ID A0A091PVR4_LEPDC Unreviewed; 344 AA.
AC A0A091PVR4;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 27-MAR-2024, entry version 42.
DE RecName: Full=E-selectin {ECO:0000256|ARBA:ARBA00040812};
DE AltName: Full=CD62 antigen-like family member E {ECO:0000256|ARBA:ARBA00041401};
DE AltName: Full=CD62 antigen-like family member L {ECO:0000256|ARBA:ARBA00030282};
DE AltName: Full=Endothelial leukocyte adhesion molecule 1 {ECO:0000256|ARBA:ARBA00042113};
DE AltName: Full=L-selectin {ECO:0000256|ARBA:ARBA00014208};
DE AltName: Full=Leukocyte adhesion molecule 1 {ECO:0000256|ARBA:ARBA00031844};
DE AltName: Full=Leukocyte-endothelial cell adhesion molecule 1 {ECO:0000256|ARBA:ARBA00032968};
DE AltName: Full=Leukocyte-endothelial cell adhesion molecule 2 {ECO:0000256|ARBA:ARBA00043124};
DE AltName: Full=Lymph node homing receptor {ECO:0000256|ARBA:ARBA00030610};
DE Flags: Fragment;
GN ORFNames=N330_02405 {ECO:0000313|EMBL:KFQ11441.1};
OS Leptosomus discolor (Madagascar cuckoo roller) (Cuculus discolor).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Coraciiformes; Leptosomidae; Leptosomus.
OX NCBI_TaxID=188344 {ECO:0000313|EMBL:KFQ11441.1, ECO:0000313|Proteomes:UP000053001};
RN [1] {ECO:0000313|EMBL:KFQ11441.1, ECO:0000313|Proteomes:UP000053001}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BGI_N330 {ECO:0000313|EMBL:KFQ11441.1};
RA Zhang G., Li C.;
RT "Genome evolution of avian class.";
RL Submitted (APR-2014) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBUNIT: Interaction with SELPLG/PSGL1 and PODXL2 is required for
CC promoting recruitment and rolling of leukocytes. This interaction is
CC dependent on the sialyl Lewis X glycan modification of SELPLG and
CC PODXL2, and tyrosine sulfation modifications of SELPLG. Sulfation on
CC 'Tyr-51' of SELPLG is important for L-selectin binding.
CC {ECO:0000256|ARBA:ARBA00011813}.
CC -!- SUBUNIT: Interacts with SELPLG/PSGL1 and PODXL2 through the sialyl
CC Lewis X epitope. SELPLG sulfation appears not to be required for this
CC interaction. {ECO:0000256|ARBA:ARBA00038738}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|ARBA:ARBA00004251};
CC Single-pass type I membrane protein {ECO:0000256|ARBA:ARBA00004251}.
CC Membrane {ECO:0000256|ARBA:ARBA00004479}; Single-pass type I membrane
CC protein {ECO:0000256|ARBA:ARBA00004479}.
CC -!- SIMILARITY: Belongs to the selectin/LECAM family.
CC {ECO:0000256|ARBA:ARBA00007360}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00076}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; KK679215; KFQ11441.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A091PVR4; -.
DR PhylomeDB; A0A091PVR4; -.
DR Proteomes; UP000053001; Unassembled WGS sequence.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0030246; F:carbohydrate binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0007155; P:cell adhesion; IEA:InterPro.
DR GO; GO:0050900; P:leukocyte migration; IEA:InterPro.
DR CDD; cd00033; CCP; 3.
DR CDD; cd03592; CLECT_selectins_like; 1.
DR CDD; cd00054; EGF_CA; 1.
DR Gene3D; 2.10.70.10; Complement Module, domain 1; 3.
DR Gene3D; 2.10.25.10; Laminin; 1.
DR Gene3D; 3.10.100.10; Mannose-Binding Protein A, subunit A; 1.
DR InterPro; IPR001304; C-type_lectin-like.
DR InterPro; IPR016186; C-type_lectin-like/link_sf.
DR InterPro; IPR018378; C-type_lectin_CS.
DR InterPro; IPR016187; CTDL_fold.
DR InterPro; IPR000742; EGF-like_dom.
DR InterPro; IPR016348; L-selectin.
DR InterPro; IPR033991; Selectin_CTLD.
DR InterPro; IPR002396; Selectin_superfamily.
DR InterPro; IPR035976; Sushi/SCR/CCP_sf.
DR InterPro; IPR000436; Sushi_SCR_CCP_dom.
DR PANTHER; PTHR19325; COMPLEMENT COMPONENT-RELATED SUSHI DOMAIN-CONTAINING; 1.
