG000059545; -.
HOVERGEN; HBG103455; -.
InParanoid; Q8BHC0; -.
KO; K19012; -.
OMA; SGFETCS; -.
OrthoDB; EOG091G09EL; -.
PhylomeDB; Q8BHC0; -.
TreeFam; TF334173; -.
Reactome; R-MMU-2160916; Hyaluronan uptake and degradation.
PRO; PR:Q8BHC0; -.
Proteomes; UP000000589; Chromosome 7.
Bgee; ENSMUSG00000030787; -.
Genevisible; Q8BHC0; MM.
GO; GO:0071944; C:cell periphery; IDA:MGI.
GO; GO:0070062; C:extracellular exosome; ISO:MGI.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0005886; C:plasma membrane; IDA:MGI.
GO; GO:0005540; F:hyaluronic acid binding; IDA:MGI.
GO; GO:0004888; F:transmembrane signaling receptor activity; IDA:MGI.
GO; GO:0007155; P:cell adhesion; IEA:InterPro.
GO; GO:0006027; P:glycosaminoglycan catabolic process; IDA:MGI.
GO; GO:0006810; P:transport; IEA:UniProtKB-KW.
Gene3D; 3.10.100.10; -; 1.
InterPro; IPR016186; C-type_lectin-like/link.
InterPro; IPR016187; CTDL_fold.
InterPro; IPR000538; Link_dom.
Pfam; PF00193; Xlink; 1.
SMART; SM00445; LINK; 1.
SUPFAM; SSF56436; SSF56436; 1.
PROSITE; PS01241; LINK_1; 1.
PROSITE; PS50963; LINK_2; 1.
1: Evidence at protein level;
Complete proteome; Disulfide bond; Glycoprotein; Membrane; Receptor;
Reference proteome; Signal; Transmembrane; Transmembrane helix;
Transport.
SIGNAL 1 23 {ECO:0000255}.
CHAIN 24 318 Lymphatic vessel endothelial hyaluronic
acid receptor 1.
/FTId=PRO_0000252134.
TOPO_DOM 24 234 Extracellular. {ECO:0000255}.
TRANSMEM 235 255 Helical. {ECO:0000255}.
TOPO_DOM 256 318 Cytoplasmic. {ECO:0000255}.
DOMAIN 39 129 Link. {ECO:0000255|PROSITE-
ProRule:PRU00323}.
CARBOHYD 52 52 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:17330941}.
CARBOHYD 129 129 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 60 127 {ECO:0000255|PROSITE-ProRule:PRU00323}.
DISULFID 84 105 {ECO:0000255|PROSITE-ProRule:PRU00323}.
CONFLICT 9 10 LL -> FF (in Ref. 1; CAC33082).
{ECO:0000305}.
CONFLICT 60 60 C -> G (in Ref. 2; BAE36050).
{ECO:0000305}.
CONFLICT 124 124 K -> E (in Ref. 2; BAE36050).
{ECO:0000305}.
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


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