ID A0A8I3S0I2_CANLF Unreviewed; 1049 AA.
AC A0A8I3S0I2;
DT 25-MAY-2022, integrated into UniProtKB/TrEMBL.
DT 25-MAY-2022, sequence version 1.
DT 28-JAN-2026, entry version 20.
DE RecName: Full=Signal peptide, CUB and EGF-like domain-containing protein 1 {ECO:0000256|ARBA:ARBA00067369};
GN Name=SCUBE1 {ECO:0000313|Ensembl:ENSCAFP00845019639.1};
OS Canis lupus familiaris (Dog) (Canis familiaris).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Caniformia; Canidae; Canis.
OX NCBI_TaxID=9615 {ECO:0000313|Ensembl:ENSCAFP00845019639.1, ECO:0000313|Proteomes:UP000805418};
RN [1] {ECO:0000313|Ensembl:ENSCAFP00845019639.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Labrador retriever {ECO:0000313|Ensembl:ENSCAFP00845019639.1};
RA Eory L., Zhang W., Schoenebeck J.;
RT "Long-read based genome assembly of a Labrador retriever dog.";
RL Submitted (MAR-2020) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSCAFP00845019639.1}
RP IDENTIFICATION.
RC STRAIN=Boxer {ECO:0000313|Ensembl:ENSCAFP00845019639.1};
RG Ensembl;
RL Submitted (AUG-2025) to UniProtKB.
RN [3] {ECO:0000313|Ensembl:ENSCAFP00845019639.1}
RP IDENTIFICATION.
RC STRAIN=Boxer {ECO:0000313|Ensembl:ENSCAFP00845019639.1};
RG Ensembl;
RL Submitted (SEP-2025) to UniProtKB.
CC -!- FUNCTION: Could function as an adhesive molecule and its matrix bound
CC and soluble fragments may play a critical role in vascular biology.
CC {ECO:0000256|ARBA:ARBA00054446}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|ARBA:ARBA00004202};
CC Peripheral membrane protein {ECO:0000256|ARBA:ARBA00004202}. Secreted
CC {ECO:0000256|ARBA:ARBA00004613}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00076}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR AlphaFoldDB; A0A8I3S0I2; -.
DR Ensembl; ENSCAFT00845024967.1; ENSCAFP00845019639.1; ENSCAFG00845013737.1.
DR GeneTree; ENSGT00940000153185; -.
DR OrthoDB; 4062651at2759; -.
DR Proteomes; UP000805418; Chromosome 10.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR CDD; cd00041; CUB; 1.
DR CDD; cd00054; EGF_CA; 2.
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:000006; Signal peptide, CUB domain and EGF like domain containing 3; 1.
DR FunFam; 2.10.25.10:FF:000110; Signal peptide, CUB domain and EGF-like domain-containing 1; 1.
DR FunFam; 2.10.50.10:FF:000022; 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; 2.60.120.290: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; SSF57184; Growth factor receptor domain; 5.
DR SUPFAM; SSF49854; Spermadhesin, CUB domain; 1.
DR PROSITE; PS00010; ASX_HYDROXYL; 6.
DR PROSITE; PS01180; CUB; 1.
DR PROSITE; PS01186; EGF_2; 4.
DR PROSITE; PS50026; EGF_3; 2.
DR PROSITE; PS01187; EGF_CA; 2.
PE 4: Predicted;
KW Calcium {ECO:0000256|ARBA:ARBA00022837};
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475};
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 Membrane {ECO:0000256|ARBA:ARBA00023136};
KW Reference proteome {ECO:0000313|Proteomes:UP000805418};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Secreted {ECO:0000256|ARBA:ARBA00022525};
KW Signal {ECO:0000256|ARBA:ARBA00022729}.
FT DOMAIN 89..129
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 379..417
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 853..965
FT /note="CUB"
FT /evidence="ECO:0000259|PROSITE:PS01180"
FT REGION 1..49
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1020..1049
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..11
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 36..49
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT DISULFID 383..393
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
SQ SEQUENCE 1049 AA; 114282 MW; 52013031C9501F97 CRC64;
MRARLSARQP RRLGGWEPER WPRSQQPGAL GERRVGGVPA PRTPARPAGP ARLAASMGAA
AVRWHLCVLL ALGARGRLAG GSGLPGPVDV DECSEGTDDC HIDAICQNTP KSYKCLCKPG
YKGEGRQCED IDECENDYYN GGCVHECINI PGNYRCTCFD GFMLAHDGHN CLDVDECQDN
NGGCQQICVN AMGSYECQCH SGFFLSDNQH TCIHRSNEGM NCMNKDHGCA HICRETPKGG
VACDCRPGFD LAQNQKDCTL TCNYGNGGCQ HSCEDTDTGP MCGCHQKYAL HSDGRTCIET
CAVNNGGCDR TCRDTATGVR CSCPVGFTLQ PDGKTCKDIN ECLTNNGGCD HFCRNTVGSF
ECGCRKGYKL LTDERTCQDI DECSFERTCD HICINSPGSF QCLCHRGYTL YGTTHCGDVD
ECSMNNGSCD QGCINTRGSY ECVCPPGRRL HWNQKDCVEM GKCLSRAKAS PWAQLSCSKV
GGVESCSLSC PAHSLFVPDS ENSYSLSCGV PGLQGKMLQK RNSTSSSTGP SCSGVPAPIR
QKARFKIRDA KCHLRPHSRE PAKEALRQLL LENCHLTFVT LKCDSSKKRR RGRKSPSKEV
THITAEFEVE IKMEEASDTC EADCMRKRAE QSLQAAIKTL RKSIGRQHFS IQVAGTEYAM
AQWPAKALEG QGACSTGQVL QDGKCVACGP GTHFSGEPGQ CVPCVPGTYQ DRDSQLSCTP
CPSSDGLGLT GARNVSECGG QCSPGFFSQD GFRPCQACPV GTYQPEPGRT GCFSCGGGLL
TKHEGTVSFQ DCETKVHCSP GHHYNTTTHR CIRCPIGTYQ PEFGQNHCIT CPGNTSTDFD
GSTNVTHCKN QHCGGELGDY TGYIESPNYP GDYPANAECV WHISPPPKRR ILIVVPEIFL
PVEDECGDVL VMRKSASPAS ITTYETCQTY ERPIAFTSRS RKLWIQFKSN EGNSGKGFQV
PYVTYDEDYQ QLIEDIVRDG RLYASENHQE ILKVSDLLYG KGSRVIPGWW PVVVRAIPVP
TPTPSPQRRE RRRGAGPGSR ASVLADQEG
//
