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Database: UniProt
Entry: A0A663DY63_AQUCH
LinkDB: A0A663DY63_AQUCH
Original site: A0A663DY63_AQUCH 
ID   A0A663DY63_AQUCH        Unreviewed;      1228 AA.
AC   A0A663DY63;
DT   17-JUN-2020, integrated into UniProtKB/TrEMBL.
DT   17-JUN-2020, sequence version 1.
DT   28-JAN-2026, entry version 23.
DE   SubName: Full=Multiple EGF like domains 6 {ECO:0000313|Ensembl:ENSACCP00020004694.1};
GN   Name=MEGF6 {ECO:0000313|Ensembl:ENSACCP00020004694.1};
OS   Aquila chrysaetos chrysaetos.
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Neognathae; Neoaves; Telluraves; Accipitrimorphae;
OC   Accipitriformes; Accipitridae; Accipitrinae; Aquila.
OX   NCBI_TaxID=223781 {ECO:0000313|Ensembl:ENSACCP00020004694.1, ECO:0000313|Proteomes:UP000472275};
RN   [1] {ECO:0000313|Ensembl:ENSACCP00020004694.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (AUG-2025) to UniProtKB.
RN   [2] {ECO:0000313|Ensembl:ENSACCP00020004694.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (SEP-2025) 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; A0A663DY63; -.
DR   Ensembl; ENSACCT00020004894.1; ENSACCP00020004694.1; ENSACCG00020003162.1.
DR   GeneTree; ENSGT00940000156971; -.
DR   Proteomes; UP000472275; Chromosome 6.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR   FunFam; 2.10.25.10:FF:000326; Multiple EGF like domains 6; 1.
DR   FunFam; 2.170.300.10:FF:000002; Multiple epidermal growth factor-like domains 10; 2.
DR   FunFam; 2.10.25.10:FF:000010; Pro-epidermal growth factor; 1.
DR   FunFam; 2.10.25.10:FF:000028; Signal peptide, CUB domain and EGF-like domain-containing 2; 1.
DR   FunFam; 2.10.25.10:FF:000037; Signal peptide, CUB domain and EGF-like domain-containing 2; 2.
DR   FunFam; 2.170.300.10:FF:000041; Tyrosine protein kinase receptor tie-1, putative; 2.
DR   FunFam; 2.10.25.10:FF:000240; Vitamin K-dependent protein S; 1.
DR   Gene3D; 2.10.25.10; Laminin; 9.
DR   Gene3D; 2.170.300.10; Tie2 ligand-binding domain superfamily; 4.
DR   InterPro; IPR026823; cEGF.
DR   InterPro; IPR000742; EGF.
DR   InterPro; IPR001881; EGF-like_Ca-bd_dom.
DR   InterPro; IPR000152; EGF-type_Asp/Asn_hydroxyl_site.
DR   InterPro; IPR018097; EGF_Ca-bd_CS.
DR   InterPro; IPR009030; Growth_fac_rcpt_cys_sf.
DR   InterPro; IPR002049; LE_dom.
DR   InterPro; IPR052108; MEGF/SIB.
DR   InterPro; IPR049883; NOTCH1_EGF-like.
DR   PANTHER; PTHR24035; MULTIPLE EPIDERMAL GROWTH FACTOR-LIKE DOMAINS PROTEIN; 1.
DR   PANTHER; PTHR24035:SF137; MULTIPLE EPIDERMAL GROWTH FACTOR-LIKE DOMAINS PROTEIN 6; 1.
DR   Pfam; PF12662; cEGF; 1.
DR   Pfam; PF07645; EGF_CA; 2.
DR   Pfam; PF00053; EGF_laminin; 4.
DR   Pfam; PF14670; FXa_inhibition; 4.
DR   PRINTS; PR00011; EGFLAMININ.
DR   SMART; SM00181; EGF; 22.
DR   SMART; SM00179; EGF_CA; 7.
DR   SMART; SM00180; EGF_Lam; 14.
DR   SUPFAM; SSF57184; Growth factor receptor domain; 3.
DR   PROSITE; PS00010; ASX_HYDROXYL; 2.
DR   PROSITE; PS00022; EGF_1; 12.
DR   PROSITE; PS01186; EGF_2; 6.
DR   PROSITE; PS50026; EGF_3; 8.
DR   PROSITE; PS01187; EGF_CA; 3.
DR   PROSITE; PS50027; EGF_LAM_2; 1.
