ID   EDIL3_PONAB             Reviewed;         480 AA.
AC   Q5R7K9;
DT   02-SEP-2008, integrated into UniProtKB/Swiss-Prot.
DT   21-DEC-2004, sequence version 1.
DT   25-MAY-2022, entry version 82.
DE   RecName: Full=EGF-like repeat and discoidin I-like domain-containing protein 3;
DE   Flags: Precursor;
GN   Name=EDIL3;
OS   Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Pongo.
OX   NCBI_TaxID=9601;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Heart;
RG   The German cDNA consortium;
RL   Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Promotes adhesion of endothelial cells through interaction
CC       with the alpha-v/beta-3 integrin receptor. Inhibits formation of
CC       vascular-like structures. May be involved in regulation of vascular
CC       morphogenesis of remodeling in embryonic development (By similarity).
CC       {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
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DR   EMBL; CR860106; CAH92251.1; -; mRNA.
DR   RefSeq; NP_001126317.1; NM_001132845.1.
DR   AlphaFoldDB; Q5R7K9; -.
DR   SMR; Q5R7K9; -.
DR   STRING; 9601.ENSPPYP00000017457; -.
DR   GeneID; 100173296; -.
DR   KEGG; pon:100173296; -.
DR   CTD; 10085; -.
DR   eggNOG; ENOG502QU9M; Eukaryota.
DR   InParanoid; Q5R7K9; -.
DR   OrthoDB; 441415at2759; -.
DR   Proteomes; UP000001595; Unplaced.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR   GO; GO:0007155; P:cell adhesion; IEA:UniProtKB-KW.
DR   CDD; cd00057; FA58C; 2.
DR   InterPro; IPR001881; EGF-like_Ca-bd_dom.
DR   InterPro; IPR013032; EGF-like_CS.
DR   InterPro; IPR000742; EGF-like_dom.
DR   InterPro; IPR000152; EGF-type_Asp/Asn_hydroxyl_site.
DR   InterPro; IPR018097; EGF_Ca-bd_CS.
DR   InterPro; IPR000421; FA58C.
DR   InterPro; IPR008979; Galactose-bd-like_sf.
DR   Pfam; PF00008; EGF; 2.
DR   Pfam; PF00754; F5_F8_type_C; 2.
DR   Pfam; PF12661; hEGF; 1.
DR   SMART; SM00181; EGF; 3.
DR   SMART; SM00179; EGF_CA; 3.
DR   SMART; SM00231; FA58C; 2.
DR   SUPFAM; SSF49785; SSF49785; 2.
DR   PROSITE; PS00010; ASX_HYDROXYL; 1.
DR   PROSITE; PS00022; EGF_1; 2.
DR   PROSITE; PS01186; EGF_2; 2.
DR   PROSITE; PS50026; EGF_3; 3.
DR   PROSITE; PS01187; EGF_CA; 1.
DR   PROSITE; PS01285; FA58C_1; 2.
DR   PROSITE; PS01286; FA58C_2; 2.
DR   PROSITE; PS50022; FA58C_3; 2.
PE   2: Evidence at transcript level;
KW   Cell adhesion; Developmental protein; Disulfide bond; EGF-like domain;
KW   Reference proteome; Repeat; Secreted; Signal.
FT   SIGNAL          1..23
FT                   /evidence="ECO:0000255"
FT   CHAIN           24..480
FT                   /note="EGF-like repeat and discoidin I-like domain-
FT                   containing protein 3"
FT                   /id="PRO_0000347231"
FT   DOMAIN          24..60
FT                   /note="EGF-like 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT   DOMAIN          74..117
FT                   /note="EGF-like 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT   DOMAIN          119..155
FT                   /note="EGF-like 3; calcium-binding"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT   DOMAIN          158..314
FT                   /note="F5/8 type C 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00081"
FT   DOMAIN          319..476
FT                   /note="F5/8 type C 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00081"
FT   MOTIF           96..98
FT                   /note="Cell attachment site"
FT                   /evidence="ECO:0000255"
FT   DISULFID        26..37
FT                   /evidence="ECO:0000250"
FT   DISULFID        31..48
FT                   /evidence="ECO:0000250"
FT   DISULFID        50..59
FT                   /evidence="ECO:0000250"
FT   DISULFID        78..89
FT                   /evidence="ECO:0000250"
FT   DISULFID        83..105
FT                   /evidence="ECO:0000250"
FT   DISULFID        107..116
FT                   /evidence="ECO:0000250"
FT   DISULFID        123..134
FT                   /evidence="ECO:0000250"
FT   DISULFID        128..143
FT                   /evidence="ECO:0000250"
FT   DISULFID        145..154
FT                   /evidence="ECO:0000250"
FT   DISULFID        158..314
FT                   /evidence="ECO:0000250"
FT   DISULFID        301..305
FT                   /evidence="ECO:0000250"
FT   DISULFID        319..476
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   480 AA;  53754 MW;  7FECDD016BFF37B4 CRC64;
     MKRSVAVWLL VGLSLGVPQF GKGDICDPNP CENGGICLPG LADGSFSCEC PDGFTDPNCS
     SVVEVASDEE EPTSAGPCTP NPCHNGGTCE ISEAYRGDTF IGYVCKCPRG FNGIHCQHNI
     NECEVEPCKN GGICTDLVAN YSCECPGEFM GRNCQYKCSG PLGIEGGIIS NQQITASSTH
     RALFGLQKWY PYYARLNKKG LINAWTAAEN DRWPWIQINL QRKMRVTGVI TQGAKRIGSP
     EYIKSYKIAY SNDGKTWAMY KVKGTNEDMV FRGNIDNNTP YANSFTPPTK AQYVRLYPQV
     CRRHCTLRME LLGCELSGCS EPLGMKSGHI QDYQITASSI FRTLNMDMFT WEPRKARLDK
     QGKVNAWTSG HNDQSQWLQV DLLVPTKVTG IITQGAKDFG HVQFVGSYKL AYSNDGEHWT
     VYQDEKQRKD KVFQGNFDND THRKNVIDPP IYARHIRILP WSWYGRNTLR SELLGCTEEE