LYAM1_BOVIN
ID LYAM1_BOVIN Reviewed; 370 AA.
AC P98131;
DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1996, sequence version 1.
DT 03-AUG-2022, entry version 124.
DE RecName: Full=L-selectin;
DE AltName: Full=CD62 antigen-like family member L;
DE AltName: Full=Leukocyte adhesion molecule 1;
DE Short=LAM-1;
DE AltName: Full=Leukocyte-endothelial cell adhesion molecule 1 {ECO:0000303|PubMed:1371468};
DE Short=LECAM1 {ECO:0000303|PubMed:1371468};
DE AltName: Full=Lymph node homing receptor {ECO:0000303|PubMed:1371468};
DE AltName: CD_antigen=CD62L;
DE Flags: Precursor;
GN Name=SELL;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBCELLULAR LOCATION, AND TISSUE
RP SPECIFICITY.
RC TISSUE=Lymphocyte;
RX PubMed=1371468; DOI=10.1002/eji.1830220227;
RA Walcheck B., White M., Kurk S., Kishimoto T.K., Jutila M.A.;
RT "Characterization of the bovine peripheral lymph node homing receptor: a
RT lectin cell adhesion molecule (LECAM).";
RL Eur. J. Immunol. 22:469-476(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBCELLULAR LOCATION, AND TISSUE
RP SPECIFICITY.
RC TISSUE=Lymphocyte;
RX PubMed=7694420; DOI=10.1016/0165-2427(93)90194-9;
RA Bosworth B.T., Dowbenko D., Shuster D.E., Harp J.A.;
RT "Bovine L-selectin: a peripheral lymphocyte homing receptor.";
RL Vet. Immunol. Immunopathol. 37:201-215(1993).
CC -!- FUNCTION: Calcium-dependent lectin that mediates cell adhesion by
CC binding to glycoproteins on neighboring cells. Mediates the adherence
CC of lymphocytes to endothelial cells of high endothelial venules in
CC peripheral lymph nodes. Promotes initial tethering and rolling of
CC leukocytes in endothelia. {ECO:0000269|PubMed:1371468,
CC ECO:0000269|PubMed:7694420}.
CC -!- SUBUNIT: Interaction with SELPLG/PSGL1 and PODXL2 is required for
CC promoting recruitment and rolling of leukocytes. This interaction is
CC dependent on the sialyl Lewis X glycan modification of SELPLG and
CC PODXL2, and tyrosine sulfation modifications of SELPLG. Sulfation on
CC 'Tyr-51' of SELPLG is important for L-selectin binding.
CC {ECO:0000250|UniProtKB:P14151}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:1371468,
CC ECO:0000269|PubMed:7694420}; Single-pass type I membrane protein
CC {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Highly expressed in lymphocytes from peripheral
CC lymph nodes. Low in lymphocytes isolated from Peyer patches.
CC {ECO:0000269|PubMed:1371468, ECO:0000269|PubMed:7694420}.
CC -!- PTM: N-glycosylated. {ECO:0000250|UniProtKB:P14151}.
CC -!- SIMILARITY: Belongs to the selectin/LECAM family. {ECO:0000305}.
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DR EMBL; X62882; CAA44676.1; -; mRNA.
DR PIR; S22124; S22124.
DR RefSeq; NP_776607.1; NM_174182.1.
DR AlphaFoldDB; P98131; -.
DR SMR; P98131; -.
DR STRING; 9913.ENSBTAP00000044113; -.
DR PaxDb; P98131; -.
DR PRIDE; P98131; -.
DR GeneID; 281485; -.
DR KEGG; bta:281485; -.
DR CTD; 6402; -.
DR eggNOG; KOG4297; Eukaryota.
DR InParanoid; P98131; -.
DR OrthoDB; 445079at2759; -.
DR Proteomes; UP000009136; Unplaced.
DR GO; GO:0016021; C:integral component of membrane; TAS:AgBase.
DR GO; GO:0005887; C:integral component of plasma membrane; ISS:UniProtKB.
DR GO; GO:0005509; F:calcium ion binding; ISS:UniProtKB.
