ID G5BGQ9_HETGA Unreviewed; 866 AA.
AC G5BGQ9;
DT 14-DEC-2011, integrated into UniProtKB/TrEMBL.
DT 14-DEC-2011, sequence version 1.
DT 24-JAN-2024, entry version 48.
DE RecName: Full=Extracellular sulfatase {ECO:0000256|PIRNR:PIRNR036665};
DE EC=3.1.6.- {ECO:0000256|PIRNR:PIRNR036665};
GN ORFNames=GW7_19605 {ECO:0000313|EMBL:EHB08470.1};
OS Heterocephalus glaber (Naked mole rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Hystricomorpha; Bathyergidae;
OC Heterocephalus.
OX NCBI_TaxID=10181 {ECO:0000313|EMBL:EHB08470.1, ECO:0000313|Proteomes:UP000006813};
RN [1] {ECO:0000313|EMBL:EHB08470.1, ECO:0000313|Proteomes:UP000006813}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=21993625; DOI=10.1038/nature10533;
RA Kim E.B., Fang X., Fushan A.A., Huang Z., Lobanov A.V., Han L.,
RA Marino S.M., Sun X., Turanov A.A., Yang P., Yim S.H., Zhao X.,
RA Kasaikina M.V., Stoletzki N., Peng C., Polak P., Xiong Z., Kiezun A.,
RA Zhu Y., Chen Y., Kryukov G.V., Zhang Q., Peshkin L., Yang L., Bronson R.T.,
RA Buffenstein R., Wang B., Han C., Li Q., Chen L., Zhao W., Sunyaev S.R.,
RA Park T.J., Zhang G., Wang J., Gladyshev V.N.;
RT "Genome sequencing reveals insights into physiology and longevity of the
RT naked mole rat.";
RL Nature 479:223-227(2011).
CC -!- FUNCTION: Exhibits arylsulfatase activity and highly specific
CC endoglucosamine-6-sulfatase activity. It can remove sulfate from the C-
CC 6 position of glucosamine within specific subregions of intact heparin.
CC {ECO:0000256|PIRNR:PIRNR036665}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Hydrolysis of the 6-sulfate groups of the N-acetyl-D-
CC glucosamine 6-sulfate units of heparan sulfate and keratan sulfate.;
CC EC=3.1.6.14; Evidence={ECO:0000256|ARBA:ARBA00034997};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=an aryl sulfate + H2O = a phenol + H(+) + sulfate;
CC Xref=Rhea:RHEA:17261, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:16189, ChEBI:CHEBI:33853, ChEBI:CHEBI:140317; EC=3.1.6.1;
CC Evidence={ECO:0000256|ARBA:ARBA00034984};
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: Endoplasmic reticulum
CC {ECO:0000256|PIRNR:PIRNR036665}. Golgi apparatus, Golgi stack
CC {ECO:0000256|ARBA:ARBA00004348, ECO:0000256|PIRNR:PIRNR036665}. Cell
CC surface {ECO:0000256|PIRNR:PIRNR036665}.
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, ECO:0000256|PIRNR:PIRNR036665}.
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DR EMBL; JH170216; EHB08470.1; -; Genomic_DNA.
DR STRING; 10181.G5BGQ9; -.
DR eggNOG; KOG3731; Eukaryota.
DR InParanoid; G5BGQ9; -.
DR Proteomes; UP000006813; Unassembled WGS sequence.
DR GO; GO:0009986; C:cell surface; IEA:UniProtKB-SubCell.
DR GO; GO:0005783; C:endoplasmic reticulum; IEA:UniProtKB-SubCell.
DR GO; GO:0005615; C:extracellular space; IEA:UniProtKB-UniRule.
DR GO; GO:0005795; C:Golgi stack; IEA:UniProtKB-SubCell.
DR GO; GO:0004065; F:arylsulfatase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0005509; F:calcium ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0008449; F:N-acetylglucosamine-6-sulfatase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0060348; P:bone development; IEA:UniProtKB-UniRule.
DR GO; GO:0002063; P:chondrocyte development; IEA:UniProtKB-UniRule.
DR GO; GO:0048706; P:embryonic skeletal system development; IEA:UniProtKB-UniRule.
DR GO; GO:0014846; P:esophagus smooth muscle contraction; IEA:UniProtKB-UniRule.
DR GO; GO:0035860; P:glial cell-derived neurotrophic factor receptor signaling pathway; IEA:UniProtKB-UniRule.
DR GO; GO:0030201; P:heparan sulfate proteoglycan metabolic process; IEA:UniProtKB-UniRule.
DR GO; GO:0060384; P:innervation; IEA:UniProtKB-UniRule.
DR GO; GO:0001822; P:kidney development; IEA:UniProtKB-UniRule.
DR GO; GO:0040037; P:negative regulation of fibroblast growth factor receptor signaling pathway; IEA:UniProtKB-UniRule.
