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Database: UniProt
Entry: P98131
LinkDB: P98131
Original site: P98131 
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   16-JAN-2019, entry version 116.
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;
OC   Mammalia; Eutheria; Laurasiatheria; Cetartiodactyla; Ruminantia;
OC   Pecora; Bovidae; 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:
RT   a 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
CC       adherence of lymphocytes to endothelial cells of high endothelial
CC       venules in peripheral lymph nodes. Promotes initial tethering and
CC       rolling of 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
CC       is dependent on the sialyl Lewis X glycan modification of SELPLG
CC       and PODXL2, and tyrosine sulfation modifications of SELPLG.
CC       Sulfation on 'Tyr-51' of SELPLG is important for L-selectin
CC       binding. {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
CC       peripheral lymph nodes. Low in lymphocytes isolated from Peyer
CC       patches. {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}.
DR   EMBL; X62882; CAA44676.1; -; mRNA.
DR   PIR; S22124; S22124.
DR   RefSeq; NP_776607.1; NM_174182.1.
DR   UniGene; Bt.2314; -.
DR   ProteinModelPortal; 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; ENOG410IS3T; Eukaryota.
DR   eggNOG; ENOG410YB82; LUCA.
DR   HOGENOM; HOG000236254; -.
DR   HOVERGEN; HBG052375; -.
DR   InParanoid; P98131; -.
DR   KO; K06495; -.
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; IPR013032; EGF-like_CS.
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; Complete proteome;
KW   Disulfide bond; EGF-like domain; Glycoprotein; Lectin; Membrane;
KW   Metal-binding; Reference proteome; Repeat; Signal; Sushi;
KW   Transmembrane; Transmembrane helix.
FT   SIGNAL        1     28       {ECO:0000255}.
FT   PROPEP       29     38       {ECO:0000255}.
FT                                /FTId=PRO_0000017473.
FT   CHAIN        39    370       L-selectin.
FT                                /FTId=PRO_0000017474.
FT   TOPO_DOM     39    333       Extracellular. {ECO:0000255}.
FT   TRANSMEM    334    354       Helical. {ECO:0000255}.
FT   TOPO_DOM    355    370       Cytoplasmic. {ECO:0000255}.
FT   DOMAIN       55    155       C-type lectin. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00040}.
FT   DOMAIN      156    192       EGF-like. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00076}.
FT   DOMAIN      195    256       Sushi 1. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00302}.
FT   DOMAIN      257    318       Sushi 2. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00302}.
FT   METAL       118    118       Calcium. {ECO:0000250|UniProtKB:P14151}.
FT   METAL       120    120       Calcium. {ECO:0000250|UniProtKB:P14151}.
FT   METAL       126    126       Calcium. {ECO:0000250|UniProtKB:P14151}.
FT   METAL       143    143       Calcium. {ECO:0000250|UniProtKB:P14151}.
FT   METAL       144    144       Calcium. {ECO:0000250|UniProtKB:P14151}.
FT   CARBOHYD     60     60       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD     77     77       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    104    104       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    177    177       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    216    216       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    226    226       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    246    246       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    308    308       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    320    320       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   DISULFID     57    155       {ECO:0000250|UniProtKB:P14151}.
FT   DISULFID    128    160       {ECO:0000250|UniProtKB:P14151}.
FT   DISULFID    128    147       {ECO:0000250|UniProtKB:P14151}.
FT   DISULFID    160    171       {ECO:0000250|UniProtKB:P14151}.
FT   DISULFID    165    180       {ECO:0000250}.
FT   DISULFID    182    191       {ECO:0000250|UniProtKB:P14151}.
FT   DISULFID    197    241       {ECO:0000250}.
FT   DISULFID    227    254       {ECO:0000250}.
FT   DISULFID    259    303       {ECO:0000250}.
FT   DISULFID    289    316       {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
//
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