DR GO; GO:0070492; F:oligosaccharide binding; ISS:UniProtKB.
DR GO; GO:0016339; P:calcium-dependent cell-cell adhesion via plasma membrane cell adhesion molecules; ISS:UniProtKB.
DR GO; GO:0007155; P:cell adhesion; NAS:AgBase.
DR GO; GO:0050901; P:leukocyte tethering or rolling; ISS:UniProtKB.
DR CDD; cd00033; CCP; 2.
DR Gene3D; 3.10.100.10; -; 1.
DR InterPro; IPR001304; C-type_lectin-like.
DR InterPro; IPR016186; C-type_lectin-like/link_sf.
DR InterPro; IPR018378; C-type_lectin_CS.
DR InterPro; IPR016187; CTDL_fold.
DR InterPro; IPR000742; EGF-like_dom.
DR InterPro; IPR016348; L-selectin.
DR InterPro; IPR002396; Selectin_superfamily.
DR InterPro; IPR035976; Sushi/SCR/CCP_sf.
DR InterPro; IPR000436; Sushi_SCR_CCP_dom.
DR Pfam; PF00059; Lectin_C; 1.
DR Pfam; PF00084; Sushi; 2.
DR PIRSF; PIRSF002421; L-selectin; 1.
DR PRINTS; PR00343; SELECTIN.
DR SMART; SM00032; CCP; 2.
DR SMART; SM00034; CLECT; 1.
DR SMART; SM00181; EGF; 1.
DR SUPFAM; SSF56436; SSF56436; 1.
DR SUPFAM; SSF57535; SSF57535; 2.
DR PROSITE; PS00615; C_TYPE_LECTIN_1; 1.
DR PROSITE; PS50041; C_TYPE_LECTIN_2; 1.
DR PROSITE; PS00022; EGF_1; 1.
DR PROSITE; PS01186; EGF_2; 1.
DR PROSITE; PS50026; EGF_3; 1.
DR PROSITE; PS50923; SUSHI; 2.
PE 2: Evidence at transcript level;
KW Calcium; Cell adhesion; Cell membrane; Disulfide bond; EGF-like domain;
KW Glycoprotein; Lectin; Membrane; Metal-binding; Reference proteome; Repeat;
KW Signal; Sushi; Transmembrane; Transmembrane helix.
FT SIGNAL 1..28
FT /evidence="ECO:0000255"
FT PROPEP 29..38
FT /evidence="ECO:0000255"
FT /id="PRO_0000017473"
FT CHAIN 39..370
FT /note="L-selectin"
FT /id="PRO_0000017474"
FT TOPO_DOM 39..333
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 334..354
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 355..370
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 55..155
FT /note="C-type lectin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
FT DOMAIN 156..192
FT /note="EGF-like"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 195..256
FT /note="Sushi 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT DOMAIN 257..318
FT /note="Sushi 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT BINDING 118
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:P14151"
FT BINDING 120
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:P14151"
FT BINDING 126
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:P14151"
FT BINDING 143
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:P14151"
FT BINDING 144
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:P14151"
FT CARBOHYD 60
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 77
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 104
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 177
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 216
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 226
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 246
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 308
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 320
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 57..155
FT /evidence="ECO:0000250|UniProtKB:P14151"
FT DISULFID 128..160
FT /evidence="ECO:0000250|UniProtKB:P14151"
FT DISULFID 128..147
FT /evidence="ECO:0000250|UniProtKB:P14151"
FT DISULFID 160..171
FT /evidence="ECO:0000250|UniProtKB:P14151"
FT DISULFID 165..180
FT /evidence="ECO:0000250"
FT DISULFID 182..191
FT /evidence="ECO:0000250|UniProtKB:P14151"
FT DISULFID 197..241
FT /evidence="ECO:0000250"
FT DISULFID 227..254
FT /evidence="ECO:0000250"
FT DISULFID 259..303
FT /evidence="ECO:0000250"
FT DISULFID 289..316
FT /evidence="ECO:0000250"
SQ 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
