ID A0A340XDK7_LIPVE Unreviewed; 549 AA.
AC A0A340XDK7;
DT 10-OCT-2018, integrated into UniProtKB/TrEMBL.
DT 10-OCT-2018, sequence version 1.
DT 24-JAN-2024, entry version 23.
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_007458187.1};
OS Lipotes vexillifer (Yangtze river dolphin).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Whippomorpha; Cetacea; Odontoceti;
OC Lipotidae; Lipotes.
OX NCBI_TaxID=118797 {ECO:0000313|Proteomes:UP000265300, ECO:0000313|RefSeq:XP_007458187.1};
RN [1] {ECO:0000313|RefSeq:XP_007458187.1}
RP IDENTIFICATION.
RG RefSeq;
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 RefSeq; XP_007458187.1; XM_007458125.1.
DR AlphaFoldDB; A0A340XDK7; -.
DR GeneID; 103071026; -.
DR CTD; 6401; -.
DR OrthoDB; 3035244at2759; -.
DR Proteomes; UP000265300; Unplaced.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0030246; F:carbohydrate binding; IEA:UniProtKB-KW.
DR GO; GO:0007155; P:cell adhesion; IEA:UniProtKB-KW.
DR CDD; cd00033; CCP; 5.
DR CDD; cd03592; CLECT_selectins_like; 1.
DR CDD; cd00054; EGF_CA; 1.
DR Gene3D; 2.10.70.10; Complement Module, domain 1; 5.
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; IPR001881; EGF-like_Ca-bd_dom.
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; 5.
DR PRINTS; PR00343; SELECTIN.
DR SMART; SM00032; CCP; 5.
DR SMART; SM00034; CLECT; 1.
DR SMART; SM00181; EGF; 2.
DR SMART; SM00179; EGF_CA; 1.
DR SUPFAM; SSF56436; C-type lectin-like; 1.
DR SUPFAM; SSF57535; Complement control module/SCR domain; 5.
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; 5.
PE 3: Inferred from homology;
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157, ECO:0000256|PROSITE-
KW ProRule:PRU00076};
KW EGF-like domain {ECO:0000256|ARBA:ARBA00022536, ECO:0000256|PROSITE-
KW ProRule:PRU00076}; 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:UP000265300};
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..24
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 25..549
FT /note="E-selectin"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5016357497"
FT TRANSMEM 495..517
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 20..140
FT /note="C-type lectin"
FT /evidence="ECO:0000259|PROSITE:PS50041"
FT DOMAIN 140..176
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 179..240
FT /note="Sushi"
FT /evidence="ECO:0000259|PROSITE:PS50923"
FT DOMAIN 241..302
FT /note="Sushi"
FT /evidence="ECO:0000259|PROSITE:PS50923"
FT DOMAIN 303..365
FT /note="Sushi"
FT /evidence="ECO:0000259|PROSITE:PS50923"
FT DOMAIN 366..428
FT /note="Sushi"
FT /evidence="ECO:0000259|PROSITE:PS50923"
FT DOMAIN 429..487
FT /note="Sushi"
FT /evidence="ECO:0000259|PROSITE:PS50923"
FT DISULFID 166..175
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 211..238
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00302"
FT DISULFID 273..300
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00302"
FT DISULFID 336..363
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00302"
FT DISULFID 399..426
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00302"
FT DISULFID 458..485
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00302"
SQ SEQUENCE 549 AA; 59532 MW; 951F050B7057BB1A CRC64;
MIASQFVSAL TFVLLLLKES GAWSYNASTE TMTFDEASAY CQQRYTHLVA IQNQEEIKHL
NSTFSYSPSY YWIGIRKVNN TWTWIGTQKP LTEEATNWAP GEPNNKQSKE DCVEIYIKRE
KDSGKWNDER CSKKKLALCY TAACTPTSCS GHGDCRETIN SYTCQCHPGF KGLKCEQVVT
CQAQEAPEHG SLVCNDPLGK FSYNSSCSVS CGEGYLPSSP EATQCTSSGE WSVPLPACSV
AKCDVLTNPV NGVVKCFQSH GSFLWNTTCE FECNEGYKLT GPQHLQCISS GIWDNKKPTC
KAVTCDAISH PQNGAVSFSH SPAGEFTYKS SCHFTCAEGF VLQGPAQVEC TTQGQWTQQV
PVCEAVKCDA IPQPRSGSVN CTHSPTGEFT YKSSCAISCE EGFELHGSAQ LECTSQGQWT
QEVPSCQVVQ CSSLEVPGKI DINCSGEPVF GTKCTLACPE GWTLNGSAAL TCGATGHWSG
MLPTCEAPSK SQTPLAVGLS AAGVSLMTLA SFLLWLLKRL QKKAKKFVPA SSCQSLQSDG
SYQMLSELI
//