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Q5FYB1

- ARSI_HUMAN

UniProt

Q5FYB1 - ARSI_HUMAN

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Protein

Arylsulfatase I

Gene

ARSI

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

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.2 Publications

Cofactori

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

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi55 – 551CalciumBy similarity
Metal bindingi56 – 561CalciumBy similarity
Metal bindingi93 – 931Calcium; via 3-oxoalanineBy similarity
Binding sitei147 – 1471SubstrateBy similarity
Active sitei149 – 1491By similarity
Binding sitei239 – 2391SubstrateBy similarity
Metal bindingi297 – 2971CalciumBy similarity
Metal bindingi298 – 2981CalciumBy similarity
Binding sitei315 – 3151SubstrateBy similarity

GO - Molecular functioni

  1. arylsulfatase activity Source: HGNC
  2. metal ion binding Source: UniProtKB-KW

GO - Biological processi

  1. cellular protein metabolic process Source: Reactome
  2. glycosphingolipid metabolic process Source: Reactome
  3. post-translational protein modification Source: Reactome
  4. small molecule metabolic process Source: Reactome
  5. sphingolipid metabolic process Source: Reactome
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Keywords - Ligandi

Calcium, Metal-binding

Enzyme and pathway databases

ReactomeiREACT_116105. Glycosphingolipid metabolism.
REACT_121036. The activation of arylsulfatases.

Names & Taxonomyi

Protein namesi
Recommended name:
Arylsulfatase I (EC:3.1.6.-)
Short name:
ASI
Gene namesi
Name:ARSI
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Unplaced

Organism-specific databases

HGNCiHGNC:32521. ARSI.

Subcellular locationi

Secreted 1 Publication. Endoplasmic reticulum 1 Publication
Note: Localized in the intracellular granular structures.

GO - Cellular componenti

  1. endoplasmic reticulum lumen Source: Reactome
  2. extracellular region Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Endoplasmic reticulum, Secreted

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi93 – 931C → S: No arylsulfatase activity in the media of retinal epithelium cell. 1 Publication

Organism-specific databases

Orphaneti401815. Autosomal recessive spastic paraplegia type 66.
PharmGKBiPA143485309.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2323Sequence AnalysisAdd
BLAST
Chaini24 – 569546Arylsulfatase IPRO_0000042216Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei93 – 9313-oxoalanine (Cys)1 Publication
Glycosylationi276 – 2761N-linked (GlcNAc...)Sequence Analysis
Glycosylationi288 – 2881N-linked (GlcNAc...)Sequence Analysis
Glycosylationi466 – 4661N-linked (GlcNAc...)Sequence Analysis
Glycosylationi496 – 4961N-linked (GlcNAc...)Sequence Analysis

Post-translational modificationi

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.1 Publication

Keywords - PTMi

Glycoprotein, Oxidation

Proteomic databases

PaxDbiQ5FYB1.
PRIDEiQ5FYB1.

PTM databases

PhosphoSiteiQ5FYB1.

Expressioni

Tissue specificityi

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

Gene expression databases

BgeeiQ5FYB1.
CleanExiHS_ARSI.
ExpressionAtlasiQ5FYB1. baseline and differential.
GenevestigatoriQ5FYB1.

Organism-specific databases

HPAiHPA038386.

Interactioni

Protein-protein interaction databases

STRINGi9606.ENSP00000333395.

Structurei

3D structure databases

ProteinModelPortaliQ5FYB1.
SMRiQ5FYB1. Positions 45-523.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi527 – 5337Poly-Glu

Sequence similaritiesi

Belongs to the sulfatase family.Curated

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiCOG3119.
GeneTreeiENSGT00760000119062.
HOGENOMiHOG000135354.
HOVERGENiHBG004282.
InParanoidiQ5FYB1.
KOiK12375.
OMAiQRASHIL.
OrthoDBiEOG7MKW5Q.
PhylomeDBiQ5FYB1.
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]

Sequences (2)i

Sequence statusi: Complete.

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

This entry describes 2 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: Q5FYB1-1) [UniParc]FASTAAdd to Basket

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.

