ID A0A2U9BZU4_SCOMX Unreviewed; 1012 AA.
AC A0A2U9BZU4;
DT 12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT 12-SEP-2018, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE RecName: Full=Protein Wnt {ECO:0000256|RuleBase:RU003500};
GN ORFNames=SMAX5B_014796 {ECO:0000313|EMBL:AWP09721.1};
OS Scophthalmus maximus (Turbot) (Psetta maxima).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Carangaria; Pleuronectiformes; Pleuronectoidei; Scophthalmidae;
OC Scophthalmus.
OX NCBI_TaxID=52904 {ECO:0000313|EMBL:AWP09721.1, ECO:0000313|Proteomes:UP000246464};
RN [1] {ECO:0000313|EMBL:AWP09721.1, ECO:0000313|Proteomes:UP000246464}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Martinez P.;
RT "Integrating genomic resources of turbot (Scophthalmus maximus) in depth
RT evaluation of genetic and physical mapping variation across individuals.";
RL Submitted (DEC-2017) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Ligand for members of the frizzled family of seven
CC transmembrane receptors. {ECO:0000256|RuleBase:RU003500}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=3.6.4.13;
CC Evidence={ECO:0000256|ARBA:ARBA00001556};
CC -!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular
CC matrix {ECO:0000256|ARBA:ARBA00004498, ECO:0000256|RuleBase:RU003500}.
CC -!- SIMILARITY: Belongs to the DNA2/NAM7 helicase family. SDE3 subfamily.
CC {ECO:0000256|ARBA:ARBA00005601}.
CC -!- SIMILARITY: Belongs to the Wnt family. {ECO:0000256|ARBA:ARBA00005683,
CC ECO:0000256|RuleBase:RU003500}.
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DR EMBL; CP026253; AWP09721.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2U9BZU4; -.
DR STRING; 52904.ENSSMAP00000007931; -.
DR Proteomes; UP000246464; Chromosome 11.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
DR GO; GO:0032574; F:5'-3' RNA helicase activity; IEA:InterPro.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR GO; GO:0003723; F:RNA binding; IEA:InterPro.
DR GO; GO:0005102; F:signaling receptor binding; IEA:InterPro.
DR GO; GO:0048513; P:animal organ development; IEA:UniProt.
DR GO; GO:0031047; P:regulatory ncRNA-mediated gene silencing; IEA:UniProtKB-KW.
DR GO; GO:0048731; P:system development; IEA:UniProt.
DR GO; GO:0016055; P:Wnt signaling pathway; IEA:UniProtKB-KW.
DR CDD; cd18038; DEXXQc_Helz-like; 1.
DR CDD; cd18808; SF1_C_Upf1; 1.
DR CDD; cd19346; Wnt_Wnt2b; 1.
DR Gene3D; 3.30.2460.20; -; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR041679; DNA2/NAM7-like_C.
DR InterPro; IPR041677; DNA2/NAM7_AAA_11.
DR InterPro; IPR049080; MOV-10-like_beta-barrel.
DR InterPro; IPR026122; MOV-10/SDE3_DEXXQ/H-box.
DR InterPro; IPR049079; Mov-10_helical.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR047187; SF1_C_Upf1.
DR InterPro; IPR005817; Wnt.
DR InterPro; IPR009140; Wnt2.
DR InterPro; IPR043158; Wnt_C.
DR InterPro; IPR018161; Wnt_CS.
DR PANTHER; PTHR12027:SF93; PROTEIN WNT-2B; 1.
DR PANTHER; PTHR12027; WNT RELATED; 1.
DR Pfam; PF13086; AAA_11; 2.
DR Pfam; PF13087; AAA_12; 1.
DR Pfam; PF21634; MOV-10_beta-barrel; 1.
DR Pfam; PF21635; Mov-10_helical; 1.
DR Pfam; PF00110; wnt; 1.
DR PRINTS; PR01842; WNT2PROTEIN.
DR PRINTS; PR01349; WNTPROTEIN.
DR SMART; SM00382; AAA; 1.
DR SMART; SM00097; WNT1; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR PROSITE; PS00246; WNT1; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000313|EMBL:AWP09721.1};
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Developmental protein {ECO:0000256|ARBA:ARBA00022473,
KW ECO:0000256|RuleBase:RU003500};
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW Extracellular matrix {ECO:0000256|ARBA:ARBA00022530};
KW Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW Helicase {ECO:0000313|EMBL:AWP09721.1};
KW Hydrolase {ECO:0000313|EMBL:AWP09721.1};
KW Lipoprotein {ECO:0000256|ARBA:ARBA00023288};
KW Nucleotide-binding {ECO:0000313|EMBL:AWP09721.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000246464};
KW Secreted {ECO:0000256|ARBA:ARBA00022525};
KW Wnt signaling pathway {ECO:0000256|ARBA:ARBA00022687,
KW ECO:0000256|RuleBase:RU003500}.
FT DOMAIN 582..762
FT /note="AAA+ ATPase"
FT /evidence="ECO:0000259|SMART:SM00382"
SQ SEQUENCE 1012 AA; 114483 MW; 7A76C0369CAE0D35 CRC64;
MIFNDKKNEE SRRRWCGPNH RAKISTSSAC QGMGIHAELI PGLPDWYIGA LGARVICDNI
PGLVNKQRQL CQRHPDIMQA IGEGTKEWIR ECQHQFRHHR WNCSTLDRDH TVFGRVLLRS
SREAAFVYAI SSAGVVYALT RACSQGELKT CNCDPHKRGR AGDERGEFDW GGCSDNINYG
IKFAKAFIDA KERTVRDARA LMNLHNNRCG RTAVKRFMKL ECKCHGVSGS CTLRTCWMAM
SDFRKTGDFL RRKYNGAIEV TMNQDGTGFA VANKAFRKAT KNDLVYFENS PDYCLQDKSA
GSLGTAGRVC NKTSRGTDGC EVMCCGRGYD TTRVKQITKC ECKFKWCCAV ECKDCEEAVD
IHTCKAPKRA ECINTDMIGL FSFCLLGLLK SPLRWNNYSE KFHLLLELEE QQMNRALIKY
NIPNRNMKYA VMFRDRVNSD LLVLEVPGVS NNCSSLLNGA EVCVFPTGYT MSVYGYRDFH
GCVHSVKLDS IELQFRSDLL DYFEDGMMFK VCFTVNRLTL ALQHRAVILA VKHTLGKVLF
PAPPPYSSQQ PELPNLSVFD AQLKENPEQY RAVQHIVAGS SKPAPYLVFG PPGTGKTVTL
VEAIKQIDLT QASCHILACA SCNSAADLLC MKIVDHVDKG KVLRMYAKSW DSDCIPEKLK
ACSNLKEGKY FFHAKEELKK YRIIVTTLFT AGRLVTSRIR QGHFTHVFVD EAGHAVETEC
LIPLAGLLDS KTGQVVLAGD PKQLGPIIKN FSAQKFGLGV SFLERLMNNF SLYQRDKRNR
KFNNRFVTKL LRNYRSHPAI LEIPKELFYD NELQCHADEN SRNSYCRWEH LPRKEFPVIF
HEVTGQDERD ASSSSFFNTT EVTVLMDYVK KLLQTQGKTI SPKDIGIISP YRQQVQEIRR
ALEKVGKAHK VKDINTLKVG VVEEFQGQER DVILVSIVRS SHVNAKTDRK FNMGLINNNK
GFNVTVNRAK ALLIVVGNPN TIKTDRTWKR FIDYCRHNGG HIGDARSSSN QQ
//
