Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

N-acetylgalactosamine-6-sulfatase

Gene

Galns

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

Functioni

Catalytic activityi

Hydrolysis of the 6-sulfate groups of the N-acetyl-D-galactosamine 6-sulfate units of chondroitin sulfate and of the D-galactose 6-sulfate units of keratan sulfate.

Cofactori

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

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi40 – 401CalciumBy similarity
Metal bindingi41 – 411CalciumBy similarity
Metal bindingi80 – 801Calcium; via 3-oxoalanineBy similarity
Metal bindingi290 – 2901CalciumBy similarity
Metal bindingi291 – 2911CalciumBy similarity

GO - Molecular functioni

Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Keywords - Ligandi

Calcium, Metal-binding

Enzyme and pathway databases

ReactomeiR-RNO-2022857. Keratan sulfate degradation.

Names & Taxonomyi

Protein namesi
Recommended name:
N-acetylgalactosamine-6-sulfatase (EC:3.1.6.4)
Alternative name(s):
Chondroitinsulfatase
Short name:
Chondroitinase
Galactose-6-sulfate sulfatase
N-acetylgalactosamine-6-sulfate sulfatase
Short name:
GalNAc6S sulfatase
Gene namesi
Name:Galns
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Chromosome 19

Organism-specific databases

RGDi1565391. Galns.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Lysosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2727By similarityAdd
BLAST
Chaini28 – 524497N-acetylgalactosamine-6-sulfatasePRO_0000273150Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei80 – 8013-oxoalanine (Cys)By similarity
Glycosylationi205 – 2051N-linked (GlcNAc...)Sequence analysis
Disulfide bondi310 ↔ 421By similarity
Glycosylationi425 – 4251N-linked (GlcNAc...)Sequence analysis
Disulfide bondi491 ↔ 520By similarity
Disulfide bondi503 ↔ 509By similarity

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

Disulfide bond, Glycoprotein

Proteomic databases

PaxDbiQ32KJ6.
PRIDEiQ32KJ6.

Expressioni

Gene expression databases

ExpressionAtlasiQ32KJ6. baseline and differential.

Interactioni

Subunit structurei

Homodimer.By similarity

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000019528.

Structurei

3D structure databases

ProteinModelPortaliQ32KJ6.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni28 – 381354Catalytic domainBy similarityAdd
BLAST

Sequence similaritiesi

Belongs to the sulfatase family.Curated

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiKOG3867. Eukaryota.
COG3119. LUCA.
GeneTreeiENSGT00760000119062.
HOGENOMiHOG000135352.
HOVERGENiHBG004283.
InParanoidiQ32KJ6.
KOiK01132.
OMAiWRVEHAF.
OrthoDBiEOG7QZG9J.
PhylomeDBiQ32KJ6.
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.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

Q32KJ6-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MTACSTAIRA QQLLLPVLSA LGLLAAGAPQ PPNIVLLLMD DMGWGDLGVY
60 70 80 90 100
GEPSRETPNL DRMAAEGMLF PSFYSANPLC SPSRAALLTG RLPIRNGFYT
110 120 130 140 150
TNAHARNAYT PQEIMGGIPN SEHLLPELLK KAGYTNKIVG KWHLGHRPQF
160 170 180 190 200
HPLKHGFDEW FGSPNCHFGP YDNKVKPNIP VYRDWEMVGR FYEEFPINLK
210 220 230 240 250
TGEANLTQLY LQEALDFIRT QHARQSPFFL YWAIDATHAP VYASKQFLGT
260 270 280 290 300
SLRGRYGDAV REIDDSVGKI LSLLQNLGIS KNTFVFFTSD NGAALISAPK
310 320 330 340 350
EGGSNGPFLC GKQTTFEGGM REPAIAWWPG HIAAGQVSHQ LGSIMDLFTT
360 370 380 390 400
SLSLAGLKPP SDRVIDGLDL LPTMLQGHII DRPIFYYRGN TLMAVTLGQY
410 420 430 440 450
KAHLWTWTNS WEEFRQGIDF CPGQNVSGVT THTQEEHTEL PLIFHLGRDP
460 470 480 490 500
GERFPLRFTS NEYQDALSRT TQVIQQHQKS LVPGQPQLNV CNQAVMNWAP
510 520
PGCEKLGKCL TPPESVPEKC FWAH
Length:524
Mass (Da):58,302
Last modified:December 6, 2005 - v1
Checksum:iA089BA7083017AF5
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AC134009 Genomic DNA. No translation available.
BN000741 mRNA. Translation: CAI84987.1.
RefSeqiNP_001041316.1. NM_001047851.1.
UniGeneiRn.101398.

Genome annotation databases

EnsembliENSRNOT00000019528; ENSRNOP00000019528; ENSRNOG00000014461.
GeneIDi292073.
KEGGirno:292073.
UCSCiRGD:1565391. rat.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AC134009 Genomic DNA. No translation available.
BN000741 mRNA. Translation: CAI84987.1.
RefSeqiNP_001041316.1. NM_001047851.1.
UniGeneiRn.101398.

3D structure databases

ProteinModelPortaliQ32KJ6.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000019528.

Proteomic databases

PaxDbiQ32KJ6.
PRIDEiQ32KJ6.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSRNOT00000019528; ENSRNOP00000019528; ENSRNOG00000014461.
GeneIDi292073.
KEGGirno:292073.
UCSCiRGD:1565391. rat.

Organism-specific databases

CTDi2588.
RGDi1565391. Galns.

Phylogenomic databases

eggNOGiKOG3867. Eukaryota.
COG3119. LUCA.
GeneTreeiENSGT00760000119062.
HOGENOMiHOG000135352.
HOVERGENiHBG004283.
InParanoidiQ32KJ6.
KOiK01132.
OMAiWRVEHAF.
OrthoDBiEOG7QZG9J.
PhylomeDBiQ32KJ6.
TreeFamiTF314186.

Enzyme and pathway databases

ReactomeiR-RNO-2022857. Keratan sulfate degradation.

Miscellaneous databases

PROiQ32KJ6.

Gene expression databases

ExpressionAtlasiQ32KJ6. baseline and differential.

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.
[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. Lubec G., Kang S.U., Lubec S.
    Submitted (SEP-2007) to UniProtKB
    Cited for: PROTEIN SEQUENCE OF 85-91, IDENTIFICATION BY MASS SPECTROMETRY.
    Strain: Sprague-Dawley.
    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 nameiGALNS_RAT
AccessioniPrimary (citable) accession number: Q32KJ6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 23, 2007
Last sequence update: December 6, 2005
Last modified: June 8, 2016
This is version 75 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, Direct protein sequencing, 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.