ID A0A665W8R8_ECHNA Unreviewed; 967 AA.
AC A0A665W8R8;
DT 17-JUN-2020, integrated into UniProtKB/TrEMBL.
DT 17-JUN-2020, sequence version 1.
DT 27-MAR-2024, entry version 19.
DE SubName: Full=Signal peptide, CUB domain and EGF like domain containing 3 {ECO:0000313|Ensembl:ENSENLP00000040459.1};
GN Name=scube3 {ECO:0000313|Ensembl:ENSENLP00000040459.1};
OS Echeneis naucrates (Live sharksucker).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Carangaria; Carangiformes; Echeneidae; Echeneis.
OX NCBI_TaxID=173247 {ECO:0000313|Ensembl:ENSENLP00000040459.1, ECO:0000313|Proteomes:UP000472264};
RN [1] {ECO:0000313|Ensembl:ENSENLP00000040459.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-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 AlphaFoldDB; A0A665W8R8; -.
DR Ensembl; ENSENLT00000041495.1; ENSENLP00000040459.1; ENSENLG00000016657.1.
DR Proteomes; UP000472264; Unplaced.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0048513; P:animal organ development; IEA:UniProt.
DR CDD; cd00041; CUB; 1.
DR CDD; cd00054; EGF_CA; 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; 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; 4.
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; 1.
DR SUPFAM; SSF57184; Growth factor receptor domain; 4.
DR SUPFAM; SSF49854; Spermadhesin, CUB domain; 1.
DR PROSITE; PS00010; ASX_HYDROXYL; 6.
DR PROSITE; PS01180; CUB; 1.
DR PROSITE; PS01186; EGF_2; 6.
DR PROSITE; PS50026; EGF_3; 3.
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}; Reference proteome {ECO:0000313|Proteomes:UP000472264};
KW Repeat {ECO:0000256|ARBA:ARBA00022737}.
FT DOMAIN 10..50
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 280..320
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 321..359
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 777..889
FT /note="CUB"
FT /evidence="ECO:0000259|PROSITE:PS01180"
FT DISULFID 325..335
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
SQ SEQUENCE 967 AA; 106808 MW; C4422BBDAC97E5EA CRC64;
NTNFQDSIAY VDECAEALDN CSIDAICQNT LKSYKCICKS GYKGDGKHCE DVDECATDYN
GGCVHECINI PGNYRCTCYD GFRLAHDGHN CLDVDECSEG NGGCQQICVN MMGSYECRCR
EGFLLSDNQH TCIQRPKEGT KDGPTCMDKN HGCAHICRET QKGGISCECR PGFQLTRNMK
DCKLTCNYGN GGCQHICEET DHGPKCSCHM KFVLHSDGKT CVGDKHAHTY ILSPTQAQIY
LTCAVNNGGC DSTCHDSVTG VRCSCPVGFT LQPDRKTCKD IDECRLNNGG CDHVCRNTVG
SFECSCKKGY KLLTNERTCQ DIDECSFDRA CDHFCVNSAG SFQCLCHKGY VLYGLAHCGD
IDECSINRGG CKYGCINTLG SFECTCPTGF KLHWNKKDCI ELVKCPPGLV APKATLTCSK
TGKKESCSLT CASKAHYLAE SDNSYSVSCG IPILRGKSPA RVNSSSSQSC IGSTIPQLTE
DRGRTLGPGG QPCSNCLVTF VNLKCDSSKK VKGRRARNPS NKEVTRITLE LEAEVKPGDT
TGSCNLSCLR QRMEKQVKTY IKALKKSINQ ERFLIRVAGL EYEVAQKLPQ AAPDQENCGP
GWERDSGRCV RCLPGSYYHG EQERCVQCPP GTFQEKEGQL ACDLCPGSDG HGPVGARNIS
SCAGQCPTGS FSSDGFKPCQ PCPQGTYQPD LGRTLCFPCG GGLSTKREGA SSFHDCEVKV
QCSPGHYYNT TVHRCIRCPV GTYQTEFRQN YCISCPGNTT TDFDGATSVS QCKNRQCGGE
MGEFMGYIES PNYPGNYPAN VECIWNINPP SKRKILIVVP EIFLPSEDEC GDVLVMRKNW
SATSITTYET CQTYERPIAF TARSRRLWIN FKSNEANSAR GFQIPYVTYD EDYEQLVEDI
VRDGRLYASE NHQEILKDKK LIKTLFDVLA HPNNYFKYTT RESNEMLPRS FIRLISSKVS
AFLRPYK
//
