SULF2_HUMAN
ID SULF2_HUMAN Reviewed; 870 AA.
AC Q8IWU5; E1P5U6; Q5JYE1; Q6UX86; Q96SG2; Q9H1H0; Q9UJR3; Q9ULH3;
DT 19-JUL-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 166.
DE RecName: Full=Extracellular sulfatase Sulf-2;
DE Short=hSulf-2;
DE EC=3.1.6.-;
DE Flags: Precursor;
GN Name=SULF2; Synonyms=KIAA1247; ORFNames=UNQ559/PRO1120;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), CHARACTERIZATION, AND MUTAGENESIS
RP OF 88-CYS-CYS-89.
RC TISSUE=Lung;
RX PubMed=12368295; DOI=10.1074/jbc.m205131200;
RA Morimoto-Tomita M., Uchimura K., Werb Z., Hemmerich S., Rosen S.D.;
RT "Cloning and characterization of two extracellular heparin-degrading
RT endosulfatases in mice and humans.";
RL J. Biol. Chem. 277:49175-49185(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT THR-76.
RC TISSUE=Brain;
RX PubMed=10574462; DOI=10.1093/dnares/6.5.337;
RA Nagase T., Ishikawa K., Kikuno R., Hirosawa M., Nomura N., Ohara O.;
RT "Prediction of the coding sequences of unidentified human genes. XV. The
RT complete sequences of 100 new cDNA clones from brain which code for large
RT proteins in vitro.";
RL DNA Res. 6:337-345(1999).
RN [3]
RP SEQUENCE REVISION.
RX PubMed=12168954; DOI=10.1093/dnares/9.3.99;
RA Nakajima D., Okazaki N., Yamakawa H., Kikuno R., Ohara O., Nagase T.;
RT "Construction of expression-ready cDNA clones for KIAA genes: manual
RT curation of 330 KIAA cDNA clones.";
RL DNA Res. 9:99-106(2002).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RX PubMed=12975309; DOI=10.1101/gr.1293003;
RA Clark H.F., Gurney A.L., Abaya E., Baker K., Baldwin D.T., Brush J.,
RA Chen J., Chow B., Chui C., Crowley C., Currell B., Deuel B., Dowd P.,
RA Eaton D., Foster J.S., Grimaldi C., Gu Q., Hass P.E., Heldens S., Huang A.,
RA Kim H.S., Klimowski L., Jin Y., Johnson S., Lee J., Lewis L., Liao D.,
RA Mark M.R., Robbie E., Sanchez C., Schoenfeld J., Seshagiri S., Simmons L.,
RA Singh J., Smith V., Stinson J., Vagts A., Vandlen R.L., Watanabe C.,
RA Wieand D., Woods K., Xie M.-H., Yansura D.G., Yi S., Yu G., Yuan J.,
RA Zhang M., Zhang Z., Goddard A.D., Wood W.I., Godowski P.J., Gray A.M.;
RT "The secreted protein discovery initiative (SPDI), a large-scale effort to
RT identify novel human secreted and transmembrane proteins: a bioinformatics
RT assessment.";
RL Genome Res. 13:2265-2270(2003).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Fetal skin;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D.,
RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=11780052; DOI=10.1038/414865a;
RA Deloukas P., Matthews L.H., Ashurst J.L., Burton J., Gilbert J.G.R.,
RA Jones M., Stavrides G., Almeida J.P., Babbage A.K., Bagguley C.L.,
RA Bailey J., Barlow K.F., Bates K.N., Beard L.M., Beare D.M., Beasley O.P.,
RA Bird C.P., Blakey S.E., Bridgeman A.M., Brown A.J., Buck D., Burrill W.D.,
RA Butler A.P., Carder C., Carter N.P., Chapman J.C., Clamp M., Clark G.,
RA Clark L.N., Clark S.Y., Clee C.M., Clegg S., Cobley V.E., Collier R.E.,
RA Connor R.E., Corby N.R., Coulson A., Coville G.J., Deadman R., Dhami P.D.,
RA Dunn M., Ellington A.G., Frankland J.A., Fraser A., French L., Garner P.,
RA Grafham D.V., Griffiths C., Griffiths M.N.D., Gwilliam R., Hall R.E.,
RA Hammond S., Harley J.L., Heath P.D., Ho S., Holden J.L., Howden P.J.,
RA Huckle E., Hunt A.R., Hunt S.E., Jekosch K., Johnson C.M., Johnson D.,
