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P18337 (LYAM1_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 137. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
L-selectin
Alternative name(s):
CD62 antigen-like family member L
Leukocyte adhesion molecule 1
Short name=LAM-1
Leukocyte-endothelial cell adhesion molecule 1
Short name=LECAM1
Lymph node homing receptor
Lymphocyte antigen 22
Short name=Ly-22
Lymphocyte surface MEL-14 antigen
CD_antigen=CD62L
Gene names
Name:Sell
Synonyms:Lnhr, Ly-22, Ly22
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length372 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at transcript level

General annotation (Comments)

Function

Cell surface adhesion protein. Mediates the adherence of lymphocytes to endothelial cells of high endothelial venules in peripheral lymph nodes. Promotes initial tethering and rolling of leukocytes in endothelia By similarity. Ref.2

Subunit structure

Interaction with PSGL1/SELPLG and PODXL2 is required for promoting recruitment and rolling of leukocytes. This interaction is dependent on the sialyl Lewis X glycan modification of PSGL1 and PODXL2, and tyrosine sulfation modifications of PSGL1. Sulfation on 'Tyr-51' of PSGL1 is important for L-selectin binding By similarity.

Subcellular location

Membrane; Single-pass type I membrane protein.

Tissue specificity

Predominantly expressed in lymphoid tissue. Ref.1

Sequence similarities

Belongs to the selectin/LECAM family.

Contains 1 C-type lectin domain.

Contains 1 EGF-like domain.

Contains 2 Sushi (CCP/SCR) domains.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2828
Propeptide29 – 3810
PRO_0000017479
Chain39 – 372334L-selectin
PRO_0000017480

Regions

Topological domain39 – 332294Extracellular Potential
Transmembrane333 – 35523Helical; Potential
Topological domain356 – 37217Cytoplasmic Potential
Domain55 – 155101C-type lectin
Domain156 – 19237EGF-like
Domain195 – 25662Sushi 1
Domain257 – 31862Sushi 2

Amino acid modifications

Glycosylation601N-linked (GlcNAc...) Potential
Glycosylation1041N-linked (GlcNAc...) Potential
Glycosylation1771N-linked (GlcNAc...) Potential
Glycosylation2161N-linked (GlcNAc...) Potential
Glycosylation2261N-linked (GlcNAc...) Potential
Glycosylation2461N-linked (GlcNAc...) Potential
Glycosylation2781N-linked (GlcNAc...) Potential
Glycosylation2881N-linked (GlcNAc...) Potential
Glycosylation3081N-linked (GlcNAc...) Potential
Glycosylation3201N-linked (GlcNAc...) Potential
Disulfide bond57 ↔ 155 By similarity
Disulfide bond128 ↔ 147 By similarity
Disulfide bond160 ↔ 171 By similarity
Disulfide bond165 ↔ 180 By similarity
Disulfide bond182 ↔ 191 By similarity
Disulfide bond197 ↔ 241 By similarity
Disulfide bond227 ↔ 254 By similarity
Disulfide bond259 ↔ 303 By similarity
Disulfide bond289 ↔ 316 By similarity

Experimental info

Sequence conflict321I → T in AAA75651. Ref.5

Sequences

Sequence LengthMass (Da)Tools
P18337 [UniParc].

Last modified November 1, 1990. Version 1.
Checksum: 4433EDF6E4CB2B78

FASTA37242,288
        10         20         30         40         50         60 
MVFPWRCEGT YWGSRNILKL WVWTLLCCDF LIHHGTHCWT YHYSEKPMNW ENARKFCKQN 

        70         80         90        100        110        120 
YTDLVAIQNK REIEYLENTL PKSPYYYWIG IRKIGKMWTW VGTNKTLTKE AENWGAGEPN 

       130        140        150        160        170        180 
NKKSKEDCVE IYIKRERDSG KWNDDACHKR KAALCYTASC QPGSCNGRGE CVETINNHTC 

       190        200        210        220        230        240 
ICDAGYYGPQ CQYVVQCEPL EAPELGTMDC IHPLGNFSFQ SKCAFNCSEG RELLGTAETQ 

