ID A0A3Q1CRY4_AMPOC Unreviewed; 858 AA.
AC A0A3Q1CRY4;
DT 10-APR-2019, integrated into UniProtKB/TrEMBL.
DT 10-APR-2019, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE SubName: Full=Signal peptide, CUB domain and EGF like domain containing 1 {ECO:0000313|Ensembl:ENSAOCP00000029910.1};
OS Amphiprion ocellaris (Clown anemonefish).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Pomacentridae; Amphiprion.
OX NCBI_TaxID=80972 {ECO:0000313|Ensembl:ENSAOCP00000029910.1, ECO:0000313|Proteomes:UP000257160};
RN [1] {ECO:0000313|Ensembl:ENSAOCP00000029910.1}
RP IDENTIFICATION.
RG Ensembl;
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 AlphaFoldDB; A0A3Q1CRY4; -.
DR STRING; 80972.ENSAOCP00000029910; -.
DR Ensembl; ENSAOCT00000024502.1; ENSAOCP00000029910.1; ENSAOCG00000020545.1.
DR GeneTree; ENSGT00940000153185; -.
DR OMA; YQDVEGQ; -.
DR Proteomes; UP000257160; 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; 3.
DR Gene3D; 2.10.25.10; Laminin; 7.
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: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; 1.
DR Pfam; PF07699; Ephrin_rec_like; 3.
DR Pfam; PF14670; FXa_inhibition; 4.
DR SMART; SM00042; CUB; 1.
DR SMART; SM00181; EGF; 8.
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; 3.
DR SUPFAM; SSF49854; Spermadhesin, CUB domain; 1.
DR PROSITE; PS00010; ASX_HYDROXYL; 6.
DR PROSITE; PS01180; CUB; 1.
DR PROSITE; PS01186; EGF_2; 3.
DR PROSITE; PS50026; EGF_3; 4.
DR PROSITE; PS01187; EGF_CA; 4.
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:UP000257160};
KW Repeat {ECO:0000256|ARBA:ARBA00022737}; Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..24
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 25..858
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5018787254"
FT DOMAIN 30..70
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 113..149
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 238..276
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 277..317
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 668..780
FT /note="CUB"
FT /evidence="ECO:0000259|PROSITE:PS01180"
FT DISULFID 242..252
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
SQ SEQUENCE 858 AA; 95334 MW; 5B40F2D6C48E1F6E CRC64;
MGSACFSRDV CLFILLINTC RVMGNVGLAD ADECAEGSDD CHIDALCQNT AKSYNCICKP
GYKGDGKQCE DMDECENDYN GGCVHECINI PGNYRCTCYD GFMLAHDGHN CLDVDECLDN
NGGCQQVCVN TMGSYECQCT NGFFLSDNQH TCIHRSDETC AVNNGGCDRT CKDTATGVRC
SCPVGFTLQP DGKTCKDIDE CLENNGGCDH YCRNTVGSFE CSCQKGHKLL TDERTCQDID
ECSFERTCDH TCINYPGSFE CLCNKGYILY GLTHCGDIDE CSINNGSCEH GCINTQGSYE
CVCPPGQKLH WNKKDCIGKH QLDSENSYTL SCGVPVQPGK APQKRNATTA LPTCADTLAP
PIKQKARFKI KDAKCHLRPR GQFPCTDDCQ VTFVNLKCDS SKKRRRGRKS PTKEVSHITA
EFEMEMKEEE ASDSCNVDCV RERMKQKLQS AMRTLRKSIN KQQFYIQFSG TEYEVAQKPS
RVPEGAETCS TGQVLRDGKC VSCAVGTFYS GEQEQCVQCP PGTYQDTEGQ LSCEPCPSTE
GQGIAGAKNV SQCGGQCPAG QFSADGFRPC QSCPLGSYQP EPGRVLCFTC GGGLMTRYEG
SVSFRDCEAK VHCAPGHYYN SSTHRCIRCP AGTYQSEFGQ NYCITCPGNT TTDFDGATNV
SHCKNQLCGG ELGEYTGYIE SPNYPGDYPS NVDCVWTINP PHKRRILIVV PEIFLPIEDE
CGDVLVMRKS ALPTSITTYE TCQTYERPIA FTSRSRKLWI QFKSNEGNSG KGFQVPYVTY
DEDYQQLIED IVRDGRLYAS ENHQEILKDK KLIKALFDVL AHPQNYFRYT AQESKEMFPR
SFIKLLRSKV TRFLRPYK
//