RA Kay M.P., Kimberley A.M., King A., Knights A., Laird G.K., Lawlor S.,
RA Lehvaeslaiho M.H., Leversha M.A., Lloyd C., Lloyd D.M., Lovell J.D.,
RA Marsh V.L., Martin S.L., McConnachie L.J., McLay K., McMurray A.A.,
RA Milne S.A., Mistry D., Moore M.J.F., Mullikin J.C., Nickerson T.,
RA Oliver K., Parker A., Patel R., Pearce T.A.V., Peck A.I.,
RA Phillimore B.J.C.T., Prathalingam S.R., Plumb R.W., Ramsay H., Rice C.M.,
RA Ross M.T., Scott C.E., Sehra H.K., Shownkeen R., Sims S., Skuce C.D.,
RA Smith M.L., Soderlund C., Steward C.A., Sulston J.E., Swann R.M.,
RA Sycamore N., Taylor R., Tee L., Thomas D.W., Thorpe A., Tracey A.,
RA Tromans A.C., Vaudin M., Wall M., Wallis J.M., Whitehead S.L.,
RA Whittaker P., Willey D.L., Williams L., Williams S.A., Wilming L.,
RA Wray P.W., Hubbard T., Durbin R.M., Bentley D.R., Beck S., Rogers J.;
RT "The DNA sequence and comparative analysis of human chromosome 20.";
RL Nature 414:865-871(2001).
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Colon;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [9]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 527-870 (ISOFORM 1).
RA Stavrides G.S., Huckle E.J., Deloukas P.;
RL Submitted (NOV-1999) to the EMBL/GenBank/DDBJ databases.
RN [10]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-198.
RC TISSUE=Liver;
RX PubMed=19159218; DOI=10.1021/pr8008012;
RA Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.;
RT "Glycoproteomics analysis of human liver tissue by combination of multiple
RT enzyme digestion and hydrazide chemistry.";
RL J. Proteome Res. 8:651-661(2009).
RN [11]
RP VARIANTS [LARGE SCALE ANALYSIS] HIS-531 AND ASN-573.
RX PubMed=16959974; DOI=10.1126/science.1133427;
RA Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D.,
RA Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P.,
RA Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V.,
RA Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H.,
RA Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W.,
RA Velculescu V.E.;
RT "The consensus coding sequences of human breast and colorectal cancers.";
RL Science 314:268-274(2006).
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 -!- COFACTOR:
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000250};
CC Note=Binds 1 Ca(2+) ion per subunit. {ECO:0000250};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC pH dependence:
CC Optimum pH is 7.0-8.0.;
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum {ECO:0000250}. Golgi
CC apparatus, Golgi stack {ECO:0000250}. Cell surface {ECO:0000250}.
CC Note=Also localized on the cell surface. {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q8IWU5-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8IWU5-2; Sequence=VSP_013362;
CC -!- TISSUE SPECIFICITY: Expressed at highest levels in the ovary, skeletal
CC muscle, stomach, brain, uterus, heart, kidney and placenta.
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:0000250}.
CC -!- MISCELLANEOUS: [Isoform 2]: May be due to a competing acceptor splice
CC site. {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the sulfatase family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH20962.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=BAA86561.2; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=CAB61349.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AY101176; AAM76861.1; -; mRNA.