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};
KW   Laminin EGF-like domain {ECO:0000256|PROSITE-ProRule:PRU00460};
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Reference proteome {ECO:0000313|Proteomes:UP000472275};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737};
KW   Secreted {ECO:0000256|ARBA:ARBA00022525};
KW   Signal {ECO:0000256|ARBA:ARBA00022729};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        12..30
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          171..211
FT                   /note="EGF-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50026"
FT   DOMAIN          295..335
FT                   /note="EGF-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50026"
FT   DOMAIN          526..562
FT                   /note="EGF-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50026"
FT   DOMAIN          570..605
FT                   /note="EGF-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50026"
FT   DOMAIN          664..710
FT                   /note="Laminin EGF-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50027"
FT   DOMAIN          783..819
FT                   /note="EGF-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50026"
FT   DOMAIN          827..862
FT                   /note="EGF-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50026"
FT   DOMAIN          960..995
FT                   /note="EGF-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50026"
FT   DOMAIN          1008..1038
FT                   /note="EGF-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50026"
FT   DISULFID        552..561
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT   DISULFID        595..604
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT   DISULFID        683..692
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT   DISULFID        809..818
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT   DISULFID        852..861
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT   DISULFID        985..994
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT   DISULFID        1028..1037
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
SQ   SEQUENCE   1228 AA;  130918 MW;  4127C8275D8E112C CRC64;
     RPNDMLLRNA DDMIILYVLL LPVGGGTALF SQQRADPRTP LFLCARPNVC AEQELAIVGH
     RQPCAQAFTR TVKVWKQDCG GQRWCTGYER RYVFFLRACF APRSGLLSCG SPTRSGSSSS
     PALPFSSLPD VNECEAGNGG CESQCCNTIG SFYCKCAAGL RLEPDGKACA DVDECQVHNG
     GCQHRCVNTL GSYYCECKPG FRLHTDGRTC IAVNTCALNN GGCEHNCVQV TLTQHQCQCR
     HNYQLREDGK RCVRENPCTD RNGGCMHRCH NHRGTARCEC HPGYRLAPDN KACEDVNECL
     TGLAMCAHRC LNTRGSFKCT CNPGYELGAD GKQCYRIEME IVNSCEANNG GCSHTCHHTS
     SGPVCTCNFG YRLEEDQKTC TDINECDSGS HCCQQDCYNY PGGYECACYA GYRLGTDGCG
     CDDVDECSSH NGGCEHTCQN QLGSFQCGCE IGYKLDDDRR SCIPIEDPVE ALDGRRPVIR
     PIPHVAILRD EFTQLFNDDY EEEEEEMEAR GEHTLSEKFV CLEHTFGPDC SLTCEDCQNG
     ATCDAEETGC ECPAGWTGIL CNQTCPVGTF GRNCSLTCRC QNGGTCDPAT GACRCPPGVA
     GELCQDGCPK GFFGKQCRKK CNCANRGRCH RIYGACLCDP GLYGRYCHLV CPKWAFGPGC
     SEECRCVQQN TQDCDKRDGS CRCKPGYRGK RCCDPGYYGD GCKKKCSCSP EASCDRVTGE
     CWKECPPGYH GENCGQECPE GKFGAGCRRS CSCGGSPCDR STGQCLCLPG WTGHDCACPD
     GRWGQGCQEI CPECANNASC DPATGACLCP PGYTGSRCQD VCPPGWFGPD CQLSCSCGND
     GHCHPVTGTC SCAPGWTGYN CQRACDAGRW GPDCAHTCNC SNSDGSCSAE TGQCVCDAGY
     TGGRCEKSEC CPAQGLFGAR CEEPCDCGDN VSCHHVTGAC DCPRGWRGRR CEKGCPAGRY
     GKDCARVCSC GEGATCHPVT GDCVCPPGRA GPTCEQGCEK HRYGAGCRQT CSCRNGGLCD
     AADGSCLCAL GWTGKSCELE CPPGRYGASC QLRCACLHNA TCDPGTGACR CSAGRYGPLC
     EHSCPPGFHG AGCRERCDCE HGAGCDPATG RCRCPAGLRG ERCQTGCKEG TYGEGCQHLC
     DCAGDAPCHP ATGRCLCPPG KTGPKCGSGE RQKALCLILR SATTASSCLS APPHQTAGRP
     STAPTAACPA SVPPAAPTVM LRTASASV
//
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