SPHM_HUMAN
ID SPHM_HUMAN Reviewed; 502 AA.
AC P51688; A8K5E2;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 187.
DE RecName: Full=N-sulphoglucosamine sulphohydrolase;
DE EC=3.10.1.1 {ECO:0000269|PubMed:15146460, ECO:0000269|PubMed:24816101, ECO:0000269|PubMed:7493035};
DE AltName: Full=Sulfoglucosamine sulfamidase;
DE AltName: Full=Sulphamidase;
DE Flags: Precursor;
GN Name=SGSH; Synonyms=HSS;
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], PROTEIN SEQUENCE OF 21-45, CATALYTIC ACTIVITY,
RP AND FUNCTION.
RC TISSUE=Kidney, and Testis;
RX PubMed=7493035; DOI=10.1038/ng1295-465;
RA Scott H.S., Blanch L., Guo X.-H., Freeman C., Orsborn A., Baker E.,
RA Sutherland G.R., Morris C.P., Hopwood J.J.;
RT "Cloning of the sulphamidase gene and identification of mutations in
RT Sanfilippo A syndrome.";
RL Nat. Genet. 11:465-467(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Karageorgos L.E., Guo X.H., Blanch L., Weber B., Anson D.S., Scott H.S.,
RA Hopwood J.J.;
RL Submitted (NOV-1996) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Pancreas;
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 [5]
RP GLYCOSYLATION AT ASN-41 AND ASN-264.
RX PubMed=12754519; DOI=10.1038/nbt827;
RA Zhang H., Li X.-J., Martin D.B., Aebersold R.;
RT "Identification and quantification of N-linked glycoproteins using
RT hydrazide chemistry, stable isotope labeling and mass spectrometry.";
RL Nat. Biotechnol. 21:660-666(2003).
RN [6]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-41 AND ASN-413.
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 [7]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [8]
RP X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) IN COMPLEX WITH CALCIUM, FUNCTION,
RP CATALYTIC ACTIVITY, ACTIVE SITE, GLYCOSYLATION AT ASN-41; ASN-151; ASN-264
RP AND ASN-413, OXOALANINE AT CYS-70, AND DISULFIDE BONDS.
RX PubMed=24816101; DOI=10.1107/s1399004714002739;
RA Sidhu N.S., Schreiber K., Propper K., Becker S., Uson I., Sheldrick G.M.,
RA Gartner J., Kratzner R., Steinfeld R.;
RT "Structure of sulfamidase provides insight into the molecular pathology of
RT mucopolysaccharidosis IIIA.";
RL Acta Crystallogr. D 70:1321-1335(2014).
RN [9]
RP VARIANTS MPS3A, AND VARIANT HIS-456.
RX PubMed=9158154; DOI=10.1093/hmg/6.5.787;
RA Blanch L., Weber B., Guo X.-H., Scott H.S., Hopwood J.J.;
RT "Molecular defects in Sanfilippo syndrome type A.";
RL Hum. Mol. Genet. 6:787-791(1997).
RN [10]
RP VARIANTS MPS3A.
RX PubMed=9285796; DOI=10.1093/hmg/6.9.1573;
RA Weber B., Guo X.-H., Wraith J.E., Cooper A., Kleijer W.J., Bunge S.,
RA Hopwood J.J.;
RT "Novel mutations in Sanfilippo A syndrome: implications for enzyme
RT function.";
RL Hum. Mol. Genet. 6:1573-1579(1997).
RN [11]
RP VARIANTS MPS3A.
RX PubMed=9401012;
RX DOI=10.1002/(sici)1098-1004(1997)10:6<479::aid-humu10>3.0.co;2-x;
RA Bunge S., Ince H., Steglich C., Kleijer W.J., Beck M., Zaremba J.,
RA van Diggelen O.P., Weber B., Hopwood J.J., Gal A.;
RT "Identification of 16 sulfamidase gene mutations including the common R74C
RT in patients with mucopolysaccharidosis type IIIA (Sanfilippo A).";
RL Hum. Mutat. 10:479-485(1997).
RN [12]
RP VARIANTS MPS3A ASN-40; THR-44; TRP-66; CYS-74; ARG-122; LEU-128; PRO-146;
RP GLN-150; ASN-179; CYS-182; ARG-227; LYS-369 AND CYS-377, AND VARIANTS
RP ALA-226 AND HIS-456.
RX PubMed=9554748;
RX DOI=10.1002/(sici)1098-1004(1998)11:4<313::aid-humu9>3.0.co;2-p;
RA di Natale P., Balzano N., Esposito S., Villani G.R.D.;
RT "Identification of molecular defects in Italian Sanfilippo A patients
RT including 13 novel mutations.";
RL Hum. Mutat. 11:313-320(1998).
RN [13]
RP VARIANTS MPS3A ARG-85; PRO-206; PRO-354 AND ARG-386.
RX PubMed=9744479;
RX DOI=10.1002/(sici)1098-1004(1998)12:4<274::aid-humu9>3.0.co;2-f;
RA Montfort M., Vilageliu L., Garcia-Giralt N., Guidi S., Coll M.J.,
RA Chabas A., Grinberg D.;
RT "Mutation 1091delC is highly prevalent in Spanish Sanfilippo syndrome type
RT A patients.";
RL Hum. Mutat. 12:274-279(1998).
RN [14]
RP VARIANTS MPS3A GLY-32; TRP-66; CYS-74; PRO-79; TYR-84; ARG-122; TRP-150;
RP ASN-235; HIS-245; ASN-273; PRO-298; SER-322; LYS-355; HIS-374; GLN-ARG-381
RP INS; TRP-433; 436-TRP--LEU-438 DEL AND PHE-486, AND VARIANT HIS-456.