« Hide

        10         20         30         40         50
MHTLTGFSLV SLLSFGYLSW DWAKPSFVAD GPGEAGEQPS AAPPQPPHII
60 70 80 90 100
FILTDDQGYH DVGYHGSDIE TPTLDRLAAK GVKLENYYIQ PICTPSRSQL
110 120 130 140 150
LTGRYQIHTG LQHSIIRPQQ PNCLPLDQVT LPQKLQEAGY STHMVGKWHL
160 170 180 190 200
GFYRKECLPT RRGFDTFLGS LTGNVDYYTY DNCDGPGVCG FDLHEGENVA
210 220 230 240 250
WGLSGQYSTM LYAQRASHIL ASHSPQRPLF LYVAFQAVHT PLQSPREYLY
260 270 280 290 300
RYRTMGNVAR RKYAAMVTCM DEAVRNITWA LKRYGFYNNS VIIFSSDNGG
310 320 330 340 350
QTFSGGSNWP LRGRKGTYWE GGVRGLGFVH SPLLKRKQRT SRALMHITDW
360 370 380 390 400
YPTLVGLAGG TTSAADGLDG YDVWPAISEG RASPRTEILH NIDPLYNHAQ
410 420 430 440 450
HGSLEGGFGI WNTAVQAAIR VGEWKLLTGD PGYGDWIPPQ TLATFPGSWW
460 470 480 490 500
NLERMASVRQ AVWLFNISAD PYEREDLAGQ RPDVVRTLLA RLAEYNRTAI
510 520 530 540 550
PVRYPAENPR AHPDFNGGAW GPWASDEEEE EEEGRARSFS RGRRKKKCKI
560
CKLRSFFRKL NTRLMSQRI
Length:569
Mass (Da):64,030
Last modified:March 1, 2005 - v1
Checksum:iD2F33EDD33ED211C
GO
Isoform 2 (identifier: Q5FYB1-2) [UniParc]FASTAAdd to Basket

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

Show »
Length:426
Mass (Da):48,253
Checksum:i2A12FCB6D9DCFA32
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti171 – 1711L → F in BAG53634. (PubMed:14702039)Curated
Sequence conflicti211 – 2111L → P in BAG53634. (PubMed:14702039)Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 143143Missing in isoform 2. 1 PublicationVSP_036022Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS34275.1. [Q5FYB1-1]
RefSeqiNP_001012301.1. NM_001012301.2. [Q5FYB1-1]
UniGeneiHs.591252.

Genome annotation databases

EnsembliENST00000328668; ENSP00000333395; ENSG00000183876. [Q5FYB1-1]
ENST00000515301; ENSP00000426879; ENSG00000183876. [Q5FYB1-2]
GeneIDi340075.
KEGGihsa:340075.
UCSCiuc003lrv.2. human. [Q5FYB1-1]

Polymorphism databases

DMDMi74722581.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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 .
CCDSi CCDS34275.1. [Q5FYB1-1 ]
RefSeqi NP_001012301.1. NM_001012301.2. [Q5FYB1-1 ]
UniGenei Hs.591252.

3D structure databases

ProteinModelPortali Q5FYB1.
SMRi Q5FYB1. Positions 45-523.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 9606.ENSP00000333395.

PTM databases

PhosphoSitei Q5FYB1.

Polymorphism databases

DMDMi 74722581.

Proteomic databases

PaxDbi Q5FYB1.
PRIDEi Q5FYB1.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000328668 ; ENSP00000333395 ; ENSG00000183876 . [Q5FYB1-1 ]
ENST00000515301 ; ENSP00000426879 ; ENSG00000183876 . [Q5FYB1-2 ]
GeneIDi 340075.
KEGGi hsa:340075.
UCSCi uc003lrv.2. human. [Q5FYB1-1 ]

Organism-specific databases

CTDi 340075.
GeneCardsi GC05M149657.
HGNCi HGNC:32521. ARSI.
HPAi HPA038386.
MIMi 610009. gene.
neXtProti NX_Q5FYB1.
Orphaneti 401815. Autosomal recessive spastic paraplegia type 66.
PharmGKBi PA143485309.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG3119.
GeneTreei ENSGT00760000119062.
HOGENOMi HOG000135354.
HOVERGENi HBG004282.
InParanoidi Q5FYB1.
KOi K12375.
OMAi QRASHIL.
OrthoDBi EOG7MKW5Q.
PhylomeDBi Q5FYB1.
TreeFami TF314186.

Enzyme and pathway databases

Reactomei REACT_116105. Glycosphingolipid metabolism.
REACT_121036. The activation of arylsulfatases.

Miscellaneous databases

GenomeRNAii 340075.
NextBioi 97681.
PROi Q5FYB1.
SOURCEi Search...

Gene expression databases

Bgeei Q5FYB1.
CleanExi HS_ARSI.
ExpressionAtlasi Q5FYB1. baseline and differential.
Genevestigatori Q5FYB1.

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. "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, OXOALANINE 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.
    , 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).

Entry informationi

Entry nameiARSI_HUMAN
AccessioniPrimary (citable) accession number: Q5FYB1
Secondary accession number(s): A1L3B0, B3KV22, B7XD03
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 11, 2005
Last sequence update: March 1, 2005
Last modified: November 26, 2014
This is version 91 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (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.

Miscellaneousi

Caution

According to PubMed:16500042, has no arylsulfatase activity.Curated

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Human chromosome 5
    Human chromosome 5: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3