LYAM3_MOUSE
ID LYAM3_MOUSE Reviewed; 768 AA.
AC Q01102; Q32MF1;
DT 01-APR-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-APR-1993, sequence version 1.
DT 03-AUG-2022, entry version 190.
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; Synonyms=Grmp;
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], AND INDUCTION.
RX PubMed=1378846; DOI=10.1016/s0021-9258(18)42162-x;
RA Weller A., Isenmann S., Vestweber D.;
RT "Cloning of the mouse endothelial selectins. Expression of both E- and P-
RT selectin is inducible by tumor necrosis factor alpha.";
RL J. Biol. Chem. 267:15176-15183(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], AND INDUCTION.
RX PubMed=1379089;
RA Sanders W.E. Jr., Wilson R.W., Ballantyne C.M., Beaudet A.L.;
RT "Molecular cloning and analysis of in vivo expression of murine P-
RT selectin.";
RL Blood 80:795-800(1992).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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.
RX PubMed=12370362; DOI=10.4049/jimmunol.169.8.4307;
RA Hirata T., Furie B.C., Furie B.;
RT "P-, E-, and L-selectin mediate migration of activated CD8+ T lymphocytes
RT into inflamed skin.";
RL J. Immunol. 169:4307-4313(2002).
RN [5]
RP INTERACTION WITH SELPLG.
RX PubMed=12393631; DOI=10.1182/blood-2001-11-0036;
RA Xia L., Ramachandran V., McDaniel J.M., Nguyen K.N., Cummings R.D.,
RA McEver R.P.;
RT "N-terminal residues in murine P-selectin glycoprotein ligand-1 required
RT for binding to murine P-selectin.";
RL Blood 101:552-559(2003).
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 ECO:0000269|PubMed:12370362}.
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, ECO:0000269|PubMed:12393631}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:P16109};
CC Single-pass type I membrane protein {ECO:0000250|UniProtKB:P16109}.
CC -!- TISSUE SPECIFICITY: Stored in the alpha-granules of platelets and
CC Weibel-Palade bodies of endothelial cells. Upon cell activation by
CC agonists, P-selectin is transported rapidly to the cell surface.
CC -!- INDUCTION: By TNF-alpha. Induced expression in lung, liver, kidney and
CC heart after endotoxin treatment. {ECO:0000269|PubMed:1378846,
CC ECO:0000269|PubMed:1379089}.
CC -!- SIMILARITY: Belongs to the selectin/LECAM family. {ECO:0000305}.
CC -!- WEB RESOURCE: Name=Functional Glycomics Gateway - Glycan Binding;
CC Note=P-selectin;
CC URL="http://www.functionalglycomics.org/glycomics/GBPServlet?&operationType=view&cbpId=cbp_mou_Ctlect_284";
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DR EMBL; M87861; AAA40008.1; -; mRNA.
DR EMBL; M72332; AAA37712.1; -; mRNA.
DR EMBL; BC109158; AAI09159.1; -; mRNA.
DR EMBL; BC109159; AAI09160.1; -; mRNA.
DR CCDS; CCDS48422.1; -.
DR PIR; A42755; A42755.
DR RefSeq; NP_035477.1; NM_011347.2.
DR PDB; 4GXB; X-ray; 1.80 A; B=735-768.
DR PDBsum; 4GXB; -.
DR AlphaFoldDB; Q01102; -.
DR SMR; Q01102; -.
DR STRING; 10090.ENSMUSP00000123924; -.
DR BindingDB; Q01102; -.
DR ChEMBL; CHEMBL2455; -.
DR GlyGen; Q01102; 5 sites.
DR iPTMnet; Q01102; -.
DR PhosphoSitePlus; Q01102; -.
DR CPTAC; non-CPTAC-3590; -.
DR MaxQB; Q01102; -.
DR PaxDb; Q01102; -.
DR PeptideAtlas; Q01102; -.
DR PRIDE; Q01102; -.
DR ProteomicsDB; 291976; -.
DR Antibodypedia; 794; 1238 antibodies from 44 providers.
DR DNASU; 20344; -.
DR Ensembl; ENSMUST00000162746; ENSMUSP00000123924; ENSMUSG00000026580.
DR GeneID; 20344; -.
DR KEGG; mmu:20344; -.
DR UCSC; uc007dhz.2; mouse.
DR CTD; 6403; -.
DR MGI; MGI:98280; Selp.
DR VEuPathDB; HostDB:ENSMUSG00000026580; -.
DR eggNOG; KOG4297; Eukaryota.
DR GeneTree; ENSGT00940000161063; -.
DR HOGENOM; CLU_020848_0_0_1; -.
DR InParanoid; Q01102; -.
DR OMA; EQGTMSC; -.
DR OrthoDB; 445079at2759; -.
DR PhylomeDB; Q01102; -.
DR TreeFam; TF326910; -.
DR Reactome; R-MMU-114608; Platelet degranulation.
DR Reactome; R-MMU-202733; Cell surface interactions at the vascular wall.
DR BioGRID-ORCS; 20344; 0 hits in 74 CRISPR screens.
DR PRO; PR:Q01102; -.
DR Proteomes; UP000000589; Chromosome 1.
DR RNAct; Q01102; protein.
DR Bgee; ENSMUSG00000026580; Expressed in endothelial cell of lymphatic vessel and 83 other tissues.
DR ExpressionAtlas; Q01102; baseline and differential.
