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-MAR-2024, entry version 10. 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 (NOV-2023) 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}. 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 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 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|PIRSR:PIRSR036665-52}; KW Coiled coil {ECO:0000256|SAM:Coils}; 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 //