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Protein

Arylsulfatase D

Gene

ARSD

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Cofactori

Ca2+By similarityNote: Binds 1 Ca2+ ion per subunit.By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi49 – 491CalciumBy similarity
Metal bindingi50 – 501CalciumBy similarity
Metal bindingi89 – 891Calcium; via 3-oxoalanineBy similarity
Binding sitei148 – 1481SubstrateBy similarity
Active sitei150 – 1501By similarity
Binding sitei304 – 3041SubstrateBy similarity
Metal bindingi356 – 3561CalciumBy similarity
Metal bindingi357 – 3571CalciumBy similarity
Binding sitei381 – 3811SubstrateBy similarity

GO - Molecular functioni

  • arylsulfatase activity Source: ProtInc
  • metal ion binding Source: UniProtKB-KW

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Keywords - Ligandi

Calcium, Metal-binding

Enzyme and pathway databases

ReactomeiREACT_116105. Glycosphingolipid metabolism.
REACT_121036. The activation of arylsulfatases.

Names & Taxonomyi

Protein namesi
Recommended name:
Arylsulfatase D (EC:3.1.6.-)
Short name:
ASD
Gene namesi
Name:ARSD
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome X

Organism-specific databases

HGNCiHGNC:717. ARSD.

Subcellular locationi

GO - Cellular componenti

  • endoplasmic reticulum lumen Source: Reactome
  • extracellular exosome Source: UniProtKB
  • lysosome Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Lysosome

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA25008.

Polymorphism and mutation databases

BioMutaiARSD.
DMDMi212276422.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 3333Sequence AnalysisAdd
BLAST
Chaini34 – 593560Arylsulfatase DPRO_0000033424Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi61 – 611N-linked (GlcNAc...)Sequence Analysis
Modified residuei89 – 8913-oxoalanine (Cys)By similarity
Glycosylationi128 – 1281N-linked (GlcNAc...)Sequence Analysis
Glycosylationi347 – 3471N-linked (GlcNAc...)1 Publication

Post-translational modificationi

The conversion to 3-oxoalanine (also known as C-formylglycine, FGly), of a serine or cysteine residue in prokaryotes and of a cysteine residue in eukaryotes, is critical for catalytic activity.By similarity

Keywords - PTMi

Glycoprotein

Proteomic databases

MaxQBiP51689.
PaxDbiP51689.
PRIDEiP51689.

Expressioni

Tissue specificityi

Expressed in the pancreas, kidney, liver, lung, placenta, brain and heart.

Gene expression databases

BgeeiP51689.
CleanExiHS_ARSD.
ExpressionAtlasiP51689. baseline and differential.
GenevisibleiP51689. HS.

Organism-specific databases

HPAiHPA004694.

Interactioni

Protein-protein interaction databases

STRINGi9606.ENSP00000370546.

Structurei

3D structure databases

ProteinModelPortaliP51689.
SMRiP51689. Positions 38-577.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the sulfatase family.Curated

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiCOG3119.
GeneTreeiENSGT00760000119062.
HOGENOMiHOG000135352.
HOVERGENiHBG004283.
InParanoidiP51689.
KOiK12374.
OMAiTPRFHPK.
OrthoDBiEOG7QZG9J.
PhylomeDBiP51689.
TreeFamiTF314186.

Family and domain databases

Gene3Di3.40.720.10. 2 hits.
InterProiIPR017849. Alkaline_Pase-like_a/b/a.
IPR017850. Alkaline_phosphatase_core.
IPR000917. Sulfatase.
IPR024607. Sulfatase_CS.
[Graphical view]
PfamiPF00884. Sulfatase. 1 hit.
[Graphical view]
SUPFAMiSSF53649. SSF53649. 1 hit.
PROSITEiPS00523. SULFATASE_1. 1 hit.
PS00149. SULFATASE_2. 1 hit.
[Graphical view]

