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Database: UniProt
Entry: A0A2A2LQV1_9BILA
LinkDB: A0A2A2LQV1_9BILA
Original site: A0A2A2LQV1_9BILA 
ID   A0A2A2LQV1_9BILA        Unreviewed;       528 AA.
AC   A0A2A2LQV1;
DT   20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT   20-DEC-2017, sequence version 1.
DT   24-JAN-2024, entry version 26.
DE   RecName: Full=Protein Wnt {ECO:0000256|RuleBase:RU003500};
GN   ORFNames=WR25_16339 {ECO:0000313|EMBL:PAV88622.1};
OS   Diploscapter pachys.
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Diploscapter.
OX   NCBI_TaxID=2018661 {ECO:0000313|EMBL:PAV88622.1, ECO:0000313|Proteomes:UP000218231};
RN   [1] {ECO:0000313|EMBL:PAV88622.1, ECO:0000313|Proteomes:UP000218231}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PF1309 {ECO:0000313|EMBL:PAV88622.1};
RA   Fradin H., Zegar C., Gutwein M., Lucas J., Kovtun M., Corcoran D.,
RA   Baugh L.R., Kiontke K., Gunsalus K., Fitch D.H., Piano F.;
RT   "Genome architecture and evolution of a unichromosomal asexual nematode.";
RL   Curr. Biol. 0:0-0(2017).
CC   -!- FUNCTION: Ligand for members of the frizzled family of seven
CC       transmembrane receptors. {ECO:0000256|RuleBase:RU003500}.
CC   -!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular
CC       matrix {ECO:0000256|ARBA:ARBA00004498, ECO:0000256|RuleBase:RU003500}.
CC   -!- SIMILARITY: Belongs to the Wnt family. {ECO:0000256|ARBA:ARBA00005683,
CC       ECO:0000256|RuleBase:RU003500}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:PAV88622.1}.
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DR   EMBL; LIAE01006508; PAV88622.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2A2LQV1; -.
DR   STRING; 2018661.A0A2A2LQV1; -.
DR   Proteomes; UP000218231; Unassembled WGS sequence.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
DR   GO; GO:0005102; F:signaling receptor binding; IEA:InterPro.
DR   GO; GO:0048699; P:generation of neurons; IEA:UniProt.
DR   GO; GO:0006629; P:lipid metabolic process; IEA:InterPro.
DR   GO; GO:0016055; P:Wnt signaling pathway; IEA:UniProtKB-KW.
DR   CDD; cd00519; Lipase_3; 1.
DR   CDD; cd13113; Wnt; 1.
DR   Gene3D; 3.30.2460.20; -; 1.
DR   Gene3D; 3.40.50.1820; alpha/beta hydrolase; 1.
DR   InterPro; IPR029058; AB_hydrolase.
DR   InterPro; IPR002921; Fungal_lipase-like.
DR   InterPro; IPR005817; Wnt.
DR   InterPro; IPR043158; Wnt_C.
DR   InterPro; IPR018161; Wnt_CS.
DR   PANTHER; PTHR12027:SF114; PROTEIN MOM-2; 1.
DR   PANTHER; PTHR12027; WNT RELATED; 1.
DR   Pfam; PF01764; Lipase_3; 1.
DR   Pfam; PF00110; wnt; 1.
DR   PRINTS; PR01349; WNTPROTEIN.
DR   SMART; SM00097; WNT1; 1.
DR   SUPFAM; SSF53474; alpha/beta-Hydrolases; 1.
DR   PROSITE; PS00246; WNT1; 1.
PE   3: Inferred from homology;
KW   Developmental protein {ECO:0000256|ARBA:ARBA00022473,
KW   ECO:0000256|RuleBase:RU003500};
KW   Extracellular matrix {ECO:0000256|ARBA:ARBA00022530};
KW   Reference proteome {ECO:0000313|Proteomes:UP000218231};
KW   Secreted {ECO:0000256|ARBA:ARBA00022525};
KW   Wnt signaling pathway {ECO:0000256|ARBA:ARBA00022687,
KW   ECO:0000256|RuleBase:RU003500}.
FT   DOMAIN          364..455
FT                   /note="Fungal lipase-like"
FT                   /evidence="ECO:0000259|Pfam:PF01764"
SQ   SEQUENCE   528 AA;  58031 MW;  BD179528B4311154 CRC64;
     MESTSRYQNV NTLSLTNAGI VPASRESAFV YALTSAGVTH SISKACAKGL IEDCGCGSLL
     SESAPAISQQ SSYYQTTFSN QAHASQFAWS GCSDNVKFGN SFGRKFLDAG EKVDENASAR
     WLMNVHNNRV GRRVAANTMR TECKCHGVSG SCVTKTCWKV VNRLSNITTL LHKKYTNAQQ
     VIVKPNSNAL IIQSMTSSGR GRTERYLSEA KANKVAKSDL IYLEDSPDYC NIDMSGRECG
     DNCNEICCGR GWKTIRELVE EPCHCQFVWC CEVKCQACRK MLSLVLSACL VGLLSAATYS
     DDVARNKMLP LAAAAYSNNP QLCLTSKFTN AVLKKEYNIG CDLLHADTCS GYLATLNGDK
     AILLAFRGTQ GFFQLIMEAD KSVFKEHVNW IAGGQVSKYF SDAFMAVWNH GMKNDYLTLR
     SQYPSYKVWV TGHSLGGAMA NLAASYLIAN KLADAANVVP HIPEEAFGYK HQQYEAFYHN
     DMKPGATYKV CQGDEDNGCS DGLLITASIA DHLTYFQHDI SDWGTFEL
//
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