ID A0A3Q7SES0_VULVU Unreviewed; 616 AA.
AC A0A3Q7SES0;
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=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};
GN Name=SELE {ECO:0000313|RefSeq:XP_025859119.1};
OS Vulpes vulpes (Red fox).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Caniformia; Canidae; Vulpes.
OX NCBI_TaxID=9627 {ECO:0000313|Proteomes:UP000286640, ECO:0000313|RefSeq:XP_025859119.1};
RN [1]
RP IDENTIFICATION.
RG RefSeq;
RL Submitted (JAN-2019) to UniProtKB.
RN [2] {ECO:0000313|RefSeq:XP_025859119.1}
RP IDENTIFICATION.
RC STRAIN=TameXAggressive cross {ECO:0000313|RefSeq:XP_025859119.1};
RC TISSUE=Blood {ECO:0000313|RefSeq:XP_025859119.1};
RG RefSeq;
RL Submitted (NOV-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 RefSeq; XP_025859119.1; XM_026003334.1.
DR AlphaFoldDB; A0A3Q7SES0; -.
DR STRING; 9627.ENSVVUP00000036607; -.
DR KEGG; vvp:112923483; -.
DR OrthoDB; 3035244at2759; -.
DR Proteomes; UP000286640; Unplaced.
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 SMART; SM00181; EGF; 2.
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:UP000286640};
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..31
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 32..616
FT /note="E-selectin"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5018738876"
FT TRANSMEM 563..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 616 AA; 66804 MW; 82A13D2CA543C459 CRC64;
MKRTLEVMIT SQLLPALTLV LLLFKEGGAW SYNASTEAMT FDEASTYCQQ RYTHLVAIQN
QEEIKYLNSM FSYTPTYYWI GIRKVNKKWT WIGTQKLLTE EAKNWAPGEP NNKQNNEDCV
EIYIKRDKDS GKWNDERCDK KKLALCYTAA CTPTSCSGHG ECVETVNNYT CKCHPGFSGL
RCEQVVTCQA QEAPEHGSLV CTHPLGTFSY NSSCFVSCDK GYLPSSTEAT QCTSTGEWSA
SPPACNVVEC SALTNPANGV MDCLQSSGNF PWNTTCTFEC EEGFELMGPK RLQCTSSGNW
DNRKPTCKAV TCGAIGHPQN GSVSCSHSPA GEFTVRSSCN FTCKEGFLMQ GPAQIECTAQ
GQWSQQVPVC KASQCKALSS PERGYMSCLP GASGSFQSGS SCEFFCEQGF VLKGSKTLQC
GLTGKWDSEE PTCEAVKCDA VQQPQDGLVR CAHSSTGEFT YKSSCAFSCE EGFELHGSAQ
LECTSQGRWS QEVPSCQVVQ CSSLAVSGKM NISCSGEPVF GAVCAFACPE GWTLNGSAAL
MCDATGHWSG MLPTCEAPTE SSIPLAVGLT AGGTSLLTVA SFLLWLLKRL RKRAKKFVPA
SSCQSLQSDG SYHMPL
//