Sequences (3)i

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 3 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: P51689-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MRSAARRGRA APAARDSLPV LLFLCLLLKT CEPKTANAFK PNILLIMADD
60 70 80 90 100
LGTGDLGCYG NNTLRTPNID QLAEEGVRLT QHLAAAPLCT PSRAAFLTGR
110 120 130 140 150
HSFRSGMDAS NGYRALQWNA GSGGLPENET TFARILQQHG YATGLIGKWH
160 170 180 190 200
QGVNCASRGD HCHHPLNHGF DYFYGMPFTL TNDCDPGRPP EVDAALRAQL
210 220 230 240 250
WGYTQFLALG ILTLAAGQTC GFFSVSARAV TGMAGVGCLF FISWYSSFGF
260 270 280 290 300
VRRWNCILMR NHDVTEQPMV LEKTASLMLK EAVSYIERHK HGPFLLFLSL
310 320 330 340 350
LHVHIPLVTT SAFLGKSQHG LYGDNVEEMD WLIGKVLNAI EDNGLKNSTF
360 370 380 390 400
TYFTSDHGGH LEARDGHSQL GGWNGIYKGG KGMGGWEGGI RVPGIFHWPG
410 420 430 440 450
VLPAGRVIGE PTSLMDVFPT VVQLVGGEVP QDRVIDGHSL VPLLQGAEAR
460 470 480 490 500
SAHEFLFHYC GQHLHAARWH QKDSGSVWKV HYTTPQFHPE GAGACYGRGV
510 520 530 540 550
CPCSGEGVTH HRPPLLFDLS RDPSEARPLT PDSEPLYHAV IARVGAAVSE
560 570 580 590
HRQTLSPVPQ QFSMSNILWK PWLQPCCGHF PFCSCHEDGD GTP
Length:593
Mass (Da):64,860
Last modified:November 4, 2008 - v2
Checksum:i982B29D0FCEF9D34
GO
Isoform 2 (identifier: P51689-2) [UniParc]FASTAAdd to basket

Also known as: Beta

The sequence of this isoform differs from the canonical sequence as follows:
     334-382: GKVLNAIEDN...WNGIYKGGKG → ASDFMSSSEV...PVRLQILKRA
     383-593: Missing.

Show »
Length:382
Mass (Da):42,315
Checksum:iC9A8FFBE567654DD
GO
Isoform 3 (identifier: P51689-3) [UniParc]FASTAAdd to basket

Also known as: Alpha

The sequence of this isoform differs from the canonical sequence as follows:
     504-593: Missing.

Show »
Length:503
Mass (Da):54,934
Checksum:iCC4F3F8C7D201877
GO

Sequence cautioni

The sequence CAA58555.1 differs from that shown. Reason: Frameshift at several positions. Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti224 – 2241S → C.1 Publication
Corresponds to variant rs211653 [ dbSNP | Ensembl ].
VAR_052508
Natural varianti500 – 5001V → I.
Corresponds to variant rs2229557 [ dbSNP | Ensembl ].
VAR_052509
Natural varianti564 – 5641M → T.
Corresponds to variant rs2228431 [ dbSNP | Ensembl ].
VAR_052510

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei334 – 38249GKVLN…KGGKG → ASDFMSSSEVTESEAIKLMF RTMQRRCLPSMAFKKPWRGP VRLQILKRA in isoform 2. 1 PublicationVSP_015798Add
BLAST
Alternative sequencei383 – 593211Missing in isoform 2. 1 PublicationVSP_015799Add
BLAST
Alternative sequencei504 – 59390Missing in isoform 3. 1 PublicationVSP_035667Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X83572 mRNA. Translation: CAA58555.1. Frameshift.
AF160499 mRNA. Translation: AAF22253.1.
AC005295 Genomic DNA. No translation available.
BC020229 mRNA. No translation available.
CCDSiCCDS35196.1. [P51689-1]
PIRiI37186.
RefSeqiNP_001660.2. NM_001669.3. [P51689-1]
UniGeneiHs.528631.

