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L-selectin (CD62 antigen-like family member L) (Leukocyte adhesion molecule 1) (LAM-1) (Leukocyte-endothelial cell adhesion molecule 1) (LECAM1) (Lymph node homing receptor) (CD antigen CD62L)

 LYAM1_MACMU             Reviewed;         372 AA.
Q95198;
01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
01-FEB-1997, sequence version 1.
31-JAN-2018, entry version 109.
RecName: Full=L-selectin;
AltName: Full=CD62 antigen-like family member L;
AltName: Full=Leukocyte adhesion molecule 1;
Short=LAM-1;
AltName: Full=Leukocyte-endothelial cell adhesion molecule 1;
Short=LECAM1;
AltName: Full=Lymph node homing receptor;
AltName: CD_antigen=CD62L;
Flags: Precursor;
Name=SELL;
Macaca mulatta (Rhesus macaque).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Cercopithecidae; Cercopithecinae; Macaca.
NCBI_TaxID=9544;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
Budman J.I., Fu H., Johnson C.E., Thakur A.B., Berg E.L.,
Tsurushita N.;
"Cloning of the cDNA encoding L-selectin from nonhuman primates.";
Submitted (NOV-1996) to the EMBL/GenBank/DDBJ databases.
-!- FUNCTION: Calcium-dependent lectin that mediates cell adhesion by
binding to glycoproteins on neighboring cells. 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.
{ECO:0000250|UniProtKB:P14151}.
-!- SUBUNIT: Interaction with SELPLG/PSGL1 and PODXL2 is required for
promoting recruitment and rolling of leukocytes. This interaction
is dependent on the sialyl Lewis X glycan modification of SELPLG
and PODXL2, and tyrosine sulfation modifications of SELPLG.
Sulfation on 'Tyr-51' of SELPLG is important for L-selectin
binding. {ECO:0000250|UniProtKB:P14151}.
-!- SUBCELLULAR LOCATION: Cell membrane
{ECO:0000250|UniProtKB:P14151}; Single-pass type I membrane
protein {ECO:0000250|UniProtKB:P14151}.
-!- PTM: N-glycosylated. {ECO:0000250|UniProtKB:P14151}.
-!- SIMILARITY: Belongs to the selectin/LECAM family. {ECO:0000305}.
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EMBL; U73730; AAB18246.1; -; mRNA.
RefSeq; NP_001036228.1; NM_001042763.1.
UniGene; Mmu.3394; -.
ProteinModelPortal; Q95198; -.
SMR; Q95198; -.
STRING; 9544.ENSMMUP00000021783; -.
GeneID; 701419; -.
KEGG; mcc:701419; -.
CTD; 6402; -.
eggNOG; ENOG410IS3T; Eukaryota.
eggNOG; ENOG410YB82; LUCA.
HOGENOM; HOG000236254; -.
HOVERGEN; HBG052375; -.
InParanoid; Q95198; -.
KO; K06495; -.
Proteomes; UP000006718; Unplaced.
GO; GO:0005887; C:integral component of plasma membrane; ISS:UniProtKB.
GO; GO:0005509; F:calcium ion binding; ISS:UniProtKB.
GO; GO:0070492; F:oligosaccharide binding; ISS:UniProtKB.
GO; GO:0016339; P:calcium-dependent cell-cell adhesion via plasma membrane cell adhesion molecules; ISS:UniProtKB.
GO; GO:0050901; P:leukocyte tethering or rolling; ISS:UniProtKB.
CDD; cd00033; CCP; 2.
CDD; cd03592; CLECT_selectins_like; 1.
Gene3D; 3.10.100.10; -; 1.
InterPro; IPR001304; C-type_lectin-like.
InterPro; IPR016186; C-type_lectin-like/link_sf.
InterPro; IPR018378; C-type_lectin_CS.
InterPro; IPR016187; CTDL_fold.
InterPro; IPR013032; EGF-like_CS.
InterPro; IPR000742; EGF-like_dom.
InterPro; IPR016348; L-selectin.
InterPro; IPR033991; Selectin_CTLD.
InterPro; IPR002396; Selectin_superfamily.
InterPro; IPR035976; Sushi/SCR/CCP_sf.
InterPro; IPR000436; Sushi_SCR_CCP_dom.
