ID A0A1L8GNL2_XENLA Unreviewed; 1023 AA.
AC A0A1L8GNL2;
DT 15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT 15-MAR-2017, sequence version 1.
DT 27-MAR-2024, entry version 29.
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=selp.L {ECO:0000313|RefSeq:XP_041446619.1};
OS Xenopus laevis (African clawed frog).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX NCBI_TaxID=8355 {ECO:0000313|Proteomes:UP000186698, ECO:0000313|RefSeq:XP_041446619.1};
RN [1] {ECO:0000313|RefSeq:XP_041446619.1}
RP IDENTIFICATION.
RC STRAIN=J_2021 {ECO:0000313|RefSeq:XP_041446619.1};
RC TISSUE=Erythrocytes {ECO:0000313|RefSeq:XP_041446619.1};
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_041446619.1; XM_041590685.1.
DR AlphaFoldDB; A0A1L8GNL2; -.
DR STRING; 8355.A0A1L8GNL2; -.
DR PaxDb; 8355-A0A1L8GNL2; -.
DR KEGG; xla:108713554; -.
DR OMA; FVKCPEN; -.
DR OrthoDB; 3035244at2759; -.
DR Proteomes; UP000186698; Chromosome 4L.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0007155; P:cell adhesion; IEA:InterPro.
DR CDD; cd00033; CCP; 13.
DR CDD; cd03592; CLECT_selectins_like; 1.
DR Gene3D; 2.10.70.10; Complement Module, domain 1; 13.
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; PF00059; Lectin_C; 1.
DR Pfam; PF00084; Sushi; 13.
DR PRINTS; PR00343; SELECTIN.
DR SMART; SM00032; CCP; 13.
DR SMART; SM00034; CLECT; 1.
DR SMART; SM00181; EGF; 1.
DR SUPFAM; SSF56436; C-type lectin-like; 1.
DR SUPFAM; SSF57535; Complement control module/SCR domain; 13.
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; 13.
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 Membrane {ECO:0000256|ARBA:ARBA00022989};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000186698};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Sushi {ECO:0000256|PROSITE-ProRule:PRU00302};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989}.
FT DISULFID 163..172
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 208..235
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00302"
FT DISULFID 270..297
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00302"
FT DISULFID 332..359
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00302"
FT DISULFID 394..421
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00302"
FT DISULFID 453..480
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00302"
FT DISULFID 512..539
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00302"
FT DISULFID 571..598
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00302"
FT DISULFID 630..657
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00302"
FT DISULFID 689..716
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00302"
FT DISULFID 748..775
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00302"
FT DISULFID 807..834
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00302"
FT DISULFID 866..893
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00302"
FT DISULFID 928..955
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00302"
SQ SEQUENCE 1023 AA; 112135 MW; 9F44DC63B51036DE CRC64;
MISIFYCSLT AFVLAGVQGW SYHYSNTNMT YEHARKFCRT TYTDLVAIQN REENEYLNSI
LPFNPNYYWI GIRLIKNHWT WEGTKKILTE EAKNWALGEP NNKKSNEDCV EMYIKRTNDS
GKWNDEPCKK KKVALCYTAA CSPSSCSGHG DCIETINNYT CSCYEGFYGS ACEHVVECPR
LVVPELGSMK CEDENGKFKY NSNCSFSCNE GFALTDSNAL QCTASGSWSL DVPACEAVVC
PTIPVPEHGS MECEDDYGEF QYNSKCSFSC NEGFILTGSN SLHCTSSGSW SSGVPTCEAV
VCPPITIPEH SSMECEDDYG EFQYNSNCSF SCKEGFILTG SNSLHCNSSR SWSSDVPACK
ALDCSRLVVP ELGSMECVDE YGEFQYNSKC SFSCNEGFIL TGSKSVQCTS SGSWSSDVPA
CQVVQCDTLK DPTNGFVKCP ENLEYNSTCS FTCAEGYNLV GLSEVQCLAS GDWMSPPPIC
EVVQCTSLNN PKNGWVKCEE KPHYKSRCTY ACAEGYKLSG SSERQCLASG EWTSSVPTCE
AVQCEPLKHP ENGFVKCPEN SEYNSTCSFT CAEGYNLVGL SEVQCLASGE WMSPPPICEV
VQCTSLNNPE NGWVKCEEKP HYKSKCTYAC AEGYKLSGSS ERQCLASGKW TSSVPTCEVV
QCETLKQPEN GFVKCPENPE YNSTCSFTCA EGYNLVGLSE VQCLASGEWM SPPPICKVVQ
CTSLNNPKNG WVKCEEKPHY KSKCTYACAE GYKLSGSSEV QCLASGEWTS SVPTCEAVQC
EPLKQPENGF VKCPENPEYN STCSFTCAEG YNLVGLSEVQ CLASAKWASP PPICEVVRCA
SLNNPENGWV KCQEKPYYKS KCSYACAEGY KLSGSSERQC LPSGEWTFSA PTCEAVECKV
PLIPDMGTMN CSHPFGDFKY GSVCKFDCEG DRLLNGTNTL ECKSTGTWSS EVPACEAPKI
VPDSGVINVA VGVAATGASL LSVTSLLVWL VKRLRKSAKK FTPSSSCQKL EEAGVYQNIE
DHI
//