DR EMBL; AB033073; BAA86561.2; ALT_INIT; mRNA.
DR EMBL; AY358461; AAQ88826.1; -; mRNA.
DR EMBL; CR749319; CAH18174.1; -; mRNA.
DR EMBL; AL354813; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL034418; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471077; EAW75690.1; -; Genomic_DNA.
DR EMBL; CH471077; EAW75693.1; -; Genomic_DNA.
DR EMBL; CH471077; EAW75694.1; -; Genomic_DNA.
DR EMBL; CH471077; EAW75695.1; -; Genomic_DNA.
DR EMBL; BC020962; AAH20962.1; ALT_INIT; mRNA.
DR EMBL; BC110539; AAI10540.1; -; mRNA.
DR EMBL; AL133001; CAB61349.1; ALT_INIT; mRNA.
DR CCDS; CCDS13408.1; -. [Q8IWU5-1]
DR CCDS; CCDS13409.2; -. [Q8IWU5-2]
DR RefSeq; NP_001155313.1; NM_001161841.1. [Q8IWU5-1]
DR RefSeq; NP_061325.1; NM_018837.3. [Q8IWU5-1]
DR RefSeq; NP_940998.2; NM_198596.2. [Q8IWU5-2]
DR RefSeq; XP_005260515.1; XM_005260458.2. [Q8IWU5-1]
DR RefSeq; XP_006723893.1; XM_006723830.1. [Q8IWU5-1]
DR RefSeq; XP_016883444.1; XM_017027955.1. [Q8IWU5-1]
DR AlphaFoldDB; Q8IWU5; -.
DR SMR; Q8IWU5; -.
DR BioGRID; 121010; 121.
DR IntAct; Q8IWU5; 20.
DR MINT; Q8IWU5; -.
DR STRING; 9606.ENSP00000353007; -.
DR GlyConnect; 1232; 6 N-Linked glycans (4 sites).
DR GlyGen; Q8IWU5; 12 sites, 13 N-linked glycans (5 sites).
DR iPTMnet; Q8IWU5; -.
DR PhosphoSitePlus; Q8IWU5; -.
DR BioMuta; SULF2; -.
DR DMDM; 33112446; -.
DR EPD; Q8IWU5; -.
DR jPOST; Q8IWU5; -.
DR MassIVE; Q8IWU5; -.
DR MaxQB; Q8IWU5; -.
DR PaxDb; Q8IWU5; -.
DR PeptideAtlas; Q8IWU5; -.
DR PRIDE; Q8IWU5; -.
DR ProteomicsDB; 70897; -. [Q8IWU5-1]
DR ProteomicsDB; 70898; -. [Q8IWU5-2]
DR TopDownProteomics; Q8IWU5-2; -. [Q8IWU5-2]
DR Antibodypedia; 1101; 342 antibodies from 33 providers.
DR DNASU; 55959; -.
DR Ensembl; ENST00000359930.8; ENSP00000353007.4; ENSG00000196562.15. [Q8IWU5-1]
DR Ensembl; ENST00000467815.5; ENSP00000418442.1; ENSG00000196562.15. [Q8IWU5-2]
DR Ensembl; ENST00000484875.5; ENSP00000418290.1; ENSG00000196562.15. [Q8IWU5-1]
DR Ensembl; ENST00000688720.1; ENSP00000508753.1; ENSG00000196562.15. [Q8IWU5-1]
DR GeneID; 55959; -.
DR KEGG; hsa:55959; -.
DR MANE-Select; ENST00000688720.1; ENSP00000508753.1; NM_001387048.1; NP_001373977.1.
DR UCSC; uc002xto.4; human. [Q8IWU5-1]
DR CTD; 55959; -.
DR DisGeNET; 55959; -.
DR GeneCards; SULF2; -.
DR HGNC; HGNC:20392; SULF2.
DR HPA; ENSG00000196562; Low tissue specificity.
DR MIM; 610013; gene.
