ID   Q28629_RABIT            Unreviewed;       376 AA.
AC   Q28629; G1TJM3;
DT   01-NOV-1996, integrated into UniProtKB/TrEMBL.
DT   01-NOV-1996, sequence version 1.
DT   27-MAR-2024, entry version 166.
DE   RecName: Full=L-selectin {ECO:0000256|ARBA:ARBA00014208, ECO:0000256|PIRNR:PIRNR002421};
GN   Name=SELL {ECO:0000313|Ensembl:ENSOCUP00000017151.2};
OS   Oryctolagus cuniculus (Rabbit).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Lagomorpha; Leporidae; Oryctolagus.
OX   NCBI_TaxID=9986 {ECO:0000313|EMBL:AAA67896.1};
RN   [1] {ECO:0000313|EMBL:AAA67896.1}
RP   NUCLEOTIDE SEQUENCE.
RC   TISSUE=Kidney {ECO:0000313|EMBL:AAA67896.1};
RA   Qian J., Marks R.M.;
RT   "cDNA for rabbit L-selectin.";
RL   Submitted (MAY-1995) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Ensembl:ENSOCUP00000017151.2, ECO:0000313|Proteomes:UP000001811}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Thorbecke inbred {ECO:0000313|Ensembl:ENSOCUP00000017151.2,
RC   ECO:0000313|Proteomes:UP000001811};
RX   PubMed=21993624; DOI=10.1038/nature10530;
RA   Lindblad-Toh K., Garber M., Zuk O., Lin M.F., Parker B.J., Washietl S.,
RA   Kheradpour P., Ernst J., Jordan G., Mauceli E., Ward L.D., Lowe C.B.,
RA   Holloway A.K., Clamp M., Gnerre S., Alfoldi J., Beal K., Chang J.,
RA   Clawson H., Cuff J., Di Palma F., Fitzgerald S., Flicek P., Guttman M.,
RA   Hubisz M.J., Jaffe D.B., Jungreis I., Kent W.J., Kostka D., Lara M.,
RA   Martins A.L., Massingham T., Moltke I., Raney B.J., Rasmussen M.D.,
RA   Robinson J., Stark A., Vilella A.J., Wen J., Xie X., Zody M.C., Baldwin J.,
RA   Bloom T., Chin C.W., Heiman D., Nicol R., Nusbaum C., Young S.,
RA   Wilkinson J., Worley K.C., Kovar C.L., Muzny D.M., Gibbs R.A., Cree A.,
RA   Dihn H.H., Fowler G., Jhangiani S., Joshi V., Lee S., Lewis L.R.,
RA   Nazareth L.V., Okwuonu G., Santibanez J., Warren W.C., Mardis E.R.,
RA   Weinstock G.M., Wilson R.K., Delehaunty K., Dooling D., Fronik C.,
RA   Fulton L., Fulton B., Graves T., Minx P., Sodergren E., Birney E.,
RA   Margulies E.H., Herrero J., Green E.D., Haussler D., Siepel A., Goldman N.,
RA   Pollard K.S., Pedersen J.S., Lander E.S., Kellis M.;
RT   "A high-resolution map of human evolutionary constraint using 29 mammals.";
RL   Nature 478:476-482(2011).
RN   [3] {ECO:0000313|Ensembl:ENSOCUP00000017151.2}
RP   IDENTIFICATION.
RC   STRAIN=Thorbecke {ECO:0000313|Ensembl:ENSOCUP00000017151.2};
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}.
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; AAGW02000040; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AAGW02000041; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; U26535; AAA67896.1; -; mRNA.
DR   PIR; JC4892; JC4892.
DR   RefSeq; NP_001075821.1; NM_001082352.1.
DR   STRING; 9986.ENSOCUP00000017151; -.
DR   PaxDb; 9986-ENSOCUP00000017151; -.
DR   Ensembl; ENSOCUT00000029156.3; ENSOCUP00000017151.2; ENSOCUG00000017432.4.
DR   GeneID; 100009204; -.
DR   KEGG; ocu:100009204; -.
DR   CTD; 6402; -.
DR   eggNOG; KOG4297; Eukaryota.
DR   GeneTree; ENSGT00940000162076; -.
DR   HOGENOM; CLU_065067_0_0_1; -.
DR   OMA; EPSCQVI; -.
DR   OrthoDB; 3035244at2759; -.
DR   TreeFam; TF326910; -.
DR   Proteomes; UP000001811; Chromosome 13.
DR   Bgee; ENSOCUG00000017432; Expressed in blood and 16 other cell types or tissues.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005509; F:calcium ion binding; IEA:Ensembl.
DR   GO; GO:0070492; F:oligosaccharide binding; IEA:Ensembl.
DR   GO; GO:0002020; F:protease binding; IEA:Ensembl.
DR   GO; GO:0016339; P:calcium-dependent cell-cell adhesion via plasma membrane cell adhesion molecules; IEA:UniProtKB-UniRule.
DR   GO; GO:0050901; P:leukocyte tethering or rolling; IEA:Ensembl.
DR   CDD; cd00033; CCP; 2.
DR   CDD; cd03592; CLECT_selectins_like; 1.
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; 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: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   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   2: Evidence at transcript level;
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, ECO:0000313|EMBL:AAA67896.1};
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:UP000001811};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737};
KW   Signal {ECO:0000256|ARBA:ARBA00022729};
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   TRANSMEM        334..355
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          34..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   376 AA;  42346 MW;  59F6AD530F490947 CRC64;
     MIFPWKCQSP QRGLWNVFKL WVWATLCCDF LAYHGTNCWT YHYSEKPMNW ERARKFCREN
     YTDLVAIQNK GEIEYLEKTL PFSRSYYWIG IRKIGNIWTW VGTNKSLTAE AENWGEGEPN
     NKKTKEDCVE IYIKRLRDSG KWNDDSCQKR KAALCYTASC HPGSCSGHGE CVEVINNYTC
     SCDVGYYGPQ CQFVMQCEPL EAPELGTMAC THPLGEFSFS SQCGFSCLEG TNLTGIEETT
     CGPLGNWSSL RPTCQVIQCE PLTAPDLGTI DCSHPRAVFG FTSTCTFSCS EGAELIGMKK
     TVCGSSGIWS SPTPKCQKVD RSFSMIKEGD YNPLFIPVAV MVTAFSGLAF IIWLARRLKK
     GKKSQKSKDD ILIHPL
//