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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   01-OCT-2014, entry version 100.
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   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], AND TISSUE 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], AND TISSUE 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: Cell surface adhesion protein. Mediates the adherence of
CC       lymphocytes to endothelial cells of high endothelial venules in
CC       peripheral lymph nodes. Promotes initial tethering and rolling of
CC       leukocytes in endothelia (By similarity). {ECO:0000250}.
CC   -!- SUBUNIT: Interaction with PSGL1/SELPLG 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 PSGL1
CC       and PODXL2, and tyrosine sulfation modifications of PSGL1.
CC       Sulfation on 'Tyr-51' of PSGL1 is important for L-selectin binding
CC       (By similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane
CC       protein.
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   -!- SIMILARITY: Belongs to the selectin/LECAM family. {ECO:0000305}.
CC   -!- SIMILARITY: Contains 1 C-type lectin domain. {ECO:0000255|PROSITE-
CC       ProRule:PRU00040}.
CC   -!- SIMILARITY: Contains 1 EGF-like domain. {ECO:0000255|PROSITE-
CC       ProRule:PRU00076}.
CC   -!- SIMILARITY: Contains 2 Sushi (CCP/SCR) domains.
CC       {ECO:0000255|PROSITE-ProRule:PRU00302}.
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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; 39-194.
DR   STRING; 9913.ENSBTAP00000044113; -.
DR   PRIDE; P98131; -.
DR   GeneID; 281485; -.
DR   KEGG; bta:281485; -.
DR   CTD; 6402; -.
DR   eggNOG; NOG258998; -.
DR   HOGENOM; HOG000236254; -.
DR   HOVERGEN; HBG052375; -.
DR   KO; K06495; -.
DR   NextBio; 20805460; -.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0030246; F:carbohydrate binding; IEA:InterPro.
DR   GO; GO:0007155; P:cell adhesion; NAS:AgBase.
DR   Gene3D; 3.10.100.10; -; 1.
DR   InterPro; IPR001304; C-type_lectin.
DR   InterPro; IPR016186; C-type_lectin-like.
DR   InterPro; IPR018378; C-type_lectin_CS.
DR   InterPro; IPR016187; C-type_lectin_fold.
DR   InterPro; IPR000742; EG-like_dom.
DR   InterPro; IPR013032; EGF-like_CS.
DR   InterPro; IPR016348; L-selectin.
DR   InterPro; IPR002396; Selectin_superfamily.
DR   InterPro; IPR000436; Sushi_SCR_CCP.
DR   Pfam; PF00008; EGF; 1.
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   Cell adhesion; Complete proteome; Disulfide bond; EGF-like domain;
KW   Glycoprotein; Lectin; Membrane; Reference proteome; Repeat; Signal;
KW   Sushi; 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   CARBOHYD     60     60       N-linked (GlcNAc...). {ECO:0000255}.
FT   CARBOHYD     77     77       N-linked (GlcNAc...). {ECO:0000255}.
FT   CARBOHYD    104    104       N-linked (GlcNAc...). {ECO:0000255}.
FT   CARBOHYD    177    177       N-linked (GlcNAc...). {ECO:0000255}.
FT   CARBOHYD    216    216       N-linked (GlcNAc...). {ECO:0000255}.
FT   CARBOHYD    226    226       N-linked (GlcNAc...). {ECO:0000255}.
FT   CARBOHYD    246    246       N-linked (GlcNAc...). {ECO:0000255}.
FT   CARBOHYD    308    308       N-linked (GlcNAc...). {ECO:0000255}.
FT   CARBOHYD    320    320       N-linked (GlcNAc...). {ECO:0000255}.
FT   DISULFID     57    155       {ECO:0000250}.
FT   DISULFID    128    147       {ECO:0000250}.
FT   DISULFID    160    171       {ECO:0000250}.
FT   DISULFID    165    180       {ECO:0000250}.
FT   DISULFID    182    191       {ECO:0000250}.
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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