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P51689

- ARSD_HUMAN

UniProt

P51689 - ARSD_HUMAN

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Protein

Arylsulfatase D

Gene

ARSD

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

Functioni

Cofactori

Binds 1 calcium 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

  1. arylsulfatase activity Source: ProtInc
  2. metal ion binding Source: UniProtKB-KW

GO - Biological processi

  1. cellular protein metabolic process Source: Reactome
  2. glycosphingolipid metabolic process Source: Reactome
  3. post-translational protein modification Source: Reactome
  4. small molecule metabolic process Source: Reactome
  5. sphingolipid metabolic process Source: Reactome
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: Chromosome X

Organism-specific databases

HGNCiHGNC:717. ARSD.

Subcellular locationi

Lysosome Curated

GO - Cellular componenti

  1. endoplasmic reticulum lumen Source: Reactome
  2. extracellular vesicular exosome Source: UniProt
  3. lysosome Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Lysosome

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA25008.

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.
GenevestigatoriP51689.

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.
OMAiCLFFISW.
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. Align

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.

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:
EMBL
GenBank
DDBJ
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. [P51689-1]
GeneIDi414.
KEGGihsa:414.
UCSCiuc004cqy.3. human. [P51689-1]

Polymorphism databases

DMDMi212276422.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X83572 mRNA. Translation: CAA58555.1 . Frameshift.
AF160499 mRNA. Translation: AAF22253.1 .
AC005295 Genomic DNA. No translation available.
BC020229 mRNA. No translation available.
CCDSi CCDS35196.1. [P51689-1 ]
PIRi I37186.
RefSeqi NP_001660.2. NM_001669.3. [P51689-1 ]
UniGenei Hs.528631.

3D structure databases

ProteinModelPortali P51689.
SMRi P51689. Positions 38-577.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 9606.ENSP00000370546.

Polymorphism databases

DMDMi 212276422.

Proteomic databases

MaxQBi P51689.
PaxDbi P51689.
PRIDEi P51689.

Protocols and materials databases

DNASUi 414.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000381154 ; ENSP00000370546 ; ENSG00000006756 . [P51689-1 ]
GeneIDi 414.
KEGGi hsa:414.
UCSCi uc004cqy.3. human. [P51689-1 ]

Organism-specific databases

CTDi 414.
GeneCardsi GC0XM002818.
HGNCi HGNC:717. ARSD.
HPAi HPA004694.
MIMi 300002. gene.
neXtProti NX_P51689.
PharmGKBi PA25008.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG3119.
GeneTreei ENSGT00760000119062.
HOGENOMi HOG000135352.
HOVERGENi HBG004283.
InParanoidi P51689.
KOi K12374.
OMAi CLFFISW.
OrthoDBi EOG7QZG9J.
PhylomeDBi P51689.
TreeFami TF314186.

Enzyme and pathway databases

Reactomei REACT_116105. Glycosphingolipid metabolism.
REACT_121036. The activation of arylsulfatases.

Miscellaneous databases

ChiTaRSi ARSD. human.
GenomeRNAii 414.
NextBioi 1749.
PROi P51689.
SOURCEi Search...

Gene expression databases

Bgeei P51689.
CleanExi HS_ARSD.
ExpressionAtlasi P51689. baseline and differential.
Genevestigatori P51689.

Family and domain databases

Gene3Di 3.40.720.10. 2 hits.
InterProi IPR017849. Alkaline_Pase-like_a/b/a.
IPR017850. Alkaline_phosphatase_core.
IPR000917. Sulfatase.
IPR024607. Sulfatase_CS.
[Graphical view ]
Pfami PF00884. Sulfatase. 1 hit.
[Graphical view ]
SUPFAMi SSF53649. SSF53649. 1 hit.
PROSITEi PS00523. SULFATASE_1. 1 hit.
PS00149. SULFATASE_2. 1 hit.
[Graphical view ]
ProtoNeti Search...

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: October 29, 2014
This is version 116 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