Genome annotation databases

EnsembliENST00000381154; ENSP00000370546; ENSG00000006756.
GeneIDi414.
KEGGihsa:414.
UCSCiuc004cqy.3. human. [P51689-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X83572 mRNA. Translation: CAA58555.1. Frameshift.
AF160499 mRNA. Translation: AAF22253.1.
AC005295 Genomic DNA. No translation available.
BC020229 mRNA. No translation available.
CCDSiCCDS35196.1. [P51689-1]
PIRiI37186.
RefSeqiNP_001660.2. NM_001669.3. [P51689-1]
UniGeneiHs.528631.

3D structure databases

ProteinModelPortaliP51689.
SMRiP51689. Positions 38-577.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi9606.ENSP00000370546.

Polymorphism and mutation databases

BioMutaiARSD.
DMDMi212276422.

Proteomic databases

MaxQBiP51689.
PaxDbiP51689.
PRIDEiP51689.

Protocols and materials databases

DNASUi414.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000381154; ENSP00000370546; ENSG00000006756.
GeneIDi414.
KEGGihsa:414.
UCSCiuc004cqy.3. human. [P51689-1]

Organism-specific databases

CTDi414.
GeneCardsiGC0XM002818.
HGNCiHGNC:717. ARSD.
HPAiHPA004694.
MIMi300002. gene.
neXtProtiNX_P51689.
PharmGKBiPA25008.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiCOG3119.
GeneTreeiENSGT00760000119062.
HOGENOMiHOG000135352.
HOVERGENiHBG004283.
InParanoidiP51689.
KOiK12374.
OMAiTPRFHPK.
OrthoDBiEOG7QZG9J.
PhylomeDBiP51689.
TreeFamiTF314186.

Enzyme and pathway databases

ReactomeiREACT_116105. Glycosphingolipid metabolism.
REACT_121036. The activation of arylsulfatases.

Miscellaneous databases

ChiTaRSiARSD. human.
GenomeRNAii414.
NextBioi1749.
PROiP51689.
SOURCEiSearch...

Gene expression databases

BgeeiP51689.
CleanExiHS_ARSD.
ExpressionAtlasiP51689. baseline and differential.
GenevisibleiP51689. HS.

