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P-selectin (CD62 antigen-like family member P) (Granule membrane protein 140) (GMP-140) (Leukocyte-endothelial cell adhesion molecule 3) (LECAM3) (Platelet activation dependent granule-external membrane protein) (PADGEM) (CD antigen CD62P)

 LYAM3_RAT               Reviewed;         768 AA.
P98106;
01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
01-FEB-1996, sequence version 1.
31-JAN-2018, entry version 135.
RecName: Full=P-selectin;
AltName: Full=CD62 antigen-like family member P;
AltName: Full=Granule membrane protein 140;
Short=GMP-140;
AltName: Full=Leukocyte-endothelial cell adhesion molecule 3;
Short=LECAM3;
AltName: Full=Platelet activation dependent granule-external membrane protein;
Short=PADGEM;
AltName: CD_antigen=CD62P;
Flags: Precursor;
Name=Selp;
Rattus norvegicus (Rat).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Rattus.
NCBI_TaxID=10116;
[1]
NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, AND INDUCTION BY
BACTERIAL LIPOPOLYSACCHARIDE.
TISSUE=Lung;
PubMed=7520013; DOI=10.1016/0378-1119(94)90015-9;
Auchampach J.A., Oliver M.G., Anderson D.C., Manning A.M.;
"Cloning, sequence comparison and in vivo expression of the gene
encoding rat P-selectin.";
Gene 145:251-255(1994).
-!- FUNCTION: Ca(2+)-dependent receptor for myeloid cells that binds
to carbohydrates on neutrophils and monocytes. Mediates the
interaction of activated endothelial cells or platelets with
leukocytes. The ligand recognized is sialyl-Lewis X. Mediates
rapid rolling of leukocyte rolling over vascular surfaces during
the initial steps in inflammation through interaction with SELPLG.
{ECO:0000250|UniProtKB:P16109}.
-!- SUBUNIT: Interacts with SNX17. Interacts with SELPLG/PSGL1 and
PODXL2 and mediates neutrophil adhesion and leukocyte rolling.
This interaction requires the sialyl-Lewis X epitope of SELPLG and
PODXL2, and specific tyrosine sulfation on SELPLG.
{ECO:0000250|UniProtKB:P16109}.
-!- SUBCELLULAR LOCATION: Cell membrane
{ECO:0000250|UniProtKB:P16109}; Single-pass type I membrane
protein {ECO:0000250|UniProtKB:P16109}.
-!- TISSUE SPECIFICITY: Not detected in the absence of exposure to
lipopolysaccharide (LPS). Detected only after exposure to
lipopolysaccharide (LPS) in the tissues examined: spleen, lung,
brain, liver, heart, kidney, thymus and small intestine.
{ECO:0000269|PubMed:7520013}.
-!- INDUCTION: By exposure to bacterial lipopolysaccharide (LPS).
{ECO:0000269|PubMed:7520013}.
-!- SIMILARITY: Belongs to the selectin/LECAM family. {ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; L23088; AAA60325.1; -; mRNA.
PIR; I53821; I53821.
RefSeq; NP_037246.1; NM_013114.1.
UniGene; Rn.10012; -.
ProteinModelPortal; P98106; -.
SMR; P98106; -.
STRING; 10116.ENSRNOP00000003759; -.
PaxDb; P98106; -.
PRIDE; P98106; -.
GeneID; 25651; -.
KEGG; rno:25651; -.
UCSC; RGD:3656; rat.
CTD; 6403; -.
RGD; 3656; Selp.
eggNOG; ENOG410IS44; Eukaryota.
eggNOG; ENOG410Y5JF; LUCA.
HOGENOM; HOG000236254; -.
HOVERGEN; HBG052375; -.
InParanoid; P98106; -.
KO; K06496; -.
PhylomeDB; P98106; -.
PRO; PR:P98106; -.
Proteomes; UP000002494; Unplaced.
GO; GO:0009897; C:external side of plasma membrane; IDA:RGD.
GO; GO:0005615; C:extracellular space; IDA:RGD.
GO; GO:0005887; C:integral component of plasma membrane; ISS:UniProtKB.
GO; GO:0016020; C:membrane; ISO:RGD.
GO; GO:0031092; C:platelet alpha granule membrane; ISO:RGD.
GO; GO:0005509; F:calcium ion binding; ISS:UniProtKB.
GO; GO:0048306; F:calcium-dependent protein binding; ISO:RGD.
GO; GO:0042806; F:fucose binding; ISO:RGD.
GO; GO:0008201; F:heparin binding; ISO:RGD.
GO; GO:0001530; F:lipopolysaccharide binding; ISO:RGD.
GO; GO:0070492; F:oligosaccharide binding; ISS:UniProtKB.
