ID J3JTZ1_DENPD Unreviewed; 357 AA.
AC J3JTZ1;
DT 03-OCT-2012, integrated into UniProtKB/TrEMBL.
DT 03-OCT-2012, sequence version 1.
DT 27-MAR-2024, entry version 35.
DE RecName: Full=Wnt inhibitory factor 1 {ECO:0008006|Google:ProtNLM};
OS Dendroctonus ponderosae (Mountain pine beetle).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Coleoptera; Polyphaga; Cucujiformia;
OC Curculionidae; Scolytinae; Dendroctonus.
OX NCBI_TaxID=77166 {ECO:0000313|EMBL:AEE61663.1};
RN [1] {ECO:0000313|EMBL:AEE61663.1}
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Whole larvae {ECO:0000313|EMBL:AEE61663.1};
RX PubMed=22516182; DOI=10.1016/j.ibmb.2012.03.010;
RA Keeling C.I., Henderson H., Li M., Yuen M., Clark E.L., Fraser J.D.,
RA Huber D.P., Liao N.Y., Roderick Docking T., Birol I., Chan S.K.,
RA Taylor G.A., Palmquist D., Jones S.J., Bohlmann J.;
RT "Transcriptome and full-length cDNA resources for the mountain pine beetle,
RT Dendroctonus ponderosae Hopkins, a major insect pest of pine forests.";
RL Insect Biochem. Mol. Biol. 42:525-536(2012).
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; BT126701; AEE61663.1; -; mRNA.
DR RefSeq; XP_019760585.1; XM_019905026.1.
DR AlphaFoldDB; J3JTZ1; -.
DR GeneID; 109537996; -.
DR HOGENOM; CLU_041961_0_0_1; -.
DR OrthoDB; 5475408at2759; -.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR Gene3D; 2.10.25.10; Laminin; 4.
DR Gene3D; 2.60.40.2170; Wnt, WIF domain; 1.
DR InterPro; IPR000742; EGF-like_dom.
DR InterPro; IPR003306; WIF.
DR InterPro; IPR038677; WIF_sf.
DR PANTHER; PTHR14949:SF50; 3-PHYTASE; 1.
DR PANTHER; PTHR14949; EGF-LIKE-DOMAIN, MULTIPLE 7, 8; 1.
DR Pfam; PF02019; WIF; 1.
DR SMART; SM00181; EGF; 5.
DR SMART; SM00469; WIF; 1.
DR SUPFAM; SSF57196; EGF/Laminin; 1.
DR PROSITE; PS00022; EGF_1; 4.
DR PROSITE; PS01186; EGF_2; 4.
DR PROSITE; PS50026; EGF_3; 3.
DR PROSITE; PS50814; WIF; 1.
PE 2: Evidence at transcript level;
KW Disulfide bond {ECO:0000256|PROSITE-ProRule:PRU00076};
KW EGF-like domain {ECO:0000256|PROSITE-ProRule:PRU00076};
KW Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW Membrane {ECO:0000256|SAM:Phobius}; Signal {ECO:0000256|ARBA:ARBA00022729};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 7..24
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 40..177
FT /note="WIF"
FT /evidence="ECO:0000259|PROSITE:PS50814"
FT DOMAIN 184..216
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 248..280
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 281..312
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DISULFID 188..198
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 206..215
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 252..262
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 270..279
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 284..294
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 302..311
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
SQ SEQUENCE 357 AA; 39841 MW; 83051EBCFEF72ADD CRC64;
MYKNRTVMYY VLFYSLTVVT LVLSRNDPKN DPRNSSDLTL WIDEKQVKMF SGVSMEIYAI
VNGNVLPYIL DPNFENYLPV IPSEVNYVNF TWKAGNKKYN YNFDKLQSYD ESILEAPVIS
IKTKGRVPKR PKEFSIFLPC IGNSSGKARF EIGLLIETRK GKSLNGTPLR LKLKKECSIS
QRSPDPECDK KCANQGWCNN EKICQCPEGY MGQYCKTALC YPQCMNGGNC TSPGVCSCPT
GFQGTHCEGG ICSKKCLNGG KCVQKDTCEC SKGYYGPRCE FSRCIIPCLN DGRCRGVNKC
KCLRGFRGDH CEVARAKLAR AACSLNCRHG SCAPDGEAAC ICEKGWHGRL CQHATTM
//