RX PubMed=11182930; DOI=10.1136/jmg.37.9.704;
RA Beesley C.E., Young E.P., Vellodi A., Winchester B.G.;
RT "Mutational analysis of Sanfilippo syndrome type A (MPS IIIA):
RT identification of 13 novel mutations.";
RL J. Med. Genet. 37:704-707(2000).
RN [15]
RP VARIANTS MPS3A LYS-42; ASN-235; SER-293 AND CYS-377, VARIANT HIS-456,
RP CHARACTERIZATION OF VARIANTS MPS3A LYS-42; ASN-235; SER-293 AND CYS-377,
RP AND CHARACTERIZATION OF VARIANT HIS-456.
RX PubMed=12000360; DOI=10.1034/j.1399-0004.2002.610304.x;
RA Lee-Chen G.J., Lin S.P., Ko M.H., Chuang C.K., Chen C.P., Lee H.H.,
RA Cheng S.C., Shen C.H., Tseng K.L., Li C.L.;
RT "Identification and characterization of mutations underlying Sanfilippo
RT syndrome type A (mucopolysaccharidosis type IIIA).";
RL Clin. Genet. 61:192-197(2002).
RN [16]
RP VARIANTS MPS3A CYS-74 AND SER-288.
RX PubMed=11793481; DOI=10.1002/humu.9009;
RA Emre S., Terzioglu M., Tokatli A., Coskun T., Ozalp I., Weber B.,
RA Hopwood J.J.;
RT "Sanfilippo syndrome in Turkey: identification of novel mutations in
RT subtypes A and B.";
RL Hum. Mutat. 19:184-185(2002).
RN [17]
RP VARIANTS MPS3A LEU-128; LYS-369 AND GLN-433, AND VARIANT HIS-456.
RX PubMed=12702166; DOI=10.1034/j.1399-0004.2003.00053.x;
RA Di Natale P., Villani G.R.D., Di Domenico C., Daniele A., Dionisi Vici C.,
RA Bartuli A.;
RT "Analysis of Sanfilippo A gene mutations in a large pedigree.";
RL Clin. Genet. 63:314-318(2003).
RN [18]
RP VARIANTS MPS3A CYS-74; ARG-106; PRO-163; ARG-191; TYR-403 DEL AND TRP-433,
RP CHARACTERIZATION OF VARIANTS MPS3A CYS-74; ARG-106; PRO-163; ARG-191;
RP TYR-403 DEL AND TRP-433, CATALYTIC ACTIVITY, FUNCTION, AND SUBCELLULAR
RP LOCATION.
RX PubMed=15146460; DOI=10.1002/humu.20037;
RA Muschol N., Storch S., Ballhausen D., Beesley C., Westermann J.-C., Gal A.,
RA Ullrich K., Hopwood J.J., Winchester B., Braulke T.;
RT "Transport, enzymatic activity, and stability of mutant sulfamidase (SGSH)
RT identified in patients with mucopolysaccharidosis type III A.";
RL Hum. Mutat. 23:559-566(2004).
RN [19]
RP VARIANT MPS3A PRO-206, VARIANT HIS-456, AND CHARACTERIZATION OF VARIANT
RP MPS3A PRO-206.
RX PubMed=15637719; DOI=10.1002/ajmg.a.30552;
RA Gabrielli O., Coppa G.V., Bruni S., Villani G.R.D., Pontarelli G.,
RA Di Natale P.;
RT "An adult Sanfilippo type A patient with homozygous mutation R206P in the
RT sulfamidase gene.";
RL Am. J. Med. Genet. A 133:85-89(2005).
RN [20]
RP VARIANTS MPS3A VAL-300 AND PRO-307.
RX PubMed=15902564; DOI=10.1007/s10545-005-0601-0;
RA Bekri S., Armana G., De Ricaud D., Osenda M., Maire I., Van Obberghen E.,
RA Froissart R.;
RT "Early diagnosis of mucopolysaccharidosis III A with a nonsense mutation
RT and two de novo missense mutations in SGSH gene.";
RL J. Inherit. Metab. Dis. 28:601-602(2005).
RN [21]
RP VARIANT MPS3A THR-293, AND VARIANTS LEU-304 AND MET-387.
RX PubMed=17128482;
RA Di Natale P., Pontarelli G., Villani G.R.D., Di Domenico C.;
RT "Gene symbol: SGSH. Disease: Sanfilippo type A syndrome,
RT mucopolysaccharidosis IIIA.";
RL Hum. Genet. 119:679-679(2006).
RN [22]
RP VARIANT MPS3A THR-88.
RX PubMed=16311287; DOI=10.1093/humrep/dei382;
RA Fiorentino F., Biricik A., Nuccitelli A., De Palma R., Kahraman S.,
RA Iacobelli M., Trengia V., Caserta D., Bonu M.A., Borini A., Baldi M.;
RT "Strategies and clinical outcome of 250 cycles of Preimplantation Genetic
RT Diagnosis for single gene disorders.";
RL Hum. Reprod. 21:670-684(2006).
RN [23]
RP VARIANTS MPS3A GLU-32; CYS-74; HIS-245; ALA-251 AND PRO-298, AND
RP ASSOCIATION OF VARIANT MPS3A PRO-298 WITH SLOWLY PROGRESSIVE PHENOTYPE.
