ID A0A7L2X5Y0_9PASS Unreviewed; 966 AA.
AC A0A7L2X5Y0;
DT 07-APR-2021, integrated into UniProtKB/TrEMBL.
DT 07-APR-2021, sequence version 1.
DT 28-JAN-2026, entry version 23.
DE RecName: Full=Signal peptide, CUB and EGF-like domain-containing protein 3 {ECO:0000256|ARBA:ARBA00067360};
DE Flags: Fragment;
GN Name=Scube3 {ECO:0000313|EMBL:NXS78026.1};
GN ORFNames=ERPZAN_R01556 {ECO:0000313|EMBL:NXS78026.1};
OS Erpornis zantholeuca.
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Neoaves; Telluraves; Australaves;
OC Passeriformes; Sylvioidea; Timaliidae; Erpornis.
OX NCBI_TaxID=1112836 {ECO:0000313|EMBL:NXS78026.1, ECO:0000313|Proteomes:UP000545329};
RN [1] {ECO:0000313|EMBL:NXS78026.1, ECO:0000313|Proteomes:UP000545329}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=B10K-DU-002-58 {ECO:0000313|EMBL:NXS78026.1};
RC TISSUE=Muscle {ECO:0000313|EMBL:NXS78026.1};
RA Zhang G.;
RT "Bird 10,000 Genomes (B10K) Project - Family phase.";
RL Submitted (SEP-2019) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBUNIT: Forms homooligomers. Forms heterooligomers with SCUBE1 and
CC SCUBE2. Interacts with TGFBR2 through the CUB domain; this interaction
CC does not affect TGFB1-binding to TGFBR2. Interacts with BMP2, BMP4 and
CC BMP7; the interaction is mediated by the CUB domain. Interacts with
CC BMPR1A, BMPR1B and BMPR2; the interaction with BMPR1A and BMPR1B is
CC BMP2- and BMP4-dependent. {ECO:0000256|ARBA:ARBA00064610}.
CC -!- SUBCELLULAR LOCATION: Cell surface {ECO:0000256|ARBA:ARBA00004241}.
CC Secreted {ECO:0000256|ARBA:ARBA00004613}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00076}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:NXS78026.1}.
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DR EMBL; VZTN01001861; NXS78026.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A7L2X5Y0; -.
DR OrthoDB; 4062651at2759; -.
DR Proteomes; UP000545329; Unassembled WGS sequence.
DR GO; GO:0009986; C:cell surface; IEA:UniProtKB-SubCell.
DR GO; GO:0005615; C:extracellular space; IEA:TreeGrafter.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0045669; P:positive regulation of osteoblast differentiation; IEA:UniProtKB-ARBA.
DR GO; GO:0009966; P:regulation of signal transduction; IEA:UniProtKB-ARBA.
DR GO; GO:0007165; P:signal transduction; IEA:TreeGrafter.
DR CDD; cd00041; CUB; 1.
DR CDD; cd00054; EGF_CA; 3.
DR FunFam; 2.10.25.10:FF:000510; Signal peptide, CUB and EGF-like domain-containing protein 1; 1.
DR FunFam; 2.10.25.10:FF:000032; signal peptide, CUB and EGF-like domain-containing protein 2 isoform X1; 1.
DR FunFam; 2.10.50.10:FF:000002; signal peptide, CUB and EGF-like domain-containing protein 2 isoform X1; 1.
DR FunFam; 2.10.50.10:FF:000006; Signal peptide, CUB domain and EGF like domain containing 3; 1.
DR FunFam; 2.10.25.10:FF:000028; Signal peptide, CUB domain and EGF-like domain-containing 2; 1.
DR FunFam; 2.10.25.10:FF:000030; Signal peptide, CUB domain and EGF-like domain-containing 2; 1.
DR FunFam; 2.10.25.10:FF:000035; Signal peptide, CUB domain and EGF-like domain-containing 2; 1.
DR FunFam; 2.10.25.10:FF:000037; Signal peptide, CUB domain and EGF-like domain-containing 2; 1.
DR FunFam; 2.60.120.290:FF:000002; Signal peptide, CUB domain and EGF-like domain-containing 2; 1.
