Lipid Modification Database
Tag Content
LipidDB ID
LipidDB-9606-00036
Entry Name
UniProt Accession
Theoretical PI
6.17
Molecular Weight
90833.89
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
P-selectin
Protein Synonyms/Alias
CD62 antigen-like family member P; Granule membrane protein 140; GMP-140; Leukocyte-endothelial cell adhesion molecule 3; LECAM3; Platelet activation dependent granule-external membrane protein; PADGEM; CD62P;
Gene Name
SELP
Gene Synonyms/Alias
GMRP; GRMP;
Created Date
01-APR-1990
 Lipid Modification Sites 
 Position   Sequence Form   Peptide   References   Modification Type 
807
Canonical
RQKDDGKCPLNPHSH
[1]
S-Palmitoylation
Organism
Homo sapiens (Human)
NCBI Taxa ID
9606
Reference
[1] Fujimoto T, Stroud E, Whatley RE, Prescott SM, Muszbek L, Laposata M, McEverRP. P-selectin is acylated with palmitic acid and stearic acid at cysteine 766through a thioester linkage. J Biol Chem. 1993 May 25;268(15):11394-400. PubMedPMID: 7684381.[PMID:7684381]
Functional Description
Ca(2+)-dependent receptor for myeloid cells that binds to carbohydrates on neutrophils and monocytes. Mediates the interaction of activated endothelial cells or platelets with leukocytes. The ligand recognized is sialyl-Lewis X. Mediates rapid rolling of leukocyte rolling over vascular surfaces during the initial steps in inflammation through interaction with PSGL1.
Sequence Annotation
Topological domain: 42 771 Extracellular.
Transmembrane: 772 795 Helical.
Topological domain: 796 830 Cytoplasmic.
Domain: 58 158 C-type lectin.
Domain: 159 195 EGF-like.
Domain: 198 259 Sushi 1.
Domain: 260 321 Sushi 2.
Domain: 322 383 Sushi 3.
Domain: 384 445 Sushi 4.
Domain: 446 507 Sushi 5.
Domain: 508 569 Sushi 6.
Domain: 570 631 Sushi 7.
Domain: 640 701 Sushi 8.
Domain: 702 763 Sushi 9.
Region: 821 830 Interaction with SNX17.
Motif: 818 821 Endocytosis signal.
Protein Length
830 AA.
Protein Sequence
(Canonical)
MANCQIAILY QRFQRVVFGI SQLLCFSALI SELTNQKEVA AWTYHYSTKA YSWNISRKYC  60
QNRYTDLVAI QNKNEIDYLN KVLPYYSSYY WIGIRKNNKT WTWVGTKKAL TNEAENWADN  120
EPNNKRNNED CVEIYIKSPS APGKWNDEHC LKKKHALCYT ASCQDMSCSK QGECLETIGN  180
YTCSCYPGFY GPECEYVREC GELELPQHVL MNCSHPLGNF SFNSQCSFHC TDGYQVNGPS  240
KLECLASGIW TNKPPQCLAA QCPPLKIPER GNMTCLHSAK AFQHQSSCSF SCEEGFALVG  300
PEVVQCTASG VWTAPAPVCK AVQCQHLEAP SEGTMDCVHP LTAFAYGSSC KFECQPGYRV  360
RGLDMLRCID SGHWSAPLPT CEAISCEPLE SPVHGSMDCS PSLRAFQYDT NCSFRCAEGF  420
MLRGADIVRC DNLGQWTAPA PVCQALQCQD LPVPNEARVN CSHPFGAFRY QSVCSFTCNE  480
GLLLVGASVL QCLATGNWNS VPPECQAIPC TPLLSPQNGT MTCVQPLGSS SYKSTCQFIC  540
DEGYSLSGPE RLDCTRSGRW TDSPPMCEAI KCPELFAPEQ GSLDCSDTRG EFNVGSTCHF  600
SCDNGFKLEG PNNVECTTSG RWSATPPTCK GIASLPTPGL QCPALTTPGQ GTMYCRHHPG  660
TFGFNTTCYF GCNAGFTLIG DSTLSCRPSG QWTAVTPACR AVKCSELHVN KPIAMNCSNL  720
WGNFSYGSIC SFHCLEGQLL NGSAQTACQE NGHWSTTVPT CQAGPLTIQE ALTYFGGAVA  780
STIGLIMGGT LLALLRKRFR QKDDGKCPLN PHSHLGTYGV FTNAAFDPSP             830
FASTA
(Canonical)
>LipidDB-9606-00036|P16109
MANCQIAILYQRFQRVVFGISQLLCFSALISELTNQKEVAAWTYHYSTKAYSWNISRKYC
