ID A0A091LPV2_CATAU Unreviewed; 283 AA.
AC A0A091LPV2;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 27-MAR-2024, entry version 34.
DE RecName: Full=Wnt inhibitory factor 1 {ECO:0000256|ARBA:ARBA00013854};
DE Flags: Fragment;
GN ORFNames=N323_03102 {ECO:0000313|EMBL:KFP59185.1};
OS Cathartes aura (Turkey vulture) (Vultur aura).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Accipitriformes; Cathartidae; Cathartes.
OX NCBI_TaxID=43455 {ECO:0000313|EMBL:KFP59185.1, ECO:0000313|Proteomes:UP000053745};
RN [1] {ECO:0000313|EMBL:KFP59185.1, ECO:0000313|Proteomes:UP000053745}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BGI_N323 {ECO:0000313|EMBL:KFP59185.1};
RA Zhang G., Li C.;
RT "Genome evolution of avian class.";
RL Submitted (APR-2014) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Binds to WNT proteins and inhibits their activities. May be
CC involved in mesoderm segmentation. {ECO:0000256|ARBA:ARBA00003309}.
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 EMBL; KL334567; KFP59185.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A091LPV2; -.
DR Proteomes; UP000053745; Unassembled WGS sequence.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR Gene3D; 2.10.25.10; Laminin; 2.
DR Gene3D; 2.60.40.2170; Wnt, WIF domain; 1.
DR InterPro; IPR013032; EGF-like_CS.
DR InterPro; IPR000742; EGF-like_dom.
DR InterPro; IPR013111; EGF_extracell.
DR InterPro; IPR003306; WIF.
DR InterPro; IPR038677; WIF_sf.
DR InterPro; IPR013309; Wnt-inh.
DR PANTHER; PTHR14949:SF50; 3-PHYTASE; 1.
DR PANTHER; PTHR14949; EGF-LIKE-DOMAIN, MULTIPLE 7, 8; 1.
DR Pfam; PF21700; DL-JAG_EGF-like; 1.
DR Pfam; PF07974; EGF_2; 1.
DR Pfam; PF12661; hEGF; 3.
DR Pfam; PF02019; WIF; 1.
DR PRINTS; PR01901; WIFPROTEIN.
DR SMART; SM00181; EGF; 5.
DR SMART; SM00469; WIF; 1.
DR PROSITE; PS00022; EGF_1; 3.
DR PROSITE; PS01186; EGF_2; 3.
DR PROSITE; PS50026; EGF_3; 3.
DR PROSITE; PS50814; WIF; 1.
PE 4: Predicted;
KW Disulfide bond {ECO:0000256|PROSITE-ProRule:PRU00076};
KW EGF-like domain {ECO:0000256|PROSITE-ProRule:PRU00076};
KW Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW Reference proteome {ECO:0000313|Proteomes:UP000053745};
KW Signal {ECO:0000256|ARBA:ARBA00022729};
KW Wnt signaling pathway {ECO:0000256|ARBA:ARBA00022687}.
FT DOMAIN 1..81
FT /note="WIF"
FT /evidence="ECO:0000259|PROSITE:PS50814"
FT DOMAIN 82..114
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 146..178
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 179..210
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT REGION 249..283
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT DISULFID 86..96
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 104..113
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 150..160
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 168..177
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 182..192
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 200..209
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:KFP59185.1"
FT NON_TER 283
FT /evidence="ECO:0000313|EMBL:KFP59185.1"
SQ SEQUENCE 283 AA; 30619 MW; 51587C8A58E482E5 CRC64;
AEYFYEFLSL RSLDKGIMAD PTINIPLLGT VPHKASVVQV GFPCLGKQDG VAAFEVNVII
MNSEGSIILQ TPQNAIFFKT CQQAECPGGC RNGGFCNKRH VCECPDGFYG PHCEKALCAP
RCMNGGLCIT PGLCICPPGF YGINCDKANC TTTCFNGGTC FYLGKCICPS GYEGDQCEIS
KCHQPCRNGG KCTGKNKCKC SKGYQGDLCS KPVCEPGCGL YGTCAEPNKC QCKEGWHGRH
CNKRHGASGL SALRPAGSKH RQHTPLPKRA EERHVPPESN YIW
//
