NOT1_XENLA
ID NOT1_XENLA Reviewed; 488 AA.
AC A0A0D3QS99;
DT 24-JUN-2015, integrated into UniProtKB/Swiss-Prot.
DT 27-MAY-2015, sequence version 1.
DT 03-AUG-2022, entry version 20.
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:AJQ30101.1};
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}.
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DR EMBL; KP781855; AJQ30101.1; -; mRNA.
DR RefSeq; XP_018089834.1; XM_018234345.1.
DR AlphaFoldDB; A0A0D3QS99; -.
DR SMR; A0A0D3QS99; -.
DR DNASU; 444338; -.
DR GeneID; 444338; -.
DR CTD; 444338; -.
DR Xenbase; XB-GENE-996989; notum.L.
DR OrthoDB; 610784at2759; -.
DR BRENDA; 3.1.1.98; 6725.
DR Proteomes; UP000186698; Chromosome 9_10L.
DR Bgee; 444338; Expressed in internal ear and 15 other tissues.
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..20
FT /evidence="ECO:0000255"
FT CHAIN 21..488
FT /note="Palmitoleoyl-protein carboxylesterase notum1"
FT /evidence="ECO:0000255"
FT /id="PRO_0000433427"
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; 54784 MW; 6E10FED9C12EAB5A CRC64;
MAGALCVTLL LLLSTNTVSG RKTWRRRGQQ IVPSGRERSE GGDESFPLDF TAVEGNMDNF
MAQIKSLAQS LYPCSAQRLD DEMKLHILHN KSVTCNDGSS AGYYLKESKG SRRWLVFLEG
GWYCISHENC DLRYDTMRRL MSSKAWPPAK TASGILSTQP EENPHWWNAN MVFIPYCSSD
VWSGASPKTE KSGYAFMGSL IIQEVVKELL GKGLDAAKVL LLAGSSAGGT GVLLNVDLVA
DLLEELGYPG IQVRGLSDSG WFLDNKQYRR TDCTDIITCA PTEAIQRGIR YWSSMVPERC
KQQFKEGEEW NCFFGYKIYP TLRSPVFVVQ WLFDEAQLTV DNVHLSGQPV QESQWLYIQN
LGRELRNTLK DVGASFAPAC LAHEVITRSH WTEIQVRGTS LPRALHCWDR RLQETNKNSK
VPLKGCPFHL MDSCPWPQCN PTCPSIRDHF TGQEMSVVQF LMHLGFDVQK MASQQGMEPG
KLLGVLSS
