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Q5FYB1 (ARSI_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 87. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Arylsulfatase I

Short name=ASI
EC=3.1.6.-
Gene names
Name:ARSI
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length569 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.2 Ref.3

Cofactor

Binds 1 calcium ion per subunit By similarity.

Subcellular location

Secreted. Endoplasmic reticulum. Note: Localized in the intracellular granular structures. Ref.3

Tissue specificity

Expressed in placenta, in embryonic stem cells, fetal eyes and lens. Ref.2 Ref.3

Post-translational modification

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.

Sequence similarities

Belongs to the sulfatase family.

Caution

According to Ref.2, has no arylsulfatase activity.

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q5FYB1-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform 2 (identifier: Q5FYB1-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1-143: Missing.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2323 Potential
Chain24 – 569546Arylsulfatase I
PRO_0000042216

Regions

Compositional bias527 – 5337Poly-Glu

Sites

Active site1491 By similarity
Metal binding551Calcium By similarity
Metal binding561Calcium By similarity
Metal binding931Calcium; via 3-oxoalanine By similarity
Metal binding2971Calcium By similarity
Metal binding2981Calcium By similarity
Binding site1471Substrate By similarity
Binding site2391Substrate By similarity
Binding site3151Substrate By similarity

Amino acid modifications

Modified residue9313-oxoalanine (Cys)
Glycosylation2761N-linked (GlcNAc...) Potential
Glycosylation2881N-linked (GlcNAc...) Potential
Glycosylation4661N-linked (GlcNAc...) Potential
Glycosylation4961N-linked (GlcNAc...) Potential

Natural variations

Alternative sequence1 – 143143Missing in isoform 2.
VSP_036022

Experimental info

Mutagenesis931C → S: No arylsulfatase activity in the media of retinal epithelium cell. Ref.3
Sequence conflict1711L → F in BAG53634. Ref.4
Sequence conflict2111L → P in BAG53634. Ref.4

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified March 1, 2005. Version 1.
Checksum: D2F33EDD33ED211C

FASTA56964,030
        10         20         30         40         50         60 
MHTLTGFSLV SLLSFGYLSW DWAKPSFVAD GPGEAGEQPS AAPPQPPHII FILTDDQGYH 

        70         80         90        100        110        120 
DVGYHGSDIE TPTLDRLAAK GVKLENYYIQ PICTPSRSQL LTGRYQIHTG LQHSIIRPQQ 

       130        140        150        160        170        180 
PNCLPLDQVT LPQKLQEAGY STHMVGKWHL GFYRKECLPT RRGFDTFLGS LTGNVDYYTY 

       190        200        210        220        230        240 
DNCDGPGVCG FDLHEGENVA WGLSGQYSTM LYAQRASHIL ASHSPQRPLF LYVAFQAVHT 

       250        260        270        280        290        300 
PLQSPREYLY RYRTMGNVAR RKYAAMVTCM DEAVRNITWA LKRYGFYNNS VIIFSSDNGG 

       310        320        330        340        350        360 
QTFSGGSNWP LRGRKGTYWE GGVRGLGFVH SPLLKRKQRT SRALMHITDW YPTLVGLAGG 

       370        380        390        400        410        420 
TTSAADGLDG YDVWPAISEG RASPRTEILH NIDPLYNHAQ HGSLEGGFGI WNTAVQAAIR 

       430        440        450        460        470        480 
VGEWKLLTGD PGYGDWIPPQ TLATFPGSWW NLERMASVRQ AVWLFNISAD PYEREDLAGQ 

       490        500        510        520        530        540 
RPDVVRTLLA RLAEYNRTAI PVRYPAENPR AHPDFNGGAW GPWASDEEEE EEEGRARSFS 

       550        560 
RGRRKKKCKI CKLRSFFRKL NTRLMSQRI 

« Hide

Isoform 2 [UniParc].

Checksum: 2A12FCB6D9DCFA32
Show »

FASTA42648,253

References

« Hide 'large scale' references
[1]"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: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
[2]"Molecular cloning and initial characterization of three novel human sulfatases."
Obaya A.J.
Gene 372:110-117(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY, FUNCTION.
[3]"Characterization of the arylsulfatase I (ARSI) gene preferentially expressed in the human retinal pigment epithelium cell line ARPE-19."
Oshikawa M., Usami R., Kato S.
Mol. Vis. 15:482-494(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, SUBCELLULAR LOCATION, MUTAGENESIS OF CYS-93, OXIDATION AT CYS-93, TISSUE SPECIFICITY.
[4]"Complete sequencing and characterization of 21,243 full-length human cDNAs."
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. expand/collapse author list , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
Tissue: Lung.
[5]"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] (ISOFORM 1).

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AY875937 mRNA. Translation: AAW66665.1.
AB448735 mRNA. Translation: BAH11166.1.
AK122641 mRNA. Translation: BAG53634.1.
BC129995 mRNA. Translation: AAI29996.1.
BC129996 mRNA. Translation: AAI29997.1.
CCDSCCDS34275.1. [Q5FYB1-1]
RefSeqNP_001012301.1. NM_001012301.2. [Q5FYB1-1]
UniGeneHs.591252.

3D structure databases

ProteinModelPortalQ5FYB1.
SMRQ5FYB1. Positions 45-523.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING9606.ENSP00000333395.

PTM databases

PhosphoSiteQ5FYB1.

Polymorphism databases

DMDM74722581.

Proteomic databases

PaxDbQ5FYB1.
PRIDEQ5FYB1.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000328668; ENSP00000333395; ENSG00000183876. [Q5FYB1-1]
ENST00000515301; ENSP00000426879; ENSG00000183876. [Q5FYB1-2]
GeneID340075.
KEGGhsa:340075.
UCSCuc003lrv.2. human. [Q5FYB1-1]

Organism-specific databases

CTD340075.
GeneCardsGC05M149657.
HGNCHGNC:32521. ARSI.
HPAHPA038386.
MIM610009. gene.
neXtProtNX_Q5FYB1.
PharmGKBPA143485309.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG3119.
HOGENOMHOG000135354.
HOVERGENHBG004282.
InParanoidQ5FYB1.
KOK12375.
OMAQRASHIL.
OrthoDBEOG7MKW5Q.
PhylomeDBQ5FYB1.
TreeFamTF314186.

Enzyme and pathway databases

ReactomeREACT_111217. Metabolism.
REACT_17015. Metabolism of proteins.

Gene expression databases

ArrayExpressQ5FYB1.
BgeeQ5FYB1.
CleanExHS_ARSI.
GenevestigatorQ5FYB1.

Family and domain databases

Gene3D3.40.720.10. 1 hit.
InterProIPR017849. Alkaline_Pase-like_a/b/a.
IPR017850. Alkaline_phosphatase_core.
IPR000917. Sulfatase.
IPR024607. Sulfatase_CS.
[Graphical view]
PfamPF00884. Sulfatase. 1 hit.
[Graphical view]
SUPFAMSSF53649. SSF53649. 1 hit.
PROSITEPS00523. SULFATASE_1. 1 hit.
PS00149. SULFATASE_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

GenomeRNAi340075.
NextBio97681.
PROQ5FYB1.
SOURCESearch...

Entry information

Entry nameARSI_HUMAN
AccessionPrimary (citable) accession number: Q5FYB1
Secondary accession number(s): A1L3B0, B3KV22, B7XD03
Entry history
Integrated into UniProtKB/Swiss-Prot: October 11, 2005
Last sequence update: March 1, 2005
Last modified: July 9, 2014
This is version 87 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human chromosome 5

Human chromosome 5: entries, gene names and cross-references to MIM