ID A0A3B3X6B7_9TELE Unreviewed; 744 AA.
AC A0A3B3X6B7;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE RecName: Full=Selectin E {ECO:0008006|Google:ProtNLM};
OS Poecilia mexicana.
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Atherinomorphae; Cyprinodontiformes; Poeciliidae; Poeciliinae;
OC Poecilia.
OX NCBI_TaxID=48701 {ECO:0000313|Ensembl:ENSPMEP00000010515.1, ECO:0000313|Proteomes:UP000261480};
RN [1] {ECO:0000313|Ensembl:ENSPMEP00000010515.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
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; A0A3B3X6B7; -.
DR STRING; 48701.ENSPMEP00000010515; -.
DR Ensembl; ENSPMET00000017378.1; ENSPMEP00000010515.1; ENSPMEG00000012465.1.
DR Proteomes; UP000261480; Unplaced.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0048856; P:anatomical structure development; IEA:UniProt.
DR GO; GO:0007155; P:cell adhesion; IEA:InterPro.
DR CDD; cd00033; CCP; 8.
DR CDD; cd03592; CLECT_selectins_like; 1.
DR CDD; cd00054; EGF_CA; 1.
DR Gene3D; 2.10.70.10; Complement Module, domain 1; 8.
DR Gene3D; 2.10.25.10; Laminin; 1.
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:SF543; L-SELECTIN; 1.
DR Pfam; PF00059; Lectin_C; 1.
DR Pfam; PF00084; Sushi; 8.
DR PRINTS; PR00343; SELECTIN.
DR SMART; SM00032; CCP; 8.
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; 8.
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; 8.
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:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Signal {ECO:0000256|ARBA:ARBA00022729, 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..744
FT /note="Selectin E"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5017465474"
FT TRANSMEM 688..711
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 20..148
FT /note="C-type lectin"
FT /evidence="ECO:0000259|PROSITE:PS50041"
FT DOMAIN 148..183
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 186..249
FT /note="Sushi"
FT /evidence="ECO:0000259|PROSITE:PS50923"
FT DOMAIN 250..313
FT /note="Sushi"
FT /evidence="ECO:0000259|PROSITE:PS50923"
FT DOMAIN 327..376
FT /note="Sushi"
FT /evidence="ECO:0000259|PROSITE:PS50923"
FT DOMAIN 377..435
FT /note="Sushi"
FT /evidence="ECO:0000259|PROSITE:PS50923"
FT DOMAIN 436..496
FT /note="Sushi"
FT /evidence="ECO:0000259|PROSITE:PS50923"
FT DOMAIN 497..559
FT /note="Sushi"
FT /evidence="ECO:0000259|PROSITE:PS50923"
FT DOMAIN 560..621
FT /note="Sushi"
FT /evidence="ECO:0000259|PROSITE:PS50923"
FT DOMAIN 622..681
FT /note="Sushi"
FT /evidence="ECO:0000259|PROSITE:PS50923"
FT REGION 722..744
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT DISULFID 152..162
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 173..182
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 220..247
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00302"
FT DISULFID 347..374
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00302"
FT DISULFID 406..433
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00302"
FT DISULFID 438..481
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00302"
FT DISULFID 467..494
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00302"
FT DISULFID 530..557
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00302"
FT DISULFID 592..619
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00302"
FT DISULFID 652..679
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00302"
SQ SEQUENCE 744 AA; 81990 MW; 40731EEF41A5390E CRC64;
MIPQCNTCLC SLFKVLCMWT GVECWSYFHS EITMDWVSAR KWCQTSYTDM VAIQNREEIE
HLKRMLPRKA GYYWIGIRKV GDVWTWVGTN KSLTAEATNW ADGEPNNGQN GMISGQAEDC
VEMYIKREKD EGKWNDERCS KKKTALCYTA ACKSDSCVHG ECVETINSHM CKCSPGFYGE
KCEQVVQCDK DQVIAPGNGN VTCSHKHKNF SYDSFCQYSC EEGYQLSMPE PQKCQETGTW
SKQSPTCELI QCQELSAPER GFMECSDPLR SFSYRSSCSF TCMEGYELDD SSSITLQCES
SGKWNASEPS CVAVQCPALQ NPDNGFVTCE DDTDMRFSYG KRCSFSCDPG YHLIGSEMIT
CTSEAVWSDK MSLCEAVQCP ALKDPENGSV KCEDGHGYEK NCSFNCEPGF ELQGVHTIQC
SEDGQWSNGI PTCKAVQCPA LQGLENGALS CDTEMRFSYR TSCSFICDPG FELQGVHSIQ
CSEDKRWTDA VPSCTAVQCP ALLDLENGAM TCENDVEMRF SYKKSCSFTC VPGHRLVGPS
EVTCTADAEW SGTIPHCEAI TCQNPDGAAH MIVECSKPST DLGPSSTCSF RCESGFELRG
ANTTTCSQDG QWSEALPTCN AIRCPPLEAP ENGHINCSDS QPLFNSQCSF ACDQDYTLDG
HEILTCDRRG SWTGKNPTCQ ASPASATVIA TGVAGGATAL VSGVSLTMWI LKKMKQRASK
FELNSTSDSE EPLQVYKSSD DSLI
//