DR PANTHER; PTHR19325:SF493; E-SELECTIN; 1.
DR Pfam; PF00008; EGF; 1.
DR Pfam; PF00059; Lectin_C; 1.
DR Pfam; PF00084; Sushi; 3.
DR PIRSF; PIRSF002421; L-selectin; 2.
DR PRINTS; PR00343; SELECTIN.
DR SMART; SM00032; CCP; 3.
DR SMART; SM00034; CLECT; 1.
DR SMART; SM00181; EGF; 1.
DR SUPFAM; SSF56436; C-type lectin-like; 1.
DR SUPFAM; SSF57535; Complement control module/SCR domain; 3.
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; 3.
PE 3: Inferred from homology;
KW Calcium {ECO:0000256|ARBA:ARBA00022837, ECO:0000256|PIRSR:PIRSR002421-2};
KW Cell adhesion {ECO:0000256|ARBA:ARBA00022889};
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157,
KW ECO:0000256|PIRSR:PIRSR002421-1};
KW EGF-like domain {ECO:0000256|PROSITE-ProRule:PRU00076};
KW Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW Lectin {ECO:0000313|EMBL:KFQ11441.1};
KW Membrane {ECO:0000256|ARBA:ARBA00022989};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|PIRSR:PIRSR002421-2};
KW Reference proteome {ECO:0000313|Proteomes:UP000053001};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Sushi {ECO:0000256|PROSITE-ProRule:PRU00302};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989}.
FT DOMAIN 1..118
FT /note="C-type lectin"
FT /evidence="ECO:0000259|PROSITE:PS50041"
FT DOMAIN 118..154
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 157..218
FT /note="Sushi"
FT /evidence="ECO:0000259|PROSITE:PS50923"
FT DOMAIN 219..280
FT /note="Sushi"
FT /evidence="ECO:0000259|PROSITE:PS50923"
FT DOMAIN 281..342
FT /note="Sushi"
FT /evidence="ECO:0000259|PROSITE:PS50923"
FT BINDING 80
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000256|PIRSR:PIRSR002421-2"
FT BINDING 82
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000256|PIRSR:PIRSR002421-2"
FT BINDING 88
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000256|PIRSR:PIRSR002421-2"
FT BINDING 105
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000256|PIRSR:PIRSR002421-2"
FT BINDING 106
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000256|PIRSR:PIRSR002421-2"
FT DISULFID 19..117
FT /evidence="ECO:0000256|PIRSR:PIRSR002421-1"
FT DISULFID 90..109
FT /evidence="ECO:0000256|PIRSR:PIRSR002421-1"
FT DISULFID 122..133
FT /evidence="ECO:0000256|PIRSR:PIRSR002421-1"
FT DISULFID 127..142
FT /evidence="ECO:0000256|PIRSR:PIRSR002421-1"
FT DISULFID 144..153
FT /evidence="ECO:0000256|PIRSR:PIRSR002421-1,
FT ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 159..203
FT /evidence="ECO:0000256|PIRSR:PIRSR002421-1"
FT DISULFID 189..216
FT /evidence="ECO:0000256|PIRSR:PIRSR002421-1,
FT ECO:0000256|PROSITE-ProRule:PRU00302"
FT DISULFID 221..265
FT /evidence="ECO:0000256|PIRSR:PIRSR002421-1"
FT DISULFID 251..278
FT /evidence="ECO:0000256|PIRSR:PIRSR002421-1,
FT ECO:0000256|PROSITE-ProRule:PRU00302"
FT DISULFID 313..340
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00302"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:KFQ11441.1"
FT NON_TER 344
FT /evidence="ECO:0000313|EMBL:KFQ11441.1"
SQ SEQUENCE 344 AA; 38524 MW; 15F3E39EB7B882FD CRC64;
WTYHYSDTNM TYREAEMWCK KRYTNMVAIQ NKEEINYLNN FLPFNPGYYW IGIRKINEVW
TWIGTNKELT EEAKNWASGE PNGKGNNEDC VEIYIKRGKD DGKWNDEQCE KKKVALCYTA
SCNPSLCSGR GECIETINNY TCRCNPGFYG PECEFVESCD PLKKPNHGSL ECNHPLENFS
YNSSCTVECE EGFELTALES VYCTSSGVWS APLATCKAVT CPALEMPAYG AVNCSHPSVE
LTWGTTCEFT CEEGFALTGP ATLQCGSSGA WDRQQPSCAA VRCEAVTWPE EGFVTCDHAP
ADLTYRSRCD FRCNEGFVLD GPSSIECTAQ GRWSEPVPKC KGKT
//
