ID A0A099ZL94_TINGU Unreviewed; 329 AA.
AC A0A099ZL94;
DT 07-JAN-2015, integrated into UniProtKB/TrEMBL.
DT 07-JAN-2015, sequence version 1.
DT 27-MAR-2024, entry version 33.
DE RecName: Full=Wnt inhibitory factor 1 {ECO:0000256|ARBA:ARBA00013854};
DE Flags: Fragment;
GN ORFNames=N309_05471 {ECO:0000313|EMBL:KGL82502.1};
OS Tinamus guttatus (White-throated tinamou).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Palaeognathae; Tinamiformes; Tinamidae; Tinamus.
OX NCBI_TaxID=94827 {ECO:0000313|EMBL:KGL82502.1, ECO:0000313|Proteomes:UP000053641};
RN [1] {ECO:0000313|EMBL:KGL82502.1, ECO:0000313|Proteomes:UP000053641}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BGI_N309 {ECO:0000313|EMBL:KGL82502.1};
RA Zhang G., Li C.;
RT "Genome evolution of avian class.";
RL Submitted (JUN-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; KL895232; KGL82502.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A099ZL94; -.
DR STRING; 94827.A0A099ZL94; -.
DR Proteomes; UP000053641; 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; PF07974; EGF_2; 1.
DR Pfam; PF12661; hEGF; 2.
DR Pfam; PF21795; JAG1-like_EGF2; 1.
DR Pfam; PF02019; WIF; 1.
DR PRINTS; PR01901; WIFPROTEIN.
DR SMART; SM00181; EGF; 5.
DR SMART; SM00469; WIF; 1.
DR PROSITE; PS00022; EGF_1; 4.
DR PROSITE; PS01186; EGF_2; 4.
DR PROSITE; PS50026; EGF_3; 4.
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:UP000053641};
KW Signal {ECO:0000256|ARBA:ARBA00022729};
KW Wnt signaling pathway {ECO:0000256|ARBA:ARBA00022687}.
FT DOMAIN 1..127
FT /note="WIF"
FT /evidence="ECO:0000259|PROSITE:PS50814"
FT DOMAIN 128..160
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 192..224
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 225..256
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 257..288
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT REGION 294..329
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT DISULFID 132..142
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 150..159
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 196..206
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 214..223
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 228..238
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 246..255
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 260..270
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 278..287
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:KGL82502.1"
FT NON_TER 329
FT /evidence="ECO:0000313|EMBL:KGL82502.1"
SQ SEQUENCE 329 AA; 35813 MW; E6F006937708DB8F CRC64;
FEEDILIVSE GRMAPFTHDF RKAQQRMPAI PVSIPAMNFT WQATGRAEYF YEFLSLRSLD
KGIMADPTIN IPLLGTVPHK ASVVQVGFPC LGKQDGVAAF EVNVIIMNSE GNIILQTPQN
AIFFKTCQQA ECPGGCRNGG FCNERHVCEC PDGFYGPHCE KALCAPRCMN GGLCITPGLC
ICPPGFYGIN CDKANCTTTC FNGGTCFYLG KCICPSGFEG DQCEISKCHQ PCRNGGKCTG
KNKCKCSKGY QGDLCSKPVC EPGCGSYGTC VEPNKCQCKE GWHGRHCNKR YGGGLASAPR
PGGPKQRQLT PSPKRAEERR PPPDSNYVW
//
