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P-selectin glycoprotein ligand 1 (PSGL-1) (Selectin P ligand) (CD antigen CD162)

 SELPL_MOUSE             Reviewed;         397 AA.
Q62170;
01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
27-JUL-2011, sequence version 2.
30-AUG-2017, entry version 127.
RecName: Full=P-selectin glycoprotein ligand 1;
Short=PSGL-1;
AltName: Full=Selectin P ligand;
AltName: CD_antigen=CD162;
Flags: Precursor;
Name=Selplg; Synonyms=Selp1, Selpl;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], INTERACTION WITH SELE AND
SELP, AND TISSUE SPECIFICITY.
STRAIN=BALB/cJ;
PubMed=8639776;
Yang J., Galipeau J., Kozak C., Furie B.C., Furie B.;
"Mouse P-selectin glycoprotein ligand-1: molecular cloning,
chromosomal localization, and expression of a functional P-selectin
receptor.";
Blood 87:4176-4186(1996).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=C57BL/6J;
PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
Lindblad-Toh K., Eichler E.E., Ponting C.P.;
"Lineage-specific biology revealed by a finished genome assembly of
the mouse.";
PLoS Biol. 7:E1000112-E1000112(2009).
[3]
INTERACTION WITH SELE AND SELP, AND FUNCTION.
PubMed=11104809; DOI=10.1084/jem.192.11.1669;
Hirata T., Merrill-Skoloff G., Aab M., Yang J., Furie B.C., Furie B.;
"P-Selectin glycoprotein ligand 1 (PSGL-1) is a physiological ligand
for E-selectin in mediating T helper 1 lymphocyte migration.";
J. Exp. Med. 192:1669-1676(2000).
[4]
FUNCTION.
PubMed=12370362; DOI=10.4049/jimmunol.169.8.4307;
Hirata T., Furie B.C., Furie B.;
"P-, E-, and L-selectin mediate migration of activated CD8+ T
lymphocytes into inflamed skin.";
J. Immunol. 169:4307-4313(2002).
[5]
INTERACTION WITH SELP, SULFATION AT TYR-54, AND MUTAGENESIS OF TYR-54;
THR-55; TYR-56 AND THR-58.
PubMed=12393631; DOI=10.1182/blood-2001-11-0036;
Xia L., Ramachandran V., McDaniel J.M., Nguyen K.N., Cummings R.D.,
McEver R.P.;
"N-terminal residues in murine P-selectin glycoprotein ligand-1
required for binding to murine P-selectin.";
Blood 101:552-559(2003).
[6]
FUNCTION.
PubMed=17442598; DOI=10.1016/j.immuni.2007.03.011;
Hidalgo A., Peired A.J., Wild M.K., Vestweber D., Frenette P.S.;
"Complete identification of E-selectin ligands on neutrophils reveals
distinct functions of PSGL-1, ESL-1, and CD44.";
Immunity 26:477-489(2007).
[7]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
Thibault P.;
"The phagosomal proteome in interferon-gamma-activated macrophages.";
Immunity 30:143-154(2009).
[8]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Lung;
PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
"A tissue-specific atlas of mouse protein phosphorylation and
expression.";
Cell 143:1174-1189(2010).
-!- 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}.
-!- SUBUNIT: Homodimer; disulfide-linked. Interacts with P- and E-
selectins, through their lectin/EGF domains. Interaction with P-
selectin requires sialyl Lewis X glycan modification and tyrosine
sulfation, probably on Tyr-54, for high affinity binding (By
similarity). Dimerization appears not to be required for P-
selectin/SELP binding (By similarity). Interacts with SNX20 (By
similarity). Interacts with MSN and SYK; mediates SYK activation
downstream of SELPLG (By similarity). {ECO:0000250}.
-!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Single-pass
membrane protein {ECO:0000305}.
-!- TISSUE SPECIFICITY: Highly expressed in blood, bone marrow, brain,
adipose tissue, spleen, and thymus. Also expressed in heart,
kidney, liver, muscle, ovary, and stomach.
{ECO:0000269|PubMed:8639776}.
-!- 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}.
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EMBL; X91144; CAA62583.1; -; mRNA.
EMBL; AC159240; -; NOT_ANNOTATED_CDS; Genomic_DNA.
UniGene; Mm.332590; -.
PDB; 2EMT; X-ray; 2.80 A; C/D/E=331-348.
PDBsum; 2EMT; -.
SMR; Q62170; -.
DIP; DIP-59330N; -.
STRING; 10090.ENSMUSP00000098436; -.
iPTMnet; Q62170; -.
PhosphoSitePlus; Q62170; -.
SwissPalm; Q62170; -.
EPD; Q62170; -.
PaxDb; Q62170; -.
PRIDE; Q62170; -.
MGI; MGI:106689; Selplg.
eggNOG; ENOG410JASD; Eukaryota.
eggNOG; ENOG410Y5S5; LUCA.
