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   24-JAN-2024, entry version 198.
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   GlyCosmos; Q01102; 5 sites, No reported glycans.
DR   GlyGen; Q01102; 5 sites.
DR   iPTMnet; Q01102; -.
DR   PhosphoSitePlus; Q01102; -.
DR   SwissPalm; Q01102; -.
DR   CPTAC; non-CPTAC-3590; -.
DR   MaxQB; Q01102; -.
DR   PaxDb; 10090-ENSMUSP00000123924; -.
DR   PeptideAtlas; Q01102; -.
DR   ProteomicsDB; 291976; -.
DR   Antibodypedia; 794; 1461 antibodies from 45 providers.
DR   DNASU; 20344; -.
DR   Ensembl; ENSMUST00000162746.2; ENSMUSP00000123924.2; ENSMUSG00000026580.17.
DR   GeneID; 20344; -.
DR   KEGG; mmu:20344; -.
DR   UCSC; uc007dhz.2; mouse.
DR   AGR; MGI:98280; -.
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; DWCPEPP; -.
DR   OrthoDB; 3035244at2759; -.
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 79 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 85 other cell types or tissues.
DR   ExpressionAtlas; Q01102; baseline and differential.
DR   GO; GO:0009897; C:external side of plasma membrane; IDA:MGI.
DR   GO; GO:0005615; C:extracellular space; ISO:MGI.
DR   GO; GO:0016020; C:membrane; IDA:MGI.
DR   GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
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:0051897; P:positive regulation of phosphatidylinositol 3-kinase/protein kinase B signal transduction; 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   CDD; cd00054; EGF_CA; 1.
DR   Gene3D; 2.10.70.10; Complement Module, domain 1; 8.
DR   Gene3D; 2.10.25.10; Laminin; 1.
DR   Gene3D; 3.10.100.10; Mannose-Binding Protein A, subunit A; 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   PANTHER; PTHR19325; COMPLEMENT COMPONENT-RELATED SUSHI DOMAIN-CONTAINING; 1.
DR   PANTHER; PTHR19325:SF484; P-SELECTIN; 1.
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; C-type lectin-like; 1.
DR   SUPFAM; SSF57535; Complement control module/SCR domain; 8.
DR   SUPFAM; SSF57196; EGF/Laminin; 1.
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.
DR   Genevisible; Q01102; MM.
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
//