SELPLG
entrez
6404
canonical
uniprot
Q14242
canonical
ensembl
ENSG00000110876
resolver
ensp
ENSP00000228463
resolver
ensp
ENSP00000447752
resolver
genesymbol
SELPLG
resolver
hgnc
HGNC:10722
resolver
uniprot
A8K2Y0
resolver
uniprot
B4DQC3
resolver
uniprot
B7Z5C7
resolver
uniprot
J3KMX6
resolver
uniprot
Q12775
resolver
uniprot
Q6GTW7
resolver
uniprot
Q8N7J7
resolver
uniprot_entry
SELPL_HUMAN
resolver
uniprot_sec
A8K2Y0
resolver
uniprot_sec
B4DQC3
resolver
uniprot_sec
B7Z5C7
resolver
uniprot_sec
J3KMX6
resolver
uniprot_sec
Q12775
resolver
uniprot_sec
Q6GTW7
resolver
uniprot_sec
Q8N7J7
resolver
amino_acid_sequence
MPLQLLLLLILLGPGNSLQLWDTWADEAEKALGPLLARDRRQATEYEYLDYDFLPETEPPEMLRNSTDTTPLTGPGTPESTTVEPAARRSTGLDAGGAVTELTTELANMGNLSTDSAAMEIQTTQPAATEAQTTQPVPTEAQTTPLAATEAQTTRLTATEAQTTPLAATEAQTTPPAATEAQTTQPTGLEAQTTAPAAMEAQTTAPAAMEAQTTPPAAMEAQTTQTTAMEAQTTAPEATEAQTTQPTATEAQTTPLAAMEALSTEPSATEALSMEPTTKRGLFIPFSVSSVTHKGIPMAASNLSVNYPVGAPDHISVKQCLLAILILALVATIFFVCTVVLAVRLSRKGHMYPVRNYSPTEMVCISSLLPDGGEGPSATANGGLSKAKSPGLTPEPREDREGDDLTLHSFLP
uniprot
proteins
function
FUNCTION: A SLe(x)-type proteoglycan, which through high affinity, calcium-dependent interactions with E-, P- and L-selectins, mediates rapid rolling of leukocytes over vascular surfaces during the initial steps in inflammation. Critical for the initial leukocyte capture. {ECO:0000269|PubMed:11566773, ECO:0000269|PubMed:12403782}.; FUNCTION: (Microbial infection) Acts as a receptor for enterovirus 71. {ECO:0000269|PubMed:19543284}.
uniprot
proteins
mass_dalton
43201
uniprot
proteins
mutagenesis
MUTAGEN 44; /note="T->A: No effect on L-selectin binding nor neutrophil rolling."; /evidence="ECO:0000269|PubMed:12403782"; MUTAGEN 46..52; /note="YEYLDYD->FEFLDFE: No sulfation. Almost complete loss of P-selectin binding. No effect on E-selectin binding."; /evidence="ECO:0000269|PubMed:7585949"; MUTAGEN 46..51; /note="YEYLDY->FEFLDF: No sulfation. Almost complete loss of P-selectin binding. No effect on E-selectin binding."; MUTAGEN 46; /note="Y->F: Binding L-selectin reduced by 20%, neutrophil recruitment reduced by 30%, and lymphocyte rolling reduced by 32%; when associated with F-48. Binding L-selectin reduced by 86%, neutrophil recruitment reduced by 75%, and lymphocyte rolling reduced by 69%; when associated with F-51. Binding L-selectin reduced by 89%, and neutrophil recruitment reduced by 90%; when associated with F-48 and F-51. Binding of L-selectin reduced by 91%; when associated with F-48; F-51 and A-57."; /evidence="ECO:0000269|PubMed:7585950"; MUTAGEN 48; /note="Y->F: Binding L-selectin reduced by 20%, neutrophil recruitment reduced by 30%, and lymphocyte rolling reduced by 32%; when associated with F-46. Binding L-lectin reduced by 31%, neutrophil recruitment reduced by 52%, and lymphocyte rolling reduced by 52%; when associated with F-51. Binding L-selectin reduced by 89%, and neutrophil recruitment reduced by 90%; when associated with F-46 and F-51. Binding of L-selectin reduced by 91%; when associated with F-46; F-51 and A-57."; /evidence="ECO:0000269|PubMed:12403782, ECO:0000269|PubMed:7585950"; MUTAGEN 51; /note="Y->F: Binding L-selectin reduced by 86%, neutrophil recruitment reduced by 75% and, lymphocyte rolling reduced by 69%; when