RX PubMed=18407553; DOI=10.1002/humu.20738;
RA Meyer A., Kossow K., Gal A., Steglich C., Muehlhausen C., Ullrich K.,
RA Braulke T., Muschol N.;
RT "The mutation p.Ser298Pro in the sulphamidase gene (SGSH) is associated
RT with a slowly progressive clinical phenotype in mucopolysaccharidosis type
RT IIIA (Sanfilippo A syndrome).";
RL Hum. Mutat. 29:770-770(2008).
RN [24]
RP VARIANTS MPS3A TRP-66; CYS-74; HIS-245; ALA-251 AND PRO-298, AND
RP CHARACTERIZATION OF VARIANT MPS3A PRO-298.
RX PubMed=21671382; DOI=10.1002/ajmg.a.34053;
RA Muschol N., Pohl S., Meyer A., Gal A., Ullrich K., Braulke T.;
RT "Residual activity and proteasomal degradation of p.Ser298Pro sulfamidase
RT identified in patients with a mild clinical phenotype of Sanfilippo A
RT syndrome.";
RL Am. J. Med. Genet. A 155A:1634-1639(2011).
RN [25]
RP VARIANTS MPS3A 365-GLN--LEU-502 DEL AND ASN-477.
RX PubMed=28101780; DOI=10.1007/s12519-017-0005-x;
RA Ouesleti S., Coutinho M.F., Ribeiro I., Miled A., Mosbahi D.S., Alves S.;
RT "Update of the spectrum of mucopolysaccharidoses type III in Tunisia:
RT identification of three novel mutations and in silico structural analysis
RT of the missense mutations.";
RL World J. Pediatr. 13:374-380(2017).
CC -!- FUNCTION: Catalyzes a step in lysosomal heparan sulfate degradation.
CC {ECO:0000269|PubMed:15146460, ECO:0000269|PubMed:24816101,
CC ECO:0000269|PubMed:7493035}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + N-sulfo-D-glucosamine = D-glucosamine + sulfate;
CC Xref=Rhea:RHEA:17881, ChEBI:CHEBI:15377, ChEBI:CHEBI:16189,
CC ChEBI:CHEBI:57868, ChEBI:CHEBI:58723; EC=3.10.1.1;
CC Evidence={ECO:0000269|PubMed:15146460, ECO:0000269|PubMed:24816101,
CC ECO:0000269|PubMed:7493035};
CC -!- COFACTOR:
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC Evidence={ECO:0000269|PubMed:24816101};
CC Note=Binds 1 Ca(2+) ion per subunit. {ECO:0000269|PubMed:24816101};
CC -!- INTERACTION:
CC P51688; Q8NBK3: SUMF1; NbExp=2; IntAct=EBI-2907521, EBI-2853497;
CC -!- SUBCELLULAR LOCATION: Lysosome {ECO:0000269|PubMed:15146460}.
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:0000269|PubMed:24816101}.
CC -!- DISEASE: Mucopolysaccharidosis 3A (MPS3A) [MIM:252900]: A severe form
CC of mucopolysaccharidosis type 3, an autosomal recessive lysosomal
CC storage disease due to impaired degradation of heparan sulfate. MPS3 is
CC characterized by severe central nervous system degeneration, but only
CC mild somatic disease. Onset of clinical features usually occurs between
CC 2 and 6 years; severe neurologic degeneration occurs in most patients
CC between 6 and 10 years of age, and death occurs typically during the
CC second or third decade of life. MPS3A is characterized by earlier
CC onset, rapid progression of symptoms and shorter survival.
CC {ECO:0000269|PubMed:11182930, ECO:0000269|PubMed:11793481,
CC ECO:0000269|PubMed:12000360, ECO:0000269|PubMed:12702166,
CC ECO:0000269|PubMed:15146460, ECO:0000269|PubMed:15637719,
CC ECO:0000269|PubMed:15902564, ECO:0000269|PubMed:16311287,
CC ECO:0000269|PubMed:17128482, ECO:0000269|PubMed:18407553,
CC ECO:0000269|PubMed:21671382, ECO:0000269|PubMed:28101780,
CC ECO:0000269|PubMed:9158154, ECO:0000269|PubMed:9285796,
CC ECO:0000269|PubMed:9401012, ECO:0000269|PubMed:9554748,
CC ECO:0000269|PubMed:9744479}. Note=The disease is caused by variants
CC affecting the gene represented in this entry.
CC -!- SIMILARITY: Belongs to the sulfatase family. {ECO:0000305}.
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DR EMBL; U30894; AAA86530.1; -; mRNA.
DR EMBL; U60111; AAB17952.1; -; Genomic_DNA.
DR EMBL; U60107; AAB17952.1; JOINED; Genomic_DNA.
DR EMBL; U60108; AAB17952.1; JOINED; Genomic_DNA.
DR EMBL; U60109; AAB17952.1; JOINED; Genomic_DNA.
DR EMBL; U60110; AAB17952.1; JOINED; Genomic_DNA.
DR EMBL; AK291257; BAF83946.1; -; mRNA.
DR EMBL; BC047318; AAH47318.1; -; mRNA.
DR CCDS; CCDS11770.1; -.
DR RefSeq; NP_000190.1; NM_000199.3.
DR PDB; 4MHX; X-ray; 2.00 A; A/B=1-502.
DR PDB; 4MIV; X-ray; 2.40 A; A/B/C/D/E/F/G/H=1-502.
DR PDBsum; 4MHX; -.
DR PDBsum; 4MIV; -.
DR AlphaFoldDB; P51688; -.
DR SMR; P51688; -.
DR BioGRID; 112346; 104.
DR IntAct; P51688; 8.
DR MINT; P51688; -.
DR STRING; 9606.ENSP00000314606; -.
DR GlyConnect; 1576; 1 N-Linked glycan (1 site).
