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Protein

Arylsulfatase K

Gene

Arsk

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at transcript leveli

Functioni

Cofactori

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

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi40 – 401CalciumBy similarity
Metal bindingi80 – 801Calcium; via 3-oxoalanineBy similarity
Binding sitei128 – 1281SubstrateBy similarity
Binding sitei249 – 2491SubstrateBy similarity
Metal bindingi311 – 3111CalciumBy similarity
Metal bindingi312 – 3121CalciumBy similarity

GO - Molecular functioni

Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Keywords - Ligandi

Calcium, Metal-binding

Enzyme and pathway databases

ReactomeiR-RNO-1660662. Glycosphingolipid metabolism.
R-RNO-1663150. The activation of arylsulfatases.

Names & Taxonomyi

Protein namesi
Recommended name:
Arylsulfatase K (EC:3.1.6.-)
Short name:
ASK
Gene namesi
Name:Arsk
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Chromosome 2

Organism-specific databases

RGDi1310182. Arsk.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 1717Sequence analysisAdd
BLAST
Chaini18 – 563546Arylsulfatase KPRO_0000356287Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei80 – 8013-oxoalanine (Cys)By similarity
Glycosylationi108 – 1081N-linked (GlcNAc...)Sequence analysis
Glycosylationi191 – 1911N-linked (GlcNAc...)Sequence analysis
Glycosylationi260 – 2601N-linked (GlcNAc...)Sequence analysis
Glycosylationi373 – 3731N-linked (GlcNAc...)Sequence analysis
Glycosylationi411 – 4111N-linked (GlcNAc...)Sequence analysis
Glycosylationi496 – 4961N-linked (GlcNAc...)Sequence analysis

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

PaxDbiQ32KJ2.
PRIDEiQ32KJ2.

Expressioni

Gene expression databases

GenevisibleiQ32KJ2. RN.

Interactioni

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000029855.

Structurei

3D structure databases

ProteinModelPortaliQ32KJ2.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the sulfatase family.Curated

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiKOG3731. Eukaryota.
COG3119. LUCA.
GeneTreeiENSGT00730000110906.
HOGENOMiHOG000034080.
HOVERGENiHBG054703.
InParanoidiQ32KJ2.
KOiK12376.
OMAiTYMLRTD.
OrthoDBiEOG75B853.
PhylomeDBiQ32KJ2.

Family and domain databases

Gene3Di3.40.720.10. 1 hit.
InterProiIPR017849. Alkaline_Pase-like_a/b/a.
IPR017850. Alkaline_phosphatase_core.
IPR000917. Sulfatase_N.
[Graphical view]
PfamiPF00884. Sulfatase. 1 hit.
[Graphical view]
SUPFAMiSSF53649. SSF53649. 2 hits.

Sequencei

Sequence statusi: Complete.

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

Q32KJ2-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MLLLLVSVIV ALALVAPAPE TQEKRLQVAQ APNVVLVASD SFDGRLTFQP
60 70 80 90 100
GSQVVKLPFI NFMRARGTTF LNAYTNSPIC CPSRAAMWSG LFTHLTESWN
110 120 130 140 150
NFKGLDPNYT TWMDVMEKHG YQTQKFGKLD YSSGHHSISN RVEAWTRDVA
160 170 180 190 200
FLLRQEGRPI INLIPDKNRR RVMDKDWQNT DKAIAWLRQV NSTKPFVLYL
210 220 230 240 250
GLNLPHPYPS PSSGENFGSS TFHTSLYWLE KVAYDAIKIP KWLALSEMHP
260 270 280 290 300
VDYYSSYTKN CTGKFTENEI KNIRAFYYAM CAETDAMLGE IILALHKLNL
310 320 330 340 350
LQKTIVIYTS DHGEMAMEHR QFYKMSMYEA SAHVPILMMG PGIKANLQVP
360 370 380 390 400
SLVSLVDIYP TMLDIAGIPL PLNLSGYSLL PLSSNTSAND QAFRVHHPPW
410 420 430 440 450
ILSEFHGCNA NASTYMLRTG QWKYIAYSDG TLVQPQLFDL SLDPDELTNI
460 470 480 490 500
ATEFPEITYS LDQQLRSVIN YPKVSASVHR YNKEQFIMWK QSVAQNYSNY
510 520 530 540 550
IAHLRWHQDW QKDPRKYENA IQRWLAIHSS PPTHSPLSLV HQWLTTHSSP
560
IAVDNKKTFS SYT
Length:563
Mass (Da):64,273
Last modified:December 6, 2005 - v1
Checksum:i1B784F33678AC5A8
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AABR03012430 Genomic DNA. No translation available.
AABR03016345 Genomic DNA. No translation available.
AABR03016385 Genomic DNA. No translation available.
BN000745 mRNA. Translation: CAI84991.1.
RefSeqiNP_001041382.1. NM_001047917.1.
UniGeneiRn.202360.

