LYAM3_BOVIN
ID LYAM3_BOVIN Reviewed; 646 AA.
AC P42201;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 1.
DT 03-AUG-2022, entry version 125.
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 Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND SUBCELLULAR LOCATION.
RC TISSUE=Capillary endothelium;
RX PubMed=7683458; DOI=10.1006/bbrc.1993.1420;
RA Strubel N.A., Nguyen M., Kansas G.S., Tedder T.F., Bischoff J.;
RT "Isolation and characterization of a bovine cDNA encoding a functional
RT homolog of human P-selectin.";
RL Biochem. Biophys. Res. Commun. 192:338-344(1993).
CC -!- FUNCTION: Ca(2+)-dependent receptor for myeloid cells that binds to
CC carbohydrates on neutrophils and monocytes (PubMed:7683458). Mediates
CC the interaction of activated endothelial cells or platelets with
CC leukocytes. The ligand recognized is sialyl-Lewis X. Mediates rapid
CC rolling of leukocyte rolling over vascular surfaces during the initial
CC steps in inflammation through interaction with SELPLG (By similarity).
CC {ECO:0000250|UniProtKB:P16109, ECO:0000269|PubMed:7683458}.
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:0000269|PubMed:7683458};
CC Single-pass type I membrane protein {ECO:0000305}.
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 {ECO:0000303|PubMed:7683458}.
CC -!- SIMILARITY: Belongs to the selectin/LECAM family. {ECO:0000305}.
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DR EMBL; L12041; AAA30743.1; -; mRNA.
DR PIR; JN0473; JN0473.
DR RefSeq; NP_776608.1; NM_174183.2.
DR AlphaFoldDB; P42201; -.
DR SMR; P42201; -.
DR PRIDE; P42201; -.
DR GeneID; 281486; -.
DR KEGG; bta:281486; -.
DR CTD; 6403; -.
DR InParanoid; P42201; -.
DR OrthoDB; 445079at2759; -.
DR Proteomes; UP000009136; Unplaced.
DR GO; GO:0005887; C:integral component of plasma membrane; ISS:UniProtKB.
DR GO; GO:0005509; F:calcium ion binding; ISS:UniProtKB.
DR GO; GO:0070492; F:oligosaccharide binding; ISS:UniProtKB.
DR GO; GO:0016339; P:calcium-dependent cell-cell adhesion via plasma membrane cell adhesion molecules; ISS:UniProtKB.
DR GO; GO:0050901; P:leukocyte tethering or rolling; ISS:UniProtKB.
DR GO; GO:1903238; P:positive regulation of leukocyte tethering or rolling; ISS:UniProtKB.
DR CDD; cd00033; CCP; 6.
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; PF00008; EGF; 1.
DR Pfam; PF00059; Lectin_C; 1.
DR Pfam; PF00084; Sushi; 6.
DR PRINTS; PR00343; SELECTIN.
DR SMART; SM00032; CCP; 6.
DR SMART; SM00034; CLECT; 1.
DR SMART; SM00181; EGF; 2.
DR SUPFAM; SSF56436; SSF56436; 1.
DR SUPFAM; SSF57535; SSF57535; 6.
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; 6.
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..41
FT /evidence="ECO:0000250"
FT CHAIN 42..646
FT /note="P-selectin"
FT /id="PRO_0000017497"
FT TOPO_DOM 42..587
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 588..611
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 612..646
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 456..517
FT /note="Sushi 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT DOMAIN 518..579
FT /note="Sushi 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT REGION 637..646
FT /note="Interaction with SNX17"
FT /evidence="ECO:0000250"
FT MOTIF 634..637
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 48
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 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 336
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 481
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 532
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 539
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 557
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 458..502
FT /evidence="ECO:0000250"
FT DISULFID 488..515
FT /evidence="ECO:0000250"
FT DISULFID 520..564
FT /evidence="ECO:0000250"
FT DISULFID 550..577
FT /evidence="ECO:0000250"
SQ SEQUENCE 646 AA; 71229 MW; 573912A4627A6ACA CRC64;
MASCPKAIWN WRFQRAVFRT VQLLCFSVLI FEVINQKEVS AWTYHYSNKT YSWNYSRAFC
QKYYTDLVAI QNKNEIAYLN ETIPYYNSYY WIGIRKINNK WTWVGTKKTL TEEAENWADN
EPNNKRNNQD CVEIYIKSLS APGKWNDEPC WKRKRALCYR ASCQDMSCSK QGECIETIGN
YTCSCYPGFY GPECEYVREC GEFDLPQHVH MNCSHPLGNF SFNSHCSFHC AEGYALNGPS
ELECLASGIW TNSPPQCVAV QCPALKSPEQ GSMSCVQSAE AFQHQSSCSF SCEEGFALVG
PEVVHCTALG VWTAPTPVCK ALQCQDLPTS TKARVNCSHP FGDFRYQSTC SFTCDEGSFL
VGASVLQCLD TGNWDAPFPE CQAVTCAALP NPQNGEKTCV QPLGGSSYES TCWFTCHEGF
SLSGPERLDC TPSGHWTGSP PTCEEVDTVS APAPGVQCPT LIAPKQGTMS CQHHVRNFGL
NTTCHFGCKA GFTLLGDSAL QCRPSRQWTA AAPTCRAVKC AKLPVTEPIV MNCSNPWGNF
SYGSTCSFHC PEGQLLNGSE RTVCQENGQW STTMPTCQAG PLTIQETLTY VGGAAAGTTG
LVTGSILLAL LRRRCRQKDD GKSPLNPQSH LGTYGVFTNA AFDPSP
