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Database: UniProt
Entry: P98110
LinkDB: P98110
Original site: P98110 
ID   LYAM2_PIG               Reviewed;         484 AA.
AC   P98110;
DT   01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1996, sequence version 1.
DT   19-FEB-2014, entry version 102.
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   Sus scrofa (Pig).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Laurasiatheria; Cetartiodactyla; Suina; Suidae;
OC   Sus.
OX   NCBI_TaxID=9823;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Aortic endothelium;
RX   PubMed=7526854; DOI=10.1006/bbrc.1994.2525;
RA   Rollins S.A., Evans M.J., Johnson K.K., Elliot E.A., Squinto S.P.,
RA   Matis L.A., Rother R.P.;
RT   "Molecular and functional analysis of porcine E-selectin reveals a
RT   potential role in xenograft rejection.";
RL   Biochem. Biophys. Res. Commun. 204:763-771(1994).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Aortic endothelium;
RX   PubMed=7516159; DOI=10.1006/bbrc.1994.1772;
RA   Tsang Y.T.M., Haskard D.O., Robinson M.K.;
RT   "Cloning and expression kinetics of porcine vascular cell adhesion
RT   molecule.";
RL   Biochem. Biophys. Res. Commun. 201:805-812(1994).
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   -!- MISCELLANEOUS: Important in acute cellular allograft rejection and
CC       probably also in xenograft rejection.
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 4 Sushi (CCP/SCR) domains.
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DR   EMBL; L39076; AAA61545.1; -; mRNA.
DR   EMBL; U08350; AAA21541.1; -; mRNA.
DR   RefSeq; NP_999433.1; NM_214268.1.
DR   UniGene; Ssc.16297; -.
DR   ProteinModelPortal; P98110; -.
DR   SMR; P98110; 23-179.
DR   STRING; 9823.ENSSSCP00000006699; -.
DR   GeneID; 397508; -.
DR   KEGG; ssc:397508; -.
DR   CTD; 6401; -.
DR   eggNOG; NOG242963; -.
DR   HOGENOM; HOG000236254; -.
DR   HOVERGEN; HBG052375; -.
DR   KO; K06494; -.
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; PF00059; Lectin_C; 1.
DR   Pfam; PF00084; Sushi; 4.
DR   PRINTS; PR00343; SELECTIN.
DR   SMART; SM00032; CCP; 4.
DR   SMART; SM00034; CLECT; 1.
DR   SMART; SM00181; EGF; 1.
DR   SUPFAM; SSF56436; SSF56436; 1.
DR   SUPFAM; SSF57535; SSF57535; 4.
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; 4.
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       Potential.
FT   CHAIN        23    484       E-selectin.
FT                                /FTId=PRO_0000017494.
FT   TOPO_DOM     23    429       Extracellular (Potential).
FT   TRANSMEM    430    451       Helical; (Potential).
FT   TOPO_DOM    452    484       Cytoplasmic (Potential).
FT   DOMAIN       23    140       C-type lectin.
FT   DOMAIN      141    176       EGF-like.
FT   DOMAIN      179    237       Sushi 1.
FT   DOMAIN      251    300       Sushi 2.
FT   DOMAIN      301    363       Sushi 3.
FT   DOMAIN      364    422       Sushi 4.
FT   CARBOHYD     61     61       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD     65     65       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD     79     79       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    160    160       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    201    201       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    254    254       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    376    376       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    400    400       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    222       By similarity.
FT   DISULFID    208    235       By similarity.
FT   DISULFID    240    285       By similarity.
FT   DISULFID    271    298       By similarity.
FT   DISULFID    303    348       By similarity.
FT   DISULFID    334    361       By similarity.
FT   DISULFID    366    407       By similarity.
FT   DISULFID    393    420       By similarity.
FT   CONFLICT    253    253       C -> Y (in Ref. 2; AAA21541).
FT   CONFLICT    313    313       L -> F (in Ref. 2; AAA21541).
FT   CONFLICT    321    321       T -> N (in Ref. 2; AAA21541).
FT   CONFLICT    327    327       K -> N (in Ref. 2; AAA21541).
FT   CONFLICT    363    363       V -> A (in Ref. 2; AAA21541).
FT   CONFLICT    384    384       V -> M (in Ref. 2; AAA21541).
FT   CONFLICT    461    484       KFVPSSSSECLQPNGSYQMPSDLI -> NLFLPAAPNAFNP
FT                                MDPTKCLLT (in Ref. 2; AAA21541).
SQ   SEQUENCE   484 AA;  52567 MW;  AFF74FE25C1FD013 CRC64;
     MIASQFLSAL PLVLLLLRES GAWSYSASTE TMTFDDASAY CQQRYTHLVA IQNHAEIEYL
     NSTFNYSASY YWIGIRKING TWTWIGTKKA LTPEATNWAP GEPNNKQSNE DCVEIYIKRD
     KDSGKWNDER CSKKKLALCY TAACTPTSCS GHGECIETIN SSTCQCYPGF RGLQCEQVVE
     CDALENPVNG VVTCPQSLPW NTTCAFECKE GFELIGPEHL QCTSSGSWDG KKPTCKAVTC
     DTVGHPQNGD VSCNHSSIGE FAYKSTCHFT CAEGFGLQGP AQIECTAQGQ WTQQAPVCKA
     VKCPAVSQPK NGLVKFTHSP TGEFTYKSSC AFSCEEGFEL RGSAQLACTS QGQWTQEVPS
     CQVVQCSSLE VPREINMSCS GEPVFGAVCT FACPEGWMLN GSVALTCGAT GHWSGMLPTC
     EAPAESKIPL AMGLAAGGVS FMTSASFLLW LLKRLRKRAK KFVPSSSSEC LQPNGSYQMP
     SDLI
//
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