DR neXtProt; NX_Q8IWU5; -.
DR OpenTargets; ENSG00000196562; -.
DR PharmGKB; PA134902131; -.
DR VEuPathDB; HostDB:ENSG00000196562; -.
DR eggNOG; KOG3731; Eukaryota.
DR GeneTree; ENSGT00940000159151; -.
DR HOGENOM; CLU_006332_2_0_1; -.
DR InParanoid; Q8IWU5; -.
DR OMA; PQMDGRS; -.
DR OrthoDB; 1273622at2759; -.
DR PhylomeDB; Q8IWU5; -.
DR TreeFam; TF313545; -.
DR PathwayCommons; Q8IWU5; -.
DR SignaLink; Q8IWU5; -.
DR BioGRID-ORCS; 55959; 10 hits in 1074 CRISPR screens.
DR ChiTaRS; SULF2; human.
DR GeneWiki; SULF2; -.
DR GenomeRNAi; 55959; -.
DR Pharos; Q8IWU5; Tbio.
DR PRO; PR:Q8IWU5; -.
DR Proteomes; UP000005640; Chromosome 20.
DR RNAct; Q8IWU5; protein.
DR Bgee; ENSG00000196562; Expressed in decidua and 183 other tissues.
DR ExpressionAtlas; Q8IWU5; baseline and differential.
DR Genevisible; Q8IWU5; HS.
DR GO; GO:0009986; C:cell surface; IDA:UniProtKB.
DR GO; GO:0005783; C:endoplasmic reticulum; IDA:UniProtKB.
DR GO; GO:0005615; C:extracellular space; NAS:UniProtKB.
DR GO; GO:0005795; C:Golgi stack; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
DR GO; GO:0004065; F:arylsulfatase activity; IDA:UniProtKB.
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; IDA:UniProtKB.
DR GO; GO:0060348; P:bone development; ISS:BHF-UCL.
DR GO; GO:0051216; P:cartilage development; ISS:UniProtKB.
DR GO; GO:0002063; P:chondrocyte development; ISS:UniProtKB.
DR GO; GO:0048706; P:embryonic skeletal system development; ISS:UniProtKB.
DR GO; GO:0014846; P:esophagus smooth muscle contraction; ISS:UniProtKB.
DR GO; GO:0035860; P:glial cell-derived neurotrophic factor receptor signaling pathway; ISS:UniProtKB.
DR GO; GO:0032836; P:glomerular basement membrane development; ISS:UniProtKB.
DR GO; GO:0003094; P:glomerular filtration; ISS:UniProtKB.
DR GO; GO:0030201; P:heparan sulfate proteoglycan metabolic process; IDA:UniProtKB.
DR GO; GO:0060384; P:innervation; ISS:UniProtKB.
DR GO; GO:0001822; P:kidney development; ISS:BHF-UCL.
DR GO; GO:0040037; P:negative regulation of fibroblast growth factor receptor signaling pathway; ISS:UniProtKB.
DR GO; GO:0010575; P:positive regulation of vascular endothelial growth factor production; ISS:UniProtKB.
DR GO; GO:0030177; P:positive regulation of Wnt signaling pathway; IDA:UniProtKB.
DR Gene3D; 3.40.720.10; -; 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 Pfam; PF12548; DUF3740; 1.
DR Pfam; PF00884; Sulfatase; 1.
DR PIRSF; PIRSF036665; Sulf1; 1.
DR SUPFAM; SSF53649; SSF53649; 2.
DR PROSITE; PS00523; SULFATASE_1; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Calcium; Endoplasmic reticulum; Glycoprotein;
KW Golgi apparatus; Hydrolase; Metal-binding; Reference proteome; Signal.
