ID A0A8C9NRG4_SERCA Unreviewed; 949 AA.
AC A0A8C9NRG4;
DT 19-JAN-2022, integrated into UniProtKB/TrEMBL.
DT 19-JAN-2022, sequence version 1.
DT 28-JAN-2026, entry version 21.
DE RecName: Full=Signal peptide, CUB and EGF-like domain-containing protein 2 {ECO:0000256|ARBA:ARBA00067359};
DE AltName: Full=Signal peptide, CUB and EGF-like domain-containing protein 3 {ECO:0000256|ARBA:ARBA00067360};
GN Name=SCUBE3 {ECO:0000313|Ensembl:ENSSCAP00000022083.1};
OS Serinus canaria (Island canary) (Fringilla canaria).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Neoaves; Telluraves; Australaves;
OC Passeriformes; Passeroidea; Fringillidae; Carduelinae; Serinus.
OX NCBI_TaxID=9135 {ECO:0000313|Ensembl:ENSSCAP00000022083.1, ECO:0000313|Proteomes:UP000694409};
RN [1] {ECO:0000313|Ensembl:ENSSCAP00000022083.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (AUG-2025) to UniProtKB.
RN [2] {ECO:0000313|Ensembl:ENSSCAP00000022083.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2025) to UniProtKB.
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}.
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DR AlphaFoldDB; A0A8C9NRG4; -.
DR Ensembl; ENSSCAT00000024615.1; ENSSCAP00000022083.1; ENSSCAG00000015844.1.
DR GeneTree; ENSGT00940000153185; -.
DR Proteomes; UP000694409; 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:0009967; P:positive 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:000032; signal peptide, CUB and EGF-like domain-containing protein 2 isoform X1; 1.
DR FunFam; 2.10.25.10:FF:000199; signal peptide, CUB and EGF-like domain-containing protein 2 isoform X2; 1.
DR FunFam; 2.10.25.10:FF:000110; Signal peptide, CUB domain and EGF-like domain-containing 1; 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; 2.10.50.10: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; 2.
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; 2.
DR Pfam; PF14670; FXa_inhibition; 4.
DR SMART; SM00042; CUB; 1.
DR SMART; SM00181; EGF; 10.
DR SMART; SM00179; EGF_CA; 7.
DR SMART; SM01411; Ephrin_rec_like; 3.
DR SUPFAM; SSF57196; EGF/Laminin; 3.
DR SUPFAM; SSF57184; Growth factor receptor domain; 2.
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; 4.
PE 4: Predicted;
KW Calcium {ECO:0000256|ARBA:ARBA00022837};
KW Developmental protein {ECO:0000256|ARBA:ARBA00022473};
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:UP000694409};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Secreted {ECO:0000256|ARBA:ARBA00022525};
KW Signal {ECO:0000256|ARBA:ARBA00022729}.
FT DOMAIN 6..46
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 89..125
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 254..294
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 295..333
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 760..872
FT /note="CUB"
FT /evidence="ECO:0000259|PROSITE:PS01180"
FT DISULFID 299..309
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
SQ SEQUENCE 949 AA; 105079 MW; 072CDE2B57DA5324 CRC64;
IPLLQYVDEC VEGTDNCHID AICQNTPKSY KCICKSGYTG DGKHCKDVDE CEREDNAGCV
HECVNIPGNY RCTCYDGFRL AHDGHNCLDL DECSEGNGGC QQTCVNMMGS YECFCREGFF
LSDNQHTCIQ RPEEGMNCMN KNHGCAHICR ETPKGGIACE CRPGFELTKN QRDCKLTCNY
GNGGCQHTCD DTDQGPKCGC HVKFLLHSDG VTCIETCAVN NGGCDSKCHD AATGVHCSCP
MGFMLQPDRK TCKDIDECRL NNGGCDHICR NTVGSFECSC KKGYKLLINE RNCQDIDECS
FDRTCDHLCI NTPGSFQCLC HKGYTLYGLT HCGDIDECSI NRGGCKFGCI NTPGSYQCTC
PAGCKLHWNK KDCLVKCLPG SVPPRATLTC NKMGKKDSCA LSCTSKARFL PESDSSYTVS
CGTPVLRQGS QHRPTNSSQQ CLETVAAPVK QKASFKIKDA KCHLHPRAKG KQEEAGKAGA
QGGSAPCSDC QVTFVNLKCD SSKKGKGRRA RNSPNKEVTR ITLEFEAEIK PEEITGGCNL
HCLRQRVEKK LKSAIKALKK SINQERFLLR FSGMEYEVAR KLSVAPERQE SCGPGQQRLA
SKCVSCSQGT YYHGQTEQCV PCPPGTYQEK EGQLSCDLCP RGDTFGPIGA TNITGCTGKE
GTGGPADRKV LSIPRAHRSC WFGCLLFRGD PKKGSTCSGH VGLQCSPGHY YNTSVHRCIR
CAVGTYQPDF RQNYCISCPG NTTTDFDGST SVSQCKNRQC GGELGEYTGY IESPNYPGNY
PANIECTWNI NPPPKRKILI VVPEIFLPSE DECGDVLVMR KNSSPSSITT YETCQTYERP
IAFTARSRKL WINFKTSEAN SARGFQIPYV TYDEDYEQLV EDIVRDGRLY ASENHQEILK
DKKLIKAFFD VLAHPQNYFK YTEKHKEMLP RSFIKLLRSK VSSFLRPYK
//
