Q62170
uniprot
Q62170
canonical
amino_acid_sequence
MSPSFLVLLTILGPGNSLQLQDPWGHETKEAPGPVHLRERRQVVGDDDFEDPDYTYNTDPPELLKNVTNTVAAHPELPTTVVMLERDSTSAGTSERATEKIATTDPTAPGTGGTAVGMLSTDSATQWSLTSVETVQPASTEVETSQPAPMEAETSQPAPMEAETSQPAPMEAETSQPAPMEADTSQPAPMEAETSQPAPNEAETSKPAPTEAETSKPAPTEAETTQLPRIQAVKTLFTTSAATEVPSTEPTTMETASTESNESTIFLGPSVTHLPDSGLKKGLIVTPGNSPAPTLPGSSDLIPVKQCLLIILILASLATIFLVCTVVLAVRLSRKTHMYPVRNYSPTEMICISSLLPEGGDGAPVTANGGLPKVQDLKTEPSGDRDGDDLTLHSFLP
uniprot
proteins
function
FUNCTION: A SLe(x)-type proteoglycan, which through high affinity, calcium-dependent interactions with E- and P-selectins, mediates rapid rolling of leukocytes over vascular surfaces during the initial steps in inflammation. Critical for the initial leukocyte capture. {ECO:0000269|PubMed:11104809, ECO:0000269|PubMed:12370362, ECO:0000269|PubMed:17442598}.
uniprot
proteins
mass_dalton
41842
uniprot
proteins
mutagenesis
MUTAGEN 54; /note="Y->F: Greatly decreased P-selectin binding and tethering and rolling of cells. No further reduction of P-selectin binding; when associated with Y-56. Binding of P-selectin completely abolished; when associated with A-55; Y-56 and A-58."; /evidence="ECO:0000269|PubMed:12393631"; MUTAGEN 55; /note="T->A: No effect on P-selectin binding. Greatly reduced P-selectin binding and tethering and rolling of cells; when associated with A-58. Binding of P-selectin completely abolished; when associated with Y-54; Y-56 and A-58."; /evidence="ECO:0000269|PubMed:12393631"; MUTAGEN 56; /note="Y->F: No effect on P-selectin binding. Greatly decreased P-selectin binding and tethering and rolling of cells; when associated with Y-54. Binding of P-selectin completely abolished; when associated with Y-54; A-55 and A-58."; /evidence="ECO:0000269|PubMed:12393631"; MUTAGEN 58; /note="T->A: Greatly decreased P-selectin binding and tethering and rolling of cells. No further reduction in P-selectin binding when associated with A-55. Binding of P-selectin completely abolished; when associated with Y-54; A-55; and Y-56."; /evidence="ECO:0000269|PubMed:12393631"; MUTAGEN 66; /note="N->T: No effect on P-selectin binding; when associated with A-261."; MUTAGEN 261; /note="N->A: No effect on P-selectin binding; when associated with T-66.
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. No sulfated O-glycans. Some N-glycosylation (By similarity). {ECO:0000250}.
uniprot
proteins
pubmed
11104809
uniprot
proteins
pubmed
12370362
uniprot
proteins
pubmed
12393631
uniprot
proteins
pubmed
17442598
uniprot
proteins
pubmed
19144319
uniprot
proteins
pubmed
19468303
uniprot
proteins
pubmed
21183079
uniprot
proteins
pubmed
8639776
uniprot
proteins
sequence_length
397
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Single-pass membrane protein {ECO:0000305}.
uniprot
proteins
transmembrane_region
TRANSMEM 308..328; /note="Helical"; /evidence="ECO:0000255
uniprot
proteins