ID M4AFN0_XIPMA Unreviewed; 746 AA.
AC M4AFN0;
DT 01-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 2.
DT 27-MAR-2024, entry version 68.
DE SubName: Full=Selectin E {ECO:0000313|Ensembl:ENSXMAP00000013274.2};
OS Xiphophorus maculatus (Southern platyfish) (Platypoecilus maculatus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Atherinomorphae; Cyprinodontiformes; Poeciliidae; Poeciliinae;
OC Xiphophorus.
OX NCBI_TaxID=8083 {ECO:0000313|Ensembl:ENSXMAP00000013274.2, ECO:0000313|Proteomes:UP000002852};
RN [1] {ECO:0000313|Proteomes:UP000002852}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JP 163 A {ECO:0000313|Proteomes:UP000002852};
RA Walter R., Schartl M., Warren W.;
RL Submitted (JAN-2012) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Proteomes:UP000002852}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JP 163 A {ECO:0000313|Proteomes:UP000002852};
RX PubMed=23542700; DOI=10.1038/ng.2604;
RA Schartl M., Walter R.B., Shen Y., Garcia T., Catchen J., Amores A.,
RA Braasch I., Chalopin D., Volff J.N., Lesch K.P., Bisazza A., Minx P.,
RA Hillier L., Wilson R.K., Fuerstenberg S., Boore J., Searle S.,
RA Postlethwait J.H., Warren W.C.;
RT "The genome of the platyfish, Xiphophorus maculatus, provides insights into
RT evolutionary adaptation and several complex traits.";
RL Nat. Genet. 45:567-572(2013).
RN [3] {ECO:0000313|Ensembl:ENSXMAP00000013274.2}
RP IDENTIFICATION.
RC STRAIN=JP 163 A {ECO:0000313|Ensembl:ENSXMAP00000013274.2};
RG Ensembl;
RL Submitted (NOV-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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR AlphaFoldDB; M4AFN0; -.
DR Ensembl; ENSXMAT00000013290.2; ENSXMAP00000013274.2; ENSXMAG00000013235.2.
DR eggNOG; KOG4297; Eukaryota.
DR GeneTree; ENSGT00940000164633; -.
DR HOGENOM; CLU_020848_0_0_1; -.
DR OMA; FVTCDHA; -.
DR OrthoDB; 3035244at2759; -.
DR Proteomes; UP000002852; Unassembled WGS sequence.
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 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 Reference proteome {ECO:0000313|Proteomes:UP000002852};
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..746
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5017345372"
FT TRANSMEM 690..713
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 22..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 314..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..498
FT /note="Sushi"
FT /evidence="ECO:0000259|PROSITE:PS50923"
FT DOMAIN 499..561
FT /note="Sushi"
FT /evidence="ECO:0000259|PROSITE:PS50923"
FT DOMAIN 562..623
FT /note="Sushi"
FT /evidence="ECO:0000259|PROSITE:PS50923"
FT DOMAIN 624..683
FT /note="Sushi"
FT /evidence="ECO:0000259|PROSITE:PS50923"
FT REGION 724..746
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 469..496
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00302"
FT DISULFID 532..559
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00302"
FT DISULFID 594..621
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00302"
FT DISULFID 654..681
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00302"
SQ SEQUENCE 746 AA; 82684 MW; DB7BA247C5E91ADC CRC64;
MMAASLMPFV VFCSMLCMWT GVECWSYFYS NVTMDWESAR TWCKENYTDM VAIQNREEIE
HLKRVLPKKA GYYWIGIRKV NDVWTWVGTN KSLTAEATNW AHGEPNNGQN GIISGQAEDC
VEMYIKREKD EGKWNDERCS KKKTALCYTA ACKSDSCIHG ECVETINSHM CKCSSGFYGE
KCEQVVQCNK DQVIKPEKGS VTCSHKYKNF SYESLCQYSC EEGYRLNMSE PQKCQETGTW
SKQSPTCELI QCQELSAPER GFMNCSDPLR NFSYSSSCRF TCMEGYELDD SSSITLQCES
SGKWNASKPS CVAVQCPALQ NPDNGFITCE DDTNMRFSYG KRCNLSCAPG YHLVGPEMIT
CTSEAVWSEK MPLCEAVQCP TLKDPENGSL KCIDGHGYEK NCSFSCDPGF ELQGVHTIQC
SEDGQWSNDI PTCKAIQCPA LQDLENGALS CEGDMEMRFS YRKTCSFNCD PGFKLQGAHS
IQCSKDKTWT DATPSCTAVQ CPALQDLENG VLSCEDDTEM RFSYKKSCTF KCVPGHRLVG
PSEVTCTAEA QWSEKMPHCE AITCQNPDGA AHMIVECSKP STDLDPSSTC SFSCEAGFEL
RGANTTTCSQ DGQWNEALPT CKAIRCPLLD APENGHINCS DSQPVFNSQC SFTCDQDYTL
DGHEILTCDR RGSWTGKNPT CQASSAPATV ITTGVAAGAT ALATGVSLIM WILKKMKQRA
SKFELNSTSD SEEPLQVYKS SSDSLV
//
