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NOTU2_DANRE
ID   NOTU2_DANRE             Reviewed;         495 AA.
AC   E7F0Z8;
DT   29-APR-2015, integrated into UniProtKB/Swiss-Prot.
DT   08-MAR-2011, sequence version 1.
DT   03-AUG-2022, entry version 67.
DE   RecName: Full=Carboxylesterase notum2 {ECO:0000250|UniProtKB:Q6P988};
DE            EC=3.1.1.- {ECO:0000250|UniProtKB:Q6P988};
DE   Flags: Precursor;
GN   Name=notum2 {ECO:0000312|ZFIN:ZDB-GENE-120215-77};
OS   Danio rerio (Zebrafish) (Brachydanio rerio).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC   Danionidae; Danioninae; Danio.
OX   NCBI_TaxID=7955;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Tuebingen;
RX   PubMed=23594743; DOI=10.1038/nature12111;
RA   Howe K., Clark M.D., Torroja C.F., Torrance J., Berthelot C., Muffato M.,
RA   Collins J.E., Humphray S., McLaren K., Matthews L., McLaren S., Sealy I.,
RA   Caccamo M., Churcher C., Scott C., Barrett J.C., Koch R., Rauch G.J.,
RA   White S., Chow W., Kilian B., Quintais L.T., Guerra-Assuncao J.A., Zhou Y.,
RA   Gu Y., Yen J., Vogel J.H., Eyre T., Redmond S., Banerjee R., Chi J., Fu B.,
RA   Langley E., Maguire S.F., Laird G.K., Lloyd D., Kenyon E., Donaldson S.,
RA   Sehra H., Almeida-King J., Loveland J., Trevanion S., Jones M., Quail M.,
RA   Willey D., Hunt A., Burton J., Sims S., McLay K., Plumb B., Davis J.,
RA   Clee C., Oliver K., Clark R., Riddle C., Elliot D., Threadgold G.,
RA   Harden G., Ware D., Begum S., Mortimore B., Kerry G., Heath P.,
RA   Phillimore B., Tracey A., Corby N., Dunn M., Johnson C., Wood J., Clark S.,
RA   Pelan S., Griffiths G., Smith M., Glithero R., Howden P., Barker N.,
RA   Lloyd C., Stevens C., Harley J., Holt K., Panagiotidis G., Lovell J.,
RA   Beasley H., Henderson C., Gordon D., Auger K., Wright D., Collins J.,
RA   Raisen C., Dyer L., Leung K., Robertson L., Ambridge K., Leongamornlert D.,
RA   McGuire S., Gilderthorp R., Griffiths C., Manthravadi D., Nichol S.,
RA   Barker G., Whitehead S., Kay M., Brown J., Murnane C., Gray E.,
RA   Humphries M., Sycamore N., Barker D., Saunders D., Wallis J., Babbage A.,
RA   Hammond S., Mashreghi-Mohammadi M., Barr L., Martin S., Wray P.,
RA   Ellington A., Matthews N., Ellwood M., Woodmansey R., Clark G., Cooper J.,
RA   Tromans A., Grafham D., Skuce C., Pandian R., Andrews R., Harrison E.,
RA   Kimberley A., Garnett J., Fosker N., Hall R., Garner P., Kelly D., Bird C.,
RA   Palmer S., Gehring I., Berger A., Dooley C.M., Ersan-Urun Z., Eser C.,
RA   Geiger H., Geisler M., Karotki L., Kirn A., Konantz J., Konantz M.,
RA   Oberlander M., Rudolph-Geiger S., Teucke M., Lanz C., Raddatz G.,
RA   Osoegawa K., Zhu B., Rapp A., Widaa S., Langford C., Yang F.,
RA   Schuster S.C., Carter N.P., Harrow J., Ning Z., Herrero J., Searle S.M.,
RA   Enright A., Geisler R., Plasterk R.H., Lee C., Westerfield M.,
RA   de Jong P.J., Zon L.I., Postlethwait J.H., Nusslein-Volhard C.,
RA   Hubbard T.J., Roest Crollius H., Rogers J., Stemple D.L.;
RT   "The zebrafish reference genome sequence and its relationship to the human
RT   genome.";
RL   Nature 496:498-503(2013).
RN   [2]
RP   FUNCTION, AND TISSUE SPECIFICITY.
RX   PubMed=23365253; DOI=10.1523/jneurosci.3694-12.2013;
RA   Cantu J.A., Flowers G.P., Topczewski J.;
RT   "Notum homolog plays a novel role in primary motor innervation.";
RL   J. Neurosci. 33:2177-2187(2013).
CC   -!- FUNCTION: Carboxylesterase that mediates deacylation of target proteins
CC       (By similarity). Acts as a regulator of growth cone migration. Does not
CC       act as an inhibitor of Wnt signaling (PubMed:23365253).
