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Database: UniProt
Entry: A0A673T2W2_SURSU
LinkDB: A0A673T2W2_SURSU
Original site: A0A673T2W2_SURSU 
ID   A0A673T2W2_SURSU        Unreviewed;       619 AA.
AC   A0A673T2W2;
DT   17-JUN-2020, integrated into UniProtKB/TrEMBL.
DT   17-JUN-2020, sequence version 1.
DT   27-MAR-2024, entry version 19.
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=Endothelial leukocyte adhesion molecule 1 {ECO:0000256|ARBA:ARBA00042113};
DE   AltName: Full=Leukocyte-endothelial cell adhesion molecule 2 {ECO:0000256|ARBA:ARBA00043124};
OS   Suricata suricatta (Meerkat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Carnivora; Feliformia; Herpestidae; Suricata.
OX   NCBI_TaxID=37032 {ECO:0000313|Ensembl:ENSSSUP00005006208.1, ECO:0000313|Proteomes:UP000472268};
RN   [1] {ECO:0000313|Ensembl:ENSSSUP00005006208.1, ECO:0000313|Proteomes:UP000472268}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Dudchenko O., Lieberman Aiden E., Tung J., Barreiro L.B.,
RA   Clutton-Brock T.H.;
RT   "A Chromosome-scale Meerkat (S. suricatta) Genome Assembly.";
RL   Submitted (MAY-2019) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Ensembl:ENSSSUP00005006208.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (SEP-2023) to UniProtKB.
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}.
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DR   AlphaFoldDB; A0A673T2W2; -.
DR   Ensembl; ENSSSUT00005007180.1; ENSSSUP00005006208.1; ENSSSUG00005004026.1.
DR   OMA; FVTCDHA; -.
DR   OrthoDB; 3035244at2759; -.
DR   Proteomes; UP000472268; Chromosome 3.
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   CDD; cd00033; CCP; 6.
DR   CDD; cd03592; CLECT_selectins_like; 1.
DR   CDD; cd00054; EGF_CA; 1.
DR   Gene3D; 2.10.70.10; Complement Module, domain 1; 6.
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; 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; 6.
DR   PRINTS; PR00343; SELECTIN.
DR   SMART; SM00032; CCP; 6.
DR   SMART; SM00034; CLECT; 1.
DR   SUPFAM; SSF56436; C-type lectin-like; 1.
DR   SUPFAM; SSF57535; Complement control module/SCR domain; 6.
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; 6.
PE   3: Inferred from homology;
KW   Calcium {ECO:0000256|ARBA:ARBA00022837};
KW   Cell adhesion {ECO:0000256|ARBA:ARBA00022889};
KW   Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW   Disulfide bond {ECO:0000256|ARBA:ARBA00023157, ECO:0000256|PROSITE-
KW   ProRule:PRU00076}; EGF-like domain {ECO:0000256|PROSITE-ProRule:PRU00076};
KW   Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW   Lectin {ECO:0000256|ARBA:ARBA00022734}; Membrane {ECO:0000256|SAM:Phobius};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Reference proteome {ECO:0000313|Proteomes:UP000472268};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737}; Signal {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..29
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           30..619
FT                   /note="E-selectin"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5025595182"
FT   TRANSMEM        565..587
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          27..147
FT                   /note="C-type lectin"
FT                   /evidence="ECO:0000259|PROSITE:PS50041"
FT   DOMAIN          147..183
FT                   /note="EGF-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50026"
FT   DOMAIN          186..247
FT                   /note="Sushi"
FT                   /evidence="ECO:0000259|PROSITE:PS50923"
FT   DOMAIN          248..309
FT                   /note="Sushi"
FT                   /evidence="ECO:0000259|PROSITE:PS50923"
FT   DOMAIN          323..372
FT                   /note="Sushi"
FT                   /evidence="ECO:0000259|PROSITE:PS50923"
FT   DOMAIN          386..435
FT                   /note="Sushi"
FT                   /evidence="ECO:0000259|PROSITE:PS50923"
FT   DOMAIN          449..498
FT                   /note="Sushi"
FT                   /evidence="ECO:0000259|PROSITE:PS50923"
FT   DOMAIN          499..557
FT                   /note="Sushi"
FT                   /evidence="ECO:0000259|PROSITE:PS50923"
FT   DISULFID        173..182
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT   DISULFID        218..245
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00302"
FT   DISULFID        280..307
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00302"
FT   DISULFID        343..370
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00302"
FT   DISULFID        406..433
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00302"
FT   DISULFID        469..496
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00302"
FT   DISULFID        528..555
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00302"
SQ   SEQUENCE   619 AA;  67358 MW;  1186EA3FAC3118FB CRC64;
     MKRNLEVMGA SRLLPALTLV LLLFKGSRAW SYNASTEIMT FDEASAYCQQ HYTHLVAIQN
     QEEIEYLNSI LSYSPTYYWI GIRKVNDTWT WIGTQKPLTE EAKNWAPGEP NNKQNNEDCV
     EIYIKRDKDT GKWNDERCSK KKLALCYTAA CNPTSCSGHG ECVETVNNYM CECYPGFRGL
     GCEQVVTCQA QEDPEHGSLV CTHPLGTFSY NSFCSVSCEE GYLPSSTEAI QCTSTGEWSA
     PTPACNVVEC DALTNPTNGV MDCSQSSGNF PWNTTCDFEC EEGFELMGSQ HLQCTSSGKW
     DNKKPTCKAV TCDAIGHPQH GSVSCSHAPA GNFTFRSSCS FTCEEGFVMQ GPAQLECTAQ
     GQWSQQVPVC EALQCKALSR PERGYMSCPP SASGSFRRGS SCQFFCEEGF VLKGSRKLQC
     GPTGKWDSEE PTCEAVKCDA VRQPQSGSVT CTQSPTGEFT YKSSCAFSCE EGFGLRGSAQ
     LECTSQGQWT HEVPSCQVVG CSRLAVSGKM NVSCSGEPVF GTVCAFACPE GWTLNGSAAL
     TCDTTGHWSG MLPTCEAPTE SSIPLAVELT AAGASLMTVA SLVLWLLKRL RKRAKKFVPA
     SSCQSLQSNG SYQMPSELI
//
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