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 03-APR-2013, entry version 100.
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 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; 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; C-type_lectin_fold; 1.
DR SUPFAM; SSF57535; Complement_control_module; 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
//
