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 03-APR-2013, entry version 95.
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.
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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 OrthoDB; EOG4JT04Z; -.
DR NextBio; 20817486; -.
DR GO; GO:0016021; C:integral to 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; C-type_lectin_fold; 1.
DR SUPFAM; SSF57535; Complement_control_module; 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
//
