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Protein

Arylsulfatase I

Gene

Arsi

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

Functioni

Displays arylsulfatase activity at neutral pH, when co-expressed with SUMF1; arylsulfatase activity is measured in the secretion medium of retinal cell line, but no activity is recorded when measured in cell extracts.By similarity

Cofactori

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

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi55 – 551CalciumBy similarity
Metal bindingi56 – 561CalciumBy similarity
Metal bindingi93 – 931Calcium; via 3-oxoalanineBy similarity
Binding sitei147 – 1471SubstrateBy similarity
Active sitei149 – 1491By similarity
Binding sitei239 – 2391SubstrateBy similarity
Metal bindingi297 – 2971CalciumBy similarity
Metal bindingi298 – 2981CalciumBy similarity
Binding sitei315 – 3151SubstrateBy 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 I (EC:3.1.6.-)
Short name:
ASI
Gene namesi
Name:Arsi
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Chromosome 18

Organism-specific databases

RGDi1310242. Arsi.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Endoplasmic reticulum, Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2323Sequence analysisAdd
BLAST
Chaini24 – 573550Arylsulfatase IPRO_0000356285Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei93 – 9313-oxoalanine (Cys)By similarity
Glycosylationi276 – 2761N-linked (GlcNAc...)Sequence analysis
Glycosylationi288 – 2881N-linked (GlcNAc...)Sequence analysis
Glycosylationi466 – 4661N-linked (GlcNAc...)Sequence analysis
Glycosylationi496 – 4961N-linked (GlcNAc...)Sequence analysis

Post-translational modificationi

The oxidation of Cys-93 residue to 3-oxoalanine (also known as C(alpha)-formylglycine) by SUMF1/Sulfatase-modifying factor 1, seems critical for catalytic activity.By similarity

Keywords - PTMi

Glycoprotein

Proteomic databases

PaxDbiQ32KJ8.

PTM databases

iPTMnetiQ32KJ8.
PhosphoSiteiQ32KJ8.

Expressioni

Gene expression databases

GenevisibleiQ32KJ8. RN.

Interactioni

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000033542.

Structurei

3D structure databases

ProteinModelPortaliQ32KJ8.
SMRiQ32KJ8. Positions 45-524.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi527 – 53711Poly-GluAdd
BLAST

Sequence similaritiesi

Belongs to the sulfatase family.Curated

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiKOG3867. Eukaryota.
COG3119. LUCA.
GeneTreeiENSGT00760000119062.
HOGENOMiHOG000135354.
HOVERGENiHBG004282.
InParanoidiQ32KJ8.
KOiK12375.
OMAiPLYNHAK.
OrthoDBiEOG7MKW5Q.
PhylomeDBiQ32KJ8.
TreeFamiTF314186.

Family and domain databases

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

Sequencei

Sequence statusi: Complete.

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

Q32KJ8-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MHALSGFSLV SLLSLGYLSW DWAKPGLVAD GPAEAEDQPS AAPPQPPHII
60 70 80 90 100
FILTDDQGYH DVGYHGSDIE TPTLDRLAAE GVKLENYYIQ PICTPSRSQL
110 120 130 140 150
LTGRYQIHTG LQHSIIRPRQ PNCLPLDQVT LPQKLQEAGY STHMVGKWHL
160 170 180 190 200
GFYRKECLPT RRGFDTFLGS LTGNVDYYTY DNCDGPGVCG FDLHEGESVA
210 220 230 240 250
WGLSGQYSTM LYAQRASHIL ASHSPQKPLF LYVAFQAVHT PLQSPREYLY
260 270 280 290 300
RYRTMGNVAR RKYAAMVTCM DEAVRNITWA LKRYGFYNNS VIIFSSDNGG
310 320 330 340 350
QTFSGGSNWP LRGRKGTYWE GGVRGLGFVH SPLLKKKRRT SRALVHITDW
360 370 380 390 400
YPTLVGLAGG TTSAADGLDG YDVWPAISEG RASPRTEILH NIDPLYNHAR
410 420 430 440 450
HGSLEGGFGI WNTAVQAAIR VGEWKLLTGD PGYGDWIPPQ TLASFPGSWW
460 470 480 490 500
NLERMASIRQ AVWLFNISAD PYEREDLADQ RPDVVRTLLA RLADYNRTAI
510 520 530 540 550
PVRYPAANPR AHPDFNGGAW GPWASDEDEE EEDEEEEGRA RSFPRGRRKK
560 570
KCKICKLRSF FRKLNTRLMS HRI
Length:573
Mass (Da):64,424
Last modified:December 6, 2005 - v1
Checksum:iEEC97A0D8A57D367
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AABR03109797 Genomic DNA. No translation available.
BN000739 mRNA. Translation: CAI84985.1.
RefSeqiNP_001041346.1. NM_001047881.1.
UniGeneiRn.202490.

Genome annotation databases

EnsembliENSRNOT00000030966; ENSRNOP00000033542; ENSRNOG00000026060.
GeneIDi307404.
KEGGirno:307404.
UCSCiRGD:1310242. rat.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AABR03109797 Genomic DNA. No translation available.
BN000739 mRNA. Translation: CAI84985.1.
RefSeqiNP_001041346.1. NM_001047881.1.
UniGeneiRn.202490.

3D structure databases

ProteinModelPortaliQ32KJ8.
SMRiQ32KJ8. Positions 45-524.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000033542.

PTM databases

iPTMnetiQ32KJ8.
PhosphoSiteiQ32KJ8.

Proteomic databases

PaxDbiQ32KJ8.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSRNOT00000030966; ENSRNOP00000033542; ENSRNOG00000026060.
GeneIDi307404.
KEGGirno:307404.
UCSCiRGD:1310242. rat.

Organism-specific databases

CTDi340075.
RGDi1310242. Arsi.

Phylogenomic databases

eggNOGiKOG3867. Eukaryota.
COG3119. LUCA.
GeneTreeiENSGT00760000119062.
HOGENOMiHOG000135354.
HOVERGENiHBG004282.
InParanoidiQ32KJ8.
KOiK12375.
OMAiPLYNHAK.
OrthoDBiEOG7MKW5Q.
PhylomeDBiQ32KJ8.
TreeFamiTF314186.

Enzyme and pathway databases

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

Miscellaneous databases

PROiQ32KJ8.

Gene expression databases

GenevisibleiQ32KJ8. RN.

Family and domain databases

Gene3Di3.40.720.10. 1 hit.
InterProiIPR017849. Alkaline_Pase-like_a/b/a.
IPR017850. Alkaline_phosphatase_core.
IPR024607. Sulfatase_CS.
IPR000917. Sulfatase_N.
[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. "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 nameiARSI_RAT
AccessioniPrimary (citable) accession number: Q32KJ8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 16, 2008
Last sequence update: December 6, 2005
Last modified: June 8, 2016
This is version 71 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.