       250        260        270        280        290        300 
CGASGNWSSP EPICQVVQCE PLEAPELGTM DCIHPLGNFS FQSKCAFNCS EGRELLGTAE 

       310        320        330        340        350        360 
TQCGASGNWS SPEPICQETN RSFSKIKEGD YNPLFIPVAV MVTAFSGLAF LIWLARRLKK 

       370 
GKKSQERMDD PY 

« Hide

References

« Hide 'large scale' references
[1]"Mouse lymph node homing receptor cDNA clone encodes a glycoprotein revealing tandem interaction domains."
Siegelman M.H., van de Rijn M., Weissman I.L.
Science 243:1165-1172(1989) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY.
Tissue: Lymph node.
[2]"The mouse lymph node homing receptor is identical with the lymphocyte cell surface marker Ly-22: role of the EGF domain in endothelial binding."
Siegelman M.H., Cheng I.C., Weissman I.L., Wakeland E.K.
Cell 61:611-622(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION.
[3]"Cloning of a lymphocyte homing receptor reveals a lectin domain."
Lasky L.A., Singer M.S., Yednock T.A., Dowbenko D., Fennie C., Rodriguez H., Nguyen T., Stachel S., Rosen S.D.
Cell 56:1045-1055(1989) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Spleen.
[4]"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].
Strain: C57BL/6.
Tissue: Hematopoietic.
[5]"Characterization of the murine homing receptor gene reveals correspondence between protein domains and coding exons."
Dowbenko D.J., Diep A., Taylor B.A., Lusis A.J., Lasky L.A.
Genomics 9:270-277(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-360.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X14772 mRNA. Translation: CAA32880.1.
M36005 mRNA. Translation: AAA39722.1.
M36058 mRNA. Translation: AAA39723.1.
M25324 mRNA. Translation: AAA39431.1.
AH003204 Genomic DNA. Translation: AAA75651.1.
BC052681 mRNA. Translation: AAH52681.1.
PIRA32375.
RefSeqNP_035476.1. NM_011346.2.
UniGeneMm.1461.

3D structure databases

ProteinModelPortalP18337.
SMRP18337. Positions 39-318.
ModBaseSearch...
MobiDBSearch...

Chemistry

BindingDBP18337.
ChEMBLCHEMBL3162.

PTM databases

PhosphoSiteP18337.

Proteomic databases

PaxDbP18337.
PRIDEP18337.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000027871; ENSMUSP00000027871; ENSMUSG00000026581.
GeneID20343.
KEGGmmu:20343.
UCSCuc007dhy.2. mouse.

Organism-specific databases

CTD6402.
MGIMGI:98279. Sell.

Phylogenomic databases

eggNOGNOG258998.
HOVERGENHBG052375.
InParanoidP18337.
KOK06495.
OMAVAIQNKG.
PhylomeDBP18337.
TreeFamTF326910.

Gene expression databases

ArrayExpressP18337.
BgeeP18337.
CleanExMM_SELL.
GenevestigatorP18337.

Family and domain databases

Gene3D3.10.100.10. 1 hit.
InterProIPR001304. 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.
IPR013111. EGF_extracell.
IPR016348. L-selectin.
IPR002396. Selectin_superfamily.
IPR000436. Sushi_SCR_CCP.
[Graphical view]
PfamPF07974. EGF_2. 1 hit.
PF00059. Lectin_C. 1 hit.
PF00084. Sushi. 2 hits.
[Graphical view]
PIRSFPIRSF002421. L-selectin. 1 hit.
PRINTSPR00343. SELECTIN.
SMARTSM00032. CCP. 2 hits.
SM00034. CLECT. 1 hit.
SM00181. EGF. 1 hit.
[Graphical view]
SUPFAMSSF56436. SSF56436. 1 hit.
SSF57535. SSF57535. 2 hits.
PROSITEPS00615. 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. 2 hits.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSSELL. mouse.
NextBio298173.
PROP18337.
SOURCESearch...

Entry information

Entry nameLYAM1_MOUSE
AccessionPrimary (citable) accession number: P18337
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1990
Last sequence update: November 1, 1990
Last modified: April 16, 2014
This is version 137 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot