ID A0A3Q1LZX6_BOVIN Unreviewed; 373 AA.
AC A0A3Q1LZX6;
DT 10-APR-2019, integrated into UniProtKB/TrEMBL.
DT 10-APR-2019, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE RecName: Full=L-selectin {ECO:0000256|ARBA:ARBA00014208, ECO:0000256|PIRNR:PIRNR002421};
GN Name=SELL {ECO:0000313|Ensembl:ENSBTAP00000062903.1,
GN ECO:0000313|VGNC:VGNC:112699};
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913 {ECO:0000313|Ensembl:ENSBTAP00000062903.1, ECO:0000313|Proteomes:UP000009136};
RN [1] {ECO:0000313|Ensembl:ENSBTAP00000062903.1, ECO:0000313|Proteomes:UP000009136}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Hereford {ECO:0000313|Ensembl:ENSBTAP00000062903.1,
RC ECO:0000313|Proteomes:UP000009136};
RA Rosen B.D., Bickhart D.M., Koren S., Schnabel R.D., Hall R., Zimin A.,
RA Dreischer C., Schultheiss S., Schroeder S.G., Elsik C.G., Couldrey C.,
RA Liu G.E., Van Tassell C.P., Phillippy A.M., Smith T.P.L., Medrano J.F.;
RT "ARS-UCD1.2.";
RL Submitted (MAR-2018) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSBTAP00000062903.1}
RP IDENTIFICATION.
RC STRAIN=Hereford {ECO:0000313|Ensembl:ENSBTAP00000062903.1};
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- FUNCTION: Calcium-dependent lectin that mediates cell adhesion by
CC binding to glycoproteins on neighboring cells. Mediates the adherence
CC of lymphocytes to endothelial cells of high endothelial venules in
CC peripheral lymph nodes. Promotes initial tethering and rolling of
CC leukocytes in endothelia. {ECO:0000256|PIRNR:PIRNR002421}.
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 -!- 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, ECO:0000256|PIRNR:PIRNR002421}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00076}.
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DR AlphaFoldDB; A0A3Q1LZX6; -.
DR GlyCosmos; A0A3Q1LZX6; 3 sites, No reported glycans.
DR Ensembl; ENSBTAT00000085070.1; ENSBTAP00000062903.1; ENSBTAG00000011515.6.
DR VEuPathDB; HostDB:ENSBTAG00000011515; -.
DR VGNC; VGNC:112699; SELL.
DR GeneTree; ENSGT00940000162076; -.
DR OMA; EPSCQVI; -.
DR OrthoDB; 3035244at2759; -.
DR Proteomes; UP000009136; Chromosome 16.
DR Bgee; ENSBTAG00000011515; Expressed in neutrophil and 99 other cell types or tissues.
DR ExpressionAtlas; A0A3Q1LZX6; baseline and differential.
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:0016339; P:calcium-dependent cell-cell adhesion via plasma membrane cell adhesion molecules; IEA:UniProtKB-UniRule.
DR GO; GO:0050900; P:leukocyte migration; IEA:InterPro.
DR CDD; cd00033; CCP; 2.
DR CDD; cd00054; EGF_CA; 1.
DR Gene3D; 2.10.70.10; Complement Module, domain 1; 2.
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; 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:SF543; L-SELECTIN; 1.
DR Pfam; PF00008; EGF; 1.
DR Pfam; PF00059; Lectin_C; 1.
DR Pfam; PF00084; Sushi; 2.
DR PIRSF; PIRSF002421; L-selectin; 1.
DR PRINTS; PR00343; SELECTIN.
DR SMART; SM00032; CCP; 2.
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; 2.
DR SUPFAM; SSF57196; EGF/Laminin; 1.
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; 2.
PE 3: Inferred from homology;
KW Calcium {ECO:0000256|ARBA:ARBA00022837, ECO:0000256|PIRNR:PIRNR002421};
KW Cell adhesion {ECO:0000256|ARBA:ARBA00022889,
KW ECO:0000256|PIRNR:PIRNR002421};
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:0000256|ARBA:ARBA00022734};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|PIRSR:PIRSR002421-2};
KW Reference proteome {ECO:0000313|Proteomes:UP000009136};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP};
KW Sushi {ECO:0000256|PROSITE-ProRule:PRU00302};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT SIGNAL 1..32
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 33..373
FT /note="L-selectin"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5018553597"
FT TRANSMEM 334..355
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 36..156
FT /note="C-type lectin"
FT /evidence="ECO:0000259|PROSITE:PS50041"
FT DOMAIN 156..192
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 195..256
FT /note="Sushi"
FT /evidence="ECO:0000259|PROSITE:PS50923"
FT DOMAIN 257..318
FT /note="Sushi"
FT /evidence="ECO:0000259|PROSITE:PS50923"
FT BINDING 118
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000256|PIRSR:PIRSR002421-2"
FT BINDING 120
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000256|PIRSR:PIRSR002421-2"
FT BINDING 126
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000256|PIRSR:PIRSR002421-2"
FT BINDING 143
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000256|PIRSR:PIRSR002421-2"
FT BINDING 144
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000256|PIRSR:PIRSR002421-2"
FT CARBOHYD 60
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000256|PIRSR:PIRSR002421-3"
FT CARBOHYD 104
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000256|PIRSR:PIRSR002421-3"
FT CARBOHYD 177
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000256|PIRSR:PIRSR002421-3"
FT DISULFID 57..155
FT /evidence="ECO:0000256|PIRSR:PIRSR002421-1"
FT DISULFID 128..147
FT /evidence="ECO:0000256|PIRSR:PIRSR002421-1"
FT DISULFID 160..171
FT /evidence="ECO:0000256|PIRSR:PIRSR002421-1"
FT DISULFID 165..180
FT /evidence="ECO:0000256|PIRSR:PIRSR002421-1"
FT DISULFID 182..191
FT /evidence="ECO:0000256|PIRSR:PIRSR002421-1,
FT ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 197..241
FT /evidence="ECO:0000256|PIRSR:PIRSR002421-1"
FT DISULFID 227..254
FT /evidence="ECO:0000256|PIRSR:PIRSR002421-1,
FT ECO:0000256|PROSITE-ProRule:PRU00302"
FT DISULFID 259..303
FT /evidence="ECO:0000256|PIRSR:PIRSR002421-1"
FT DISULFID 289..316
FT /evidence="ECO:0000256|PIRSR:PIRSR002421-1,
FT ECO:0000256|PROSITE-ProRule:PRU00302"
SQ SEQUENCE 373 AA; 42419 MW; 49984D3D2FB6318D CRC64;
MLCPWKCQNA QRGLWNVFKL WVWIMLCCDF FAHRGTDCWT YHYSKRPMPW EKARAFCREN
YTDLVAIQNK GEIEYLNKTL PFSRTYYWIG IRKVEGVWTW VGTNKSLTEE AKNWGAGEPN
NRKSKEDCVE IYIKRNKDSG KWNDDACHKA KTALCYTASC KPWSCSGHGQ CVEVINNYTC
NCDLGYYGPE CQFVTQCVPL EAPKLGTMAC THPLGNFSFM SQCAFNCSKG TDMIGVEETT
CAPFGNWSSP EPTCRVIQCE PLTEPDLGTM DCNHPLVDFG FSSTCTFSCS EEAELTGEKK
TICGLSGNWS SPSPRCQKIN RTISINEESD YNPLFIPVAV MVTAFSGLAF IIWLARRLKR
KSKKSRRSMV DAY
//
