ID   A0A8M9QHJ3_DANRE        Unreviewed;       765 AA.
AC   A0A8M9QHJ3;
DT   03-AUG-2022, integrated into UniProtKB/TrEMBL.
DT   03-AUG-2022, sequence version 1.
DT   27-NOV-2024, entry version 14.
DE   SubName: Full=Sulfatase 2a isoform X3 {ECO:0000313|RefSeq:XP_021335241.1};
GN   Name=sulf2a {ECO:0000313|RefSeq:XP_021335241.1,
GN   ECO:0000313|ZFIN:ZDB-GENE-040426-759};
GN   Synonyms=Sulf1 {ECO:0000313|RefSeq:XP_021335241.1}, sulf2
GN   {ECO:0000313|RefSeq:XP_021335241.1}, zgc:55612
GN   {ECO:0000313|RefSeq:XP_021335241.1};
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 {ECO:0000313|Proteomes:UP000000437, ECO:0000313|RefSeq:XP_021335241.1};
RN   [1] {ECO:0000313|Proteomes:UP000000437}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=23594743; DOI=10.1038/nature12111;
RG   Genome Reference Consortium Zebrafish;
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., Eliott D.,
RA   Threadgold G., Harden G., Ware D., Begum S., Mortimore B., Mortimer B.,
RA   Kerry G., Heath P., Phillimore B., Tracey A., Corby N., Dunn M.,
RA   Johnson C., Wood J., Clark S., Pelan S., Griffiths G., Smith M.,
RA   Glithero R., Howden P., Barker N., Lloyd C., Stevens C., Harley J.,
RA   Holt K., Panagiotidis G., Lovell J., Beasley H., Henderson C., Gordon D.,
RA   Auger K., Wright D., Collins J., Raisen C., Dyer L., Leung K.,
RA   Robertson L., Ambridge K., Leongamornlert D., McGuire S., Gilderthorp R.,
RA   Griffiths C., Manthravadi D., Nichol S., Barker G., Whitehead S., Kay M.,
RA   Brown J., Murnane C., Gray E., Humphries M., Sycamore N., Barker D.,
RA   Saunders D., Wallis J., Babbage A., Hammond S., Mashreghi-Mohammadi M.,
RA   Barr L., Martin S., Wray P., Ellington A., Matthews N., Ellwood M.,
RA   Woodmansey R., Clark G., Cooper J., Cooper J., Tromans A., Grafham D.,
RA   Skuce C., Pandian R., Andrews R., Harrison E., Kimberley A., Garnett J.,
RA   Fosker N., Hall R., Garner P., Kelly D., Bird C., Palmer S., Gehring I.,
RA   Berger A., Dooley C.M., Ersan-Urun Z., Eser C., Geiger H., Geisler M.,
RA   Karotki L., Kirn A., Konantz J., Konantz M., Oberlander M.,
RA   Rudolph-Geiger S., Teucke M., Lanz C., Raddatz G., Osoegawa K., Zhu B.,
RA   Rapp A., Widaa S., Langford C., Yang F., Schuster S.C., Carter N.P.,
RA   Harrow J., Ning Z., Herrero J., Searle S.M., Enright A., Geisler R.,
RA   Plasterk R.H., Lee C., Westerfield M., de Jong P.J., Zon L.I.,
RA   Postlethwait J.H., Nusslein-Volhard C., Hubbard T.J., Roest Crollius H.,
RA   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] {ECO:0000313|RefSeq:XP_021335241.1}
RP   IDENTIFICATION.
RC   STRAIN=Tuebingen {ECO:0000313|RefSeq:XP_021335241.1};
RG   RefSeq;
RL   Submitted (AUG-2024) to UniProtKB.
CC   -!- COFACTOR:
CC       Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC         Evidence={ECO:0000256|PIRSR:PIRSR036665-52};
CC       Note=Binds 1 Ca(2+) ion per subunit. {ECO:0000256|PIRSR:PIRSR036665-
CC       52};
CC   -!- SUBCELLULAR LOCATION: Cell surface {ECO:0000256|ARBA:ARBA00004241}.
CC       Endoplasmic reticulum {ECO:0000256|ARBA:ARBA00004240}. Golgi apparatus,
CC       Golgi stack {ECO:0000256|ARBA:ARBA00004348}.
CC   -!- PTM: The conversion to 3-oxoalanine (also known as C-formylglycine,
CC       FGly), of a serine or cysteine residue in prokaryotes and of a cysteine
CC       residue in eukaryotes, is critical for catalytic activity.
CC       {ECO:0000256|PIRSR:PIRSR036665-50}.
CC   -!- SIMILARITY: Belongs to the sulfatase family.
CC       {ECO:0000256|ARBA:ARBA00008779}.
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DR   RefSeq; XP_021335241.1; XM_021479566.1.
DR   AGR; ZFIN:ZDB-GENE-040426-759; -.
DR   ZFIN; ZDB-GENE-040426-759; sulf2a.
DR   Proteomes; UP000000437; Chromosome 11.
DR   GO; GO:0009986; C:cell surface; IBA:GO_Central.
DR   GO; GO:0005783; C:endoplasmic reticulum; IBA:GO_Central.
DR   GO; GO:0005795; C:Golgi stack; IEA:UniProtKB-SubCell.