DR GlyGen; P51688; 5 sites, 1 N-linked glycan (1 site).
DR iPTMnet; P51688; -.
DR PhosphoSitePlus; P51688; -.
DR BioMuta; SGSH; -.
DR EPD; P51688; -.
DR jPOST; P51688; -.
DR MassIVE; P51688; -.
DR MaxQB; P51688; -.
DR PaxDb; P51688; -.
DR PeptideAtlas; P51688; -.
DR PRIDE; P51688; -.
DR ProteomicsDB; 56373; -.
DR Antibodypedia; 19766; 239 antibodies from 31 providers.
DR DNASU; 6448; -.
DR Ensembl; ENST00000326317.11; ENSP00000314606.6; ENSG00000181523.13.
DR GeneID; 6448; -.
DR KEGG; hsa:6448; -.
DR MANE-Select; ENST00000326317.11; ENSP00000314606.6; NM_000199.5; NP_000190.1.
DR UCSC; uc002jxz.5; human.
DR CTD; 6448; -.
DR DisGeNET; 6448; -.
DR GeneCards; SGSH; -.
DR GeneReviews; SGSH; -.
DR HGNC; HGNC:10818; SGSH.
DR HPA; ENSG00000181523; Low tissue specificity.
DR MalaCards; SGSH; -.
DR MIM; 252900; phenotype.
DR MIM; 605270; gene.
DR neXtProt; NX_P51688; -.
DR OpenTargets; ENSG00000181523; -.
DR Orphanet; 79269; Sanfilippo syndrome type A.
DR PharmGKB; PA35726; -.
DR VEuPathDB; HostDB:ENSG00000181523; -.
DR eggNOG; KOG3867; Eukaryota.
DR GeneTree; ENSGT00390000013080; -.
DR HOGENOM; CLU_006332_7_1_1; -.
DR InParanoid; P51688; -.
DR OMA; MAYPMRM; -.
DR OrthoDB; 464888at2759; -.
DR PhylomeDB; P51688; -.
DR TreeFam; TF323156; -.
DR BRENDA; 3.10.1.1; 2681.
DR PathwayCommons; P51688; -.
DR Reactome; R-HSA-2024096; HS-GAG degradation.
DR Reactome; R-HSA-2206307; MPS IIIA - Sanfilippo syndrome A.
DR SignaLink; P51688; -.
DR BioGRID-ORCS; 6448; 13 hits in 1080 CRISPR screens.
DR GeneWiki; SGSH; -.
DR GenomeRNAi; 6448; -.
DR Pharos; P51688; Tbio.
DR PRO; PR:P51688; -.
DR Proteomes; UP000005640; Chromosome 17.
DR RNAct; P51688; protein.
DR Bgee; ENSG00000181523; Expressed in left adrenal gland and 182 other tissues.
DR ExpressionAtlas; P51688; baseline and differential.
DR Genevisible; P51688; HS.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0043202; C:lysosomal lumen; TAS:Reactome.
DR GO; GO:0005764; C:lysosome; IDA:UniProtKB.
DR GO; GO:0005539; F:glycosaminoglycan binding; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0008449; F:N-acetylglucosamine-6-sulfatase activity; IBA:GO_Central.
DR GO; GO:0016250; F:N-sulfoglucosamine sulfohydrolase activity; IDA:UniProtKB.
DR GO; GO:0006027; P:glycosaminoglycan catabolic process; IDA:UniProtKB.
DR GO; GO:0030200; P:heparan sulfate proteoglycan catabolic process; IMP:UniProtKB.
DR Gene3D; 3.40.720.10; -; 1.
DR InterPro; IPR017850; Alkaline_phosphatase_core_sf.
DR InterPro; IPR032506; DUF4976.
DR InterPro; IPR024607; Sulfatase_CS.
DR InterPro; IPR000917; Sulfatase_N.
DR Pfam; PF16347; DUF4976; 1.
DR Pfam; PF00884; Sulfatase; 1.
DR SUPFAM; SSF53649; SSF53649; 1.
DR PROSITE; PS00523; SULFATASE_1; 1.
DR PROSITE; PS00149; SULFATASE_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Calcium; Direct protein sequencing; Disease variant;
KW Disulfide bond; Glycoprotein; Hydrolase; Lysosome; Metal-binding;
KW Mucopolysaccharidosis; Reference proteome; Signal.
