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Q01102

- LYAM3_MOUSE

UniProt

Q01102 - LYAM3_MOUSE

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Protein

P-selectin

Gene

Selp

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

Ca2+-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 PSGL1.1 Publication

GO - Molecular functioni

  1. calcium-dependent protein binding Source: MGI
  2. fucose binding Source: Ensembl
  3. glycoprotein binding Source: MGI
  4. heparin binding Source: Ensembl
  5. lipopolysaccharide binding Source: Ensembl
  6. oligosaccharide binding Source: Ensembl
  7. sialic acid binding Source: MGI

GO - Biological processi

  1. cellular response to interleukin-6 Source: MGI
  2. heterophilic cell-cell adhesion via plasma membrane cell adhesion molecules Source: MGI
  3. inflammatory response Source: MGI
  4. leukocyte cell-cell adhesion Source: MGI
  5. leukocyte migration Source: MGI
  6. leukocyte tethering or rolling Source: MGI
  7. positive regulation of leukocyte migration Source: MGI
  8. positive regulation of phosphatidylinositol 3-kinase signaling Source: UniProtKB
  9. positive regulation of platelet activation Source: BHF-UCL
  10. regulation of integrin activation Source: UniProtKB
Complete GO annotation...

Keywords - Biological processi

Cell adhesion

Keywords - Ligandi

Lectin

Enzyme and pathway databases

ReactomeiREACT_225233. Cell surface interactions at the vascular wall.

Names & Taxonomyi

Protein namesi
Recommended name:
P-selectin
Alternative name(s):
CD62 antigen-like family member P
Granule membrane protein 140
Short name:
GMP-140
Leukocyte-endothelial cell adhesion molecule 3
Short name:
LECAM3
Platelet activation dependent granule-external membrane protein
Short name:
PADGEM
CD_antigen: CD62P
Gene namesi
Name:Selp
Synonyms:Grmp
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 1

Organism-specific databases

MGIiMGI:98280. Selp.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini42 – 709668ExtracellularSequence AnalysisAdd
BLAST
Transmembranei710 – 73324HelicalSequence AnalysisAdd
BLAST
Topological domaini734 – 76835CytoplasmicSequence AnalysisAdd
BLAST

GO - Cellular componenti

  1. external side of plasma membrane Source: MGI
  2. extracellular space Source: Ensembl
  3. integral component of membrane Source: UniProtKB-KW
  4. membrane Source: MGI
  5. nucleus Source: Ensembl
  6. platelet alpha granule membrane Source: Ensembl
Complete GO annotation...

Keywords - Cellular componenti

Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 4141Sequence AnalysisAdd
BLAST
Chaini42 – 768727P-selectinPRO_0000017499Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi60 ↔ 158By similarity
Disulfide bondi131 ↔ 150By similarity
Disulfide bondi163 ↔ 174By similarity
Disulfide bondi168 ↔ 183By similarity
Disulfide bondi185 ↔ 194By similarity
Disulfide bondi200 ↔ 244By similarity
Disulfide bondi230 ↔ 257By similarity
Disulfide bondi262 ↔ 306By similarity
Disulfide bondi292 ↔ 319By similarity
Disulfide bondi324 ↔ 368By similarity
Disulfide bondi354 ↔ 381By similarity
Disulfide bondi386 ↔ 430By similarity
Glycosylationi398 – 3981N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi416 ↔ 443By similarity
Disulfide bondi448 ↔ 492By similarity
Disulfide bondi478 ↔ 505By similarity
Disulfide bondi510 ↔ 554By similarity
Disulfide bondi540 ↔ 567By similarity
Disulfide bondi580 ↔ 624By similarity
Glycosylationi603 – 6031N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi610 ↔ 637By similarity
Disulfide bondi642 ↔ 686By similarity
Glycosylationi654 – 6541N-linked (GlcNAc...)Sequence Analysis
Glycosylationi661 – 6611N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi672 ↔ 699By similarity
Glycosylationi679 – 6791N-linked (GlcNAc...)Sequence Analysis
Lipidationi745 – 7451S-palmitoyl cysteineBy similarity

Keywords - PTMi

Disulfide bond, Glycoprotein, Lipoprotein, Palmitate

Proteomic databases

PRIDEiQ01102.