Family and domain databases

Gene3Di3.40.720.10. 2 hits.
InterProiIPR017849. Alkaline_Pase-like_a/b/a.
IPR017850. Alkaline_phosphatase_core.
IPR000917. Sulfatase.
IPR024607. Sulfatase_CS.
[Graphical view]
PfamiPF00884. Sulfatase. 1 hit.
[Graphical view]
SUPFAMiSSF53649. SSF53649. 1 hit.
PROSITEiPS00523. SULFATASE_1. 1 hit.
PS00149. SULFATASE_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "A cluster of sulfatase genes on Xp22.3: mutations in chondrodysplasia punctata (CDPX) and implications for warfarin embryopathy."
    Franco B., Meroni G., Parenti G., Levilliers J., Bernard L., Gebbia M., Cox L., Maroteaux P., Sheffield L., Rappold G.A., Andria G., Petit C., Ballabio A.
    Cell 81:15-25(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3).
    Tissue: Kidney.
  2. "Arylsulfatase D gene in Xp22.3 encodes two protein isoforms."
    Urbitsch P., Salzer M.J., Hirschmann P., Vogt P.H.
    DNA Cell Biol. 19:765-773(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), VARIANT CYS-224.
    Tissue: Testis.
  3. "The DNA sequence of the human X chromosome."
    Ross M.T., Grafham D.V., Coffey A.J., Scherer S., McLay K., Muzny D., Platzer M., Howell G.R., Burrows C., Bird C.P., Frankish A., Lovell F.L., Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G., Jones M.C.
    , Hurles M.E., Andrews T.D., Scott C.E., Searle S., Ramser J., Whittaker A., Deadman R., Carter N.P., Hunt S.E., Chen R., Cree A., Gunaratne P., Havlak P., Hodgson A., Metzker M.L., Richards S., Scott G., Steffen D., Sodergren E., Wheeler D.A., Worley K.C., Ainscough R., Ambrose K.D., Ansari-Lari M.A., Aradhya S., Ashwell R.I., Babbage A.K., Bagguley C.L., Ballabio A., Banerjee R., Barker G.E., Barlow K.F., Barrett I.P., Bates K.N., Beare D.M., Beasley H., Beasley O., Beck A., Bethel G., Blechschmidt K., Brady N., Bray-Allen S., Bridgeman A.M., Brown A.J., Brown M.J., Bonnin D., Bruford E.A., Buhay C., Burch P., Burford D., Burgess J., Burrill W., Burton J., Bye J.M., Carder C., Carrel L., Chako J., Chapman J.C., Chavez D., Chen E., Chen G., Chen Y., Chen Z., Chinault C., Ciccodicola A., Clark S.Y., Clarke G., Clee C.M., Clegg S., Clerc-Blankenburg K., Clifford K., Cobley V., Cole C.G., Conquer J.S., Corby N., Connor R.E., David R., Davies J., Davis C., Davis J., Delgado O., Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S., Draper H., Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I., Eades T., Ellwood M., Emery-Cohen A., Errington H., Evans K.L., Faulkner L., Francis F., Frankland J., Fraser A.E., Galgoczy P., Gilbert J., Gill R., Gloeckner G., Gregory S.G., Gribble S., Griffiths C., Grocock R., Gu Y., Gwilliam R., Hamilton C., Hart E.A., Hawes A., Heath P.D., Heitmann K., Hennig S., Hernandez J., Hinzmann B., Ho S., Hoffs M., Howden P.J., Huckle E.J., Hume J., Hunt P.J., Hunt A.R., Isherwood J., Jacob L., Johnson D., Jones S., de Jong P.J., Joseph S.S., Keenan S., Kelly S., Kershaw J.K., Khan Z., Kioschis P., Klages S., Knights A.J., Kosiura A., Kovar-Smith C., Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L., Liu W., Lloyd C., Lloyd D.M., Loulseged H., Loveland J.E., Lovell J.D., Lozado R., Lu J., Lyne R., Ma J., Maheshwari M., Matthews L.H., McDowall J., McLaren S., McMurray A., Meidl P., Meitinger T., Milne S., Miner G., Mistry S.L., Morgan M., Morris S., Mueller I., Mullikin J.C., Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N., Okwuonu G., Palmer S., Pandian R., Parker D., Parrish J., Pasternak S., Patel D., Pearce A.V., Pearson D.M., Pelan S.E., Perez L., Porter K.M., Ramsey Y., Reichwald K., Rhodes S., Ridler K.A., Schlessinger D., Schueler M.G., Sehra H.K., Shaw-Smith C., Shen H., Sheridan E.M., Shownkeen R., Skuce C.D., Smith M.L., Sotheran E.C., Steingruber H.E., Steward C.A., Storey R., Swann R.M., Swarbreck D., Tabor P.E., Taudien S., Taylor T., Teague B., Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S., Tromans A.C., d'Urso M., Verduzco D., Villasana D., Waldron L., Wall M., Wang Q., Warren J., Warry G.L., Wei X., West A., Whitehead S.L., Whiteley M.N., Wilkinson J.E., Willey D.L., Williams G., Williams L., Williamson A., Williamson H., Wilming L., Woodmansey R.L., Wray P.W., Yen J., Zhang J., Zhou J., Zoghbi H., Zorilla S., Buck D., Reinhardt R., Poustka A., Rosenthal A., Lehrach H., Meindl A., Minx P.J., Hillier L.W., Willard H.F., Wilson R.K., Waterston R.H., Rice C.M., Vaudin M., Coulson A., Nelson D.L., Weinstock G., Sulston J.E., Durbin R.M., Hubbard T., Gibbs R.A., Beck S., Rogers J., Bentley D.R.
    Nature 434:325-337(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  4. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    Tissue: Colon.
  5. "Glycoproteomics analysis of human liver tissue by combination of multiple enzyme digestion and hydrazide chemistry."
    Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.
    J. Proteome Res. 8:651-661(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-347.
    Tissue: Liver.

Entry informationi

Entry nameiARSD_HUMAN
AccessioniPrimary (citable) accession number: P51689
Secondary accession number(s): Q9UHJ8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: November 4, 2008
Last modified: July 22, 2015
This is version 122 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Human chromosome X
    Human chromosome X: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.