ID A0A093FKX3_GAVST Unreviewed; 1017 AA.
AC A0A093FKX3;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 27-MAR-2024, entry version 35.
DE SubName: Full=Protein crumbs 1 {ECO:0000313|EMBL:KFV57245.1};
DE Flags: Fragment;
GN ORFNames=N328_02262 {ECO:0000313|EMBL:KFV57245.1};
OS Gavia stellata (Red-throated diver) (Colymbus stellatus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Gaviiformes; Gaviidae; Gavia.
OX NCBI_TaxID=37040 {ECO:0000313|EMBL:KFV57245.1, ECO:0000313|Proteomes:UP000054313};
RN [1] {ECO:0000313|EMBL:KFV57245.1, ECO:0000313|Proteomes:UP000054313}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BGI_N328 {ECO:0000313|EMBL:KFV57245.1};
RA Zhang G., Li C.;
RT "Genome evolution of avian class.";
RL Submitted (APR-2014) to the EMBL/GenBank/DDBJ databases.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00076}.
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DR EMBL; KK633710; KFV57245.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A093FKX3; -.
DR Proteomes; UP000054313; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR CDD; cd00054; EGF_CA; 9.
DR CDD; cd00110; LamG; 3.
DR Gene3D; 2.60.120.200; -; 3.
DR Gene3D; 2.10.25.10; Laminin; 9.
DR InterPro; IPR013320; ConA-like_dom_sf.
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; IPR009030; Growth_fac_rcpt_cys_sf.
DR InterPro; IPR001791; Laminin_G.
DR PANTHER; PTHR24049; CRUMBS FAMILY MEMBER; 1.
DR PANTHER; PTHR24049:SF22; DROSOPHILA CRUMBS HOMOLOG; 1.
DR Pfam; PF00008; EGF; 8.
DR Pfam; PF12661; hEGF; 1.
DR Pfam; PF02210; Laminin_G_2; 3.
DR SMART; SM00181; EGF; 9.
DR SMART; SM00179; EGF_CA; 9.
DR SMART; SM00282; LamG; 3.
DR SUPFAM; SSF49899; Concanavalin A-like lectins/glucanases; 3.
DR SUPFAM; SSF57196; EGF/Laminin; 3.
DR SUPFAM; SSF57184; Growth factor receptor domain; 1.
DR PROSITE; PS00010; ASX_HYDROXYL; 6.
DR PROSITE; PS00022; EGF_1; 8.
DR PROSITE; PS01186; EGF_2; 5.
DR PROSITE; PS50026; EGF_3; 9.
DR PROSITE; PS01187; EGF_CA; 3.
DR PROSITE; PS50025; LAM_G_DOMAIN; 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 Membrane {ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000054313};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 951..981
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 8..50
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 52..92
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 94..280
FT /note="Laminin G"
FT /evidence="ECO:0000259|PROSITE:PS50025"
FT DOMAIN 282..318
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 324..496
FT /note="Laminin G"
FT /evidence="ECO:0000259|PROSITE:PS50025"
FT DOMAIN 498..534
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 562..748
FT /note="Laminin G"
FT /evidence="ECO:0000259|PROSITE:PS50025"
FT DOMAIN 750..786
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 788..823
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 825..861
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 866..906
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 908..944
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DISULFID 82..91
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 308..317
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 524..533
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 776..785
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 792..802
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 813..822
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 851..860
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 896..905
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 934..943
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:KFV57245.1"
FT NON_TER 1017
FT /evidence="ECO:0000313|EMBL:KFV57245.1"
SQ SEQUENCE 1017 AA; 112908 MW; 8C800B7D08E5A865 CRC64;
SGAHCDEDIN ECYTNPCQNG GICENFPGNY TCHCPPADKE GIYYGGWNCT EVLHGCTDQQ
CQNNGICIPH LKNGQHGFSC ICSPGYTGIR CETVTTFSFQ GNSFLLLKNP LTPKKEFFYN
INLRFQTVQP TAFLFYRGEK NTFAKLELLN GYLHLSVQVN NQPQALLHIS HNVSDGEWHS
VEVTLARAVT LNLLDSSCVE SCLNKTSAMI DNDHVMLAFQ STFLGGLPVG NISGNSLLNI
YNIHSAPSFV GCLQDIEIDL NVITPENVSP ESSLNVRTGC TKKDWCEPHP CQNRGRCTNL
WLSYHCDCYR PYTGPSCATE YIPGRFGSED SSGYAAFSVD ATQNENLNIS MFVRTRKSSG
LLLALRNSTY LYVRVYLEGG RLTMLALNSM RLLGKHSMND GNFYLITLKI EPNKMELFQS
SQYLGFISTP VLTIQSKDIL YIGGLPDNKE TARNGRYFKG CIQDVRVNNQ PLEFFPITNP
LNSLINRTLI NVTQGCTGDN LCKSNPCHNG GVCYSIWDDF TCTCPPNTAG KACEEVKWCE
LESCPHEAQC QLVHQGFECL ANAVFSGRSS AIFYRSNGKI SRDLTNIIFG FRTRDTDVIL
LYAEKEPEFV TISIHNSKLL FQLQSGNSFY KLTLASSLPV SDGKWHQVVV SMAEPLSQFS
RWHIDIDNKK DTTTSTTTAG SLNFLREETD IYVADKAFDS LDGLRGCMST IEISGIYLPY
FDNADIPTKK PQEEQFLKIS ANPALTGCLQ VDVCSSDPCM HEGICEDFYT SYRCICPKGW
TGTHCEVNID ECSSNPCIHG NCTDGITSYE CSCEPGYTGV NCEEDIDNCR GHQCANGATC
IDGIDGYSCL CSANFTGKFC RYRRLPYTVC GNEERNLTCF NYGNCTNLSG ELTCVCLPGF
AGERCEKDID ECSSDPCLNG GLCQNLLNKF HCLCDVNYAG DRCEIDLTTD LIWNIFTSIG
SVTLALLLIL FLAVVVSVIA ANKRATQGTY SPSRQEKEGS RVEMWNMVQP PPMERLI
//
