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Database: UniProt
Entry: A0A8D2MDS8_ZONAL
LinkDB: A0A8D2MDS8_ZONAL
Original site: A0A8D2MDS8_ZONAL 
ID   A0A8D2MDS8_ZONAL        Unreviewed;       913 AA.
AC   A0A8D2MDS8;
DT   19-JAN-2022, integrated into UniProtKB/TrEMBL.
DT   19-JAN-2022, sequence version 1.
DT   28-JAN-2026, entry version 21.
DE   SubName: Full=Signal peptide, CUB domain and EGF like domain containing 1 {ECO:0000313|Ensembl:ENSZALP00000005014.1};
GN   Name=SCUBE1 {ECO:0000313|Ensembl:ENSZALP00000005014.1};
OS   Zonotrichia albicollis (White-throated sparrow) (Fringilla albicollis).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Neognathae; Neoaves; Telluraves; Australaves;
OC   Passeriformes; Passerellidae; Zonotrichia.
OX   NCBI_TaxID=44394 {ECO:0000313|Ensembl:ENSZALP00000005014.1, ECO:0000313|Proteomes:UP000694413};
RN   [1] {ECO:0000313|Ensembl:ENSZALP00000005014.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (AUG-2025) to UniProtKB.
RN   [2] {ECO:0000313|Ensembl:ENSZALP00000005014.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (SEP-2025) 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   AlphaFoldDB; A0A8D2MDS8; -.
DR   Ensembl; ENSZALT00000007500.1; ENSZALP00000005014.1; ENSZALG00000003795.1.
DR   Proteomes; UP000694413; Unassembled WGS sequence.
DR   GO; GO:0009986; C:cell surface; IEA:TreeGrafter.
DR   GO; GO:0005615; C:extracellular space; IEA:TreeGrafter.
DR   GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR   GO; GO:0007165; P:signal transduction; IEA:TreeGrafter.
DR   CDD; cd00041; CUB; 1.
DR   CDD; cd00054; EGF_CA; 2.
DR   FunFam; 2.10.25.10:FF:000510; Signal peptide, CUB and EGF-like domain-containing protein 1; 1.
DR   FunFam; 2.10.50.10:FF:000024; 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; 2.60.120.290: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; 2.10.25.10:FF:000008; Signal peptide, CUB domain, EGF-like 2; 2.
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:SF4; SIGNAL PEPTIDE, CUB AND EGF-LIKE DOMAIN-CONTAINING PROTEIN 1; 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; 7.
DR   SMART; SM01411; Ephrin_rec_like; 3.
DR   SUPFAM; SSF57196; EGF/Laminin; 1.
DR   SUPFAM; SSF57184; Growth factor receptor domain; 4.
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:UP000694413};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737};
KW   Secreted {ECO:0000256|ARBA:ARBA00022525};
KW   Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..33
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           34..913
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5034739402"
FT   DOMAIN          38..78
FT                   /note="EGF-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50026"
FT   DOMAIN          122..158
FT                   /note="EGF-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50026"
FT   DOMAIN          317..357
FT                   /note="EGF-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50026"
FT   DOMAIN          358..396
FT                   /note="EGF-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50026"
FT   DOMAIN          724..835
FT                   /note="CUB"
FT                   /evidence="ECO:0000259|PROSITE:PS01180"
FT   DISULFID        362..372
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
SQ   SEQUENCE   913 AA;  100768 MW;  57F5D2190E50FBD0 CRC64;
     PGLGGCGCGF KGNIYPCCFV ALVSLLICPL GVPSMLPDVD ECAEATDDCH IDAICQNTPK
     SYKCICKPGY KGEGKQCEDI DECENDFYNG GCVHECINIP GNYRCTCYDG FMLAHDGHNC
     LDVDECLDNN GGCQQICVNT MGSYECQCKE GFFLSDNQHT CIHRSIEGMN CMNKDHGCAH
     ICRETPKGGV ACECRPGFEL AKNQKDCKLT CNYGNGGCQH TCDDTDTGPV CGCHQKYALH
     SDGRTCIEKD EAAIESSEYN TTSVADVDKR VKRRLLMETC AVNNGGCDRT CKDTATGVRC
     SCPVGFTLQP DGKTCKDIDE CLVNNGGCDH FCRNTVGSFE CSCQKGYKLL TDERTCQDID
     ECSFERTCDH TCINYPGSFE CLCHKGYTLY GLTHCGDIDE CSISNGSCDF GCLNTMGSYE
     CVCPPGKKLH WNKKDCVEMV KCLPNAKPTP KAQLVCSKAG GIESCFLSCP SNTLFVPGCD
     FFVIISHLDT CNIDCVRKRM EQKLQTAIKT LRKSINKQQF YIQFSGTEYE VAQKPAKATE
     GHEACSTGQV LQDGKCVTCS TGTFYSGEQK QCVPCSPGTY QDTEGQLTCE PCPSNDGQGV
     AGARNVSECG GQCSPGHYSS DGFKPCTVCP LGTYQPEPGR TLCFPCGGGL VTKYEGAVSF
     QDCETKVHCS PGHYYNSTTH RCIRCPVGTY QPEFGQNYCI TCPGNTSTDF DGSTNVTHCK
     NQHCGGELGD YTGYIESPNY PGDYPANVEC IWNINPPPKR RILIVVPEIF LPIEDECGDV
     LVMRKTSPTS ITTYETCQTY ERPIAFTSRS RKLWIQFKSN EGNSGKGFQV PYVTYDEDYQ
     QLIEDIVRDG RLYASENHQE ILKDKKLIKA LFDVLAHPQN YFKYTAQESK EMFPRSFIKL
     LRSKVSRFLR PYK
//
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