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Protein

Arylsulfatase G

Gene

Arsg

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at transcript leveli

Functioni

Displays arylsulfatase activity with pseudosubstrates at acidic pH, such as p-nitrocatechol sulfate.By similarity

Cofactori

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

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi44 – 441CalciumBy similarity
Metal bindingi45 – 451CalciumBy similarity
Metal bindingi84 – 841Calcium; via 3-oxoalanineBy similarity
Binding sitei137 – 1371SubstrateBy similarity
Active sitei139 – 1391By similarity
Binding sitei162 – 1621SubstrateBy similarity
Binding sitei251 – 2511SubstrateBy similarity
Metal bindingi302 – 3021CalciumBy similarity
Metal bindingi303 – 3031CalciumBy similarity

GO - Molecular functioni

GO - Biological processi

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 G (EC:3.1.6.-)
Short name:
ASG
Gene namesi
Name:Arsg
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Chromosome 10

Organism-specific databases

RGDi1306571. Arsg.

Subcellular locationi

  • Lysosome

  • Note: Previously observed endoplasmic reticulum localization is most likely due to folding/maturation problems for overexpressed proteins.By similarity

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Lysosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 1616Sequence analysisAdd
BLAST
Chaini17 – 526510Arylsulfatase GPRO_0000238664Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei84 – 8413-oxoalanine (Cys)By similarity
Glycosylationi356 – 3561N-linked (GlcNAc...)Sequence analysis

Post-translational modificationi

N-glycosylated.By similarity
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
Glycosylated.By similarity

Keywords - PTMi

Glycoprotein

Proteomic databases

PaxDbiQ32KJ9.
PRIDEiQ32KJ9.

Expressioni

Gene expression databases

GenevisibleiQ32KJ9. RN.

Interactioni

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000005257.

Structurei

3D structure databases

ProteinModelPortaliQ32KJ9.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the sulfatase family.Curated

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiKOG3867. Eukaryota.
COG3119. LUCA.
GeneTreeiENSGT00760000119062.
HOGENOMiHOG000135352.
HOVERGENiHBG004283.
InParanoidiQ32KJ9.
KOiK12381.
OMAiCCNPYQI.
OrthoDBiEOG7QZG9J.
PhylomeDBiQ32KJ9.
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.

Q32KJ9-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MGWLFLKVLL VGMVFSGLLY PFVDFSISGE TRAPRPNIVI ILADDMGWGD
60 70 80 90 100
LGANWAETKD TTNLDKMASE GMRFVDFHAA ASTCSPSRAS LLTGRLGLRN
110 120 130 140 150
GVTHNFAVTS VGGLPLNETT LAEVLQQAGY VTAMIGKWHL GHHGSYHPSF
160 170 180 190 200
RGFDYYFGIP YSNDMGCTDN PGYNYPPCPA CPQSDGRWRN PDRDCYTDVA
210 220 230 240 250
LPLYENLNIV EQPVNLSGLA QKYAERAVEF IEQASTSGRP FLLYVGLAHM
260 270 280 290 300
HVPLSVTPPL ANPQSQRLYR ASLQEMDSLV GQIKDKVDHV AKENTLLWFA
310 320 330 340 350
GDNGPWAQKC ELAGSMGPFS GLWQTHQGGS PAKQTTWEGG HRVPALAYWP
360 370 380 390 400
GRVPVNVTST ALLSLLDIFP TVIALAGASL PPNRKFDGVD VSEVLFGKSQ
410 420 430 440 450
TGHRVLFHPN SGAAGEYGAL QTVRLDRYKA FYITGGAKAC DGGVGPEQHH
460 470 480 490 500
VSPLIFNLED DAAESSPLQK GSPEYQELLP KVTRVLADVL QDIADDNSSQ
510 520
ADYTQDPSVT PCCNPYQITC RCQPGE
Length:526
Mass (Da):57,269
Last modified:December 6, 2005 - v1
Checksum:i95C5F00354AE84A4
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AABR03073953 Genomic DNA. No translation available.
AABR03074766 Genomic DNA. No translation available.
AABR03075952 Genomic DNA. No translation available.
AABR03076519 Genomic DNA. No translation available.
AABR03076696 Genomic DNA. No translation available.
BN000738 mRNA. Translation: CAI84984.1.
RefSeqiNP_001041342.1. NM_001047877.1.
XP_006247661.1. XM_006247599.2.
XP_006247662.1. XM_006247600.2.
XP_006247663.1. XM_006247601.2.
XP_006247664.1. XM_006247602.2.
XP_006247665.1. XM_006247603.2.
XP_006247666.1. XM_006247604.2.
XP_006247668.1. XM_006247606.2.
XP_006247669.1. XM_006247607.2.
XP_006247670.1. XM_006247608.2.
XP_008766590.1. XM_008768368.1.
XP_008766591.1. XM_008768369.1.
UniGeneiRn.221856.

Genome annotation databases

EnsembliENSRNOT00000005257; ENSRNOP00000005257; ENSRNOG00000003931.
GeneIDi303631.
KEGGirno:303631.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AABR03073953 Genomic DNA. No translation available.
AABR03074766 Genomic DNA. No translation available.
AABR03075952 Genomic DNA. No translation available.
AABR03076519 Genomic DNA. No translation available.
AABR03076696 Genomic DNA. No translation available.
BN000738 mRNA. Translation: CAI84984.1.
RefSeqiNP_001041342.1. NM_001047877.1.
XP_006247661.1. XM_006247599.2.
XP_006247662.1. XM_006247600.2.
XP_006247663.1. XM_006247601.2.
XP_006247664.1. XM_006247602.2.
XP_006247665.1. XM_006247603.2.
XP_006247666.1. XM_006247604.2.
XP_006247668.1. XM_006247606.2.
XP_006247669.1. XM_006247607.2.
XP_006247670.1. XM_006247608.2.
XP_008766590.1. XM_008768368.1.
XP_008766591.1. XM_008768369.1.
UniGeneiRn.221856.

3D structure databases

ProteinModelPortaliQ32KJ9.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000005257.

Proteomic databases

PaxDbiQ32KJ9.
PRIDEiQ32KJ9.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSRNOT00000005257; ENSRNOP00000005257; ENSRNOG00000003931.
GeneIDi303631.
KEGGirno:303631.

Organism-specific databases

CTDi22901.
RGDi1306571. Arsg.

Phylogenomic databases

eggNOGiKOG3867. Eukaryota.
COG3119. LUCA.
GeneTreeiENSGT00760000119062.
HOGENOMiHOG000135352.
HOVERGENiHBG004283.
InParanoidiQ32KJ9.
KOiK12381.
OMAiCCNPYQI.
OrthoDBiEOG7QZG9J.
PhylomeDBiQ32KJ9.
TreeFamiTF314186.

Enzyme and pathway databases

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

Miscellaneous databases

NextBioi651782.
PROiQ32KJ9.

Gene expression databases

GenevisibleiQ32KJ9. 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 nameiARSG_RAT
AccessioniPrimary (citable) accession number: Q32KJ9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 30, 2006
Last sequence update: December 6, 2005
Last modified: January 20, 2016
This is version 74 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.