QNRYTDLVAIQNKNEIDYLNKVLPYYSSYYWIGIRKNNKTWTWVGTKKALTNEAENWADN
EPNNKRNNEDCVEIYIKSPSAPGKWNDEHCLKKKHALCYTASCQDMSCSKQGECLETIGN
YTCSCYPGFYGPECEYVRECGELELPQHVLMNCSHPLGNFSFNSQCSFHCTDGYQVNGPS
KLECLASGIWTNKPPQCLAAQCPPLKIPERGNMTCLHSAKAFQHQSSCSFSCEEGFALVG
PEVVQCTASGVWTAPAPVCKAVQCQHLEAPSEGTMDCVHPLTAFAYGSSCKFECQPGYRV
RGLDMLRCIDSGHWSAPLPTCEAISCEPLESPVHGSMDCSPSLRAFQYDTNCSFRCAEGF
MLRGADIVRCDNLGQWTAPAPVCQALQCQDLPVPNEARVNCSHPFGAFRYQSVCSFTCNE
GLLLVGASVLQCLATGNWNSVPPECQAIPCTPLLSPQNGTMTCVQPLGSSSYKSTCQFIC
DEGYSLSGPERLDCTRSGRWTDSPPMCEAIKCPELFAPEQGSLDCSDTRGEFNVGSTCHF
SCDNGFKLEGPNNVECTTSGRWSATPPTCKGIASLPTPGLQCPALTTPGQGTMYCRHHPG
TFGFNTTCYFGCNAGFTLIGDSTLSCRPSGQWTAVTPACRAVKCSELHVNKPIAMNCSNL
WGNFSYGSICSFHCLEGQLLNGSAQTACQENGHWSTTVPTCQAGPLTIQEALTYFGGAVA
STIGLIMGGTLLALLRKRFRQKDDGKCPLNPHSHLGTYGVFTNAAFDPSP
Gene Ontology
GO:0005737; C:cytoplasm; IDA:HPA
GO:0009897; C:external side of plasma membrane; IDA:BHF-UCL
GO:0005615; C:extracellular space; IDA:BHF-UCL
GO:0005887; C:integral component of plasma membrane; TAS:ProtInc
GO:0005634; C:nucleus; IDA:HPA
GO:0005886; C:plasma membrane; TAS:Reactome
GO:0031092; C:platelet alpha granule membrane; IDA:MGI
GO:0031088; C:platelet dense granule membrane; TAS:Reactome
GO:0042806; F:fucose binding; IDA:BHF-UCL
GO:0043208; F:glycosphingolipid binding; TAS:BHF-UCL
GO:0008201; F:heparin binding; IDA:BHF-UCL
GO:0001530; F:lipopolysaccharide binding; IMP:BHF-UCL
GO:0070492; F:oligosaccharide binding; IDA:BHF-UCL
GO:0033691; F:sialic acid binding; IDA:BHF-UCL
GO:0007596; P:blood coagulation; TAS:Reactome
GO:0007155; P:cell adhesion; TAS:ProtInc
GO:0050829; P:defense response to Gram-negative bacterium; IC:BHF-UCL
GO:0007157; P:heterophilic cell-cell adhesion; IEA:Ensembl
GO:0006954; P:inflammatory response; IEA:Ensembl
GO:0007159; P:leukocyte cell-cell adhesion; IDA:BHF-UCL
GO:0050900; P:leukocyte migration; TAS:Reactome
GO:0050901; P:leukocyte tethering or rolling; IEA:Ensembl
GO:0030168; P:platelet activation; TAS:Reactome
GO:0002576; P:platelet degranulation; TAS:Reactome
GO:0002687; P:positive regulation of leukocyte migration; IEA:Ensembl
GO:0014068; P:positive regulation of phosphatidylinositol 3-kinase signaling; IDA:UniProtKB
GO:0010572; P:positive regulation of platelet activation; ISS:BHF-UCL
GO:0033623; P:regulation of integrin activation; IMP:UniProtKB
GO:0032496; P:response to lipopolysaccharide; IC:BHF-UCL
Interpro
InterPro; IPR001304; C-type_lectin
InterPro; IPR016186; C-type_lectin-like
InterPro; IPR018378; C-type_lectin_CS
InterPro; IPR016187; C-type_lectin_fold
InterPro; IPR000742; EG-like_dom
InterPro; IPR013032; EGF-like_CS
InterPro; IPR002396; Selectin_superfamily
InterPro; IPR000436; Sushi_SCR_CCP
Pfam
Pfam; PF00059; Lectin_C;
Pfam; PF00084; Sushi;
SMART
SMART; SM00032; CCP;
SMART; SM00034; CLECT;
SMART; SM00181; EGF;
PROSITE
PROSITE; PS00615; C_TYPE_LECTIN_1;
PROSITE; PS50041; C_TYPE_LECTIN_2;
PROSITE; PS00022; EGF_1;
PROSITE; PS01186; EGF_2;
PROSITE; PS50026; EGF_3;
PROSITE; PS50923; SUSHI;
PRINTS
PRINTS; PR00343; SELECTIN;