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Database: UniProt
Entry: Q28768
LinkDB: Q28768
Original site: Q28768 
ID   LYAM1_PAPHA             Reviewed;         372 AA.
AC   Q28768;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   31-JAN-2018, entry version 95.
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;
DE   AltName: Full=Lymph node homing receptor;
DE   AltName: CD_antigen=CD62L;
DE   Flags: Precursor;
GN   Name=SELL;
OS   Papio hamadryas (Hamadryas baboon).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC   Catarrhini; Cercopithecidae; Cercopithecinae; Papio.
OX   NCBI_TaxID=9557;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=8973334; DOI=10.1016/S0378-1119(96)00457-X;
RA   Tsurushita N., Fu H., Berg E.L.;
RT   "PCR cloning of the cDNA encoding baboon L-selectin.";
RL   Gene 181:219-220(1996).
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
CC       {ECO:0000250|UniProtKB:P14151}; Single-pass type I membrane
CC       protein {ECO:0000250|UniProtKB:P14151}.
CC   -!- PTM: N-glycosylated. {ECO:0000250|UniProtKB:P14151}.
CC   -!- SIMILARITY: Belongs to the selectin/LECAM family. {ECO:0000305}.
DR   EMBL; U52074; AAB40903.1; -; mRNA.
DR   PIR; JC5377; JC5377.
DR   UniGene; Pan.4425; -.
DR   ProteinModelPortal; Q28768; -.
DR   SMR; Q28768; -.
DR   HOVERGEN; HBG052375; -.
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:0050901; P:leukocyte tethering or rolling; ISS:UniProtKB.
DR   CDD; cd00033; CCP; 2.
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   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;
KW   EGF-like domain; Glycoprotein; Lectin; Membrane; Metal-binding;
KW   Repeat; Signal; Sushi; Transmembrane; Transmembrane helix.
FT   SIGNAL        1     28       {ECO:0000250}.
FT   PROPEP       29     38       {ECO:0000250}.
FT                                /FTId=PRO_0000017483.
FT   CHAIN        39    372       L-selectin.
FT                                /FTId=PRO_0000017484.
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    232    232       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    246    246       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    271    271       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;  42091 MW;  64E7BDD5AC549D69 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 IVTAFSGLAF IIWLARRLKK
     GKKSKKSMDD PY
//
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