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Database: UniProt
Entry: P30836
LinkDB: P30836
Original site: P30836 
ID   LYAM1_RAT               Reviewed;         372 AA.
AC   P30836;
DT   01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-1993, sequence version 1.
DT   23-MAY-2018, entry version 130.
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;
DE            Short=LECAM1 {ECO:0000303|PubMed:1378303};
DE   AltName: Full=Lymph node homing receptor;
DE   AltName: Full=Lymphocyte antigen 22;
DE            Short=Ly-22;
DE   AltName: Full=Lymphocyte surface MEL-14 antigen;
DE   AltName: CD_antigen=CD62L;
DE   Flags: Precursor;
GN   Name=Sell; Synonyms=Lnhr, Ly-22;
OS   Rattus norvegicus (Rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
OC   Muroidea; Muridae; Murinae; Rattus.
OX   NCBI_TaxID=10116;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], SUBCELLULAR LOCATION, INDUCTION, AND
RP   TISSUE SPECIFICITY.
RX   PubMed=1378303; DOI=10.1016/0167-4781(92)90033-V;
RA   Watanabe T., Song Y., Hirayama Y., Tamatani T., Kuida K., Miyasaka M.;
RT   "Sequence and expression of a rat cDNA for LECAM-1.";
RL   Biochim. Biophys. Acta 1131:321-324(1992).
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.
CC       {ECO:0000250|UniProtKB:P14151}.
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:1378303};
CC       Single-pass type I membrane protein {ECO:0000305}.
CC   -!- TISSUE SPECIFICITY: Expressed in peripheral blood mononuclear
CC       cells (PBMC), spleen and thymus. {ECO:0000269|PubMed:1378303}.
CC   -!- INDUCTION: Down-regulated by mitogen stimulation of PBMC and
CC       spleen T-cells. {ECO:0000269|PubMed:1378303}.
CC   -!- PTM: N-glycosylated. {ECO:0000250|UniProtKB:P14151}.
CC   -!- SIMILARITY: Belongs to the selectin/LECAM family. {ECO:0000305}.
DR   EMBL; D10831; BAA01613.1; -; mRNA.
DR   PIR; S23936; S23936.
DR   UniGene; Rn.10461; -.
DR   ProteinModelPortal; P30836; -.
DR   SMR; P30836; -.
DR   STRING; 10116.ENSRNOP00000003733; -.
DR   SwissPalm; P30836; -.
DR   PaxDb; P30836; -.
DR   PRIDE; P30836; -.
DR   UCSC; RGD:3655; rat.
DR   RGD; 3655; Sell.
DR   eggNOG; ENOG410IS3T; Eukaryota.
DR   eggNOG; ENOG410YB82; LUCA.
DR   HOGENOM; HOG000236254; -.
DR   HOVERGEN; HBG052375; -.
DR   InParanoid; P30836; -.
DR   PhylomeDB; P30836; -.
DR   PRO; PR:P30836; -.
DR   Proteomes; UP000002494; Unplaced.
DR   GO; GO:0009986; C:cell surface; IDA:RGD.
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:0051861; F:glycolipid binding; IDA:RGD.
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:0050901; P:leukocyte tethering or rolling; ISS:UniProtKB.
DR   GO; GO:0090023; P:positive regulation of neutrophil chemotaxis; IMP:RGD.
DR   GO; GO:0042981; P:regulation of apoptotic process; IDA:RGD.
DR   GO; GO:0055093; P:response to hyperoxia; IEP:RGD.
DR   GO; GO:0070543; P:response to linoleic acid; IEP:RGD.
DR   GO; GO:0034201; P:response to oleic acid; IEP:RGD.
DR   CDD; cd00033; CCP; 1.
DR   CDD; cd03592; CLECT_selectins_like; 1.
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; IPR033991; Selectin_CTLD.
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   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:0000250}.
FT   PROPEP       29     38       {ECO:0000250}.
FT                                /FTId=PRO_0000017487.
FT   CHAIN        39    372       L-selectin.
FT                                /FTId=PRO_0000017488.
FT   TOPO_DOM     39    332       Extracellular. {ECO:0000255}.
FT   TRANSMEM    333    355       Helical. {ECO:0000255}.
FT   TOPO_DOM    356    372       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    104    104       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    177    177       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    278    278       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   372 AA;  42441 MW;  3B88AE0F1E4D191A CRC64;
     MVFPWRCQSA QRGSWSFLKL WIRTLLCCDL LPHHGTHCWT YHYSERSMNW ENARKFCKHN
     YTDLVAIQNK REIEYLEKTL PKNPTYYWIG IRKIGKTWTW VGTNKTLTKE AENWGTGEPN
     NKKSKEDCVE IYIKRERDSG KWNDDACHKR KAALCYTASC QPESCNRHGE CVETINNNTC
     ICDPGYYGPQ CQYVIQCEPL KAPELGTMNC IHPLGDFSFQ SQCAFNCSEG SELLGNAKTE
     CGASGNWTYL EPICQVIQCM PLAAPDLGTM ECSHPLANFS FTSACTFTCS EETDLIGERK
     TVCRSSGSWS SPSPICQKTK RSFSKIKEGD YNPLFIPVAV MVTAFSGLAF IIWLARRLKK
     GKKSQERMDD PY
//
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