LYAM3_RAT
ID LYAM3_RAT Reviewed; 768 AA.
AC P98106;
DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1996, sequence version 1.
DT 03-AUG-2022, entry version 150.
DE RecName: Full=P-selectin;
DE AltName: Full=CD62 antigen-like family member P;
DE AltName: Full=Granule membrane protein 140;
DE Short=GMP-140;
DE AltName: Full=Leukocyte-endothelial cell adhesion molecule 3;
DE Short=LECAM3;
DE AltName: Full=Platelet activation dependent granule-external membrane protein;
DE Short=PADGEM;
DE AltName: CD_antigen=CD62P;
DE Flags: Precursor;
GN Name=Selp;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, AND INDUCTION BY BACTERIAL
RP LIPOPOLYSACCHARIDE.
RC TISSUE=Lung;
RX PubMed=7520013; DOI=10.1016/0378-1119(94)90015-9;
RA Auchampach J.A., Oliver M.G., Anderson D.C., Manning A.M.;
RT "Cloning, sequence comparison and in vivo expression of the gene encoding
RT rat P-selectin.";
RL Gene 145:251-255(1994).
CC -!- FUNCTION: Ca(2+)-dependent receptor for myeloid cells that binds to
CC carbohydrates on neutrophils and monocytes. Mediates the interaction of
CC activated endothelial cells or platelets with leukocytes. The ligand
CC recognized is sialyl-Lewis X. Mediates rapid rolling of leukocyte
CC rolling over vascular surfaces during the initial steps in inflammation
CC through interaction with SELPLG. {ECO:0000250|UniProtKB:P16109}.
CC -!- SUBUNIT: Interacts with SNX17. Interacts with SELPLG/PSGL1 and PODXL2
CC and mediates neutrophil adhesion and leukocyte rolling. This
CC interaction requires the sialyl-Lewis X epitope of SELPLG and PODXL2,
CC and specific tyrosine sulfation on SELPLG.
CC {ECO:0000250|UniProtKB:P16109}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:P16109};
CC Single-pass type I membrane protein {ECO:0000250|UniProtKB:P16109}.
CC -!- TISSUE SPECIFICITY: Not detected in the absence of exposure to
CC lipopolysaccharide (LPS). Detected only after exposure to
CC lipopolysaccharide (LPS) in the tissues examined: spleen, lung, brain,
CC liver, heart, kidney, thymus and small intestine.
CC {ECO:0000269|PubMed:7520013}.
CC -!- INDUCTION: By exposure to bacterial lipopolysaccharide (LPS).
CC {ECO:0000269|PubMed:7520013}.
CC -!- SIMILARITY: Belongs to the selectin/LECAM family. {ECO:0000305}.
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DR EMBL; L23088; AAA60325.1; -; mRNA.
DR PIR; I53821; I53821.
DR RefSeq; NP_037246.1; NM_013114.1.
DR AlphaFoldDB; P98106; -.
DR SMR; P98106; -.
DR STRING; 10116.ENSRNOP00000068338; -.
DR ChEMBL; CHEMBL3879832; -.
DR GlyGen; P98106; 10 sites.
DR PaxDb; P98106; -.
DR PRIDE; P98106; -.
DR GeneID; 25651; -.
DR KEGG; rno:25651; -.
DR UCSC; RGD:3656; rat.
DR CTD; 6403; -.
DR RGD; 3656; Selp.
DR eggNOG; KOG4297; Eukaryota.
DR InParanoid; P98106; -.
DR OrthoDB; 445079at2759; -.
DR PhylomeDB; P98106; -.
DR Reactome; R-RNO-114608; Platelet degranulation.
DR Reactome; R-RNO-202733; Cell surface interactions at the vascular wall.
DR PRO; PR:P98106; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0009897; C:external side of plasma membrane; IDA:RGD.
DR GO; GO:0005615; C:extracellular space; IDA:RGD.
DR GO; GO:0005887; C:integral component of plasma membrane; ISS:UniProtKB.
