ID A0A1S3WNP2_ERIEU Unreviewed; 992 AA.
AC A0A1S3WNP2;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 35.
DE SubName: Full=Signal peptide, CUB and EGF-like domain-containing protein 3 isoform X4 {ECO:0000313|RefSeq:XP_016047907.1};
GN Name=SCUBE3 {ECO:0000313|RefSeq:XP_016047907.1};
OS Erinaceus europaeus (Western European hedgehog).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Eulipotyphla; Erinaceidae; Erinaceinae;
OC Erinaceus.
OX NCBI_TaxID=9365 {ECO:0000313|Proteomes:UP000079721, ECO:0000313|RefSeq:XP_016047907.1};
RN [1] {ECO:0000313|RefSeq:XP_016047907.1}
RP IDENTIFICATION.
RG RefSeq;
RL Submitted (NOV-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 RefSeq; XP_016047907.1; XM_016192421.1.
DR AlphaFoldDB; A0A1S3WNP2; -.
DR CTD; 222663; -.
DR OrthoDB; 5477406at2759; -.
DR Proteomes; UP000079721; Unplaced.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR CDD; cd00041; CUB; 1.
DR CDD; cd00054; EGF_CA; 3.
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; 3.
DR SMART; SM00042; CUB; 1.
DR SMART; SM00181; EGF; 10.
DR SMART; SM00179; EGF_CA; 8.
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; 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 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:UP000079721};
KW Repeat {ECO:0000256|ARBA:ARBA00022737}; Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..23
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 24..992
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5010208436"
FT DOMAIN 29..69
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 112..148
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 276..316
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 317..355
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 803..915
FT /note="CUB"
FT /evidence="ECO:0000259|PROSITE:PS01180"
FT DISULFID 321..331
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
SQ SEQUENCE 992 AA; 109084 MW; 287439B5095259F0 CRC64;
MGAGRVPWLS LLVLLVHARA AQSGKAAQDV DECVEGTDNC HIDAICQNTP RSYKCICKSG
YTGDGKHCKD VDECEREDNA GCVHDCVNIP GNYRCTCYDG FHLAHDGHNC LDVDECAEGN
GGCQQSCVNM MGSYECHCRE GFFLSDNQHT CIQRPEGMNC MNKNHGCAHI CRETPKGGIA
CECRPGFELT KNQRDCKLTC NYGNGGCQHT CDDTEQGPRC GCHVKFVLHT DGKTCIETCA
VNNGGCDSKC HDAATGVHCS CPVGFMLQPD RKTCKDIDEC RLNNGGCDHI CRNTVGSFEC
SCKKGYKLLI NERNCQDIDE CSFDRTCDHI CVNTPGSFQC LCHHGYLLYG VTHCGDVDEC
SINRGGCRFG CINTPGSYQC TCPSGHGRLH WNGKDCTEPV KCQSSSGASK AMLSCNRSGK
KDTCALTCPS RARFLPESEN GFTVSCGTPS PRATPAKAGH PGNSTNSNHC HEAAVLSVKQ
RASFKIKDAK CRLHLRNKGK MEEASRNPGP GGAPCSDCQV TFIHLKCDSS RKGKGRRART
PPGKEVTRLT LELEAEVRAE DTTASCGLTC LRQRMERRLK GSLKMLRKSI NQDRFLLRLA
GLDYELAHKP GLVAGERPEL LEACKPGQHR AGVKCVSCPQ GTYYHGQTEQ CVPCPAGTFQ
EREGQLSCDL CPGSDAHGPL GATNITTCAG QCSPGQHSVD GFKPCQPCPR GTYQPEAGRT
LCFPCGGGLT TKHEGAISFQ DCDTKVQCSP GHYYNTSIHR CIRCAMGSYQ PDFRQNFCTR
CPGNTSTDFD GSTSVAQCKN RQCGGELGEF TGYIESPNYP GNYPAGVECV WNINPPPKRK
ILIVVPEIFL PSEDECGDVL VMRKNSSPAS ITTYETCQTY ERPIAFTARS RKLWINFKTS
EANSARGFQI PYVTYDEDYE QLVEDIVRDG RLYASENHQE ILKDKKLIKA FFEVLAHPQN
YFKYTEKHKE MLPKSFIKLL RSKVSSFLRP YK
//
