SELPL_MOUSE
ID SELPL_MOUSE Reviewed; 397 AA.
AC Q62170;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 2.
DT 25-MAY-2022, entry version 140.
DE RecName: Full=P-selectin glycoprotein ligand 1;
DE Short=PSGL-1;
DE AltName: Full=Selectin P ligand;
DE AltName: CD_antigen=CD162;
DE Flags: Precursor;
GN Name=Selplg; Synonyms=Selp1, Selpl;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], INTERACTION WITH SELE AND SELP,
RP AND TISSUE SPECIFICITY.
RC STRAIN=BALB/cJ;
RX PubMed=8639776;
RA Yang J., Galipeau J., Kozak C., Furie B.C., Furie B.;
RT "Mouse P-selectin glycoprotein ligand-1: molecular cloning, chromosomal
RT localization, and expression of a functional P-selectin receptor.";
RL Blood 87:4176-4186(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [3]
RP INTERACTION WITH SELE AND SELP, AND FUNCTION.
RX PubMed=11104809; DOI=10.1084/jem.192.11.1669;
RA Hirata T., Merrill-Skoloff G., Aab M., Yang J., Furie B.C., Furie B.;
RT "P-Selectin glycoprotein ligand 1 (PSGL-1) is a physiological ligand for E-
RT selectin in mediating T helper 1 lymphocyte migration.";
RL J. Exp. Med. 192:1669-1676(2000).
RN [4]
RP FUNCTION.
RX PubMed=12370362; DOI=10.4049/jimmunol.169.8.4307;
RA Hirata T., Furie B.C., Furie B.;
RT "P-, E-, and L-selectin mediate migration of activated CD8+ T lymphocytes
RT into inflamed skin.";
RL J. Immunol. 169:4307-4313(2002).
RN [5]
RP INTERACTION WITH SELP, SULFATION AT TYR-54, AND MUTAGENESIS OF TYR-54;
RP THR-55; TYR-56 AND THR-58.
RX PubMed=12393631; DOI=10.1182/blood-2001-11-0036;
RA Xia L., Ramachandran V., McDaniel J.M., Nguyen K.N., Cummings R.D.,
RA McEver R.P.;
RT "N-terminal residues in murine P-selectin glycoprotein ligand-1 required
RT for binding to murine P-selectin.";
RL Blood 101:552-559(2003).
RN [6]
RP FUNCTION.
RX PubMed=17442598; DOI=10.1016/j.immuni.2007.03.011;
RA Hidalgo A., Peired A.J., Wild M.K., Vestweber D., Frenette P.S.;
RT "Complete identification of E-selectin ligands on neutrophils reveals
RT distinct functions of PSGL-1, ESL-1, and CD44.";
RL Immunity 26:477-489(2007).
RN [7]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA Thibault P.;
RT "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL Immunity 30:143-154(2009).
RN [8]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Lung;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
CC -!- FUNCTION: A SLe(x)-type proteoglycan, which through high affinity,
CC calcium-dependent interactions with E- and P-selectins, mediates rapid
CC rolling of leukocytes over vascular surfaces during the initial steps
CC in inflammation. Critical for the initial leukocyte capture.
CC {ECO:0000269|PubMed:11104809, ECO:0000269|PubMed:12370362,
CC ECO:0000269|PubMed:17442598}.
CC -!- SUBUNIT: Homodimer; disulfide-linked. Interacts with P- and E-
CC selectins, through their lectin/EGF domains. Interaction with P-
CC selectin requires sialyl Lewis X glycan modification and tyrosine
CC sulfation, probably on Tyr-54, for high affinity binding (By
CC similarity). Dimerization appears not to be required for P-
CC selectin/SELP binding (By similarity). Interacts with SNX20 (By
CC similarity). Interacts with MSN and SYK; mediates SYK activation
CC downstream of SELPLG (By similarity). Interacts with HAVCR1 (By
CC similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Single-pass membrane
CC protein {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Highly expressed in blood, bone marrow, brain,
CC adipose tissue, spleen, and thymus. Also expressed in heart, kidney,
CC liver, muscle, ovary, and stomach. {ECO:0000269|PubMed:8639776}.
CC -!- PTM: Displays complex, core-2, sialylated and fucosylated O-linked
CC oligosaccharides, at least some of which appear to contain poly-N-
CC acetyllactosamine with varying degrees of substitution. Mainly
CC disialylated or neutral forms of the core-2 tetrasaccharide,
CC Galbeta1-->4GlcNAcbeta1-->6(Galbeta1-->3)GalNAcOH. The GlcN:GalN ratio
CC is approximately 2:1 and the Man:Fuc ratio 3:5. Contains about 14%
CC fucose with alpha-1,3 linkage present in two forms: One species is a
CC disialylated, monofucosylated glycan, and the other, a monosialylated,
CC trifucosylated glycan with a polylactosamine backbone. The fucosylated
CC forms carry the Lewis antigen and are important for interaction with
CC selectins and for functioning. No sulfated O-glycans. Some N-
CC glycosylation (By similarity). {ECO:0000250}.
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DR EMBL; X91144; CAA62583.1; -; mRNA.
DR EMBL; AC159240; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR PDB; 2EMT; X-ray; 2.80 A; C/D/E=331-348.
DR PDBsum; 2EMT; -.
DR AlphaFoldDB; Q62170; -.
DR SMR; Q62170; -.
DR DIP; DIP-59330N; -.
DR IntAct; Q62170; 1.
DR STRING; 10090.ENSMUSP00000098436; -.
DR GlyGen; Q62170; 3 sites.
DR iPTMnet; Q62170; -.
DR PhosphoSitePlus; Q62170; -.