DR GO; GO:0016020; C:membrane; ISO:RGD.
DR GO; GO:0031092; C:platelet alpha granule membrane; ISO:RGD.
DR GO; GO:0005509; F:calcium ion binding; ISS:UniProtKB.
DR GO; GO:0048306; F:calcium-dependent protein binding; ISO:RGD.
DR GO; GO:0042806; F:fucose binding; ISO:RGD.
DR GO; GO:0008201; F:heparin binding; ISO:RGD.
DR GO; GO:0001530; F:lipopolysaccharide binding; ISO:RGD.
DR GO; GO:0070492; F:oligosaccharide binding; ISS:UniProtKB.
DR GO; GO:0033691; F:sialic acid binding; ISO:RGD.
DR GO; GO:0016339; P:calcium-dependent cell-cell adhesion via plasma membrane cell adhesion molecules; ISS:UniProtKB.
DR GO; GO:0035584; P:calcium-mediated signaling using intracellular calcium source; ISO:RGD.
DR GO; GO:0098609; P:cell-cell adhesion; IMP:RGD.
DR GO; GO:0007157; P:heterophilic cell-cell adhesion via plasma membrane cell adhesion molecules; ISO:RGD.
DR GO; GO:0006954; P:inflammatory response; ISO:RGD.
DR GO; GO:0007159; P:leukocyte cell-cell adhesion; ISO:RGD.
DR GO; GO:0050900; P:leukocyte migration; IMP:RGD.
DR GO; GO:0050901; P:leukocyte tethering or rolling; ISS:UniProtKB.
DR GO; GO:0045785; P:positive regulation of cell adhesion; IMP:RGD.
DR GO; GO:0002687; P:positive regulation of leukocyte migration; ISO:RGD.
DR GO; GO:1903238; P:positive regulation of leukocyte tethering or rolling; ISS:UniProtKB.
DR GO; GO:0014068; P:positive regulation of phosphatidylinositol 3-kinase signaling; ISO:RGD.
DR GO; GO:0010572; P:positive regulation of platelet activation; ISO:RGD.
DR GO; GO:0002691; P:regulation of cellular extravasation; IMP:RGD.
DR GO; GO:0033623; P:regulation of integrin activation; ISO:RGD.
DR GO; GO:0034097; P:response to cytokine; IBA:GO_Central.
DR GO; GO:0032496; P:response to lipopolysaccharide; IEP:RGD.
DR GO; GO:0014070; P:response to organic cyclic compound; IEP:RGD.
DR CDD; cd00033; CCP; 8.
DR CDD; cd03592; CLECT_selectins_like; 1.
DR Gene3D; 3.10.100.10; -; 1.
DR InterPro; IPR001304; C-type_lectin-like.
DR InterPro; IPR016186; C-type_lectin-like/link_sf.
DR InterPro; IPR018378; C-type_lectin_CS.
DR InterPro; IPR016187; CTDL_fold.
DR InterPro; IPR000742; EGF-like_dom.
DR InterPro; IPR033991; Selectin_CTLD.
DR InterPro; IPR002396; Selectin_superfamily.
DR InterPro; IPR035976; Sushi/SCR/CCP_sf.
DR InterPro; IPR000436; Sushi_SCR_CCP_dom.
DR Pfam; PF00059; Lectin_C; 1.
DR Pfam; PF00084; Sushi; 8.
DR PRINTS; PR00343; SELECTIN.
DR SMART; SM00032; CCP; 8.
DR SMART; SM00034; CLECT; 1.
DR SUPFAM; SSF56436; SSF56436; 1.
DR SUPFAM; SSF57535; SSF57535; 8.
DR PROSITE; PS00615; C_TYPE_LECTIN_1; 1.
DR PROSITE; PS50041; C_TYPE_LECTIN_2; 1.
DR PROSITE; PS00022; EGF_1; 1.
DR PROSITE; PS01186; EGF_2; 1.
DR PROSITE; PS50026; EGF_3; 1.