DR   GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR   GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR   GO; GO:0005539; F:glycosaminoglycan binding; IBA:GO_Central.
DR   GO; GO:0008449; F:N-acetylglucosamine-6-sulfatase activity; IBA:GO_Central.
DR   GO; GO:0010669; P:epithelial structure maintenance; IMP:ZFIN.
DR   GO; GO:0032836; P:glomerular basement membrane development; IBA:GO_Central.
DR   GO; GO:0030201; P:heparan sulfate proteoglycan metabolic process; IBA:GO_Central.
DR   GO; GO:0040037; P:negative regulation of fibroblast growth factor receptor signaling pathway; IBA:GO_Central.
DR   GO; GO:0014003; P:oligodendrocyte development; IMP:ZFIN.
DR   GO; GO:0010575; P:positive regulation of vascular endothelial growth factor production; IBA:GO_Central.
DR   GO; GO:0030177; P:positive regulation of Wnt signaling pathway; IBA:GO_Central.
DR   GO; GO:0021514; P:ventral spinal cord interneuron differentiation; IMP:ZFIN.
DR   CDD; cd16147; G6S; 1.
DR   FunFam; 3.40.720.10:FF:000003; Extracellular sulfatase; 1.
DR   Gene3D; 3.40.720.10; Alkaline Phosphatase, subunit A; 1.
DR   InterPro; IPR017850; Alkaline_phosphatase_core_sf.
DR   InterPro; IPR014615; Extracellular_sulfatase.
DR   InterPro; IPR024609; Extracellular_sulfatase_C.
DR   InterPro; IPR024607; Sulfatase_CS.
DR   InterPro; IPR000917; Sulfatase_N.
DR   PANTHER; PTHR43108:SF4; EXTRACELLULAR SULFATASE SULF-2; 1.
DR   PANTHER; PTHR43108; N-ACETYLGLUCOSAMINE-6-SULFATASE FAMILY MEMBER; 1.
DR   Pfam; PF12548; DUF3740; 1.
DR   Pfam; PF00884; Sulfatase; 1.
DR   PIRSF; PIRSF036665; Sulf1; 1.
DR   SUPFAM; SSF53649; Alkaline phosphatase-like; 1.
DR   PROSITE; PS00523; SULFATASE_1; 1.
PE   3: Inferred from homology;
KW   Calcium {ECO:0000256|ARBA:ARBA00022837, ECO:0000256|PIRSR:PIRSR036665-52};
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Endoplasmic reticulum {ECO:0000256|ARBA:ARBA00022824};
KW   Golgi apparatus {ECO:0000256|ARBA:ARBA00023034};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Metal-binding {ECO:0000256|PIRSR:PIRSR036665-52};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000437};
KW   Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..24
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           25..765
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5035420446"
FT   DOMAIN          46..377
FT                   /note="Sulfatase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00884"
FT   DOMAIN          534..673
FT                   /note="Extracellular sulfatase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF12548"
FT   COILED          637..664
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   ACT_SITE        90
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR036665-51"
FT   BINDING         54
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR036665-52"
FT   BINDING         55
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR036665-52"
FT   BINDING         90
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /note="via 3-oxoalanine"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR036665-52"
FT   BINDING         319
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR036665-52"
FT   BINDING         320
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR036665-52"
FT   MOD_RES         90
FT                   /note="3-oxoalanine (Cys)"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR036665-50"
SQ   SEQUENCE   765 AA;  87970 MW;  C9D513980DF1908E CRC64;
     MAVGWRPATL LLVFILTFIC LSDGSTYLSG QRQRSRLQRD RRNVRPNMIL ILTDDQDIEL
     GSMQAMNKTK RIMMQGGTHF SNAFATTPMC CPSRSTILTG KYVHNHHTYT NNENCSSPSW
     QAHHEPHTFA VHLNNSGYRT AFFGKYLNEY NGSYVPPGWR EWVALVKNSR FYNYTLCRNG
     IREKHGTQYP KDYLTDVITN DSINYFRMSK RMYPHRPVMM VLSHAAPHGP EDAAPQYSSA
     FPNASQHITP SYNHAPNPDK HWILRYTGPM KPVHMQFTNM LQRRRLQTLL SVDDSVEKVY
     NMLVETGELD NTYIIYMSDH GYHIGQFGLV KGKSMPYEFD IRIPFYVRGP NVEAGAINPH
     IVLNTDLAPT LLDMAGIDIP QDMDGKSILK LLETERPVNS FTRFHSYKKA KLWRDSFLVE
     RGKPLHKLAD GKEVEQNSLP KYQRVRDLCQ RAEYQTPCEQ PGQKWQCIED GTGMPRLYKC
     KGMAGLFAPR ALGLMAANRG QISAAHPGSD YCDCEPAAPL KRKKALTKKK LKNKKSVPRN
     RWARSVPYHL DSNVYTLDLE KGYRPLNLNT SLMLGRKQAV YGQNEEYSGM GPTEDNFNSL
     TPPAALKVTY RCSILMNDTV KCDGGLYKSL QAWKDHKLHI EHEIETLQTK IKNLREVKGH
     LKEVRPKECE CNKNMYQYSS RALFKLKSAQ THSVNRMTSK DKKQWLMKEQ KRRKKLRKLL
     KRLRNNDTCS MPGLTCFTHD NQHWQTAPFW TSTALHATAL LSDIT
//