DR SwissPalm; Q62170; -.
DR EPD; Q62170; -.
DR jPOST; Q62170; -.
DR PaxDb; Q62170; -.
DR PRIDE; Q62170; -.
DR ProteomicsDB; 256942; -.
DR MGI; MGI:106689; Selplg.
DR eggNOG; KOG4818; Eukaryota.
DR InParanoid; Q62170; -.
DR Reactome; R-MMU-202733; Cell surface interactions at the vascular wall.
DR ChiTaRS; Selplg; mouse.
DR EvolutionaryTrace; Q62170; -.
DR PRO; PR:Q62170; -.
DR Proteomes; UP000000589; Unplaced.
DR RNAct; Q62170; protein.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; ISO:MGI.
DR GO; GO:0044853; C:plasma membrane raft; ISO:MGI.
DR GO; GO:0001931; C:uropod; ISO:MGI.
DR GO; GO:0030097; P:hemopoiesis; IBA:GO_Central.
DR GO; GO:0050902; P:leukocyte adhesive activation; IMP:UniProtKB.
DR GO; GO:0050900; P:leukocyte migration; ISO:MGI.
DR GO; GO:0050901; P:leukocyte tethering or rolling; IMP:MGI.
DR IDEAL; IID50120; -.
DR InterPro; IPR026195; PSGL-1.
DR PANTHER; PTHR17384; PTHR17384; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cell adhesion; Cell membrane;
KW Cleavage on pair of basic residues; Disulfide bond; Glycoprotein; Membrane;
KW Phosphoprotein; Reference proteome; Repeat; Sialic acid; Signal; Sulfation;
KW Transmembrane; Transmembrane helix.
FT SIGNAL 1..17
FT /evidence="ECO:0000255"
FT PROPEP 18..41
FT /evidence="ECO:0000250"
FT /id="PRO_0000022304"
FT CHAIN 42..397
FT /note="P-selectin glycoprotein ligand 1"
FT /id="PRO_0000022305"
FT TOPO_DOM 18..307
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 308..328
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 329..397
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REPEAT 126..135
FT /note="1"
FT REPEAT 136..145
FT /note="2"
FT REPEAT 146..155
FT /note="3"
FT REPEAT 156..165
FT /note="4"
FT REPEAT 166..175
FT /note="5"
FT REPEAT 176..185
FT /note="6"
FT REPEAT 186..195
FT /note="7"
FT REPEAT 196..205
FT /note="8"
FT REPEAT 206..215
FT /note="9"
FT REPEAT 216..225
FT /note="10"
FT REGION 89..261
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 126..225
FT /note="10 X 10 AA tandem repeats"
FT REGION 364..390
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 54
FT /note="Sulfotyrosine"
FT /evidence="ECO:0000305|PubMed:12393631"
FT MOD_RES 391
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q14242"
FT MOD_RES 394
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q14242"
FT CARBOHYD 58
FT /note="O-linked (GalNAc...) threonine"
FT /evidence="ECO:0000305"
FT CARBOHYD 66
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 261
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 307
FT /note="Interchain"
FT /evidence="ECO:0000250"
FT MUTAGEN 54
FT /note="Y->F: Greatly decreased P-selectin binding and
FT tethering and rolling of cells. No further reduction of P-
FT selectin binding; when associated with Y-56. Binding of P-
FT selectin completely abolished; when associated with A-55;
FT Y-56 and A-58."
FT /evidence="ECO:0000269|PubMed:12393631"
FT MUTAGEN 55
FT /note="T->A: No effect on P-selectin binding. Greatly
FT reduced P-selectin binding and tethering and rolling of
FT cells; when associated with A-58. Binding of P-selectin
FT completely abolished; when associated with Y-54; Y-56 and
FT A-58."
FT /evidence="ECO:0000269|PubMed:12393631"
FT MUTAGEN 56
FT /note="Y->F: No effect on P-selectin binding. Greatly
FT decreased P-selectin binding and tethering and rolling of
FT cells; when associated with Y-54. Binding of P-selectin
FT completely abolished; when associated with Y-54; A-55 and
FT A-58."
FT /evidence="ECO:0000269|PubMed:12393631"
FT MUTAGEN 58
FT /note="T->A: Greatly decreased P-selectin binding and
FT tethering and rolling of cells. No further reduction in P-
FT selectin binding when associated with A-55. Binding of P-
FT selectin completely abolished; when associated with Y-54;
FT A-55; and Y-56."
FT /evidence="ECO:0000269|PubMed:12393631"
FT MUTAGEN 66
FT /note="N->T: No effect on P-selectin binding; when
FT associated with A-261."
FT MUTAGEN 261
FT /note="N->A: No effect on P-selectin binding; when
FT associated with T-66."
FT CONFLICT 173
FT /note="E -> D (in Ref. 1; CAA62583)"
FT /evidence="ECO:0000305"
FT CONFLICT 176
FT /note="Q -> K (in Ref. 1; CAA62583)"
FT /evidence="ECO:0000305"
FT CONFLICT 180
FT /note="M -> T (in Ref. 1; CAA62583)"
FT /evidence="ECO:0000305"
FT CONFLICT 183
FT /note="D -> E (in Ref. 1; CAA62583)"
FT /evidence="ECO:0000305"
FT CONFLICT 186
FT /note="Q -> K (in Ref. 1; CAA62583)"
FT /evidence="ECO:0000305"
FT CONFLICT 190
FT /note="M -> T (in Ref. 1; CAA62583)"
FT /evidence="ECO:0000305"
FT STRAND 337..342
FT /evidence="ECO:0007829|PDB:2EMT"
SQ 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
