Skip Header

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

P50428

- ARSA_MOUSE

UniProt

P50428 - ARSA_MOUSE

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein

Arylsulfatase A

Gene

Arsa

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

Functioni

Hydrolyzes cerebroside sulfate.

Catalytic activityi

A cerebroside 3-sulfate + H2O = a cerebroside + sulfate.

Cofactori

Ca2+By similarityNote: Binds 1 Ca(2+) ion per subunit.By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi28 – 281CalciumBy similarity
Metal bindingi29 – 291CalciumBy similarity
Metal bindingi68 – 681Calcium; via 3-oxoalanineBy similarity
Binding sitei122 – 1221SubstrateBy similarity
Active sitei124 – 1241By similarity
Binding sitei149 – 1491SubstrateBy similarity
Binding sitei228 – 2281SubstrateBy similarity
Metal bindingi280 – 2801CalciumBy similarity
Metal bindingi281 – 2811CalciumBy similarity
Binding sitei301 – 3011SubstrateBy similarity

GO - Molecular functioni

  1. arylsulfatase activity Source: Ensembl
  2. calcium ion binding Source: UniProtKB
  3. cerebroside-sulfatase activity Source: UniProtKB-EC
  4. sulfuric ester hydrolase activity Source: MGI

GO - Biological processi

  1. autophagy Source: Ensembl
  2. binding of sperm to zona pellucida Source: MGI
  3. central nervous system development Source: Ensembl
  4. response to estrogen Source: Ensembl
  5. response to ethanol Source: Ensembl
  6. response to methylmercury Source: Ensembl
  7. response to nutrient Source: Ensembl
  8. response to pH Source: Ensembl
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Keywords - Ligandi

Calcium, Metal-binding

Enzyme and pathway databases

ReactomeiREACT_198990. The activation of arylsulfatases.
REACT_199008. Glycosphingolipid metabolism.
SABIO-RKP50428.

Names & Taxonomyi

Protein namesi
Recommended name:
Arylsulfatase A (EC:3.1.6.8)
Short name:
ASA
Alternative name(s):
Cerebroside-sulfatase
Gene namesi
Name:Arsa
Synonyms:As2
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 15

Organism-specific databases

MGIiMGI:88077. Arsa.

Subcellular locationi

GO - Cellular componenti

  1. acrosomal vesicle Source: Ensembl
  2. endosome Source: Ensembl
  3. extracellular space Source: Ensembl
  4. extracellular vesicular exosome Source: Ensembl
  5. extrinsic component of external side of plasma membrane Source: Ensembl
  6. integral component of membrane Source: MGI
  7. lysosome Source: UniProtKB-KW
  8. plasma membrane Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Lysosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 1717Sequence AnalysisAdd
BLAST
Chaini18 – 506489Arylsulfatase APRO_0000033420Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei68 – 6813-oxoalanine (Cys)By similarity
Disulfide bondi155 ↔ 171By similarity
Glycosylationi157 – 1571N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi160 ↔ 167By similarity
Glycosylationi183 – 1831N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi299 ↔ 413By similarity
Glycosylationi349 – 3491N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi487 ↔ 499By similarity
Disulfide bondi488 ↔ 501By similarity
Disulfide bondi492 ↔ 498By 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

MaxQBiP50428.
PaxDbiP50428.
PRIDEiP50428.

Expressioni

Gene expression databases

BgeeiP50428.
CleanExiMM_ARSA.
GenevestigatoriP50428.

Interactioni

Subunit structurei

Homodimer at neutral pH and homooctamer at acidic pH. Exists both as a single chain of 58 kDa (component A) or as a chain of 50 kDa (component B) linked by disulfide bond(s) to a 7 kDa chain (component C). Interacts with SUMF1 (By similarity).By similarity

Protein-protein interaction databases

IntActiP50428. 2 interactions.
MINTiMINT-4128568.
STRINGi10090.ENSMUSP00000023292.

Structurei

3D structure databases

ProteinModelPortaliP50428.
SMRiP50428. Positions 19-502.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the sulfatase family.Curated

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiCOG3119.
GeneTreeiENSGT00760000119062.
HOGENOMiHOG000135352.
HOVERGENiHBG004283.
InParanoidiP50428.
KOiK01134.
OMAiETMRMSH.
OrthoDBiEOG7QZG9J.
PhylomeDBiP50428.
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.
PS00149. SULFATASE_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

