GenomeNet

Database: UniProt
Entry: P33730
LinkDB: P33730
Original site: P33730 
ID   LYAM2_CANFA             Reviewed;         611 AA.
AC   P33730;
DT   01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1994, sequence version 1.
DT   19-FEB-2014, entry version 98.
DE   RecName: Full=E-selectin;
DE   AltName: Full=CD62 antigen-like family member E;
DE   AltName: Full=Endothelial leukocyte adhesion molecule 1;
DE            Short=ELAM-1;
DE   AltName: Full=Leukocyte-endothelial cell adhesion molecule 2;
DE            Short=LECAM2;
DE   AltName: CD_antigen=CD62E;
DE   Flags: Precursor;
GN   Name=SELE;
OS   Canis familiaris (Dog) (Canis lupus familiaris).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Laurasiatheria; Carnivora; Caniformia; Canidae;
OC   Canis.
OX   NCBI_TaxID=9615;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Jugular vein;
RA   Manning A.M., Lane C.L., Auchampach J.A., Kukielka G.L.,
RA   Rosenbloom C.L., Anderson D.C.;
RT   "Molecular cloning of canine E-selectin and regulation of
RT   expression.";
RL   Submitted (AUG-1993) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Cell-surface glycoprotein having a role in
CC       immunoadhesion. Mediates in the adhesion of blood neutrophils in
CC       cytokine-activated endothelium through interaction with
CC       PSGL1/SELPLG. May have a role in capillary morphogenesis.
CC   -!- SUBUNIT: Interacts with PSGL1/SELPLG and PODXL2 through the sialyl
CC       Lewis X epitope. PSGL1 sulfation appears not to be required for
CC       this interaction (By similarity).
CC   -!- SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane
CC       protein.
CC   -!- SIMILARITY: Belongs to the selectin/LECAM family.
CC   -!- SIMILARITY: Contains 1 C-type lectin domain.
CC   -!- SIMILARITY: Contains 1 EGF-like domain.
CC   -!- SIMILARITY: Contains 6 Sushi (CCP/SCR) domains.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; L23087; AAA30843.1; -; mRNA.
DR   RefSeq; NP_001003310.1; NM_001003310.1.
DR   UniGene; Cfa.3868; -.
DR   ProteinModelPortal; P33730; -.
DR   SMR; P33730; 23-179.
DR   STRING; 9615.ENSCAFP00000022350; -.
DR   GeneID; 403999; -.
DR   KEGG; cfa:403999; -.
DR   CTD; 6401; -.
DR   eggNOG; NOG242963; -.
DR   HOGENOM; HOG000236254; -.
DR   HOVERGEN; HBG052375; -.
DR   InParanoid; P33730; -.
DR   KO; K06494; -.
DR   NextBio; 20817486; -.
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; IEA:UniProtKB-KW.
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; IPR002396; Selectin_superfamily.
DR   InterPro; IPR000436; Sushi_SCR_CCP.
DR   Pfam; PF00008; EGF; 1.
DR   Pfam; PF00059; Lectin_C; 1.
DR   Pfam; PF00084; Sushi; 6.
DR   PRINTS; PR00343; SELECTIN.
DR   SMART; SM00032; CCP; 6.
DR   SMART; SM00034; CLECT; 1.
DR   SMART; SM00181; EGF; 2.
DR   SUPFAM; SSF56436; SSF56436; 1.
DR   SUPFAM; SSF57535; SSF57535; 6.
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; 6.
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     22       By similarity.
FT   CHAIN        23    611       E-selectin.
FT                                /FTId=PRO_0000017490.
FT   TOPO_DOM     23    557       Extracellular (Potential).
FT   TRANSMEM    558    579       Helical; (Potential).
FT   TOPO_DOM    580    611       Cytoplasmic (Potential).
FT   DOMAIN       23    140       C-type lectin.
FT   DOMAIN      141    176       EGF-like.
FT   DOMAIN      179    240       Sushi 1.
FT   DOMAIN      241    302       Sushi 2.
FT   DOMAIN      316    365       Sushi 3.
FT   DOMAIN      367    428       Sushi 4.
FT   DOMAIN      430    491       Sushi 5.
FT   DOMAIN      492    550       Sushi 6.
FT   CARBOHYD     26     26       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    161    161       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    204    204       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    266    266       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    313    313       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    333    333       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    528    528       N-linked (GlcNAc...) (Potential).
FT   DISULFID     41    139       By similarity.
FT   DISULFID    112    131       By similarity.
FT   DISULFID    144    155       By similarity.
FT   DISULFID    149    164       By similarity.
FT   DISULFID    166    175       By similarity.
FT   DISULFID    181    225       By similarity.
FT   DISULFID    211    238       By similarity.
FT   DISULFID    243    287       By similarity.
FT   DISULFID    273    300       By similarity.
FT   DISULFID    305    350       By similarity.
FT   DISULFID    336    363       By similarity.
FT   DISULFID    368    413       By similarity.
FT   DISULFID    399    426       By similarity.
FT   DISULFID    431    476       By similarity.
FT   DISULFID    462    489       By similarity.
FT   DISULFID    494    535       By similarity.
FT   DISULFID    521    548       By similarity.
SQ   SEQUENCE   611 AA;  66315 MW;  35DA9E3DF225E4F6 CRC64;
     MITSQLLPAL TLVLLLFKEG GAWSYNASTE AMTFDEASTY CQQRYTHLVA IQNQEEIKYL
     NSMFTYTPTY YWIGIRKVNK KWTWIGTQKL LTEEAKNWAP GEPNNKQNDE DCVEIYIKRD
     KDSGKWNDER CDKKKLALCY TAACTPTSCS GHGECVETVN NYTCKCHPGF RGLRCEQVVT
     CQAQEAPEHG SLVCTHPLGT FSYNSSCFVS CDKGYLPSST EATQCTSTGE WSASPPACNV
     VECSALTNPC HGVMDCLQSS GNFPWNMTCT FECEEGFELM GPKRLQCTSS GNWDNRKPTC
     KAVTCGAIGH PQNGSVSCSH SPAGEFSVRS SCNFTCNEGF LMQGPAQIEC TAQGQWSQQV
     PVCKASQCKA LSSPERGYMS CLPGASGSFQ SGSSCEFFCE KGFVLKGSKT LQCGLTGKWD
     SEEPTCEAVK CDAVQQPQDG LVRCAHSSTG EFTYKSSCAF SCEEGFELHG SAQLECTSQG
     QGVTGGPSCQ VVQCFKSGSF RKDEHKLQGE PVFGAVCAFA CPEGWTLNGS AALMCDATGH
     WSGMLPTCEA PTESSIPLAV GLTAGGTSLL TVASFLLWLL KRLRKRAKKF VPASSCQSLQ
     SDGSYHMPCS I
//
DBGET integrated database retrieval system