ID A0A2U9B7E7_SCOMX Unreviewed; 784 AA.
AC A0A2U9B7E7;
DT 12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT 12-SEP-2018, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE SubName: Full=Putative endosialin {ECO:0000313|EMBL:AWO99890.1, ECO:0000313|EMBL:AWO99892.1};
DE SubName: Full=Putative endosialin isoform 4 {ECO:0000313|EMBL:AWO99893.1};
GN ORFNames=SMAX5B_006762 {ECO:0000313|EMBL:AWO99892.1};
OS Scophthalmus maximus (Turbot) (Psetta maxima).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Carangaria; Pleuronectiformes; Pleuronectoidei; Scophthalmidae;
OC Scophthalmus.
OX NCBI_TaxID=52904 {ECO:0000313|EMBL:AWO99892.1, ECO:0000313|Proteomes:UP000246464};
RN [1] {ECO:0000313|EMBL:AWO99892.1, ECO:0000313|Proteomes:UP000246464}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Martinez P.;
RT "Integrating genomic resources of turbot (Scophthalmus maximus) in depth
RT evaluation of genetic and physical mapping variation across individuals.";
RL Submitted (DEC-2017) to the EMBL/GenBank/DDBJ databases.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00076}.
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DR EMBL; CP026246; AWO99890.1; -; Genomic_DNA.
DR EMBL; CP026246; AWO99892.1; -; Genomic_DNA.
DR EMBL; CP026246; AWO99893.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2U9B7E7; -.
DR Proteomes; UP000246464; Chromosome 4.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro.
DR GO; GO:0048513; P:animal organ development; IEA:UniProt.
DR GO; GO:0071586; P:CAAX-box protein processing; IEA:InterPro.
DR CDD; cd00054; EGF_CA; 3.
DR Gene3D; 2.10.25.10; Laminin; 5.
DR InterPro; IPR026823; cEGF.
DR InterPro; IPR001881; EGF-like_Ca-bd_dom.
DR InterPro; IPR000742; EGF-like_dom.
DR InterPro; IPR000152; EGF-type_Asp/Asn_hydroxyl_site.
DR InterPro; IPR018097; EGF_Ca-bd_CS.
DR InterPro; IPR009030; Growth_fac_rcpt_cys_sf.
DR InterPro; IPR003675; Rce1-like.
DR PANTHER; PTHR14789; CHONDROLECTIN VARIANT CHODLFDELTAE; 1.
DR Pfam; PF12662; cEGF; 3.
DR Pfam; PF02517; Rce1-like; 1.
DR SMART; SM00181; EGF; 5.
DR SMART; SM00179; EGF_CA; 4.
DR SUPFAM; SSF57196; EGF/Laminin; 1.
DR SUPFAM; SSF57184; Growth factor receptor domain; 2.
DR PROSITE; PS00010; ASX_HYDROXYL; 3.
DR PROSITE; PS01186; EGF_2; 4.
DR PROSITE; PS50026; EGF_3; 3.
DR PROSITE; PS01187; EGF_CA; 2.
PE 4: Predicted;
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}; Membrane {ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000246464};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 7..25
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 78..100
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 121..145
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 179..198
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 727..750
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 452..489
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 490..528
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 529..568
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT REGION 388..408
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 569..591
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 646..719
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 392..406
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 569..584
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 646..669
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 698..719
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT DISULFID 494..504
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 533..543
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
SQ SEQUENCE 784 AA; 84893 MW; 653AA1218946AF43 CRC64;
MGVRAEGFAP AVTLPLLLTM VAYLGPLVQS AMDAPGGFTA ELQSALDVQS WRSCVGDAVW
LRNQVVAPLT EELVFRGAML PMLVPCAGPT GAIFTAPLFF GVGHLHHIIE QRRLHKDSMR
VILLVAGMQF LYTTVFGAFT SFLFMRTGHV AGPVLCHSFC NSQGLPDFSS ALQHPQRSAL
LFSYLMGALM FLVLLFPLTD PFLYGDQDGQ FTNWLREDSP GTCAAPRCVA MTVHTSESGR
ESSDNFGWLD GSCALPLDGY VCQYNYKGMC PPLEDEGRGP AVYTTPFHLV STLLTHVPYG
SVASLPCPAD SSDPDTNAEQ TVLCMERDDE TVGWSRDAPL CSSSADPKNQ DWCSGDHGCE
QYCQNTDTDY YCYCAEGFTI DEDGYSCKPD PLSQTDPPQL SSDSAGPADQ PHVKDVCVEM
GCEYDCVETQ RGIRCTCPPG YQMGPDGRRC SDVDECQQQP CPQLCVNIPG TFHCTCHSGY
QPDDDGECVD VDECLDEGSC EGTCENTVGS FTCLCNPGYE LGSGGECVDV DECVGESPCQ
QQCLNYMGGY QCYCDNGYDL QTDGLTCQPS PDDEEYSTLT PDPSDSAHIP DMDPDHDIPW
STSFTPDPNF EADTNFDVDW LTEAPEALSP DMAHGRDNHL NQWDAQSPKR YQTAPPPTQK
YNTGNEIDND AKTGGRGASG GVGAETANGS ATGTGEGSNK DRLEDFNDAA DVGDGSAAGK
RKHDKSWLLV ALLVPLCVFL VVMLALGIVY CTSCAVDKSL SLSNCYRWML PATPPDRRDG
KTQA
//