CC       {ECO:0000250|UniProtKB:Q6P988, ECO:0000269|PubMed:23365253}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:Q9VUX3}.
CC   -!- TISSUE SPECIFICITY: Specifically expressed in the muscle pioneers (MPs)
CC       during primary motor innervation. {ECO:0000269|PubMed:23365253}.
CC   -!- SIMILARITY: Belongs to the pectinacetylesterase family. Notum
CC       subfamily. {ECO:0000305}.
CC   -!- CAUTION: In contrast to other members of the family, it apparently does
CC       not inhibit the Wnt signaling pathway, suggesting that it does not
CC       mediate depalmitoleoylation of WNT proteins (PubMed:23365253). However,
CC       additional evidence is required to confirm these data.
CC       {ECO:0000269|PubMed:23365253, ECO:0000305}.
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DR   EMBL; BX546447; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BX548046; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   RefSeq; XP_694400.2; XM_689308.7.
DR   AlphaFoldDB; E7F0Z8; -.
DR   SMR; E7F0Z8; -.
DR   STRING; 7955.ENSDARP00000125786; -.
DR   ESTHER; danre-e7f0z8; Pectinacetylesterase-Notum.
DR   PaxDb; E7F0Z8; -.
DR   Ensembl; ENSDART00000151102; ENSDARP00000125786; ENSDARG00000088411.
DR   Ensembl; ENSDART00000181583; ENSDARP00000153752; ENSDARG00000088411.
DR   GeneID; 566040; -.
DR   CTD; 566040; -.
DR   ZFIN; ZDB-GENE-120215-77; notum2.
DR   eggNOG; KOG4287; Eukaryota.
DR   GeneTree; ENSGT00940000165776; -.
DR   HOGENOM; CLU_026533_1_1_1; -.
DR   InParanoid; E7F0Z8; -.
DR   OMA; TKSNWMS; -.
DR   OrthoDB; 610784at2759; -.
DR   PhylomeDB; E7F0Z8; -.
DR   TreeFam; TF324830; -.
DR   PRO; PR:E7F0Z8; -.
DR   Proteomes; UP000000437; Genome assembly.
DR   Proteomes; UP000814640; Chromosome 6.
DR   Bgee; ENSDARG00000088411; Expressed in zone of skin and 8 other tissues.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:1990699; F:palmitoleyl hydrolase activity; ISS:UniProtKB.
DR   GO; GO:0008045; P:motor neuron axon guidance; IMP:ZFIN.
DR   GO; GO:0090090; P:negative regulation of canonical Wnt signaling pathway; IBA:GO_Central.
DR   GO; GO:0030178; P:negative regulation of Wnt signaling pathway; ISS:UniProtKB.
DR   GO; GO:1990697; P:protein depalmitoleylation; ISS:UniProtKB.
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.
FT   SIGNAL          1..18
FT                   /evidence="ECO:0000255"
FT   CHAIN           19..495
FT                   /note="Carboxylesterase notum2"
FT                   /id="PRO_0000432993"
FT   REGION          24..80
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        65..80
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        234
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000250|UniProtKB:Q6P988"
FT   ACT_SITE        341
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000250|UniProtKB:Q6P988"
FT   ACT_SITE        390
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000250|UniProtKB:Q6P988"
FT   CARBOHYD        397
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ   SEQUENCE   495 AA;  54411 MW;  C3D937773F0FE359 CRC64;
     MNIFCHALFL LLLGVVSCQN NNRNVKPGGK PAKKPNNPAI EATQHGPEAD PNSGLAGAGD
     SSKETNPGGR GSSQQSASVN KPADDMKLHF LKNTAVTCND GTAAGFYLKE FKGSKRWLIF
     LEGGWCCYSK ETCDSRYKTI PRLMGSTDWP QTRRGSGLLS AQVDENPHWY NANIVFVPYC
     SSDVWSGNKA ASKPKQGKET EYAFMGSQII REVIKDLVPK GLKQAKVVML AGTSAGGTGV
     LLNIDKVSSL LEQQGAEAQV RGLVDSGWFL ESKQQKVPDC PDSASCTPAD AIKKGLRLWN
     GVVPEKCKQQ YKRGEDWHCF FGHKLYSYIS APLFVVQWLF DEEQLRVENI YMGSQSLSEQ
     QWTYMQNLGK ELKNSLKDVT AVFAPSCLSH TLITKSNWTD FQIKGTSLSR ALQCWDRSFQ
     EANKNSKTAL KGCPFHLIDN CQWPQCNPTC PALIDQATQQ EMTLLQVLAS MGLDLQKLGL
     DVRGDISAGM VSNGG
 
 
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