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Q571E4

- GALNS_MOUSE

UniProt

Q571E4 - GALNS_MOUSE

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Protein

N-acetylgalactosamine-6-sulfatase

Gene

Galns

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at transcript 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

Binds 1 calcium ion per subunit.By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi36 – 361CalciumBy similarity
Metal bindingi37 – 371CalciumBy similarity
Metal bindingi76 – 761Calcium; via 3-oxoalanineBy similarity
Metal bindingi286 – 2861CalciumBy similarity
Metal bindingi287 – 2871CalciumBy similarity

GO - Molecular functioni

  1. metal ion binding Source: UniProtKB-KW
  2. N-acetylgalactosamine-6-sulfatase activity Source: UniProtKB-EC
  3. sulfuric ester hydrolase activity Source: MGI
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Keywords - Ligandi

Calcium, Metal-binding

Enzyme and pathway databases

BRENDAi3.1.6.4. 3474.
ReactomeiREACT_198960. 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
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 8

Organism-specific databases

MGIiMGI:1355303. Galns.

Subcellular locationi

Lysosome By similarity

GO - Cellular componenti

  1. extracellular vesicular exosome Source: Ensembl
  2. lysosome Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Lysosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2323By similarityAdd
BLAST
Chaini24 – 520497N-acetylgalactosamine-6-sulfatasePRO_0000273148Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei76 – 7613-oxoalanine (Cys)By similarity
Glycosylationi201 – 2011N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi306 ↔ 417By similarity
Glycosylationi421 – 4211N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi487 ↔ 516By similarity
Disulfide bondi499 ↔ 505By 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

MaxQBiQ571E4.
PaxDbiQ571E4.
PRIDEiQ571E4.

PTM databases

PhosphoSiteiQ571E4.

Expressioni

Tissue specificityi

Widely expressed. Higher expression in liver and kidney.1 Publication

Gene expression databases

BgeeiQ571E4.
CleanExiMM_GALNS.
GenevestigatoriQ571E4.

Interactioni

Subunit structurei

Homodimer.By similarity

Structurei

3D structure databases

ProteinModelPortaliQ571E4.
SMRiQ571E4. Positions 25-518.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni24 – 377354Catalytic domainBy similarityAdd
BLAST

Sequence similaritiesi

Belongs to the sulfatase family.Curated

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiCOG3119.
GeneTreeiENSGT00760000119062.
HOGENOMiHOG000135352.
HOVERGENiHBG004283.
InParanoidiQ571E4.
KOiK01132.
OMAiLTQVYLQ.
OrthoDBiEOG7QZG9J.
PhylomeDBiQ571E4.
TreeFamiTF314186.

Family and domain databases

Gene3Di3.40.720.10. 1 hit.
InterProiIPR017849. Alkaline_Pase-like_a/b/a.
IPR017850. Alkaline_phosphatase_core.
IPR000917. Sulfatase.
IPR024607. Sulfatase_CS.
[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.

Q571E4-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MAACTAAQQL LLVLSALGLL AAGAPQPPNI VLLLMDDMGW GDLGVNGEPS
60 70 80 90 100
RETPNLDRMA AEGMLFPSFY SANPLCSPSR AALLTGRLPI RNGFYTTNAH
110 120 130 140 150
ARNAYTPQEI MGGIPNSEHL LPELLKKAGY TNKIVGKWHL GHRPQFHPLK
160 170 180 190 200
HGFDEWFGSP NCHFGPYDNK AKPNIPVYRD WEMVGRFYEE FPINRKTGEA
210 220 230 240 250
NLTQLYTQEA LDFIQTQHAR QSPFFLYWAI DATHAPVYAS RQFLGTSLRG
260 270 280 290 300
RYGDAVREID DSVGKILSLL QNLGISKNTF VFFTSDNGAA LISAPNEGGS
310 320 330 340 350
NGPFLCGKQT TFEGGMREPA IAWWPGHIAA GQVSHQLGSI MDLFTTSLSL
360 370 380 390 400
AGLKPPSDRV IDGLDLLPTM LKGQMMDRPI FYYRGNTLMA VTLGQYKAHL
410 420 430 440 450
WTWTNSWEEF TQGTDFCPGQ NVSGVTTHTQ EEHTELPLIF HLGRDPGERF
460 470 480 490 500
PLSFHSDEYQ DALSRTTQVV QEHQKSLVPG QPQLNVCNQA VMNWAPPGCE
510 520
KLGKCLTPPE SVPEKCFWAH
Length:520
Mass (Da):57,673
Last modified:January 23, 2007 - v2
Checksum:i63428DFA8843A21D
GO

Sequence cautioni

The sequence BAD90170.1 differs from that shown. Reason: Erroneous initiation.