GO; GO:0033691; F:sialic acid binding; ISO:RGD.
GO; GO:0016339; P:calcium-dependent cell-cell adhesion via plasma membrane cell adhesion molecules; ISS:UniProtKB.
GO; GO:0035584; P:calcium-mediated signaling using intracellular calcium source; ISO:RGD.
GO; GO:0098609; P:cell-cell adhesion; IMP:RGD.
GO; GO:0007157; P:heterophilic cell-cell adhesion via plasma membrane cell adhesion molecules; ISO:RGD.
GO; GO:0006954; P:inflammatory response; ISO:RGD.
GO; GO:0007159; P:leukocyte cell-cell adhesion; ISO:RGD.
GO; GO:0050900; P:leukocyte migration; IMP:RGD.
GO; GO:0050901; P:leukocyte tethering or rolling; ISS:UniProtKB.
GO; GO:0045785; P:positive regulation of cell adhesion; IMP:RGD.
GO; GO:0002687; P:positive regulation of leukocyte migration; ISO:RGD.
GO; GO:0014068; P:positive regulation of phosphatidylinositol 3-kinase signaling; ISO:RGD.
GO; GO:0010572; P:positive regulation of platelet activation; ISO:RGD.
GO; GO:0002691; P:regulation of cellular extravasation; IMP:RGD.
GO; GO:0033623; P:regulation of integrin activation; ISO:RGD.
GO; GO:0032496; P:response to lipopolysaccharide; IEP:RGD.
GO; GO:0014070; P:response to organic cyclic compound; IEP:RGD.
CDD; cd00033; CCP; 8.
CDD; cd03592; CLECT_selectins_like; 1.
Gene3D; 3.10.100.10; -; 1.
InterPro; IPR001304; C-type_lectin-like.
InterPro; IPR016186; C-type_lectin-like/link_sf.
InterPro; IPR018378; C-type_lectin_CS.
InterPro; IPR016187; CTDL_fold.
InterPro; IPR013032; EGF-like_CS.
InterPro; IPR000742; EGF-like_dom.
InterPro; IPR033991; Selectin_CTLD.
InterPro; IPR002396; Selectin_superfamily.
InterPro; IPR035976; Sushi/SCR/CCP_sf.
InterPro; IPR000436; Sushi_SCR_CCP_dom.
Pfam; PF00059; Lectin_C; 1.
Pfam; PF00084; Sushi; 8.
PRINTS; PR00343; SELECTIN.
SMART; SM00032; CCP; 8.
SMART; SM00034; CLECT; 1.
SUPFAM; SSF56436; SSF56436; 1.
SUPFAM; SSF57535; SSF57535; 8.
PROSITE; PS00615; C_TYPE_LECTIN_1; 1.
PROSITE; PS50041; C_TYPE_LECTIN_2; 1.
PROSITE; PS00022; EGF_1; 1.
PROSITE; PS01186; EGF_2; 1.
PROSITE; PS50026; EGF_3; 1.
PROSITE; PS50923; SUSHI; 8.
2: Evidence at transcript level;
Calcium; Cell adhesion; Cell membrane; Complete proteome;
Disulfide bond; EGF-like domain; Glycoprotein; Lectin; Lipoprotein;
Membrane; Metal-binding; Palmitate; Reference proteome; Repeat;
Signal; Sushi; Transmembrane; Transmembrane helix.
SIGNAL 1 41 {ECO:0000255}.
CHAIN 42 768 P-selectin.
/FTId=PRO_0000017500.
TOPO_DOM 42 709 Extracellular. {ECO:0000255}.
TRANSMEM 710 733 Helical. {ECO:0000255}.
TOPO_DOM 734 768 Cytoplasmic. {ECO:0000255}.
DOMAIN 58 158 C-type lectin. {ECO:0000255|PROSITE-
ProRule:PRU00040}.
DOMAIN 159 195 EGF-like. {ECO:0000255|PROSITE-
ProRule:PRU00076}.
DOMAIN 198 259 Sushi 1. {ECO:0000255|PROSITE-
ProRule:PRU00302}.
DOMAIN 260 321 Sushi 2. {ECO:0000255|PROSITE-
ProRule:PRU00302}.
DOMAIN 322 383 Sushi 3. {ECO:0000255|PROSITE-
ProRule:PRU00302}.
DOMAIN 384 445 Sushi 4. {ECO:0000255|PROSITE-
ProRule:PRU00302}.
DOMAIN 446 507 Sushi 5. {ECO:0000255|PROSITE-
ProRule:PRU00302}.
DOMAIN 508 569 Sushi 6. {ECO:0000255|PROSITE-
ProRule:PRU00302}.