PTM databases

PhosphoSiteiQ01102.

Expressioni

Tissue specificityi

Stored in the alpha-granules of platelets and Weibel-Palade bodies of endothelial cells. Upon cell activation by agonists, P-selectin is transported rapidly to the cell surface.

Inductioni

By TNF-alpha. Induced expression in lung, liver, kidney and heart after endotoxin treatment.2 Publications

Gene expression databases

BgeeiQ01102.
CleanExiMM_SELP.
GenevestigatoriQ01102.

Interactioni

Subunit structurei

Interacts with SNX17. Interacts with PSGL1/SEPL and PODXL2 and mediates neutrophil adhesion and leukocyte rolling. This interaction requires the sialyl-Lewis X epitope of PSGL1 and PODXL2, and specific tyrosine sulfation on PSGL1 (By similarity).By similarity

Structurei

Secondary structure

1
768
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi756 – 7605Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4GXBX-ray1.80B735-768[»]
ProteinModelPortaliQ01102.
SMRiQ01102. Positions 42-701.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini58 – 158101C-type lectinPROSITE-ProRule annotationAdd
BLAST
Domaini159 – 19537EGF-likePROSITE-ProRule annotationAdd
BLAST
Domaini198 – 25962Sushi 1PROSITE-ProRule annotationAdd
BLAST
Domaini260 – 32162Sushi 2PROSITE-ProRule annotationAdd
BLAST
Domaini322 – 38362Sushi 3PROSITE-ProRule annotationAdd
BLAST
Domaini384 – 44562Sushi 4PROSITE-ProRule annotationAdd
BLAST
Domaini446 – 50762Sushi 5PROSITE-ProRule annotationAdd
BLAST
Domaini508 – 56962Sushi 6PROSITE-ProRule annotationAdd
BLAST
Domaini578 – 63962Sushi 7PROSITE-ProRule annotationAdd
BLAST
Domaini640 – 70162Sushi 8PROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni759 – 76810Interaction with SNX17By similarity

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi756 – 7594Endocytosis signalCurated

Sequence similaritiesi

Belongs to the selectin/LECAM family.Curated
Contains 1 C-type lectin domain.PROSITE-ProRule annotation
Contains 1 EGF-like domain.PROSITE-ProRule annotation
Contains 8 Sushi (CCP/SCR) domains.PROSITE-ProRule annotation

Keywords - Domaini

EGF-like domain, Repeat, Signal, Sushi, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiNOG242963.
GeneTreeiENSGT00760000118803.
HOGENOMiHOG000236254.
HOVERGENiHBG052375.
InParanoidiQ01102.
KOiK06496.
OMAiTYGVFTN.
OrthoDBiEOG7DZ8J9.
PhylomeDBiQ01102.
TreeFamiTF326910.