HOGENOM; HOG000013048; -.
HOVERGEN; HBG061628; -.
InParanoid; Q62170; -.
EvolutionaryTrace; Q62170; -.
PRO; PR:Q62170; -.
Proteomes; UP000000589; Unplaced.
CleanEx; MM_SELPLG; -.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0005886; C:plasma membrane; ISO:MGI.
GO; GO:0044853; C:plasma membrane raft; ISO:MGI.
GO; GO:0001931; C:uropod; ISO:MGI.
GO; GO:0050902; P:leukocyte adhesive activation; IMP:UniProtKB.
GO; GO:0050900; P:leukocyte migration; ISO:MGI.
GO; GO:0050901; P:leukocyte tethering or rolling; IMP:MGI.
1: Evidence at protein level;
3D-structure; Cell adhesion; Cell membrane;
Cleavage on pair of basic residues; Complete proteome; Disulfide bond;
Glycoprotein; Membrane; Phosphoprotein; Pyrrolidone carboxylic acid;
Reference proteome; Repeat; Sialic acid; Signal; Sulfation;
Transmembrane; Transmembrane helix.
SIGNAL 1 17 {ECO:0000255}.
PROPEP 18 41 {ECO:0000250}.
/FTId=PRO_0000022304.
CHAIN 42 397 P-selectin glycoprotein ligand 1.
/FTId=PRO_0000022305.
TOPO_DOM 18 307 Extracellular. {ECO:0000255}.
TRANSMEM 308 328 Helical. {ECO:0000255}.
TOPO_DOM 329 397 Cytoplasmic. {ECO:0000255}.
REPEAT 126 135 1.
REPEAT 136 145 2.
REPEAT 146 155 3.
REPEAT 156 165 4.
REPEAT 166 175 5.
REPEAT 176 185 6.
REPEAT 186 195 7.
REPEAT 196 205 8.
REPEAT 206 215 9.
REPEAT 216 225 10.
REGION 126 225 10 X 10 AA tandem repeats.
MOD_RES 42 42 Pyrrolidone carboxylic acid.
{ECO:0000250|UniProtKB:Q14242}.
MOD_RES 54 54 Sulfotyrosine.
{ECO:0000305|PubMed:12393631}.
MOD_RES 391 391 Phosphothreonine.
{ECO:0000250|UniProtKB:Q14242}.
MOD_RES 394 394 Phosphoserine.
{ECO:0000250|UniProtKB:Q14242}.
CARBOHYD 58 58 O-linked (GalNAc...) threonine.
{ECO:0000305}.
CARBOHYD 66 66 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 261 261 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 307 307 Interchain. {ECO:0000250}.
MUTAGEN 54 54 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.
{ECO:0000269|PubMed:12393631}.
MUTAGEN 55 55 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.
{ECO:0000269|PubMed:12393631}.
MUTAGEN 56 56 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.
{ECO:0000269|PubMed:12393631}.
MUTAGEN 58 58 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.
{ECO:0000269|PubMed:12393631}.
MUTAGEN 66 66 N->T: No effect on P-selectin binding;
when associated with A-261.
MUTAGEN 261 261 N->A: No effect on P-selectin binding;
when associated with T-66.
CONFLICT 173 173 E -> D (in Ref. 1; CAA62583).
{ECO:0000305}.
CONFLICT 176 176 Q -> K (in Ref. 1; CAA62583).
{ECO:0000305}.
CONFLICT 180 180 M -> T (in Ref. 1; CAA62583).
{ECO:0000305}.
CONFLICT 183 183 D -> E (in Ref. 1; CAA62583).
{ECO:0000305}.
CONFLICT 186 186 Q -> K (in Ref. 1; CAA62583).
{ECO:0000305}.
CONFLICT 190 190 M -> T (in Ref. 1; CAA62583).
{ECO:0000305}.
STRAND 337 342 {ECO:0000244|PDB:2EMT}.
SEQUENCE 397 AA; 41842 MW; D5EB53D493AE26EE CRC64;
MSPSFLVLLT ILGPGNSLQL QDPWGHETKE APGPVHLRER RQVVGDDDFE DPDYTYNTDP
PELLKNVTNT VAAHPELPTT VVMLERDSTS AGTSERATEK IATTDPTAPG TGGTAVGMLS
TDSATQWSLT SVETVQPAST EVETSQPAPM EAETSQPAPM EAETSQPAPM EAETSQPAPM
EADTSQPAPM EAETSQPAPN EAETSKPAPT EAETSKPAPT EAETTQLPRI QAVKTLFTTS
AATEVPSTEP TTMETASTES NESTIFLGPS VTHLPDSGLK KGLIVTPGNS PAPTLPGSSD
LIPVKQCLLI ILILASLATI FLVCTVVLAV RLSRKTHMYP VRNYSPTEMI CISSLLPEGG
DGAPVTANGG LPKVQDLKTE PSGDRDGDDL TLHSFLP


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