ID A0A2Y9MIJ8_DELLE Unreviewed; 1069 AA.
AC A0A2Y9MIJ8;
DT 12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT 12-SEP-2018, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE SubName: Full=Signal peptide, CUB and EGF-like domain-containing protein 2 isoform X3 {ECO:0000313|RefSeq:XP_022418882.1};
GN Name=SCUBE2 {ECO:0000313|RefSeq:XP_022418882.1};
OS Delphinapterus leucas (Beluga whale).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Whippomorpha; Cetacea; Odontoceti;
OC Monodontidae; Delphinapterus.
OX NCBI_TaxID=9749 {ECO:0000313|Proteomes:UP000248483, ECO:0000313|RefSeq:XP_022418882.1};
RN [1] {ECO:0000313|RefSeq:XP_022418882.1}
RP IDENTIFICATION.
RC TISSUE=Blood {ECO:0000313|RefSeq:XP_022418882.1};
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_022418882.1; XM_022563174.2.
DR AlphaFoldDB; A0A2Y9MIJ8; -.
DR Proteomes; UP000248483; 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; 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:SF3; SIGNAL PEPTIDE, CUB AND EGF-LIKE DOMAIN-CONTAINING PROTEIN 2; 1.
DR Pfam; PF12662; cEGF; 1.
DR Pfam; PF00431; CUB; 1.
DR Pfam; PF12947; EGF_3; 1.
DR Pfam; PF07645; EGF_CA; 1.
DR Pfam; PF07699; Ephrin_rec_like; 3.
DR Pfam; PF14670; FXa_inhibition; 5.
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; 3.
DR SUPFAM; SSF49854; Spermadhesin, CUB domain; 1.
DR PROSITE; PS00010; ASX_HYDROXYL; 4.
DR PROSITE; PS01180; CUB; 1.
DR PROSITE; PS01186; EGF_2; 4.
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}; Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW Reference proteome {ECO:0000313|Proteomes:UP000248483};
KW Repeat {ECO:0000256|ARBA:ARBA00022737}.
FT DOMAIN 86..126
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 169..205
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 405..443
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 879..991
FT /note="CUB"
FT /evidence="ECO:0000259|PROSITE:PS01180"
FT REGION 1..26
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT DISULFID 409..419
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
SQ SEQUENCE 1069 AA; 116789 MW; 914F4D5A970CDB0B CRC64;
MRLGLGGRAG GVRARRAGRP HTPPGAAAAL AARAPQSLPA VAAPSMGVAG LGCPWAARAL
LPLLLPLLLT AAVPPGWGRA AGPPEDVDEC AQGLDDCHTN ALCQNTPTSY KCSCRPGYQG
EGRQCEDIDE CENELNGGCV HDCLNIPGNY RCTCFDGFML AHDGHNCLDV DECLENNGGC
QHTCVNVMGS YECRCKEGFF LSDNQHTCIH RSEEGLSCMN KNHGCSHICK EAPRGSVACE
CRPGFELAKN QRDCTLTCNH GNGGCHHSCE DTAAGPECSC HPQYKMHTDG RSCLEREDAA
LEVMESNATS MADGDKRVKR RLLMETCAVN NGGCDRTCKD TSTGVHCSCP VGFSLQLDGK
TCKDIDECQT HNGGCDHFCK NTVGSFDCSC KKGFKLLTDE KSCQDVDECS LDRTCDHSCI
NHPGTFACAC NKGYTLYGFT HCGDTNECSV NNGGCQQVCV NTVGSYECRC HSAHKLHWNK
KDCVEVEGVL PTSVSPHVSL QCGKSGGGDR CFLRCLSGIH LSSGLQEAYS VTCGSSSPLR
SKQQKSNDSA FGDVATIRTS VTFKLNEGKC SLKKADLFPE GLRPVLPEKH SSVKESFRYA
NLTCSSGKQV PGAPGRPSTP KEMFITVEFE LETNQKEVTA SCDPSCIIKR TEKRLRKAIR
TLRKAAHREQ FHLQLSGVDL EVAKKSPQTS EHWAESCGVG QGHVGNQCVS CRAGTYYDGV
QERCILCPNG TFQNEEGQIT CEPCPRPENP GALETPEAWN ASECGGLCQP GEYSADGFAP
CQLCALGTFQ PEAGRTSCFP CGGGLLTKHL GATSFQDCET RVQCSPGHFY NTTTHRCIRC
PAGTYQPEFG KNNCVSCPGN TTTDFDGSTN ITQCKNRRCG GELGDFTGYI ESPNYPGNYP
ANTECTWTIN PPPKRRILIV VPEIFLPIED DCGDYLVMRK TASSNSVTTY ETCQTYERPI
AFTSRSKKLW IQFKSNEGNS ARGFQVPYVT YDEDYQELIE DIVRDGRLYA SENHQEILKD
KKLIKALFDV LAHPQNYFKY TAQESREMFP RSFIRLLRSK VSRFLRPYK
//