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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_BOVIN             Reviewed;         370 AA.
P98131;
01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
01-FEB-1996, sequence version 1.
31-JAN-2018, entry version 115.
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 {ECO:0000303|PubMed:1371468};
Short=LECAM1 {ECO:0000303|PubMed:1371468};
AltName: Full=Lymph node homing receptor {ECO:0000303|PubMed:1371468};
AltName: CD_antigen=CD62L;
Flags: Precursor;
Name=SELL;
Bos taurus (Bovine).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Laurasiatheria; Cetartiodactyla; Ruminantia;
Pecora; Bovidae; Bovinae; Bos.
NCBI_TaxID=9913;
[1]
NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBCELLULAR LOCATION, AND TISSUE
SPECIFICITY.
TISSUE=Lymphocyte;
PubMed=1371468; DOI=10.1002/eji.1830220227;
Walcheck B., White M., Kurk S., Kishimoto T.K., Jutila M.A.;
"Characterization of the bovine peripheral lymph node homing receptor:
a lectin cell adhesion molecule (LECAM).";
Eur. J. Immunol. 22:469-476(1992).
[2]
NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBCELLULAR LOCATION, AND TISSUE
SPECIFICITY.
TISSUE=Lymphocyte;
PubMed=7694420; DOI=10.1016/0165-2427(93)90194-9;
Bosworth B.T., Dowbenko D., Shuster D.E., Harp J.A.;
"Bovine L-selectin: a peripheral lymphocyte homing receptor.";
Vet. Immunol. Immunopathol. 37:201-215(1993).
-!- 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:0000269|PubMed:1371468,
ECO:0000269|PubMed:7694420}.
-!- 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:0000269|PubMed:1371468,
ECO:0000269|PubMed:7694420}; Single-pass type I membrane protein
{ECO:0000305}.
-!- TISSUE SPECIFICITY: Highly expressed in lymphocytes from
peripheral lymph nodes. Low in lymphocytes isolated from Peyer
patches. {ECO:0000269|PubMed:1371468, ECO:0000269|PubMed:7694420}.
-!- PTM: N-glycosylated. {ECO:0000250|UniProtKB:P14151}.
-!- SIMILARITY: Belongs to the selectin/LECAM family. {ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; X62882; CAA44676.1; -; mRNA.
PIR; S22124; S22124.
RefSeq; NP_776607.1; NM_174182.1.
UniGene; Bt.2314; -.
ProteinModelPortal; P98131; -.
SMR; P98131; -.
STRING; 9913.ENSBTAP00000044113; -.
PaxDb; P98131; -.
PRIDE; P98131; -.
GeneID; 281485; -.
KEGG; bta:281485; -.
CTD; 6402; -.
eggNOG; ENOG410IS3T; Eukaryota.
eggNOG; ENOG410YB82; LUCA.
HOGENOM; HOG000236254; -.
HOVERGEN; HBG052375; -.
InParanoid; P98131; -.
KO; K06495; -.
Proteomes; UP000009136; Unplaced.
GO; GO:0016021; C:integral component of membrane; TAS:AgBase.
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:0007155; P:cell adhesion; NAS:AgBase.
GO; GO:0050901; P:leukocyte tethering or rolling; ISS:UniProtKB.
CDD; cd00033; CCP; 2.
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; 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:0000255}.
PROPEP 29 38 {ECO:0000255}.
/FTId=PRO_0000017473.
CHAIN 39 370 L-selectin.
/FTId=PRO_0000017474.
TOPO_DOM 39 333 Extracellular. {ECO:0000255}.
TRANSMEM 334 354 Helical. {ECO:0000255}.
TOPO_DOM 355 370 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 77 77 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 216 216 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 226 226 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 246 246 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 308 308 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 320 320 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 370 AA; 41971 MW; 92168F8116AE9228 CRC64;
MLCPWKCQNA QRGLWNVFKL WVWIMLCCDF FAHHGTDCWT YHYSKRPMPW EKARAFCREN
YTDLVAIQNK GEIEYLNKTL PFSRTYYWIG IRKVEGVWTW VGTNKSLTEE AKNWGAGEPN
NRKSKEDCVE IYIKRNKDSG KWNDDACHKA KTALCYTASC KPWSCSGHGQ CVEVINNYTC
NCDLGYYGPE CQFVTQCVPL EAPKLGTMAC THPLGNFSFM SQCAFNCSKG TDMIGVEETT
CAPFGNWSSP EPTCRVIQCE PLTEPDLGTM DCNHPLVDFG FSSTCTFSCS EEAELTGEKK
TICGLSGNWS SPSPRCQKIN RTISINEESD YNPLFIPVAV MVTAFSGLAF IIWLARRLKR
KSKKVSEKHG


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