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Protein

Arylsulfatase K

Gene

Arsk

Organism
Mus musculus (Mouse)
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

Names & Taxonomyi

Protein namesi
Recommended name:
Arylsulfatase K (EC:3.1.6.-)
Short name:
ASK
Gene namesi
Name:Arsk
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Unplaced

Organism-specific databases

MGIiMGI:1924291. 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 – 1616Sequence analysisAdd
BLAST
Chaini17 – 553537Arylsulfatase KPRO_0000356286Add
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

MaxQBiQ9D2L1.
PaxDbiQ9D2L1.
PRIDEiQ9D2L1.

PTM databases

PhosphoSiteiQ9D2L1.

Expressioni

Gene expression databases

BgeeiQ9D2L1.

Interactioni

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000113274.

Structurei

3D structure databases

ProteinModelPortaliQ9D2L1.
SMRiQ9D2L1. Positions 32-467.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the sulfatase family.Curated

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiKOG3731. Eukaryota.
COG3119. LUCA.
HOGENOMiHOG000034080.
HOVERGENiHBG054703.
InParanoidiQ9D2L1.
KOiK12376.
OrthoDBiEOG75B853.
PhylomeDBiQ9D2L1.
TreeFamiTF313545.

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.

Q9D2L1-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MLLLLVSVVA ALALAAPAPR TQKKRMQVNQ APNVVLVASD SFDGRLTFQP
60 70 80 90 100
GSQVVKLPFI NFMRAHGTTF LNAYTNSPIC CPSRAAMWSG LFTHLTESWN
110 120 130 140 150
NFKGLDPNYT TWMDIMEKHG YQTQKFGKVD YTSGHHSISN RVEAWTRDVA
160 170 180 190 200
FLLRQEGRPI INLIPDKNRR RVMTKDWQNT DKAIEWLRQV NYTKPFVLYL
210 220 230 240 250
GLNLPHPYPS PSSGENFGSS TFHTSLYWLE KVAYDAIKIP KWLTLSQMHP
260 270 280 290 300
VDFYSSYTKN CTGKFTENEI KNIRAFYYAM CAETDAMLGE IILALHKLDL
310 320 330 340 350
LQKTIVIYTS DHGEMAMEHR QFYKMSMYEA SVHVPLLMMG PGIKANLQVP
360 370 380 390 400
SVVSLVDIYP TMLDIAGIAL PPNLSGYSLL TLLSNASANE QAFKFHRPPW
410 420 430 440 450
ILSEFHGCNA NASTYMLRTG QWKYIAYADG ASVQPQLFDL SLDPDELTNI
460 470 480 490 500
ATEFPEITYS LDQKLRSIVN YPKVSASVHQ YNKEQFIMWK QSVGQNYSNV
510 520 530 540 550
IAHLRWHQDW QRDPRKYENA IQHWLTAHSS PLASSPTQST SGSQPTLPQS

TSG
Length:553
Mass (Da):62,801
Last modified:January 20, 2009 - v2
Checksum:i1C4C405D365EE507
GO