FT SIGNAL 1..20
FT /evidence="ECO:0000269|PubMed:7493035"
FT CHAIN 21..502
FT /note="N-sulphoglucosamine sulphohydrolase"
FT /id="PRO_0000033433"
FT ACT_SITE 70
FT /note="Nucleophile"
FT /evidence="ECO:0000269|PubMed:24816101"
FT BINDING 31
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000269|PubMed:24816101,
FT ECO:0007744|PDB:4MHX, ECO:0007744|PDB:4MIV"
FT BINDING 32
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000269|PubMed:24816101,
FT ECO:0007744|PDB:4MHX, ECO:0007744|PDB:4MIV"
FT BINDING 70
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /note="via 3-oxoalanine"
FT /evidence="ECO:0000269|PubMed:24816101,
FT ECO:0007744|PDB:4MHX, ECO:0007744|PDB:4MIV"
FT BINDING 273
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000269|PubMed:24816101,
FT ECO:0007744|PDB:4MHX, ECO:0007744|PDB:4MIV"
FT BINDING 274
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000269|PubMed:24816101,
FT ECO:0007744|PDB:4MHX, ECO:0007744|PDB:4MIV"
FT MOD_RES 70
FT /note="3-oxoalanine (Cys)"
FT /evidence="ECO:0000269|PubMed:24816101"
FT CARBOHYD 41
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:12754519,
FT ECO:0000269|PubMed:19159218, ECO:0000269|PubMed:24816101,
FT ECO:0007744|PDB:4MHX, ECO:0007744|PDB:4MIV"
FT CARBOHYD 142
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 151
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:24816101,
FT ECO:0007744|PDB:4MHX, ECO:0007744|PDB:4MIV"
FT CARBOHYD 264
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:12754519,
FT ECO:0000269|PubMed:24816101, ECO:0007744|PDB:4MHX,
FT ECO:0007744|PDB:4MIV"
FT CARBOHYD 413
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:19159218,
FT ECO:0000269|PubMed:24816101, ECO:0007744|PDB:4MHX,
FT ECO:0007744|PDB:4MIV"
FT DISULFID 183..194
FT /evidence="ECO:0000269|PubMed:24816101,
FT ECO:0007744|PDB:4MHX, ECO:0007744|PDB:4MIV"
FT DISULFID 481..495
FT /evidence="ECO:0000269|PubMed:24816101,
FT ECO:0007744|PDB:4MHX, ECO:0007744|PDB:4MIV"
FT VARIANT 32
FT /note="D -> E (in MPS3A; dbSNP:rs139850991)"
FT /evidence="ECO:0000269|PubMed:18407553"
FT /id="VAR_054670"
FT VARIANT 32
FT /note="D -> G (in MPS3A)"
FT /evidence="ECO:0000269|PubMed:11182930"
FT /id="VAR_054671"
FT VARIANT 40
FT /note="Y -> N (in MPS3A; intermediate; dbSNP:rs1598758001)"
FT /evidence="ECO:0000269|PubMed:9554748"
FT /id="VAR_007388"
FT VARIANT 42
FT /note="N -> K (in MPS3A; does not yield active enzyme; the
FT reduction in 62 kDa precursor and 56 kDa mature forms
FT suggests an increased degradation of the mutant enzyme)"
FT /evidence="ECO:0000269|PubMed:12000360"
FT /id="VAR_054672"
FT VARIANT 44
FT /note="A -> T (in MPS3A; severe; dbSNP:rs1057521146)"
FT /evidence="ECO:0000269|PubMed:9554748"
FT /id="VAR_007389"
FT VARIANT 66
FT /note="S -> W (in MPS3A; intermediate/severe; common
FT mutation in Italy; dbSNP:rs104894637)"
FT /evidence="ECO:0000269|PubMed:11182930,
FT ECO:0000269|PubMed:21671382, ECO:0000269|PubMed:9554748"
FT /id="VAR_007390"
FT VARIANT 74
FT /note="R -> C (in MPS3A; intermediate/severe; the mutant is
FT enzymatically inactive; rapid degradation rather than
FT decrease in synthesis is responsible for the low steady
FT state level of the mutant protein in cells; the majority of
FT newly synthesized protein probably occurs in the
FT endoplasmic reticulum; dbSNP:rs104894636)"
FT /evidence="ECO:0000269|PubMed:11182930,
FT ECO:0000269|PubMed:11793481, ECO:0000269|PubMed:15146460,
FT ECO:0000269|PubMed:18407553, ECO:0000269|PubMed:21671382,
FT ECO:0000269|PubMed:9554748"
FT /id="VAR_007391"
FT VARIANT 74
FT /note="R -> H (in MPS3A; dbSNP:rs778336949)"
FT /id="VAR_007392"
FT VARIANT 79
FT /note="T -> P (in MPS3A; severe; dbSNP:rs779703983)"
FT /evidence="ECO:0000269|PubMed:11182930"
FT /id="VAR_007393"
FT VARIANT 84..85
FT /note="Missing (in MPS3A)"
FT /id="VAR_007394"
FT VARIANT 84
FT /note="H -> Y (in MPS3A)"
FT /evidence="ECO:0000269|PubMed:11182930"
FT /id="VAR_054673"
FT VARIANT 85
FT /note="Q -> R (in MPS3A)"
FT /evidence="ECO:0000269|PubMed:9744479"
FT /id="VAR_007395"
FT VARIANT 88
