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Database: UniProt
Entry: A0A340XDK7_LIPVE
LinkDB: A0A340XDK7_LIPVE
Original site: A0A340XDK7_LIPVE 
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
//
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