ID A0A4U1EK81_MONMO Unreviewed; 764 AA.
AC A0A4U1EK81;
DT 31-JUL-2019, integrated into UniProtKB/TrEMBL.
DT 31-JUL-2019, sequence version 1.
DT 28-JAN-2026, entry version 25.
DE RecName: Full=Endosialin {ECO:0000256|ARBA:ARBA00074551};
DE AltName: Full=Tumor endothelial marker 1 {ECO:0000256|ARBA:ARBA00078437};
GN Name=CD248 {ECO:0000313|Ensembl:ENSMMNP00015023334.1};
GN ORFNames=EI555_003476 {ECO:0000313|EMBL:TKC36553.1};
OS Monodon monoceros (Narwhal) (Ceratodon monodon).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Whippomorpha; Cetacea; Odontoceti;
OC Monodontidae; Monodon.
OX NCBI_TaxID=40151 {ECO:0000313|EMBL:TKC36553.1, ECO:0000313|Proteomes:UP000308365};
RN [1] {ECO:0000313|Proteomes:UP000308365}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=31054839; DOI=10.1016/j.isci.2019.03.023;
RA Westbury M.V., Petersen B., Garde E., Heide-Jorgensen M.P., Lorenzen E.D.;
RT "Narwhal Genome Reveals Long-Term Low Genetic Diversity despite Current
RT Large Abundance Size.";
RL IScience 15:592-599(2019).
RN [2] {ECO:0000313|EMBL:TKC36553.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=MVW {ECO:0000313|EMBL:TKC36553.1};
RC TISSUE=Liver {ECO:0000313|EMBL:TKC36553.1};
RA Westbury M.V., Petersen B., Garde E., Heide-Jorgensen M.P., Lorenzen E.D.;
RT "Narwhal Genome Reveals Long-Term Low Genetic Diversity despite Current
RT Large Abundance Size.";
RL IScience 0:0-0(2019).
RN [3] {ECO:0000313|Ensembl:ENSMMNP00015023334.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (MAY-2025) to UniProtKB.
CC -!- SUBUNIT: Interacts with PDGFRA; this interaction promotes PDGF receptor
CC signaling pathway. Interacts with integrin beta-1/ITGB1. Interacts with
CC insulin receptor/INSR; this interaction diminishes INSR
CC autophosphorylation. {ECO:0000256|ARBA:ARBA00063144}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004479}; Single-
CC pass type I membrane protein {ECO:0000256|ARBA:ARBA00004479}.
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DR EMBL; RWIC01001277; TKC36553.1; -; Genomic_DNA.
DR RefSeq; XP_029064572.1; XM_029208739.1.
DR AlphaFoldDB; A0A4U1EK81; -.
DR Ensembl; ENSMMNT00015025637.1; ENSMMNP00015023334.1; ENSMMNG00015017128.1.
DR GeneID; 114887235; -.
DR CTD; 57124; -.
DR GeneTree; ENSGT00940000162405; -.
DR OrthoDB; 10045365at2759; -.
DR Proteomes; UP000308365; Unassembled WGS sequence.
DR Proteomes; UP000694561; Unplaced.
DR GO; GO:0005737; C:cytoplasm; IEA:Ensembl.
DR GO; GO:0009897; C:external side of plasma membrane; IEA:TreeGrafter.
DR GO; GO:0031012; C:extracellular matrix; IEA:TreeGrafter.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0030246; F:carbohydrate binding; IEA:UniProtKB-KW.
DR GO; GO:0050840; F:extracellular matrix binding; IEA:Ensembl.
DR GO; GO:1990430; F:extracellular matrix protein binding; IEA:TreeGrafter.
DR GO; GO:0060033; P:anatomical structure regression; IEA:Ensembl.
DR GO; GO:0072577; P:endothelial cell apoptotic process; IEA:Ensembl.
DR GO; GO:0010761; P:fibroblast migration; IEA:Ensembl.
DR GO; GO:0048144; P:fibroblast proliferation; IEA:Ensembl.
DR GO; GO:0048535; P:lymph node development; IEA:Ensembl.
DR GO; GO:2000353; P:positive regulation of endothelial cell apoptotic process; IEA:Ensembl.
DR GO; GO:0048146; P:positive regulation of fibroblast proliferation; IEA:Ensembl.