Family and domain databases

Gene3Di3.10.100.10. 1 hit.
InterProiIPR001304. C-type_lectin.
IPR016186. C-type_lectin-like.
IPR018378. C-type_lectin_CS.
IPR016187. C-type_lectin_fold.
IPR000742. EG-like_dom.
IPR013032. EGF-like_CS.
IPR002396. Selectin_superfamily.
IPR000436. Sushi_SCR_CCP.
[Graphical view]
PfamiPF00008. EGF. 1 hit.
PF00059. Lectin_C. 1 hit.
PF00084. Sushi. 8 hits.
[Graphical view]
PRINTSiPR00343. SELECTIN.
SMARTiSM00032. CCP. 8 hits.
SM00034. CLECT. 1 hit.
SM00181. EGF. 1 hit.
[Graphical view]
SUPFAMiSSF56436. SSF56436. 1 hit.
SSF57535. SSF57535. 8 hits.
PROSITEiPS00615. C_TYPE_LECTIN_1. 1 hit.
PS50041. C_TYPE_LECTIN_2. 1 hit.
PS00022. EGF_1. 1 hit.
PS01186. EGF_2. 1 hit.
PS50026. EGF_3. 1 hit.
PS50923. SUSHI. 8 hits.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q01102-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MAGCPKGSWT PRLRSVILGG AQLIWFSALI SELVNQKEVA AWTYNYSTKA
60 70 80 90 100
YSWNNSRVFC RRHFTDLVAI QNKNEIAHLN DVIPFFNSYY WIGIRKINNK
110 120 130 140 150
WTWVGTNKTL TEEAENWADN EPNNKKNNQD CVEIYIKSNS APGKWNDEPC
160 170 180 190 200
FKRKRALCYT ASCQDMSCSN QGECIETIGS YTCSCYPGFY GPECEYVKEC
210 220 230 240 250
GKVNIPQHVL MNCSHPLGEF SFNSQCTFSC AEGYELDGPG ELQCLASGIW
260 270 280 290 300
TNNPPKCDAV QCQSLEAPPH GTMACMHPIA AFAYDSSCKF ECQPGYRARG
310 320 330 340 350
SNTLHCTGSG QWSEPLPTCE AIACEPPEIP IHGSMDCVPS TGTFGYNSSC
360 370 380 390 400
TFLCAEGFVL KGNDAIQCAD SGQWTAPAPF CEALQCPEFP VPSKAQVNCS
410 420 430 440 450
DPFGTLTYQS VCSFSCDEGS LLVGASVIRC LATGHWNGAP PECQAVSCAP
460 470 480 490 500
MLSPENGSMT CVQPLGNSTY KSTCQFMCDE GFYLSGPERL DCSPSGHWTG
510 520 530 540 550
TPPTCEAIKC PGIFAPEQGN LDCSHVHGEF GVGSICHFSC NEDFELLGSE
560 570 580 590 600
NVECTVSGRW SAPPPTCKGI TSLPAPAVRC PALTTPGQGT MSCQHHLGSF
610 620 630 640 650
GPNTTCYFGC KTGFTLRGAN SLRCRASGQW TAVTPMCRAV KCSELHMDTA
660 670 680 690 700
VAMNCSNPWG NFSYGSTCTF QCPEGQSLNG SVRATCREDG HWSDAMPTCQ
710 720 730 740 750
AGTLTIQEAL TYLGGAVAST TGLAVGGTLL ALLRKRLRKK DDGKCPLNPH
760
SHLGTYGVFT NAAYDPTP
Length:768
Mass (Da):83,099
Last modified:April 1, 1993 - v1
Checksum:iE5173074D2F66E68
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti724 – 7241A → E in AAA37712. (PubMed:1379089)Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M87861 mRNA. Translation: AAA40008.1.
M72332 mRNA. Translation: AAA37712.1.
BC109158 mRNA. Translation: AAI09159.1.
BC109159 mRNA. Translation: AAI09160.1.
CCDSiCCDS48422.1.
PIRiA42755.
RefSeqiNP_035477.1. NM_011347.2.
UniGeneiMm.3337.

Genome annotation databases

EnsembliENSMUST00000162746; ENSMUSP00000123924; ENSMUSG00000026580.
GeneIDi20344.
KEGGimmu:20344.
UCSCiuc007dhz.2. mouse.

Cross-referencesi

Web resourcesi

Functional Glycomics Gateway - Glycan Binding

P-selectin

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M87861 mRNA. Translation: AAA40008.1 .
M72332 mRNA. Translation: AAA37712.1 .
BC109158 mRNA. Translation: AAI09159.1 .
BC109159 mRNA. Translation: AAI09160.1 .
CCDSi CCDS48422.1.
PIRi A42755.
RefSeqi NP_035477.1. NM_011347.2.
UniGenei Mm.3337.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
4GXB X-ray 1.80 B 735-768 [» ]
ProteinModelPortali Q01102.
SMRi Q01102. Positions 42-701.
ModBasei Search...
MobiDBi Search...