DR GO; GO:0030177; P:positive regulation of Wnt signaling pathway; IEA:UniProtKB-UniRule.
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:SF1; EXTRACELLULAR SULFATASE SULF-1; 1.
DR PANTHER; PTHR43108; N-ACETYLGLUCOSAMINE-6-SULFATASE FAMILY MEMBER; 1.
DR Pfam; PF12548; DUF3740; 2.
DR Pfam; PF00884; Sulfatase; 1.
DR PIRSF; PIRSF036665; Sulf1; 1.
DR SUPFAM; SSF53649; Alkaline phosphatase-like; 2.
DR PROSITE; PS00523; SULFATASE_1; 1.
PE 3: Inferred from homology;
KW Calcium {ECO:0000256|PIRNR:PIRNR036665, ECO:0000256|PIRSR:PIRSR036665-52};
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Endoplasmic reticulum {ECO:0000256|PIRNR:PIRNR036665};
KW Golgi apparatus {ECO:0000256|ARBA:ARBA00023034,
KW ECO:0000256|PIRNR:PIRNR036665};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|PIRNR:PIRNR036665};
KW Metal-binding {ECO:0000256|PIRNR:PIRNR036665,
KW ECO:0000256|PIRSR:PIRSR036665-52};
KW Reference proteome {ECO:0000313|Proteomes:UP000006813};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|PIRNR:PIRNR036665}.
FT SIGNAL 1..22
FT /evidence="ECO:0000256|PIRNR:PIRNR036665"
FT CHAIN 23..866
FT /note="Extracellular sulfatase"
FT /evidence="ECO:0000256|PIRNR:PIRNR036665"
FT /id="PRO_5003474304"
FT DOMAIN 43..373
FT /note="Sulfatase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00884"
FT DOMAIN 534..675
FT /note="Extracellular sulfatase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF12548"
FT DOMAIN 678..736
FT /note="Extracellular sulfatase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF12548"
FT REGION 508..531
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 575..600
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 639..666
FT /evidence="ECO:0000256|SAM:Coils"
FT ACT_SITE 87
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PIRSR:PIRSR036665-51"
FT BINDING 51
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000256|PIRSR:PIRSR036665-52"
FT BINDING 52
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000256|PIRSR:PIRSR036665-52"
FT BINDING 87
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /note="via 3-oxoalanine"
FT /evidence="ECO:0000256|PIRSR:PIRSR036665-52"
FT BINDING 316
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000256|PIRSR:PIRSR036665-52"
FT BINDING 317
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000256|PIRSR:PIRSR036665-52"
FT MOD_RES 87
FT /note="3-oxoalanine (Cys)"
FT /evidence="ECO:0000256|PIRSR:PIRSR036665-50"
SQ SEQUENCE 866 AA; 100170 MW; 46FB0450DF76DB62 CRC64;
MKYSCCALVL AVLGTELLGT LCSTVRSARF RGRTQQERKN IRPNIILVLT DDQDVELGSL
QVMNKTRKIM EHGGATFTNA FVTTPMCCPS RSSMLTGKYV HNHNVYTNNE NCSSPSWQAM
HEPRTFAVYL NNTGYRTAFF GKYLNEYNGS YIPPGWREWL GLIKNSRFYN YTVCRNGIKE
KHGFDYAKDY FTDLITNESI NYFKMSKRMY PHRPIMMVIS HAAPHGPEDS APQFSKLYPN
ASQHITPSYN YAPNMDKHWI MQYTGPMLPI HMEFTNVLQR KRLQTLMSVD DSVERLYNML
VETGELDNTY IIYTADHGYH IGQFGLVKGK SMPYDFDIRV PFFIRGPSVE PGSIVPQIVL
NIDLAPTILD IAGLDTPPDV DGKSVLKLLD LEKPGNRFRT NKKARIWRDT FLVERGKFLR
KKEESSKNIQ QSNHLPKYER VKELCQQARY QTACEQPGQK WQCIEDTSGK LRIHKCKGPS
DLLTVRQSTG KLYSGGFHNK DKECTCRESG YRTSRSQRKS QRQFLRNQGT PKYKPRFVHT
RQTRSLSVEF EGEIYDINLE EEELQVLQPR SIAKRHDEGH RGLGSRQAAS GGXXXXRADN
AVAPPATVRV THKCFILPND TIHCERELYQ SARAWKDHKA YIDKEIEALQ DKIKNLREVR
GHLKRRRPEE CSCSKQSYYN KEKGVKRQEK LKSHLHPFKE AAQEVDSKLQ LFKENRRRKK
ERKEKKRQRK GEECSLPGLT CFTHDNNHWQ TAPFWDLGSF CACTSSNNNT YWCLRTVNET
HNFLFCEFAT GFLEYFDMNT DPYQLTNTVH TVERGVLNQL HVQLMELRGC QGYKQCNPRP
KSLEGGSKDG GSYDLHRGQL WDGWEG
//