DR CDD; cd03600; CLECT_thrombomodulin_like; 1.
DR CDD; cd00054; EGF_CA; 1.
DR FunFam; 2.10.25.10:FF:000406; CD248 molecule; 1.
DR FunFam; 2.10.25.10:FF:000489; CD248 molecule; 1.
DR FunFam; 3.10.100.10:FF:000061; CD248 molecule; 1.
DR Gene3D; 2.10.25.10; Laminin; 3.
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; IPR051505; C-type_lectin_domain.
DR InterPro; IPR016187; CTDL_fold.
DR InterPro; IPR000742; EGF.
DR InterPro; IPR001881; EGF-like_Ca-bd_dom.
DR InterPro; IPR018097; EGF_Ca-bd_CS.
DR InterPro; IPR049883; NOTCH1_EGF-like.
DR InterPro; IPR057350; THBD.
DR PANTHER; PTHR14789; CHONDROLECTIN VARIANT CHODLFDELTAE; 1.
DR PANTHER; PTHR14789:SF4; ENDOSIALIN; 1.
DR Pfam; PF07645; EGF_CA; 1.
DR Pfam; PF14670; FXa_inhibition; 1.
DR Pfam; PF00059; Lectin_C; 1.
DR Pfam; PF25444; THBD; 1.
DR SMART; SM00034; CLECT; 1.
DR SMART; SM00181; EGF; 3.
DR SMART; SM00179; EGF_CA; 2.
DR SUPFAM; SSF56436; C-type lectin-like; 1.
DR SUPFAM; SSF57196; EGF/Laminin; 2.
DR PROSITE; PS50041; C_TYPE_LECTIN_2; 1.
DR PROSITE; PS01187; EGF_CA; 1.
PE 4: Predicted;
KW Calcium {ECO:0000256|ARBA:ARBA00022837};
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW EGF-like domain {ECO:0000256|ARBA:ARBA00022536};
KW Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW Lectin {ECO:0000256|ARBA:ARBA00022734};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000694561};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP};
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..17
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 18..764
FT /note="Endosialin"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5044609463"
FT TRANSMEM 693..718
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 30..147
FT /note="C-type lectin"
FT /evidence="ECO:0000259|PROSITE:PS50041"
FT REGION 605..667
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 740..764
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 613..627
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 755..764
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 764 AA; 81841 MW; 8243CE890D055209 CRC64;
MLLRLLLAWA AAVPTLGQAP WAAEPRAACG PGSCYALFPR RRTFLEAWRA CRELGGDLAT
PRTPEEARRV DSLVGPGPAS RLLWIGLQRQ ARHCQPQRPL RGFTWTTGDQ DTAFTNWAQP
ATGGPCPAQR CAALEASGEH RWLEGSCTLA VDGYLCQFGF EGSCPALPDE AGQAGPAVYT
TPFHLVSAEF QWLPFGSVAA VPCQAGREAS LLCVKQPDGG VGWSRTGPLC PGTGCGPDNG
GCEHECVEEA DGRVSCRCTE GFRLAVDGRS CEDPCAHALC EQQCEPGGPQ GYSCHCRLGF
RPAEDEPHRC VDTDECRIAG VCQQMCVNYV GGFECYCSEG HELEADGISC SPAGAVGARA
SHDLGDELLE DGEDEEDEDE AWEVFDGGWT EMPGIPWMEA TQSPDFGLAY RPSFPEDRES
RMPYLDPTWP PPLSAPRVPY HSSVLSVTRP VVVSTTRPPL PSAHQPPIVS ATRPPLTPAP
QPPVIPAVQP ALPSDHQFPK ISANSPDLPS AHRPPVISAT HPGLTPAHRP PIISAKYPEL
FPAHQSPMFP DTQNTTHLPR IPANHVPLVT TSSALQTPVS PDIPVLKAQA THHPITSTVQ
SSLITTSRPP VSPAHQVPVP AATQPPAFHT PLPPESPTNQ TLLASPTHPH SKARQVPREG
TPDPNLAPWL PSAVPTALGE ASPAGRSRRD DRWLLVALLV PTCVFLVVLL ALGIVYCTRC
GPHAPNKRVT DCYRWVTHAG SKGSTEPAPH RGSLTGVQTC RTSV
//