DR FunFam; 2.10.25.10:FF:000124; Signal peptide, CUB domain and EGF-like domain-containing 3; 1.
DR FunFam; 2.10.25.10:FF:000161; Signal peptide, CUB domain and EGF-like domain-containing 3; 1.
DR FunFam; 2.10.50.10:FF:000008; Signal peptide, CUB domain and EGF-like domain-containing 3; 1.
DR FunFam; 2.10.25.10:FF:000008; Signal peptide, CUB domain, EGF-like 2; 1.
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; IPR000742; EGF.
DR InterPro; IPR001881; EGF-like_Ca-bd_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; IPR024731; NELL2-like_EGF.
DR InterPro; IPR049883; NOTCH1_EGF-like.
DR InterPro; IPR052071; SCUB_EGF-like_domain.
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; 4.
DR PRINTS; PR00907; THRMBOMODULN.
DR SMART; SM00042; CUB; 1.
DR SMART; SM00181; EGF; 10.
DR SMART; SM00179; EGF_CA; 7.
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; 4.
DR PROSITE; PS01187; EGF_CA; 3.
PE 4: Predicted;
KW Calcium {ECO:0000256|ARBA:ARBA00022837};
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:UP000545329};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Secreted {ECO:0000256|ARBA:ARBA00022525};
KW Signal {ECO:0000256|ARBA:ARBA00022729}.
FT DOMAIN 1..41
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 84..120
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 265..305
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 306..344
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 777..889
FT /note="CUB"
FT /evidence="ECO:0000259|PROSITE:PS01180"
FT REGION 471..490
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT DISULFID 310..320
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:NXS78026.1"
FT NON_TER 966
FT /evidence="ECO:0000313|EMBL:NXS78026.1"
SQ SEQUENCE 966 AA; 106924 MW; C9B9B387AC5A73CA CRC64;
DVDECVEGTD NCHIDAICQN TPKSYKCICK SGYTGDGKHC KDVDECERED NAGCVHECVN
IPGNYRCTCY DGFRLAHDGH NCLDLDECSE GNGGCQQTCV NMMGSYECFC REGFFLSDNQ
HTCIQRPEEG MNCMNKNHGC AHICRETPKG GIACECRPGF ELTKNQRDCK LTCNYGNGGC
QHTCDDTDQG PKCGCHVKFL LHSDGVTCIG ERHFQQHVIL ETFSNETCAV NNGGCDSKCH
DAATGVHCSC PMGFMLQPDR KTCKDIDECR LNNGGCDHIC RNTVGSFECS CKKGYKLLIN
ERNCQDIDEC SFDRTCDHLC INTPGSFQCL CHKGYTLYGL THCGDIDECS INRGGCKFGC
INTPGSYQCT CPAGCKLHWN KKDCVGSVPP RATLTCNKTG KKDSCALSCT SKARFLPESD
SSYTVSCGTP VLRQGGQHRA TNSSQQCLET VAAPVKQKAS FKIKDAKCHL HPRTKGKQEE
GGKAGAQGGS APCSDCQVTF VNLKCDSSKK GKGRRARNSP NKEVTRITLE FEAEIKPEEI
TASCNLQCLR QRVEKKLKSA IKALKKSINQ ERFLLRFAGM EYEVARKLSV APERQESCGP
GQQRLASKCV SCSQGTYYHG QTEQCVPCPP GTYQEKEGQL SCDLCPRGDT FGPIGATNIT
GCTGQCPPGQ HSADGFKPCQ PCPRGSYQPE VGRALCFPCG GGLTTRHEGA LSFQDCDTKV
QCSPGHYYNT SVHRCIRCAV GTYQPDFRQN YCISCPGNTT TDFDGSTSVS QCKNRQCGGE
LGEYTGYIES PNYPGNYPAN VECTWNINPP PKRKILIVVP EIFLPSEDEC GDVLVMRKNS
SPSSITTYET CQTYERPIAF TARSRKLWIN FKTSEANSAR GFQIPYVTYD EDYEQLVEDI
VRDGRLYASE NHQEILKDKK LIKAFFDVLA HPQNYFKYTE KHKEMLPRSF IKLLRSKVSS
FLRPYK
//