FT /note="M -> T (in MPS3A; dbSNP:rs1299601360)"
FT /evidence="ECO:0000269|PubMed:16311287"
FT /id="VAR_054674"
FT VARIANT 90
FT /note="G -> R (in MPS3A; dbSNP:rs774010006)"
FT /id="VAR_007396"
FT VARIANT 106
FT /note="S -> R (in MPS3A; shows 3.3% activity of the
FT expressed wild-type enzyme; rapid degradation rather than
FT decrease in synthesis is responsible for the low steady
FT state level of the mutant protein in cells)"
FT /evidence="ECO:0000269|PubMed:15146460"
FT /id="VAR_054675"
FT VARIANT 122
FT /note="G -> R (in MPS3A; intermediate; dbSNP:rs761607612)"
FT /evidence="ECO:0000269|PubMed:11182930,
FT ECO:0000269|PubMed:9554748"
FT /id="VAR_007397"
FT VARIANT 128
FT /note="P -> L (in MPS3A; intermediate; dbSNP:rs104894642)"
FT /evidence="ECO:0000269|PubMed:12702166,
FT ECO:0000269|PubMed:9554748"
FT /id="VAR_007398"
FT VARIANT 131
FT /note="V -> M (in MPS3A; dbSNP:rs370636303)"
FT /id="VAR_007399"
FT VARIANT 139
FT /note="T -> M (in MPS3A; dbSNP:rs775112689)"
FT /id="VAR_007400"
FT VARIANT 146
FT /note="L -> P (in MPS3A; severe; dbSNP:rs749358773)"
FT /evidence="ECO:0000269|PubMed:9554748"
FT /id="VAR_007401"
FT VARIANT 150
FT /note="R -> Q (in MPS3A; severe; dbSNP:rs104894638)"
FT /evidence="ECO:0000269|PubMed:9554748"
FT /id="VAR_007402"
FT VARIANT 150
FT /note="R -> W (in MPS3A; dbSNP:rs1479831530)"
FT /evidence="ECO:0000269|PubMed:11182930"
FT /id="VAR_054676"
FT VARIANT 163
FT /note="L -> P (in MPS3A; the mutant is enzymatically
FT inactive; rapid degradation rather than decrease in
FT synthesis is responsible for the low steady state level of
FT the mutant protein in cells; the mutant protein shows
FT instability in the lysosomes)"
FT /evidence="ECO:0000269|PubMed:15146460"
FT /id="VAR_054677"
FT VARIANT 179
FT /note="D -> N (in MPS3A; severe; dbSNP:rs774773010)"
FT /evidence="ECO:0000269|PubMed:9554748"
FT /id="VAR_007403"
FT VARIANT 182
FT /note="R -> C (in MPS3A; intermediate; dbSNP:rs529855742)"
FT /evidence="ECO:0000269|PubMed:9554748"
FT /id="VAR_007404"
FT VARIANT 191
FT /note="G -> R (in MPS3A; the mutant is enzymatically
FT inactive; rapid degradation rather than decrease in
FT synthesis is responsible for the low steady state level of
FT the mutant protein in cells; the majority of newly
FT synthesized protein probably occurs in the endoplasmic
FT reticulum; dbSNP:rs753666460)"
FT /evidence="ECO:0000269|PubMed:15146460"
FT /id="VAR_054678"
FT VARIANT 193
FT /note="F -> L (in MPS3A)"
FT /id="VAR_007405"
FT VARIANT 206
FT /note="R -> P (in MPS3A; the mutant enzyme retains 8%
FT residual activity; dbSNP:rs104894643)"
FT /evidence="ECO:0000269|PubMed:15637719,
FT ECO:0000269|PubMed:9744479"
FT /id="VAR_007406"
FT VARIANT 226
FT /note="V -> A"
FT /evidence="ECO:0000269|PubMed:9554748"
FT /id="VAR_007407"
FT VARIANT 227
FT /note="P -> R (in MPS3A; severe; dbSNP:rs774602372)"
FT /evidence="ECO:0000269|PubMed:9554748"
FT /id="VAR_007408"
FT VARIANT 234
FT /note="A -> G (in MPS3A; dbSNP:rs113641837)"
FT /id="VAR_007409"
FT VARIANT 235
FT /note="D -> N (in MPS3A; does not yield active enzyme; the
FT reduction in 62 kDa precursor and 56 kDa mature forms
FT suggests an increased degradation of the mutant enzyme;
FT dbSNP:rs753472891)"
FT /evidence="ECO:0000269|PubMed:11182930,
FT ECO:0000269|PubMed:12000360"
FT /id="VAR_054679"
FT VARIANT 235
FT /note="D -> V (in MPS3A; dbSNP:rs763800418)"
FT /id="VAR_007410"
FT VARIANT 245
FT /note="R -> H (in MPS3A; severe; common mutation in Western
FT Europe and Australia; dbSNP:rs104894635)"
FT /evidence="ECO:0000269|PubMed:11182930,
FT ECO:0000269|PubMed:18407553, ECO:0000269|PubMed:21671382"
FT /id="VAR_007411"
FT VARIANT 251
FT /note="G -> A (in MPS3A; dbSNP:rs144461610)"
FT /evidence="ECO:0000269|PubMed:18407553,
FT ECO:0000269|PubMed:21671382"
FT /id="VAR_054680"
FT VARIANT 273
FT /note="D -> N (in MPS3A; dbSNP:rs1046551417)"
FT /evidence="ECO:0000269|PubMed:11182930"
FT /id="VAR_054681"
FT VARIANT 288
FT /note="P -> S (in MPS3A)"
FT /evidence="ECO:0000269|PubMed:11793481"
FT /id="VAR_054682"
FT VARIANT 293