DR Genevisible; Q01102; MM.
DR GO; GO:0009897; C:external side of plasma membrane; IDA:MGI.
DR GO; GO:0005615; C:extracellular space; ISO:MGI.
DR GO; GO:0005887; C:integral component of plasma membrane; ISS:UniProtKB.
DR GO; GO:0016020; C:membrane; IDA:MGI.
DR GO; GO:0031092; C:platelet alpha granule membrane; ISO:MGI.
DR GO; GO:0005509; F:calcium ion binding; ISS:UniProtKB.
DR GO; GO:0048306; F:calcium-dependent protein binding; IDA:MGI.
DR GO; GO:0042806; F:fucose binding; ISO:MGI.
DR GO; GO:0008201; F:heparin binding; ISO:MGI.
DR GO; GO:0001530; F:lipopolysaccharide binding; ISO:MGI.
DR GO; GO:0070492; F:oligosaccharide binding; ISS:UniProtKB.
DR GO; GO:0033691; F:sialic acid binding; IDA:MGI.
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:MGI.
DR GO; GO:0098609; P:cell-cell adhesion; ISO:MGI.
DR GO; GO:0071354; P:cellular response to interleukin-6; ISO:MGI.
DR GO; GO:0007157; P:heterophilic cell-cell adhesion via plasma membrane cell adhesion molecules; IMP:MGI.
DR GO; GO:0006954; P:inflammatory response; IMP:MGI.
DR GO; GO:0007159; P:leukocyte cell-cell adhesion; IMP:MGI.
DR GO; GO:0050900; P:leukocyte migration; IMP:MGI.
DR GO; GO:0050901; P:leukocyte tethering or rolling; IMP:MGI.
DR GO; GO:0045785; P:positive regulation of cell adhesion; ISO:MGI.
DR GO; GO:0002687; P:positive regulation of leukocyte migration; IMP:MGI.
DR GO; GO:1903238; P:positive regulation of leukocyte tethering or rolling; IMP:UniProtKB.
DR GO; GO:0014068; P:positive regulation of phosphatidylinositol 3-kinase signaling; ISS:UniProtKB.
DR GO; GO:0010572; P:positive regulation of platelet activation; IMP:BHF-UCL.
DR GO; GO:0002691; P:regulation of cellular extravasation; ISO:MGI.
DR GO; GO:0033623; P:regulation of integrin activation; ISS:UniProtKB.
DR GO; GO:0034097; P:response to cytokine; IBA:GO_Central.
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; IPR001881; EGF-like_Ca-bd_dom.
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; PF00008; EGF; 1.
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 SMART; SM00181; EGF; 1.
DR SMART; SM00179; EGF_CA; 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 1: Evidence at protein level;
KW 3D-structure; Calcium; Cell adhesion; Cell membrane; Disulfide bond;
KW EGF-like domain; Glycoprotein; Lectin; Lipoprotein; Membrane;
KW Metal-binding; Palmitate; Reference proteome; Repeat; Signal; Sushi;
KW Transmembrane; Transmembrane helix.
FT SIGNAL 1..41
FT /evidence="ECO:0000255"
FT CHAIN 42..768
FT /note="P-selectin"
FT /id="PRO_0000017499"
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 398
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 163..174
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"
FT CONFLICT 724
FT /note="A -> E (in Ref. 2; AAA37712)"
FT /evidence="ECO:0000305"
FT STRAND 756..760
FT /evidence="ECO:0007829|PDB:4GXB"
SQ SEQUENCE 768 AA; 83099 MW; E5173074D2F66E68 CRC64;
MAGCPKGSWT PRLRSVILGG AQLIWFSALI SELVNQKEVA AWTYNYSTKA YSWNNSRVFC
RRHFTDLVAI QNKNEIAHLN DVIPFFNSYY WIGIRKINNK WTWVGTNKTL TEEAENWADN
EPNNKKNNQD CVEIYIKSNS APGKWNDEPC FKRKRALCYT ASCQDMSCSN QGECIETIGS
YTCSCYPGFY GPECEYVKEC GKVNIPQHVL MNCSHPLGEF SFNSQCTFSC AEGYELDGPG
ELQCLASGIW TNNPPKCDAV QCQSLEAPPH GTMACMHPIA AFAYDSSCKF ECQPGYRARG
SNTLHCTGSG QWSEPLPTCE AIACEPPEIP IHGSMDCVPS TGTFGYNSSC TFLCAEGFVL
KGNDAIQCAD SGQWTAPAPF CEALQCPEFP VPSKAQVNCS DPFGTLTYQS VCSFSCDEGS
LLVGASVIRC LATGHWNGAP PECQAVSCAP MLSPENGSMT CVQPLGNSTY KSTCQFMCDE
GFYLSGPERL DCSPSGHWTG TPPTCEAIKC PGIFAPEQGN LDCSHVHGEF GVGSICHFSC
NEDFELLGSE NVECTVSGRW SAPPPTCKGI TSLPAPAVRC PALTTPGQGT MSCQHHLGSF
GPNTTCYFGC KTGFTLRGAN SLRCRASGQW TAVTPMCRAV KCSELHMDTA VAMNCSNPWG
NFSYGSTCTF QCPEGQSLNG SVRATCREDG HWSDAMPTCQ AGTLTIQEAL TYLGGAVAST
TGLAVGGTLL ALLRKRLRKK DDGKCPLNPH SHLGTYGVFT NAAYDPTP
