ID   NOTUM_SCHMD             Reviewed;         527 AA.
AC   F8U830;
DT   29-APR-2015, integrated into UniProtKB/Swiss-Prot.
DT   21-SEP-2011, sequence version 1.
DT   25-MAY-2022, entry version 25.
DE   RecName: Full=Palmitoleoyl-protein carboxylesterase NOTUM {ECO:0000250|UniProtKB:Q6P988};
DE            Short=Smed-notum {ECO:0000303|PubMed:21566195};
DE            EC=3.1.1.98 {ECO:0000250|UniProtKB:Q6P988};
DE   Flags: Precursor;
GN   Name=notum {ECO:0000303|PubMed:21566195};
OS   Schmidtea mediterranea (Freshwater planarian flatworm).
OC   Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Platyhelminthes;
OC   Rhabditophora; Seriata; Tricladida; Continenticola; Geoplanoidea;
OC   Dugesiidae; Schmidtea.
OX   NCBI_TaxID=79327 {ECO:0000312|EMBL:AEF01556.1};
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, TISSUE SPECIFICITY, AND INDUCTION.
RX   PubMed=21566195; DOI=10.1126/science.1202143;
RA   Petersen C.P., Reddien P.W.;
RT   "Polarized notum activation at wounds inhibits Wnt function to promote
RT   planarian head regeneration.";
RL   Science 332:852-855(2011).
CC   -!- FUNCTION: Carboxylesterase that acts as a key negative regulator of the
CC       Wnt signaling pathway (PubMed:21566195). Acts by specifically mediating
CC       depalmitoleoylation of WNT proteins. Serine palmitoleoylation of WNT
CC       proteins is required for efficient binding to frizzled receptors (By
CC       similarity). Promotes head regeneration following amputation by
CC       inhibiting the Wnt signaling pathway. {ECO:0000250|UniProtKB:Q6P988,
CC       ECO:0000269|PubMed:21566195}.
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 anterior pole.
CC       {ECO:0000269|PubMed:21566195}.
CC   -!- INDUCTION: Strongly up-regulated near anterior-facing wounds following
CC       head and tail amputation. {ECO:0000269|PubMed:21566195}.
CC   -!- SIMILARITY: Belongs to the pectinacetylesterase family. Notum
CC       subfamily. {ECO:0000305}.
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DR   EMBL; JF725701; AEF01556.1; -; mRNA.
DR   AlphaFoldDB; F8U830; -.
DR   SMR; F8U830; -.
DR   ESTHER; schmd-f8u830; Pectinacetylesterase-Notum.
DR   PRIDE; F8U830; -.
DR   BRENDA; 3.1.1.98; 12164.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:1990699; F:palmitoleyl hydrolase activity; ISS:UniProtKB.
DR   GO; GO:0030178; P:negative regulation of Wnt signaling pathway; ISS:UniProtKB.
DR   GO; GO:1990697; P:protein depalmitoleylation; ISS: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; Secreted; Serine esterase; Signal;
KW   Wnt signaling pathway.
FT   SIGNAL          1..19
FT                   /evidence="ECO:0000255"
FT   CHAIN           20..527
FT                   /note="Palmitoleoyl-protein carboxylesterase NOTUM"
FT                   /id="PRO_0000432995"
FT   ACT_SITE        203
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000250|UniProtKB:Q6P988"
FT   ACT_SITE        311
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000250|UniProtKB:Q6P988"
FT   ACT_SITE        359
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000250|UniProtKB:Q6P988"
FT   CARBOHYD        64
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        86
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        104
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        249
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        451
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ   SEQUENCE   527 AA;  60852 MW;  C4C496D15EDCD0E1 CRC64;
     MKSYLILNTL LLSLLKINGF SKSSWFSSKT SLIFDRINKL NDPQSSNSIH SRKYQYFQLK
     KFPNSTNVRC NDGSIPGYYT RPSTTNCSKK WLIFLEGGWY CFNNNTCESR RRTHYDLFSS
     EFWSSERQLG GILSNNERIN PNFHDYNSVY IPYCSSDLWS GKQLEKTNGL YFHGSRILDT
     VVDDLTQNQH FKKVHEVAFV GSSAGGIGVL LNIDRLKRRL KKKLKRKVFI HGIVDSAWFL
     DYPAYRQSNC THIYECPPEN ALRNGMKLWN PRIPRRCKKF QGRGREWKCF MGPVIYRHLK
     NPTFIIQSLF DDAQLQMSKV PILEGGSNKK FSYIQQLGGF AAQTLRQAKG VFAHSCVDHE
     ILTKSNWAYV SVNNQRLHET LNYWQAYLEG EKKKIKKKVQ KNPKLIKTGK SPCKNLRKPK
     FSGNIDQSKY QLIDSCHISQ ITSYKIQLPH NRTLSRCANA IPLIPLCNPT CSPLSHPISG
     LSMSFIDLLE LYNVRINLIA KSLGISMEQL RKMNTQQQIS LLYCSSR