FT /note="P -> S (in MPS3A; does not yield active enzyme; the
FT reduction in 62 kDa precursor and 56 kDa mature forms
FT suggests an increased degradation of the mutant enzyme;
FT dbSNP:rs143947056)"
FT /evidence="ECO:0000269|PubMed:12000360"
FT /id="VAR_054683"
FT VARIANT 293
FT /note="P -> T (in MPS3A)"
FT /evidence="ECO:0000269|PubMed:17128482"
FT /id="VAR_054684"
FT VARIANT 298
FT /note="S -> P (in MPS3A; associated with a slowly
FT progressive clinical phenotype; rapidly degraded but small
FT amounts of the mutant protein are correctly transported to
FT the lysosome; low but significant residual enzymatic
FT activity; dbSNP:rs138504221)"
FT /evidence="ECO:0000269|PubMed:11182930,
FT ECO:0000269|PubMed:18407553, ECO:0000269|PubMed:21671382"
FT /id="VAR_007412"
FT VARIANT 300
FT /note="E -> V (in MPS3A)"
FT /evidence="ECO:0000269|PubMed:15902564"
FT /id="VAR_054685"
FT VARIANT 304
FT /note="R -> L (in dbSNP:rs745884647)"
FT /evidence="ECO:0000269|PubMed:17128482"
FT /id="VAR_054686"
FT VARIANT 307
FT /note="Q -> P (in MPS3A)"
FT /evidence="ECO:0000269|PubMed:15902564"
FT /id="VAR_054687"
FT VARIANT 321
FT /note="T -> A (in MPS3A; dbSNP:rs758756630)"
FT /id="VAR_007413"
FT VARIANT 322
FT /note="I -> S (in MPS3A)"
FT /evidence="ECO:0000269|PubMed:11182930"
FT /id="VAR_054688"
FT VARIANT 354
FT /note="A -> P (in MPS3A)"
FT /evidence="ECO:0000269|PubMed:9744479"
FT /id="VAR_007414"
FT VARIANT 355
FT /note="E -> K (in MPS3A; dbSNP:rs766938111)"
FT /evidence="ECO:0000269|PubMed:11182930"
FT /id="VAR_054689"
FT VARIANT 361
FT /note="V -> I (in dbSNP:rs9894254)"
FT /id="VAR_007415"
FT VARIANT 364
FT /note="S -> R (in MPS3A; dbSNP:rs1428699412)"
FT /id="VAR_007416"
FT VARIANT 365..502
FT /note="Missing (in MPS3A)"
FT /evidence="ECO:0000269|PubMed:28101780"
FT /id="VAR_079426"
FT VARIANT 369
FT /note="E -> K (in MPS3A; intermediate; dbSNP:rs104894640)"
FT /evidence="ECO:0000269|PubMed:12702166,
FT ECO:0000269|PubMed:9554748"
FT /id="VAR_007417"
FT VARIANT 372
FT /note="M -> I (in dbSNP:rs58786455)"
FT /id="VAR_061884"
FT VARIANT 374
FT /note="Y -> H (in MPS3A; dbSNP:rs1237611456)"
FT /evidence="ECO:0000269|PubMed:11182930"
FT /id="VAR_054690"
FT VARIANT 377
FT /note="R -> C (in MPS3A; severe; does not yield active
FT enzyme; the reduction in 62 kDa precursor and 56 kDa mature
FT forms suggests an increased degradation of the mutant
FT enzyme; dbSNP:rs772311757)"
FT /evidence="ECO:0000269|PubMed:12000360,
FT ECO:0000269|PubMed:9554748"
FT /id="VAR_007418"
FT VARIANT 377
FT /note="R -> H (in MPS3A; dbSNP:rs746037899)"
FT /id="VAR_007419"
FT VARIANT 380
FT /note="Q -> R (in MPS3A; dbSNP:rs144143780)"
FT /id="VAR_007420"
FT VARIANT 381
FT /note="H -> HQR (in MPS3A)"
FT /id="VAR_054691"
FT VARIANT 386
FT /note="L -> R (in MPS3A)"
FT /evidence="ECO:0000269|PubMed:9744479"
FT /id="VAR_007421"
FT VARIANT 387
FT /note="V -> M (in dbSNP:rs62620232)"
FT /evidence="ECO:0000269|PubMed:17128482"
FT /id="VAR_054692"
FT VARIANT 389
FT /note="N -> K (in MPS3A; dbSNP:rs764057581)"
FT /id="VAR_007422"
FT VARIANT 394
FT /note="M -> I (in dbSNP:rs34297805)"
FT /id="VAR_052517"
FT VARIANT 403
FT /note="Missing (in MPS3A; the mutant is enzymatically
FT inactive; rapid degradation rather than decrease in
FT synthesis is responsible for the low steady state level of
FT the mutant protein in cells)"
FT /evidence="ECO:0000269|PubMed:15146460"
FT /id="VAR_054693"
FT VARIANT 432..435
FT /note="YRAR -> W (in MPS3A)"
FT /id="VAR_054694"
FT VARIANT 433
FT /note="R -> Q (in MPS3A; severe; dbSNP:rs104894641)"
FT /evidence="ECO:0000269|PubMed:12702166"
FT /id="VAR_054695"
FT VARIANT 433
FT /note="R -> W (in MPS3A; the mutant is enzymatically
FT inactive; rapid degradation rather than decrease in
FT synthesis is responsible for the low steady state level of
FT the mutant protein in cells; the majority of newly
FT synthesized protein probably occurs in the endoplasmic
FT reticulum; dbSNP:rs777267343)"
FT /evidence="ECO:0000269|PubMed:11182930,
FT ECO:0000269|PubMed:15146460"
FT /id="VAR_054696"
FT VARIANT 436..438