Chemistry

BindingDBi Q01102.
ChEMBLi CHEMBL2455.

PTM databases

PhosphoSitei Q01102.

Proteomic databases

PRIDEi Q01102.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000162746 ; ENSMUSP00000123924 ; ENSMUSG00000026580 .
GeneIDi 20344.
KEGGi mmu:20344.
UCSCi uc007dhz.2. mouse.

Organism-specific databases

CTDi 6403.
MGIi MGI:98280. Selp.

Phylogenomic databases

eggNOGi NOG242963.
GeneTreei ENSGT00760000118803.
HOGENOMi HOG000236254.
HOVERGENi HBG052375.
InParanoidi Q01102.
KOi K06496.
OMAi TYGVFTN.
OrthoDBi EOG7DZ8J9.
PhylomeDBi Q01102.
TreeFami TF326910.

Enzyme and pathway databases

Reactomei REACT_225233. Cell surface interactions at the vascular wall.

Miscellaneous databases

NextBioi 298177.
PROi Q01102.
SOURCEi Search...

Gene expression databases

Bgeei Q01102.
CleanExi MM_SELP.
Genevestigatori Q01102.

Family and domain databases

Gene3Di 3.10.100.10. 1 hit.
InterProi IPR001304. C-type_lectin.
IPR016186. C-type_lectin-like.
IPR018378. C-type_lectin_CS.
IPR016187. C-type_lectin_fold.
IPR000742. EG-like_dom.
IPR013032. EGF-like_CS.
IPR002396. Selectin_superfamily.
IPR000436. Sushi_SCR_CCP.
[Graphical view ]
Pfami PF00008. EGF. 1 hit.
PF00059. Lectin_C. 1 hit.
PF00084. Sushi. 8 hits.
[Graphical view ]
PRINTSi PR00343. SELECTIN.
SMARTi SM00032. CCP. 8 hits.
SM00034. CLECT. 1 hit.
SM00181. EGF. 1 hit.
[Graphical view ]
SUPFAMi SSF56436. SSF56436. 1 hit.
SSF57535. SSF57535. 8 hits.
PROSITEi PS00615. C_TYPE_LECTIN_1. 1 hit.
PS50041. C_TYPE_LECTIN_2. 1 hit.
PS00022. EGF_1. 1 hit.
PS01186. EGF_2. 1 hit.
PS50026. EGF_3. 1 hit.
PS50923. SUSHI. 8 hits.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Cloning of the mouse endothelial selectins. Expression of both E- and P-selectin is inducible by tumor necrosis factor alpha."
    Weller A., Isenmann S., Vestweber D.
    J. Biol. Chem. 267:15176-15183(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], INDUCTION.
  2. "Molecular cloning and analysis of in vivo expression of murine P-selectin."
    Sanders W.E. Jr., Wilson R.W., Ballantyne C.M., Beaudet A.L.
    Blood 80:795-800(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], INDUCTION.
  3. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
  4. "P-, E-, and L-selectin mediate migration of activated CD8+ T lymphocytes into inflamed skin."
    Hirata T., Furie B.C., Furie B.
    J. Immunol. 169:4307-4313(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  5. "N-terminal residues in murine P-selectin glycoprotein ligand-1 required for binding to murine P-selectin."
    Xia L., Ramachandran V., McDaniel J.M., Nguyen K.N., Cummings R.D., McEver R.P.
    Blood 101:552-559(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH SELPLG.

Entry informationi

Entry nameiLYAM3_MOUSE
AccessioniPrimary (citable) accession number: Q01102
Secondary accession number(s): Q32MF1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 1, 1993
Last sequence update: April 1, 1993
Last modified: November 26, 2014
This is version 143 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3