DR PROSITE; PS50923; SUSHI; 8.
PE 2: Evidence at transcript level;
KW Calcium; Cell adhesion; Cell membrane; Disulfide bond; EGF-like domain;
KW Glycoprotein; Lectin; Lipoprotein; Membrane; Metal-binding; Palmitate;
KW Reference proteome; Repeat; Signal; Sushi; Transmembrane;
KW Transmembrane helix.
FT SIGNAL 1..41
FT /evidence="ECO:0000255"
FT CHAIN 42..768
FT /note="P-selectin"
FT /id="PRO_0000017500"
FT TOPO_DOM 42..709
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 710..733
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 734..768
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 58..158
FT /note="C-type lectin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
FT DOMAIN 159..195
FT /note="EGF-like"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 198..259
FT /note="Sushi 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT DOMAIN 260..321
FT /note="Sushi 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT DOMAIN 322..383
FT /note="Sushi 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT DOMAIN 384..445
FT /note="Sushi 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT DOMAIN 446..507
FT /note="Sushi 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT DOMAIN 508..569
FT /note="Sushi 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT DOMAIN 578..639
FT /note="Sushi 7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT DOMAIN 640..701
FT /note="Sushi 8"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT REGION 759..768
FT /note="Interaction with SNX17"
FT /evidence="ECO:0000250"
FT MOTIF 756..759
FT /note="Endocytosis signal"
FT /evidence="ECO:0000305"
FT BINDING 121
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:P16109"
FT BINDING 123
FT /ligand="a carbohydrate"
FT /ligand_id="ChEBI:CHEBI:16646"
FT /evidence="ECO:0000250|UniProtKB:P16109"
FT BINDING 123
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:P16109"
FT BINDING 124
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:P16109"
FT BINDING 133
FT /ligand="a carbohydrate"
FT /ligand_id="ChEBI:CHEBI:16646"
FT /evidence="ECO:0000250|UniProtKB:P16109"
FT BINDING 146
FT /ligand="a carbohydrate"
FT /ligand_id="ChEBI:CHEBI:16646"
FT /evidence="ECO:0000250|UniProtKB:P16109"
FT BINDING 146
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:P16109"
FT BINDING 147
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:P16109"
FT LIPID 745
FT /note="S-palmitoyl cysteine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P16109"
FT LIPID 745
FT /note="S-stearoyl cysteine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P16109"
FT CARBOHYD 45
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 54
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 107
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 212
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 347
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 456
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 603
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 654
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 661
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 679
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 60..158
FT /evidence="ECO:0000250|UniProtKB:P16109"
FT DISULFID 131..150
FT /evidence="ECO:0000250|UniProtKB:P16109"
FT DISULFID 168..183
FT /evidence="ECO:0000250|UniProtKB:P16109"
FT DISULFID 185..194
FT /evidence="ECO:0000250|UniProtKB:P16109"
FT DISULFID 200..244
FT /evidence="ECO:0000250"
FT DISULFID 230..257
FT /evidence="ECO:0000250"
FT DISULFID 262..306
FT /evidence="ECO:0000250"
FT DISULFID 292..319
FT /evidence="ECO:0000250"
FT DISULFID 324..368
FT /evidence="ECO:0000250"
FT DISULFID 354..381
FT /evidence="ECO:0000250"
FT DISULFID 386..430
FT /evidence="ECO:0000250"
FT DISULFID 416..443
FT /evidence="ECO:0000250"
FT DISULFID 448..492
FT /evidence="ECO:0000250"
FT DISULFID 478..505
FT /evidence="ECO:0000250"
FT DISULFID 510..554
FT /evidence="ECO:0000250"
FT DISULFID 540..567
FT /evidence="ECO:0000250"
FT DISULFID 580..624
FT /evidence="ECO:0000250"
FT DISULFID 610..637
FT /evidence="ECO:0000250"
FT DISULFID 642..686
FT /evidence="ECO:0000250"
FT DISULFID 672..699
FT /evidence="ECO:0000250"
SQ 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