Sequence cautioni

The sequence AAH46790.3 differs from that shown. Reason: Erroneous initiation. Curated
The sequence AAH58351.3 differs from that shown. Reason: Erroneous initiation. Curated
The sequence BAB28703.1 differs from that shown. Reason: Frameshift at position 544. Curated
The sequence BAB28703.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated
The sequence BAB31772.1 differs from that shown. Reason: Erroneous initiation. Curated
The sequence BAC27279.1 differs from that shown. Reason: Erroneous initiation. Curated
The sequence BAC28035.1 differs from that shown. Reason: Erroneous initiation. Curated
The sequence BAC29070.1 differs from that shown. Reason: Erroneous initiation. Curated
The sequence BAC30444.1 differs from that shown. Reason: Erroneous initiation. Curated
The sequence BAC32696.1 differs from that shown. Reason: Erroneous initiation. Curated
The sequence BAC38801.1 differs from that shown. Reason: Erroneous initiation. Curated
The sequence BAC39115.1 differs from that shown. Reason: Erroneous initiation. Curated
The sequence BAC39714.1 differs from that shown. Reason: Erroneous initiation. Curated
The sequence BAE26079.1 differs from that shown. Reason: Erroneous initiation. Curated
The sequence BAE38491.1 differs from that shown. Reason: Erroneous initiation. Curated
The sequence CAI84997.1 differs from that shown. Reason: Erroneous initiation. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti481 – 4811Y → H in BAC39714 (PubMed:16141072).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK046378 mRNA. Translation: BAC32696.1. Different initiation.
AK013194 mRNA. Translation: BAB28703.1. Sequence problems.
AK086667 mRNA. Translation: BAC39714.1. Different initiation.
AK019515 mRNA. Translation: BAB31772.1. Different initiation.
AK031147 mRNA. Translation: BAC27279.1. Different initiation.
AK032812 mRNA. Translation: BAC28035.1. Different initiation.
AK035464 mRNA. Translation: BAC29070.1. Different initiation.
AK039765 mRNA. Translation: BAC30444.1. Different initiation.
AK083188 mRNA. Translation: BAC38801.1. Different initiation.
AK084090 mRNA. Translation: BAC39115.1. Different initiation.
AK144817 mRNA. Translation: BAE26079.1. Different initiation.
AK165970 mRNA. Translation: BAE38491.1. Different initiation.
BC046790 mRNA. Translation: AAH46790.3. Different initiation.
BC058351 mRNA. Translation: AAH58351.3. Different initiation.
BN000751 mRNA. Translation: CAI84997.1. Different initiation.
RefSeqiNP_084123.2. NM_029847.4.
UniGeneiMm.196399.

Genome annotation databases

GeneIDi77041.
KEGGimmu:77041.
UCSCiuc007rgh.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK046378 mRNA. Translation: BAC32696.1. Different initiation.
AK013194 mRNA. Translation: BAB28703.1. Sequence problems.
AK086667 mRNA. Translation: BAC39714.1. Different initiation.
AK019515 mRNA. Translation: BAB31772.1. Different initiation.
AK031147 mRNA. Translation: BAC27279.1. Different initiation.
AK032812 mRNA. Translation: BAC28035.1. Different initiation.
AK035464 mRNA. Translation: BAC29070.1. Different initiation.
AK039765 mRNA. Translation: BAC30444.1. Different initiation.
AK083188 mRNA. Translation: BAC38801.1. Different initiation.
AK084090 mRNA. Translation: BAC39115.1. Different initiation.
AK144817 mRNA. Translation: BAE26079.1. Different initiation.
AK165970 mRNA. Translation: BAE38491.1. Different initiation.
BC046790 mRNA. Translation: AAH46790.3. Different initiation.
BC058351 mRNA. Translation: AAH58351.3. Different initiation.
BN000751 mRNA. Translation: CAI84997.1. Different initiation.
RefSeqiNP_084123.2. NM_029847.4.
UniGeneiMm.196399.

3D structure databases

ProteinModelPortaliQ9D2L1.
SMRiQ9D2L1. Positions 32-467.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000113274.

PTM databases

PhosphoSiteiQ9D2L1.

Proteomic databases

MaxQBiQ9D2L1.
PaxDbiQ9D2L1.
PRIDEiQ9D2L1.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi77041.
KEGGimmu:77041.
UCSCiuc007rgh.1. mouse.

Organism-specific databases

CTDi153642.
MGIiMGI:1924291. Arsk.

Phylogenomic databases

eggNOGiKOG3731. Eukaryota.
COG3119. LUCA.
HOGENOMiHOG000034080.
HOVERGENiHBG054703.
InParanoidiQ9D2L1.
KOiK12376.
OrthoDBiEOG75B853.
PhylomeDBiQ9D2L1.
TreeFamiTF313545.

Miscellaneous databases

PROiQ9D2L1.
SOURCEiSearch...

Gene expression databases

BgeeiQ9D2L1.

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. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: C57BL/6J.
    Tissue: Corpora quadrigemina, Forelimb, Head, Hippocampus, Lung, Spinal cord, Spinal ganglion and Urinary bladder.
  2. "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].
    Strain: C57BL/6J.
    Tissue: Brain.
  3. "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_MOUSE
AccessioniPrimary (citable) accession number: Q9D2L1
Secondary accession number(s): Q6PE11
, Q8BL50, Q8BUA1, Q9CYZ0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 20, 2009
Last sequence update: January 20, 2009
Last modified: June 8, 2016
This is version 104 of the entry and version 2 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. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. 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.