Pfam; PF00059; Lectin_C; 1.
Pfam; PF00084; Sushi; 2.
PIRSF; PIRSF002421; L-selectin; 1.
PRINTS; PR00343; SELECTIN.
SMART; SM00032; CCP; 2.
SMART; SM00034; CLECT; 1.
SMART; SM00181; EGF; 1.
SUPFAM; SSF56436; SSF56436; 1.
SUPFAM; SSF57535; SSF57535; 2.
PROSITE; PS00615; C_TYPE_LECTIN_1; 1.
PROSITE; PS50041; C_TYPE_LECTIN_2; 1.
PROSITE; PS00022; EGF_1; 1.
PROSITE; PS01186; EGF_2; 1.
PROSITE; PS50026; EGF_3; 1.
PROSITE; PS50923; SUSHI; 2.
2: Evidence at transcript level;
Calcium; Cell adhesion; Cell membrane; Complete proteome;
Disulfide bond; EGF-like domain; Glycoprotein; Lectin; Membrane;
Metal-binding; Reference proteome; Repeat; Signal; Sushi;
Transmembrane; Transmembrane helix.
SIGNAL 1 28 {ECO:0000250}.
PROPEP 29 38 {ECO:0000250}.
/FTId=PRO_0000017477.
CHAIN 39 372 L-selectin.
/FTId=PRO_0000017478.
TOPO_DOM 39 332 Extracellular. {ECO:0000255}.
TRANSMEM 333 355 Helical. {ECO:0000255}.
TOPO_DOM 356 372 Cytoplasmic. {ECO:0000255}.
DOMAIN 55 155 C-type lectin. {ECO:0000255|PROSITE-
ProRule:PRU00040}.
DOMAIN 156 192 EGF-like. {ECO:0000255|PROSITE-
ProRule:PRU00076}.
DOMAIN 195 256 Sushi 1. {ECO:0000255|PROSITE-
ProRule:PRU00302}.
DOMAIN 257 318 Sushi 2. {ECO:0000255|PROSITE-
ProRule:PRU00302}.
METAL 118 118 Calcium. {ECO:0000250|UniProtKB:P14151}.
METAL 120 120 Calcium. {ECO:0000250|UniProtKB:P14151}.
METAL 126 126 Calcium. {ECO:0000250|UniProtKB:P14151}.
METAL 143 143 Calcium. {ECO:0000250|UniProtKB:P14151}.
METAL 144 144 Calcium. {ECO:0000250|UniProtKB:P14151}.
CARBOHYD 60 60 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 104 104 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 177 177 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 226 226 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 232 232 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 246 246 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 271 271 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 57 155 {ECO:0000250|UniProtKB:P14151}.
DISULFID 128 160 {ECO:0000250|UniProtKB:P14151}.
DISULFID 128 147 {ECO:0000250|UniProtKB:P14151}.
DISULFID 160 171 {ECO:0000250|UniProtKB:P14151}.
DISULFID 165 180 {ECO:0000250}.
DISULFID 182 191 {ECO:0000250|UniProtKB:P14151}.
DISULFID 197 241 {ECO:0000250}.
DISULFID 227 254 {ECO:0000250}.
DISULFID 259 303 {ECO:0000250}.
DISULFID 289 316 {ECO:0000250}.
SEQUENCE 372 AA; 42109 MW; 088D7DD5AC549D6D CRC64;
MIFPRKCQST QRDLWNIFKL WGWTMLCCDF LAHHGTDCWT YHYSENPMNW QKARRFCREN
YTDLVAIQNK AEIEYLEKTL PFSPSYYWIG IRKIGGIWTW VGTNKSLTQE AENWGDGEPN
NKKNKEDCVE IYIKRKKDAG KWNDDACHKP KAALCYTASC QPWSCSGHGE CVEIINNYTC
NCDVGYYGPQ CQFVIQCEPL EPPKLGTMDC THPLGDFSFS SQCAFNCSEG TNLTGIEETT
CGPFGNWSSP EPTCQVIQCE PLSAPDLGIM NCSHPLASFS FSSACTFSCS EGTELIGEKK
TICESSGIWS NPNPICQKLD RSFSMIKEGD YNPLFIPVAV MVTAFSGLAF IIWLARRLKK
GKKSKKSMDD PY


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