associated with F-46. Binding L-selectin reduced by 31%, neutrophil recruitment reduced by 52%, and lymphocyte rolling reduced by 52%; when associated with F-48; Binding L-selectin reduced by 89%, and neutrophil recruitment reduced by 90%; when associated with F-46 and F-48. Binding of L-selectin reduced by 91%; when associated with F-46; F-48 and A-57."; /evidence="ECO:0000269|PubMed:12403782, ECO:0000269|PubMed:7585950"; MUTAGEN 57; /note="T->A: No E- nor P-selectin binding, and very little neutrophil rolling. Binding of L-selectin reduced by 91%; when associated with F-46; F-48 and F-51."; /evidence="ECO:0000269|PubMed:12403782, ECO:0000269|PubMed:7585950"; MUTAGEN 320; /note="C->A,S: No dimer formation. No effect on P-selectin binding."; /evidence="ECO:0000269|PubMed:10713099
uniprot
proteins
post_translational_modification
PTM: Displays complex, core-2, sialylated and fucosylated O-linked oligosaccharides, at least some of which appear to contain poly-N-acetyllactosamine with varying degrees of substitution. Mainly disialylated or neutral forms of the core-2 tetrasaccharide, Galbeta1-->4GlcNAcbeta1-->6(Galbeta1-->3)GalNAcOH. The GlcN:GalN ratio is approximately 2:1 and the Man:Fuc ratio 3:5. Contains about 14% fucose with alpha-1,3 linkage present in two forms: One species is a disialylated, monofucosylated glycan, and the other, a monosialylated, trifucosylated glycan with a polylactosamine backbone. The fucosylated forms carry the Lewis antigen and are important for interaction with selectins and for functioning in leukocyte rolling. The modification containing the sialyl Lewis X glycan is on Thr-57. No sulfated O-glycans. Some N-glycosylation. {ECO:0000269|PubMed:11081633, ECO:0000269|PubMed:12736247}.; PTM: Sulfation, in conjunction with the SLe(x)-containing glycan, is necessary for P- and L-selectin binding. High affinity P-selectin binding has a preferred requirement for the isomer sulfated on both Tyr-48 and Tyr-51, whereas L-selectin binding requires predominantly sulfation on Tyr-51 with sulfation on Tyr-48 playing only a minor role. These sulfations play an important role in L- and P-selectin-mediated neutrophil recruitment, and leukocyte rolling. {ECO:0000269|PubMed:11081633}.
uniprot
proteins
pubmed
10713099
uniprot
proteins
pubmed
11081633
uniprot
proteins
pubmed
11566773
uniprot
proteins
pubmed
12387735
uniprot
proteins
pubmed
12403782
uniprot
proteins
pubmed
12736247
uniprot
proteins
pubmed
14702039
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
16541075
uniprot
proteins
pubmed
17132726
uniprot
proteins
pubmed
18045383
uniprot
proteins
pubmed
18196517
uniprot
proteins
pubmed
18669648
uniprot
proteins
pubmed
19543284
uniprot
proteins
pubmed
23186163
uniprot
proteins
pubmed
24703780
uniprot
proteins
pubmed
25102098
uniprot
proteins
pubmed
7505206
uniprot
proteins
pubmed
7521878
uniprot
proteins
pubmed
7541799
uniprot
proteins
pubmed
7559387
uniprot
proteins
pubmed
7585949
uniprot
proteins
pubmed
7585950
uniprot
proteins
pubmed
8702529
uniprot
proteins
sequence_length
412
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane protein.
uniprot
proteins
transmembrane_region
TRANSMEM 321..341; /note="Helical"; /evidence="ECO:0000255
uniprot
proteins