LYAM3_SHEEP
ID LYAM3_SHEEP Reviewed; 769 AA.
AC P98109;
DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1996, sequence version 1.
DT 03-AUG-2022, entry version 118.
DE RecName: Full=P-selectin;
DE AltName: Full=CD62 antigen-like family member P;
DE AltName: Full=CD62P antigen;
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=CD62;
DE Flags: Precursor;
GN Name=SELP;
OS Ovis aries (Sheep).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Caprinae; Ovis.
OX NCBI_TaxID=9940;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Heart;
RA Burns S.A., Neufeld E.J., Donady J.J.;
RL Submitted (JUL-1994) to the EMBL/GenBank/DDBJ databases.
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 -!- SIMILARITY: Belongs to the selectin/LECAM family. {ECO:0000305}.
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DR EMBL; L34270; AAB59261.1; -; mRNA.
DR RefSeq; NP_001009295.1; NM_001009295.1.
DR AlphaFoldDB; P98109; -.
DR SMR; P98109; -.
DR STRING; 9940.ENSOARP00000011508; -.
DR Ensembl; ENSOART00020013124; ENSOARP00020010814; ENSOARG00020008417.
DR Ensembl; ENSOART00020013246; ENSOARP00020010914; ENSOARG00020008417.
DR GeneID; 443305; -.
DR KEGG; oas:443305; -.
DR CTD; 6403; -.
DR eggNOG; KOG4297; Eukaryota.
DR OrthoDB; 445079at2759; -.
DR Proteomes; UP000002356; Unplaced.
DR GO; GO:0009897; C:external side of plasma membrane; IEA:Ensembl.
DR GO; GO:0005615; C:extracellular space; IEA:Ensembl.
DR GO; GO:0005887; C:integral component of plasma membrane; ISS:UniProtKB.
DR GO; GO:0031092; C:platelet alpha granule membrane; IEA:Ensembl.
DR GO; GO:0005509; F:calcium ion binding; ISS:UniProtKB.
DR GO; GO:0048306; F:calcium-dependent protein binding; IEA:Ensembl.
DR GO; GO:0042806; F:fucose binding; IEA:Ensembl.
DR GO; GO:0008201; F:heparin binding; IEA:Ensembl.
DR GO; GO:0001530; F:lipopolysaccharide binding; IEA:Ensembl.
DR GO; GO:0070492; F:oligosaccharide binding; ISS:UniProtKB.
DR GO; GO:0033691; F:sialic acid binding; IEA:Ensembl.
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; IEA:Ensembl.
DR GO; GO:0007157; P:heterophilic cell-cell adhesion via plasma membrane cell adhesion molecules; IEA:Ensembl.
DR GO; GO:0006954; P:inflammatory response; IEA:Ensembl.
DR GO; GO:0050901; P:leukocyte tethering or rolling; ISS:UniProtKB.
DR GO; GO:0002687; P:positive regulation of leukocyte migration; IEA:Ensembl.
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; IEA:Ensembl.
DR GO; GO:0010572; P:positive regulation of platelet activation; IEA:Ensembl.
DR GO; GO:0033623; P:regulation of integrin activation; IEA:Ensembl.
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 SMART; SM00181; EGF; 2.
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; Membrane; Metal-binding; Reference proteome; Repeat;
KW Signal; Sushi; Transmembrane; Transmembrane helix.
FT SIGNAL 1..32
FT /evidence="ECO:0000255"
FT CHAIN 33..769
FT /note="P-selectin"
FT /id="PRO_0000017501"
FT TOPO_DOM 33..717
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 718..734
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 735..769
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 579..640
FT /note="Sushi 7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT DOMAIN 641..702
FT /note="Sushi 8"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT REGION 740..769
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 760..769
FT /note="Interaction with SNX17"
FT /evidence="ECO:0000250"
FT MOTIF 757..760
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 CARBOHYD 54
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 80
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 180
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 219
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 398
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 604
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 655
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 662
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 680
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 581..625
FT /evidence="ECO:0000250"
FT DISULFID 611..638
FT /evidence="ECO:0000250"
FT DISULFID 643..687
FT /evidence="ECO:0000250"
FT DISULFID 673..700
FT /evidence="ECO:0000250"
FT VARIANT 566
FT /note="S -> T"
FT VARIANT 579
FT /note="L -> V"
SQ SEQUENCE 769 AA; 84318 MW; 23E42575D60FAB15 CRC64;
MASCPKAIWS WRFQRVVFRS VQLLCFSILI FELMTQKEVS AWTYHYSDKP YSWNYSRAFC
QKYYTDLVAI QNKNEIAYLN ETIPYYNSYY WIGIRKIDNK WTWVGTKKTL TEEAENWADN
EPNNKKNNQD CVEIYIKSPS APGKWNDEPC GKRKRALCYR ASCQDMSCSK QGECIETIGN
YTCSCYPGFY GPECEYVREC GEFDLPQNVH MNCSHPLGNF SFKSQCSFHC AEGYALNGPR
ELECLASGIW TNSPPQCVAV QCPALKSPEQ GSMSCFHSAK AFQHQSSCSF SCEEGFTLVG
PEVVHCTALG VWTAPTPVCK AIACESLESP VHGSMDCSPS PRAFQYNTSC SFRCAEGFTL
RGADTVRCAD SGEWTAPAPV CQALQCQDLP TSNKARVNCS HPFGDFRYQS TCSFTCDEGS
FLVGASVLQC LDTGNWDAPF PECQAVTCAP LPNPQNGEKT CVQPLGGSSY KSTCWFTCHE
GFSLSGPERL DCTPSGHWTG SPPTCEASKC PELSAPEQGS LDCPDTHGEF IVGSICHFSC
NEGLKLEGSN HVECTASGRW TAPPPSCKVD TVSAPAPGLR CPSLIAPNQG TMSCQHHLRN
FGLNTTCHFG CKAGFTLMGE SALQCRPSRQ WTAVAPTCRA VKCSKLPVTE PIVMNCSNPW
GNFSYGSTCS FHCPEGQLLN GSERTACQEN GQWSTTMPTC QAGPLTIQEA LTYIGGAAAG
TTGLVTSSIL LALLRRRRRQ KDDGKSPLNP QSHLGTYGVF TNAAFDPSP