Genome annotation databases

EnsembliENSRNOT00000029250; ENSRNOP00000029855; ENSRNOG00000026937.
GeneIDi365619.
KEGGirno:365619.
UCSCiRGD:1310182. rat.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AABR03012430 Genomic DNA. No translation available.
AABR03016345 Genomic DNA. No translation available.
AABR03016385 Genomic DNA. No translation available.
BN000745 mRNA. Translation: CAI84991.1.
RefSeqiNP_001041382.1. NM_001047917.1.
UniGeneiRn.202360.

3D structure databases

ProteinModelPortaliQ32KJ2.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000029855.

Proteomic databases

PaxDbiQ32KJ2.
PRIDEiQ32KJ2.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSRNOT00000029250; ENSRNOP00000029855; ENSRNOG00000026937.
GeneIDi365619.
KEGGirno:365619.
UCSCiRGD:1310182. rat.

Organism-specific databases

CTDi153642.
RGDi1310182. Arsk.

Phylogenomic databases

eggNOGiKOG3731. Eukaryota.
COG3119. LUCA.
GeneTreeiENSGT00730000110906.
HOGENOMiHOG000034080.
HOVERGENiHBG054703.
InParanoidiQ32KJ2.
KOiK12376.
OMAiTYMLRTD.
OrthoDBiEOG75B853.
PhylomeDBiQ32KJ2.

Enzyme and pathway databases

ReactomeiR-RNO-1660662. Glycosphingolipid metabolism.
R-RNO-1663150. The activation of arylsulfatases.

Miscellaneous databases

NextBioi687770.
PROiQ32KJ2.

Gene expression databases

GenevisibleiQ32KJ2. RN.

Family and domain databases

Gene3Di3.40.720.10. 1 hit.
InterProiIPR017849. Alkaline_Pase-like_a/b/a.
IPR017850. Alkaline_phosphatase_core.
IPR000917. Sulfatase_N.
[Graphical view]
PfamiPF00884. Sulfatase. 1 hit.
[Graphical view]
SUPFAMiSSF53649. SSF53649. 2 hits.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Genome sequence of the Brown Norway rat yields insights into mammalian evolution."
    Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J., Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G., Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G., Morgan M.
    , Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G., Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S., Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T., Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T., Smith D., Lee H.-M., Gustafson E., Cahill P., Kana A., Doucette-Stamm L., Weinstock K., Fechtel K., Weiss R.B., Dunn D.M., Green E.D., Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K., Zhu B., Marra M., Schein J., Bosdet I., Fjell C., Jones S., Krzywinski M., Mathewson C., Siddiqui A., Wye N., McPherson J., Zhao S., Fraser C.M., Shetty J., Shatsman S., Geer K., Chen Y., Abramzon S., Nierman W.C., Havlak P.H., Chen R., Durbin K.J., Egan A., Ren Y., Song X.-Z., Li B., Liu Y., Qin X., Cawley S., Cooney A.J., D'Souza L.M., Martin K., Wu J.Q., Gonzalez-Garay M.L., Jackson A.R., Kalafus K.J., McLeod M.P., Milosavljevic A., Virk D., Volkov A., Wheeler D.A., Zhang Z., Bailey J.A., Eichler E.E., Tuzun E., Birney E., Mongin E., Ureta-Vidal A., Woodwark C., Zdobnov E., Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J., Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D., Schmidt J., Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M., Abril J.F., Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O., Poliakov A., Huebner N., Ganten D., Goesele C., Hummel O., Kreitler T., Lee Y.-A., Monti J., Schulz H., Zimdahl H., Himmelbauer H., Lehrach H., Jacob H.J., Bromberg S., Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E., Lazar J., Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M., Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E., Webber C., Brandt P., Nyakatura G., Adetobi M., Chiaromonte F., Elnitski L., Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K., Miller W., Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S., Zhang Y., Lindpaintner K., Andrews T.D., Caccamo M., Clamp M., Clarke L., Curwen V., Durbin R.M., Eyras E., Searle S.M., Cooper G.M., Batzoglou S., Brudno M., Sidow A., Stone E.A., Payseur B.A., Bourque G., Lopez-Otin C., Puente X.S., Chakrabarti K., Chatterji S., Dewey C., Pachter L., Bray N., Yap V.B., Caspi A., Tesler G., Pevzner P.A., Haussler D., Roskin K.M., Baertsch R., Clawson H., Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J., Rosenbloom K.R., Trumbower H., Weirauch M., Cooper D.N., Stenson P.D., Ma B., Brent M., Arumugam M., Shteynberg D., Copley R.R., Taylor M.S., Riethman H., Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S., Mockrin S., Collins F.S.
    Nature 428:493-521(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: Brown Norway.
  2. "Sulfatases and sulfatase modifying factors: an exclusive and promiscuous relationship."
    Sardiello M., Annunziata I., Roma G., Ballabio A.
    Hum. Mol. Genet. 14:3203-3217(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION.

Entry informationi

Entry nameiARSK_RAT
AccessioniPrimary (citable) accession number: Q32KJ2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 16, 2008
Last sequence update: December 6, 2005
Last modified: January 20, 2016
This is version 69 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

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 one 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.