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti22 – 221A → V in AAH04002. (PubMed:15489334)Curated
Sequence conflicti154 – 1541D → N in AAF63858. (PubMed:10699374)Curated
Sequence conflicti154 – 1541D → N in AAF63155. (PubMed:10699374)Curated
Sequence conflicti207 – 2071T → L in AAH04002. (PubMed:15489334)Curated
Sequence conflicti215 – 2151Q → R in AAH04002. (PubMed:15489334)Curated
Sequence conflicti222 – 2221S → G in AAH04002. (PubMed:15489334)Curated
Sequence conflicti268 – 2681S → N in AAH04002. (PubMed:15489334)Curated

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF111346 mRNA. Translation: AAF63155.1.
AF112242
, AF112230, AF112231, AF112233, AF112232, AF112234, AF112235, AF112236, AF112237, AF112238, AF112239, AF112240, AF112241 Genomic DNA. Translation: AAF63858.1.
AK220245 mRNA. Translation: BAD90170.1. Different initiation.
AK159592 mRNA. Translation: BAE35212.1.
BC004002 mRNA. Translation: AAH04002.1.
CCDSiCCDS40504.1.
RefSeqiNP_001180574.1. NM_001193645.1.
NP_057931.3. NM_016722.4.
UniGeneiMm.34702.

Genome annotation databases

EnsembliENSMUST00000015171; ENSMUSP00000015171; ENSMUSG00000015027.
GeneIDi50917.
KEGGimmu:50917.
UCSCiuc012gmh.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF111346 mRNA. Translation: AAF63155.1 .
AF112242
, AF112230 , AF112231 , AF112233 , AF112232 , AF112234 , AF112235 , AF112236 , AF112237 , AF112238 , AF112239 , AF112240 , AF112241 Genomic DNA. Translation: AAF63858.1 .
AK220245 mRNA. Translation: BAD90170.1 . Different initiation.
AK159592 mRNA. Translation: BAE35212.1 .
BC004002 mRNA. Translation: AAH04002.1 .
CCDSi CCDS40504.1.
RefSeqi NP_001180574.1. NM_001193645.1.
NP_057931.3. NM_016722.4.
UniGenei Mm.34702.

3D structure databases

ProteinModelPortali Q571E4.
SMRi Q571E4. Positions 25-518.
ModBasei Search...
MobiDBi Search...

PTM databases

PhosphoSitei Q571E4.

Proteomic databases

MaxQBi Q571E4.
PaxDbi Q571E4.
PRIDEi Q571E4.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000015171 ; ENSMUSP00000015171 ; ENSMUSG00000015027 .
GeneIDi 50917.
KEGGi mmu:50917.
UCSCi uc012gmh.1. mouse.

Organism-specific databases

CTDi 2588.
MGIi MGI:1355303. Galns.

Phylogenomic databases

eggNOGi COG3119.
GeneTreei ENSGT00760000119062.
HOGENOMi HOG000135352.
HOVERGENi HBG004283.
InParanoidi Q571E4.
KOi K01132.
OMAi LTQVYLQ.
OrthoDBi EOG7QZG9J.
PhylomeDBi Q571E4.
TreeFami TF314186.

Enzyme and pathway databases

BRENDAi 3.1.6.4. 3474.
Reactomei REACT_198960. Keratan sulfate degradation.

Miscellaneous databases

NextBioi 307919.
PROi Q571E4.
SOURCEi Search...

Gene expression databases

Bgeei Q571E4.
CleanExi MM_GALNS.
Genevestigatori Q571E4.

Family and domain databases

Gene3Di 3.40.720.10. 1 hit.
InterProi IPR017849. Alkaline_Pase-like_a/b/a.
IPR017850. Alkaline_phosphatase_core.
IPR000917. Sulfatase.
IPR024607. Sulfatase_CS.
[Graphical view ]
Pfami PF00884. Sulfatase. 1 hit.
[Graphical view ]
SUPFAMi SSF53649. SSF53649. 1 hit.
PROSITEi PS00523. SULFATASE_1. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "The mouse N-acetylgalactosamine-6-sulfate sulfatase (Galns) gene: cDNA isolation, genomic characterization, chromosomal assignment and analysis of the 5'-flanking region."
    Montano A.M., Yamagishi A., Tomatsu S., Fukuda S., Copeland N.G., Orii K.E., Isogai K., Yamada N., Kato Z.I., Jenkins N.A., Gilbert D.J., Sukegawa K., Orii T., Kondo N.
    Biochim. Biophys. Acta 1500:323-334(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], TISSUE SPECIFICITY.
    Strain: 129/SvJ and C57BL/6.
  2. "Prediction of the coding sequences of mouse homologues of KIAA gene. The complete nucleotide sequences of mouse KIAA-homologous cDNAs identified by screening of terminal sequences of cDNA clones randomly sampled from size-fractionated libraries."
    Okazaki N., Kikuno R.F., Ohara R., Inamoto S., Seino S., Nishimura M., Nagase T., Ohara O., Koga H.
    Submitted (FEB-2005) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Pancreatic islet.
  3. "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.
  4. "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: Czech II.
    Tissue: Mammary tumor.

Entry informationi

Entry nameiGALNS_MOUSE
AccessioniPrimary (citable) accession number: Q571E4
Secondary accession number(s): Q3TWQ4, Q99KU8, Q9JHK9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 23, 2007
Last sequence update: January 23, 2007
Last modified: October 29, 2014
This is version 73 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

External Data

Dasty 3