FT SIGNAL 1..24
FT /evidence="ECO:0000255"
FT CHAIN 25..870
FT /note="Extracellular sulfatase Sulf-2"
FT /id="PRO_0000033440"
FT REGION 560..588
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 566..580
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 88
FT /note="Nucleophile"
FT /evidence="ECO:0000250|UniProtKB:P15289"
FT BINDING 52
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 53
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 88
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /note="via 3-oxoalanine"
FT /evidence="ECO:0000250"
FT BINDING 317
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 318
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT MOD_RES 88
FT /note="3-oxoalanine (Cys)"
FT /evidence="ECO:0000250|UniProtKB:P15289"
FT CARBOHYD 65
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 112
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 132
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 149
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 171
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 198
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:19159218"
FT CARBOHYD 241
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 561
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 608
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 717
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 754
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 764
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT VAR_SEQ 832..834
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:12975309"
FT /id="VSP_013362"
FT VARIANT 76
FT /note="A -> T (in dbSNP:rs56218501)"
FT /evidence="ECO:0000269|PubMed:10574462"
FT /id="VAR_061885"
FT VARIANT 531
FT /note="Y -> H (in a breast cancer sample; somatic
FT mutation)"
FT /evidence="ECO:0000269|PubMed:16959974"
FT /id="VAR_036494"
FT VARIANT 573
FT /note="D -> N (in a breast cancer sample; somatic
FT mutation)"
FT /evidence="ECO:0000269|PubMed:16959974"
FT /id="VAR_036495"
FT VARIANT 674
FT /note="R -> H (in dbSNP:rs10048853)"
FT /id="VAR_052518"
FT MUTAGEN 88..89
FT /note="CC->AA: Loss of arylsulfatase activity."
FT /evidence="ECO:0000269|PubMed:12368295"
SQ SEQUENCE 870 AA; 100455 MW; 74B1069CE2774D73 CRC64;
MGPPSLVLCL LSATVFSLLG GSSAFLSHHR LKGRFQRDRR NIRPNIILVL TDDQDVELGS
MQVMNKTRRI MEQGGAHFIN AFVTTPMCCP SRSSILTGKY VHNHNTYTNN ENCSSPSWQA
QHESRTFAVY LNSTGYRTAF FGKYLNEYNG SYVPPGWKEW VGLLKNSRFY NYTLCRNGVK
EKHGSDYSKD YLTDLITNDS VSFFRTSKKM YPHRPVLMVI SHAAPHGPED SAPQYSRLFP
NASQHITPSY NYAPNPDKHW IMRYTGPMKP IHMEFTNMLQ RKRLQTLMSV DDSMETIYNM
LVETGELDNT YIVYTADHGY HIGQFGLVKG KSMPYEFDIR VPFYVRGPNV EAGCLNPHIV
LNIDLAPTIL DIAGLDIPAD MDGKSILKLL DTERPVNRFH LKKKMRVWRD SFLVERGKLL
HKRDNDKVDA QEENFLPKYQ RVKDLCQRAE YQTACEQLGQ KWQCVEDATG KLKLHKCKGP
MRLGGSRALS NLVPKYYGQG SEACTCDSGD YKLSLAGRRK KLFKKKYKAS YVRSRSIRSV
AIEVDGRVYH VGLGDAAQPR NLTKRHWPGA PEDQDDKDGG DFSGTGGLPD YSAANPIKVT
HRCYILENDT VQCDLDLYKS LQAWKDHKLH IDHEIETLQN KIKNLREVRG HLKKKRPEEC
DCHKISYHTQ HKGRLKHRGS SLHPFRKGLQ EKDKVWLLRE QKRKKKLRKL LKRLQNNDTC
SMPGLTCFTH DNQHWQTAPF WTLGPFCACT SANNNTYWCM RTINETHNFL FCEFATGFLE
YFDLNTDPYQ LMNAVNTLDR DVLNQLHVQL MELRSCKGYK QCNPRTRNMD LGLKDGGSYE
QYRQFQRRKW PEMKRPSSKS LGQLWEGWEG
