NOT1P_XENLA
ID NOT1P_XENLA Reviewed; 488 AA.
AC A0A0D3QS98;
DT 24-JUN-2015, integrated into UniProtKB/Swiss-Prot.
DT 27-MAY-2015, sequence version 1.
DT 25-MAY-2022, entry version 18.
DE RecName: Full=Palmitoleoyl-protein carboxylesterase notum1' {ECO:0000250|UniProtKB:Q6P988};
DE EC=3.1.1.98 {ECO:0000250|UniProtKB:Q6P988};
DE Flags: Precursor;
GN Name=notum1' {ECO:0000303|PubMed:25771893};
OS Xenopus laevis (African clawed frog).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX NCBI_TaxID=8355 {ECO:0000312|EMBL:AJQ30102.1};
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, TISSUE SPECIFICITY, AND DEVELOPMENTAL
RP STAGE.
RX PubMed=25771893; DOI=10.1016/j.devcel.2015.02.014;
RA Zhang X., Cheong S.M., Amado N.G., Reis A.H., MacDonald B.T., Zebisch M.,
RA Jones E.Y., Abreu J.G., He X.;
RT "Notum is required for neural and head induction via Wnt deacylation,
RT oxidation, and inactivation.";
RL Dev. Cell 32:719-730(2015).
CC -!- FUNCTION: Carboxylesterase that acts as a key negative regulator of the
CC Wnt signaling pathway by specifically mediating depalmitoleoylation of
CC WNT proteins. Serine palmitoleoylation of WNT proteins is required for
CC efficient binding to frizzled receptors. Functions in the prospective
CC ectoderm and is required for neural induction.
CC {ECO:0000305|PubMed:25771893}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=[Wnt protein]-O-(9Z)-hexadecenoyl-L-serine + H2O = (9Z)-
CC hexadecenoate + [Wnt protein]-L-serine + H(+); Xref=Rhea:RHEA:45340,
CC Rhea:RHEA-COMP:11170, Rhea:RHEA-COMP:11171, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:32372,
CC ChEBI:CHEBI:85189; EC=3.1.1.98;
CC Evidence={ECO:0000250|UniProtKB:Q6P988};
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:Q9VUX3}.
CC -!- TISSUE SPECIFICITY: Expressed in the egg and through cleavage to
CC gastrulation stages. Enriched in the animal (prospective ectoderm) and
CC dorsal regions in early gastrula. Shows a dynamic expression during
CC embryogenesis, in particular during neural induction and antero-
CC posterior (AP) patterning. {ECO:0000269|PubMed:25771893}.
CC -!- DEVELOPMENTAL STAGE: Present in animal blastomeres at 4-cell and stage
CC 6.5. At stages 8.5 and 9.5 (blastula), detected broadly in the animal
CC region. At stage 10 (early gastrula), remains broadly expressed
CC animally, but also detected in the dorsal marginal zone (the
CC Organizer), with lower expression in the ventral marginal zone. At
CC stage 11, found in the forming neural plate in a noticeable antero-
CC posterior (AP) gradient (anterior high and posterior low), with
CC additional weaker expression in the head mesoderm. Remains detectable,
CC but becomes faint in the neural plate at stage 13. By stage 15,
CC detected at the anterior border of the neural plate and in ventro-
CC lateral epidermis excluding the neural plate. Later, it is detected in
CC the cement gland (an anterior organ) at tail bud stages (stage 25), in
CC branchial arches, the otic vesicle, and developing pronephros, with
CC diffused expression in the head (stage 35).
CC {ECO:0000269|PubMed:25771893}.
CC -!- SIMILARITY: Belongs to the pectinacetylesterase family. Notum
CC subfamily. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; KP781856; AJQ30102.1; -; mRNA.
DR RefSeq; XP_018093830.1; XM_018238341.1.
DR AlphaFoldDB; A0A0D3QS98; -.
DR SMR; A0A0D3QS98; -.
DR GeneID; 108702711; -.
DR KEGG; xla:108702711; -.
DR CTD; 108702711; -.
DR Xenbase; XB-GENE-17335322; notum.S.
DR OMA; SKENCDS; -.
DR OrthoDB; 610784at2759; -.
DR Proteomes; UP000186698; Chromosome 9_10S.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:1990699; F:palmitoleyl hydrolase activity; TAS:UniProtKB.
DR GO; GO:0030178; P:negative regulation of Wnt signaling pathway; IDA:UniProtKB.
DR GO; GO:1990697; P:protein depalmitoleylation; IDA:UniProtKB.
DR GO; GO:0016055; P:Wnt signaling pathway; IEA:UniProtKB-KW.
DR InterPro; IPR004963; PAE/NOTUM.
DR PANTHER; PTHR21562; PTHR21562; 1.
DR Pfam; PF03283; PAE; 1.
PE 2: Evidence at transcript level;
KW Glycoprotein; Hydrolase; Reference proteome; Secreted; Serine esterase;
KW Signal; Wnt signaling pathway.
FT SIGNAL 1..19
FT /evidence="ECO:0000255"
FT CHAIN 20..488
FT /note="Palmitoleoyl-protein carboxylesterase notum1'"
FT /evidence="ECO:0000255"
FT /id="PRO_0000433428"
FT ACT_SITE 226
FT /note="Charge relay system"
FT /evidence="ECO:0000250|UniProtKB:Q6P988"
FT ACT_SITE 334
FT /note="Charge relay system"
FT /evidence="ECO:0000250|UniProtKB:Q6P988"
FT ACT_SITE 383
FT /note="Charge relay system"
FT /evidence="ECO:0000250|UniProtKB:Q6P988"
FT CARBOHYD 90
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ SEQUENCE 488 AA; 54991 MW; 5C61BF6E777F81BC CRC64;
MAGTLCVTLL LLLSTIAVGG RKTWRRRSQQ IVPSSWERSE GGGESFPLDF TAVEGNMDNF
MNQIKSLAQS LYPCSAQRLD DEMKLHSLHN KSVTCNDGSP AGYYLKESKG SRRWLVFLEG
GWYCISRENC DIRYDTMRSL MSSRAWPPSK TASGILSTQP EENPHWWNAN IVFIPYCSSD
VWSGVSPKTE KSGYAFMGSL IIQEVVKELL GKGLDTAKLL LLAGSSAGGT GVLLNVDMVA
NLLEELGYPG IEVRGLSDSG WFLNNKQYWR TDCTDIITCA PTEAIQRGIR YWNSMVPERC
KQQFKEGEEW NCFFGYKIYP TLRSPVFVVQ WLFDEAQLTV DNVHLSRQPV QESQWLYIQN
LGRELRNTLK DVGASFAPAC LAHEVITRSH WTEIQVRGTS LPRALHCWDR SLQEPNKNSK
VQLKGCPFHL MDSCPWPQCN PTCPSIRDHF TGQEMSVVQF LMHLGFDVQK MASQQGMEPG
KLLGVLSS