FT /note="Missing (in MPS3A)"
FT /evidence="ECO:0000269|PubMed:11182930"
FT /id="VAR_054697"
FT VARIANT 447
FT /note="E -> K (in MPS3A; dbSNP:rs104894639)"
FT /id="VAR_007423"
FT VARIANT 456
FT /note="R -> H (does not affect enzyme activity; cells
FT transfected with the mutant enzyme contain a 62 kDa
FT precursor and a 56 kDa mature form as cells transfected
FT with the wild-type enzyme; dbSNP:rs7503034)"
FT /evidence="ECO:0000269|PubMed:11182930,
FT ECO:0000269|PubMed:12000360, ECO:0000269|PubMed:12702166,
FT ECO:0000269|PubMed:15637719, ECO:0000269|PubMed:9158154,
FT ECO:0000269|PubMed:9554748"
FT /id="VAR_007424"
FT VARIANT 477
FT /note="D -> N (in MPS3A; unknown pathological significance;
FT dbSNP:rs1064795109)"
FT /evidence="ECO:0000269|PubMed:28101780"
FT /id="VAR_079427"
FT VARIANT 486
FT /note="V -> F (in MPS3A)"
FT /evidence="ECO:0000269|PubMed:11182930"
FT /id="VAR_054698"
FT STRAND 24..32
FT /evidence="ECO:0007829|PDB:4MHX"
FT HELIX 38..40
FT /evidence="ECO:0007829|PDB:4MHX"
FT STRAND 43..45
FT /evidence="ECO:0007829|PDB:4MHX"
FT HELIX 48..54
FT /evidence="ECO:0007829|PDB:4MHX"
FT STRAND 57..64
FT /evidence="ECO:0007829|PDB:4MHX"
FT HELIX 70..77
FT /evidence="ECO:0007829|PDB:4MHX"
FT HELIX 83..86
FT /evidence="ECO:0007829|PDB:4MHX"
FT TURN 94..96
FT /evidence="ECO:0007829|PDB:4MHX"
FT HELIX 107..113
FT /evidence="ECO:0007829|PDB:4MHX"
FT STRAND 117..122
FT /evidence="ECO:0007829|PDB:4MHX"
FT TURN 129..131
FT /evidence="ECO:0007829|PDB:4MHX"
FT STRAND 135..139
FT /evidence="ECO:0007829|PDB:4MHX"
FT HELIX 145..149
FT /evidence="ECO:0007829|PDB:4MHX"
FT HELIX 152..164
FT /evidence="ECO:0007829|PDB:4MHX"
FT STRAND 171..176
FT /evidence="ECO:0007829|PDB:4MHX"
FT TURN 184..186
FT /evidence="ECO:0007829|PDB:4MHX"
FT HELIX 188..190
FT /evidence="ECO:0007829|PDB:4MHX"
FT TURN 195..198
FT /evidence="ECO:0007829|PDB:4MHX"
FT STRAND 199..201
FT /evidence="ECO:0007829|PDB:4MHX"
FT TURN 202..204
FT /evidence="ECO:0007829|PDB:4MHX"
FT TURN 217..219
FT /evidence="ECO:0007829|PDB:4MHX"
FT HELIX 230..259
FT /evidence="ECO:0007829|PDB:4MHX"
FT HELIX 263..265
FT /evidence="ECO:0007829|PDB:4MHX"
FT STRAND 266..274
FT /evidence="ECO:0007829|PDB:4MHX"
FT HELIX 287..290
FT /evidence="ECO:0007829|PDB:4MHX"
FT STRAND 294..297
FT /evidence="ECO:0007829|PDB:4MHX"
FT TURN 303..306
FT /evidence="ECO:0007829|PDB:4MHX"
FT STRAND 307..314
FT /evidence="ECO:0007829|PDB:4MHX"
FT HELIX 315..317
FT /evidence="ECO:0007829|PDB:4MHX"
FT HELIX 318..325
FT /evidence="ECO:0007829|PDB:4MHX"
FT STRAND 334..336
FT /evidence="ECO:0007829|PDB:4MHX"
FT HELIX 349..352
FT /evidence="ECO:0007829|PDB:4MHX"
FT STRAND 360..369
FT /evidence="ECO:0007829|PDB:4MHX"
FT STRAND 373..381
FT /evidence="ECO:0007829|PDB:4MHX"
FT STRAND 384..389
FT /evidence="ECO:0007829|PDB:4MHX"
FT TURN 390..393
FT /evidence="ECO:0007829|PDB:4MHX"
FT HELIX 400..403
FT /evidence="ECO:0007829|PDB:4MHX"
FT HELIX 406..417
FT /evidence="ECO:0007829|PDB:4MHX"
FT HELIX 427..431
FT /evidence="ECO:0007829|PDB:4MHX"
FT STRAND 435..440
FT /evidence="ECO:0007829|PDB:4MHX"
FT TURN 441..443
FT /evidence="ECO:0007829|PDB:4MHX"
FT HELIX 455..457
FT /evidence="ECO:0007829|PDB:4MHX"
FT HELIX 458..474
FT /evidence="ECO:0007829|PDB:4MHX"
FT TURN 478..484
FT /evidence="ECO:0007829|PDB:4MHX"
FT STRAND 485..487
FT /evidence="ECO:0007829|PDB:4MHX"
FT STRAND 491..497
FT /evidence="ECO:0007829|PDB:4MHX"
FT STRAND 500..502
FT /evidence="ECO:0007829|PDB:4MHX"
SQ SEQUENCE 502 AA; 56695 MW; 90C5CDAB4DCC3808 CRC64;
MSCPVPACCA LLLVLGLCRA RPRNALLLLA DDGGFESGAY NNSAIATPHL DALARRSLLF
RNAFTSVSSC SPSRASLLTG LPQHQNGMYG LHQDVHHFNS FDKVRSLPLL LSQAGVRTGI
IGKKHVGPET VYPFDFAYTE ENGSVLQVGR NITRIKLLVR KFLQTQDDRP FFLYVAFHDP
HRCGHSQPQY GTFCEKFGNG ESGMGRIPDW TPQAYDPLDV LVPYFVPNTP AARADLAAQY
TTVGRMDQGV GLVLQELRDA GVLNDTLVIF TSDNGIPFPS GRTNLYWPGT AEPLLVSSPE
HPKRWGQVSE AYVSLLDLTP TILDWFSIPY PSYAIFGSKT IHLTGRSLLP ALEAEPLWAT
VFGSQSHHEV TMSYPMRSVQ HRHFRLVHNL NFKMPFPIDQ DFYVSPTFQD LLNRTTAGQP
TGWYKDLRHY YYRARWELYD RSRDPHETQN LATDPRFAQL LEMLRDQLAK WQWETHDPWV
CAPDGVLEEK LSPQCQPLHN EL