P50428-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MALGTLFLAL AAGLSTASPP NILLIFADDL GYGDLGSYGH PSSTTPNLDQ
60 70 80 90 100
LAEGGLRFTD FYVPVSLCTP SRAALLTGRL PVRSGMYPGV LGPSSQGGLP
110 120 130 140 150
LEEVTLAEVL AARGYLTGMA GKWHLGVGPE GAFLPPHQGF HRFLGIPYSH
160 170 180 190 200
DQGPCQNLTC FPPDIPCKGG CDQGLVPIPL LANLTVEAQP PWLPGLEARY
210 220 230 240 250
VSFSRDLMAD AQRQGRPFFL YYASHHTHYP QFSGQSFTKR SGRGPFGDSL
260 270 280 290 300
MELDGAVGAL MTTVGDLGLL EETLVIFTAD NGPELMRMSN GGCSGLLRCG
310 320 330 340 350
KGTTFEGGVR EPALVYWPGH ITPGVTHELA SSLDLLPTLA ALTGAPLPNV
360 370 380 390 400
TLDGVDISPL LLGTGKSPRK SVFFYPPYPD EIHGVFAVRN GKYKAHFFTQ
410 420 430 440 450
GSAHSDTTSD PACHAANRLT AHEPPLLYDL SQDPGENYNV LESIEGVSPE
460 470 480 490 500
ALQALKHIQL LKAQYDAAMT FGPSQIAKGE DPALQICCQP SCTPHPVCCH

CPGSQS
Length:506
Mass (Da):53,748
Last modified:July 27, 2011 - v2
Checksum:iA12DFA369D65B1AD
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti85 – 851G → A in CAA51702. (PubMed:7910580)Curated
Sequence conflicti85 – 851G → A in CAA51703. (PubMed:7910580)Curated
Sequence conflicti104 – 1041V → L in CAA51702. (PubMed:7910580)Curated
Sequence conflicti104 – 1041V → L in CAA51703. (PubMed:7910580)Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X73230 mRNA. Translation: CAA51702.1.
X73231 Genomic DNA. Translation: CAA51703.1.
AK004540 mRNA. Translation: BAB23356.1.
AK132501 mRNA. Translation: BAE21207.1.
CH466550 Genomic DNA. Translation: EDL04336.1.
BC011284 mRNA. Translation: AAH11284.1.
BC098075 mRNA. Translation: AAH98075.1.
M82876 mRNA. Translation: AAA37260.1.
CCDSiCCDS27753.1.
PIRiA54190.
RefSeqiNP_033843.2. NM_009713.4.
UniGeneiMm.620.

Genome annotation databases

EnsembliENSMUST00000165199; ENSMUSP00000127646; ENSMUSG00000022620.
GeneIDi11883.
KEGGimmu:11883.
UCSCiuc007xgy.2. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X73230 mRNA. Translation: CAA51702.1 .
X73231 Genomic DNA. Translation: CAA51703.1 .
AK004540 mRNA. Translation: BAB23356.1 .
AK132501 mRNA. Translation: BAE21207.1 .
CH466550 Genomic DNA. Translation: EDL04336.1 .
BC011284 mRNA. Translation: AAH11284.1 .
BC098075 mRNA. Translation: AAH98075.1 .
M82876 mRNA. Translation: AAA37260.1 .
CCDSi CCDS27753.1.
PIRi A54190.
RefSeqi NP_033843.2. NM_009713.4.
UniGenei Mm.620.

3D structure databases

ProteinModelPortali P50428.
SMRi P50428. Positions 19-502.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

IntActi P50428. 2 interactions.
MINTi MINT-4128568.
STRINGi 10090.ENSMUSP00000023292.

Proteomic databases

MaxQBi P50428.
PaxDbi P50428.
PRIDEi P50428.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000165199 ; ENSMUSP00000127646 ; ENSMUSG00000022620 .
GeneIDi 11883.
KEGGi mmu:11883.
UCSCi uc007xgy.2. mouse.

Organism-specific databases

CTDi 410.
MGIi MGI:88077. Arsa.

Phylogenomic databases

eggNOGi COG3119.
GeneTreei ENSGT00760000119062.
HOGENOMi HOG000135352.
HOVERGENi HBG004283.
InParanoidi P50428.
KOi K01134.
OMAi ETMRMSH.
OrthoDBi EOG7QZG9J.
PhylomeDBi P50428.
TreeFami TF314186.

Enzyme and pathway databases

Reactomei REACT_198990. The activation of arylsulfatases.
REACT_199008. Glycosphingolipid metabolism.
SABIO-RK P50428.

Miscellaneous databases

NextBioi 279915.
PROi P50428.
SOURCEi Search...

Gene expression databases

Bgeei P50428.
CleanExi MM_ARSA.
Genevestigatori P50428.

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.
PS00149. SULFATASE_2. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
    Strain: 129/Sv and C57BL/6J.
  2. "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: Lung and Skin.
  3. Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.
    Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  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].
    Tissue: Mammary tumor and Trophoblast stem cell.
  5. "The sulfatase gene family: cross-species PCR cloning using the MOPAC technique."
    Grompe M., Pieretti M., Caskey C.T., Ballabio A.
    Genomics 12:755-760(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 32-66.

Entry informationi

Entry nameiARSA_MOUSE
AccessioniPrimary (citable) accession number: P50428
Secondary accession number(s): Q9DC66
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: July 27, 2011
Last modified: November 26, 2014
This is version 112 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