ID A0A6J3RY83_TURTR Unreviewed; 1204 AA.
AC A0A6J3RY83;
DT 07-OCT-2020, integrated into UniProtKB/TrEMBL.
DT 07-OCT-2020, sequence version 1.
DT 27-MAR-2024, entry version 18.
DE SubName: Full=Signal peptide, CUB and EGF-like domain-containing protein 3 {ECO:0000313|RefSeq:XP_033719562.1};
GN Name=SCUBE3 {ECO:0000313|RefSeq:XP_033719562.1};
OS Tursiops truncatus (Atlantic bottle-nosed dolphin) (Delphinus truncatus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Whippomorpha; Cetacea; Odontoceti;
OC Delphinidae; Tursiops.
OX NCBI_TaxID=9739 {ECO:0000313|Proteomes:UP000245320, ECO:0000313|RefSeq:XP_033719562.1};
RN [1] {ECO:0000313|RefSeq:XP_033719562.1}
RP IDENTIFICATION.
RC TISSUE=Spleen {ECO:0000313|RefSeq:XP_033719562.1};
RG RefSeq;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000256|ARBA:ARBA00004613}.
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_033719562.1; XM_033863671.1.
DR AlphaFoldDB; A0A6J3RY83; -.
DR InParanoid; A0A6J3RY83; -.
DR OrthoDB; 5477406at2759; -.
DR Proteomes; UP000245320; Chromosome 10.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR CDD; cd00041; CUB; 1.
DR CDD; cd00054; EGF_CA; 3.
DR Gene3D; 2.10.25.10; Laminin; 9.
DR Gene3D; 2.60.120.290; Spermadhesin, CUB domain; 1.
DR Gene3D; 2.10.50.10; Tumor Necrosis Factor Receptor, subunit A, domain 2; 3.
DR InterPro; IPR026823; cEGF.
DR InterPro; IPR000859; CUB_dom.
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; IPR024731; EGF_dom.
DR InterPro; IPR009030; Growth_fac_rcpt_cys_sf.
DR InterPro; IPR035914; Sperma_CUB_dom_sf.
DR InterPro; IPR011641; Tyr-kin_ephrin_A/B_rcpt-like.
DR PANTHER; PTHR24046; SIGNAL PEPTIDE, CUB AND EGF-LIKE DOMAIN-CONTAINING; 1.
DR PANTHER; PTHR24046:SF2; SIGNAL PEPTIDE, CUB AND EGF-LIKE DOMAIN-CONTAINING PROTEIN 3; 1.
DR Pfam; PF12662; cEGF; 1.
DR Pfam; PF00431; CUB; 1.
DR Pfam; PF12947; EGF_3; 1.
DR Pfam; PF07645; EGF_CA; 2.
DR Pfam; PF07699; Ephrin_rec_like; 3.
DR Pfam; PF14670; FXa_inhibition; 3.
DR SMART; SM00042; CUB; 1.
DR SMART; SM00181; EGF; 10.
DR SMART; SM00179; EGF_CA; 8.
DR SMART; SM01411; Ephrin_rec_like; 4.
DR SUPFAM; SSF57196; EGF/Laminin; 3.
DR SUPFAM; SSF57184; Growth factor receptor domain; 3.
DR SUPFAM; SSF49854; Spermadhesin, CUB domain; 1.
DR PROSITE; PS00010; ASX_HYDROXYL; 5.
DR PROSITE; PS01180; CUB; 1.
DR PROSITE; PS01186; EGF_2; 4.
DR PROSITE; PS50026; EGF_3; 5.
DR PROSITE; PS01187; EGF_CA; 3.
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}; Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW Reference proteome {ECO:0000313|Proteomes:UP000245320};
KW Repeat {ECO:0000256|ARBA:ARBA00022737}.
FT DOMAIN 246..286
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 329..365
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 494..534
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 535..573
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 574..615
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 1015..1127
FT /note="CUB"
FT /evidence="ECO:0000259|PROSITE:PS01180"
FT REGION 1..140
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 71..89
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 90..107
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT DISULFID 539..549
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
SQ SEQUENCE 1204 AA; 132445 MW; 262E63D51AAF6EA6 CRC64;
MEGEKMQSWC ECKPASHSPH RVRARGRTLA PPLFPPVDRT SRSRVLFGLE PSGSGPAAWG
GGRRARARRG SGRRAEAPFE RKKGTEKEVV EEEGEEEENE KERGEEEKEE EEEKGGPARF
RPPRAARPAP AARPPVASAM GSGRVPGLCL LVLLVHARAA QHSKAVQGER LEEPGAVRVS
EKFGEPWAEV TTHLRILPDF ILTPASSKDF LSSRKERGFC PEGPPSRHPL GGTKRGSHVF
LLPLPDVDEC VEGTDNCHID AICQNTPRSY KCICKSGYTG DGKHCKDVDE CEREDNAGCV
HDCVNIPGNY RCTCYDGFHL AHDGHNCLDV DECAEGNGGC QQSCVNMMGS YECHCREGFF
LSDNQHTCIQ RPEEGMNCMN KNHGCAHICR ETPKGGIACE CRPGFELTKN QRDCKLTCNY
GNGGCQHTCD DTEQGPRCGC HVKFVLHTDG KTCIETCAVN NGGCDSKCHD AATGVHCSCP
VGFMLQPDRK TCKDIDECRL NNGGCDHICR NTVGSFECSC KKGYKLLINE RNCQDIDECS
FDRTCDHICV NTPGSFQCLC HHGYLLYGVT HCGDVDECSI NRGGCRFGCI NTPGSYQCTC
PAGQGRLHWN GKDCTEPVKC HSSPGASKAM ISCSRSGKKD TCALSCPSRA RFLPESENGF
TVSCGIPSPR AAPGRAGHTG NSTNSNHCHE AAVLTVKQRA SFKIKDAKCR LHLRNKGKTE
EASGAPCSDC QVTFIHLKCD SSRKGKGRRA RTPPGKEVTR LTLELEAEVR AEETTAGCGL
PCLRQRMERR LKGSLKMLRK SINQDRFLLR LAGLDYELAH KPGPVAGERA EPVEACRPGQ
HRSGAKCVSC PQGTYYHGQT EQCVPCPAGT FQEREGQLSC DLCPGSDAHG PLGATNVTTC
AGQCSPGQHS VDGFKPCQPC PRGTYQPEAG RTLCFPCGGS LTTKHEGAAS FQDCDTKVQC
SPGHYYNTSI HRCIRCAMGS YQPDFRQNFC TRCPGNTSTD FDGSTSVAQC KNRQCGGELG
EFTGYIESPN YPGNYPAGVE CVWNINPPPK RKILIVVPEI FLPSEDECGD VLVMRKNSSP
SSITTYETCQ TYERPIAFTA RSRKLWINFK TSEANSARGF QIPYVTYDED YEQLVEDIVR
DGRLYASENH QEILKDKKLI KAFFEVLAHP QNYFKYTEKH KEMLPKSFIK LLRSKVSSFL
RPYK
//