DOMAIN 578 639 Sushi 7. {ECO:0000255|PROSITE-
ProRule:PRU00302}.
DOMAIN 640 701 Sushi 8. {ECO:0000255|PROSITE-
ProRule:PRU00302}.
REGION 759 768 Interaction with SNX17. {ECO:0000250}.
MOTIF 756 759 Endocytosis signal. {ECO:0000305}.
METAL 121 121 Calcium. {ECO:0000250|UniProtKB:P16109}.
METAL 123 123 Calcium. {ECO:0000250|UniProtKB:P16109}.
METAL 124 124 Calcium. {ECO:0000250|UniProtKB:P16109}.
METAL 146 146 Calcium. {ECO:0000250|UniProtKB:P16109}.
METAL 147 147 Calcium. {ECO:0000250|UniProtKB:P16109}.
BINDING 123 123 Carbohydrate.
{ECO:0000250|UniProtKB:P16109}.
BINDING 133 133 Carbohydrate.
{ECO:0000250|UniProtKB:P16109}.
BINDING 146 146 Carbohydrate.
{ECO:0000250|UniProtKB:P16109}.
LIPID 745 745 S-palmitoyl cysteine; alternate.
{ECO:0000250|UniProtKB:P16109}.
LIPID 745 745 S-stearoyl cysteine; alternate.
{ECO:0000250|UniProtKB:P16109}.
CARBOHYD 45 45 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 54 54 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 107 107 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 212 212 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 347 347 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 456 456 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 603 603 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 654 654 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 661 661 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 679 679 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 60 158 {ECO:0000250|UniProtKB:P16109}.
DISULFID 131 150 {ECO:0000250|UniProtKB:P16109}.
DISULFID 168 183 {ECO:0000250|UniProtKB:P16109}.
DISULFID 185 194 {ECO:0000250|UniProtKB:P16109}.
DISULFID 200 244 {ECO:0000250}.
DISULFID 230 257 {ECO:0000250}.
DISULFID 262 306 {ECO:0000250}.
DISULFID 292 319 {ECO:0000250}.
DISULFID 324 368 {ECO:0000250}.
DISULFID 354 381 {ECO:0000250}.
DISULFID 386 430 {ECO:0000250}.
DISULFID 416 443 {ECO:0000250}.
DISULFID 448 492 {ECO:0000250}.
DISULFID 478 505 {ECO:0000250}.
DISULFID 510 554 {ECO:0000250}.
DISULFID 540 567 {ECO:0000250}.
DISULFID 580 624 {ECO:0000250}.
DISULFID 610 637 {ECO:0000250}.
DISULFID 642 686 {ECO:0000250}.
DISULFID 672 699 {ECO:0000250}.
SEQUENCE 768 AA; 83517 MW; 26FD7E8A5F3F1316 CRC64;
MAGCPKGSWK PRLRSVVLGA AQLIWLSALI SELVNRKKVA TWTYNYSTKA YSWNNSRAFC
KRHFTDLVAI QNKNEIAHLN DVIPYVNSYY WIGIRKINNK WTWVGTNKTL TAEAENWADN
EPNNKRNNQD CVEIYIKSNS APGKWNDEPC FKRKRALCYT ASCQDMSCNS QGERIETIGS
YTCSCYPGFY GPECEYVQEC GKFDIPQHVL MNCSHPLGDF SFSSQCTFSC PEGYDLNGPS
EMQCLASGIW TNNPPQCKAV QCQSLEAPLH GTMDCTHPLA AFAYDSSCKF ECQPGYRMRG
SDILHCTDSG QWSEPLPTCE AIACEPLESP LHGSMDCFPS TGAFGYNSSC TFRCTEGFVL
MGNDAIHCAD LGQWTAPAPV CEALQCQEFP VPSKAQVSCS DPFGPLKYQS ACSFSCDEGS
LLVGASVIRC LATGHWSEAP PECQAVSCTP LLSPENGTMT CIQPLGHSNY KSTCQFMCDE
GFYLSGPERL DCSPSGHWTG SPPMCEAIKC PEIFAPEQGS LDCSHVHGEF SVGSTCHFSC
NEEFELLGSR NVECTVSGRW SAPPPTCKGV TSLPVPSVRC PALTTPGQGT MSCRHHLESF
GPNTTCYFGC KTGFTLRGAN SLRCGASGQW TAVTPVCRAV KCSELHMDTA VAMNCSNPWG
NFSYGSTCAF HCPEGQSLNG SARTTCGEDG HWSDAMPTCQ AGTLTIQEAL TYLGGALAST
SGLAVGGTLL ALLRKRLRKK DDGKCPLNPH SHLGTYGVFT NAAYDPTP


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