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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

Binds 1 calcium ion per subunit By similarity.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi55 – 551Calcium By similarity
Metal bindingi56 – 561Calcium By similarity
Metal bindingi93 – 931Calcium; via 3-oxoalanine By similarity
Binding sitei147 – 1471Substrate By similarity
Active sitei149 – 1491 By similarity
Binding sitei239 – 2391Substrate By similarity
Metal bindingi297 – 2971Calcium By similarity
Metal bindingi298 – 2981Calcium By similarity
Binding sitei315 – 3151Substrate By 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: Chromosome 5

Organism-specific databases

HGNCiHGNC:32521. ARSI.

Subcellular locationi

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

GO - Cellular componenti

  1. endoplasmic reticulum lumen Source: Reactome
  2. extracellular region Source: UniProtKB-SubCell
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

PharmGKBiPA143485309.

PTM / Processingi

Molecule processing

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

Amino acid modifications

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

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.

Keywords - PTMi

Glycoprotein

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

ArrayExpressiQ5FYB1.
BgeeiQ5FYB1.
CleanExiHS_ARSI.
GenevestigatoriQ5FYB1.

Organism-specific databases

HPAiHPA038386.

Interactioni

Protein-protein interaction databases

STRINGi9606.ENSP00000333395.

Structurei

3D structure databases

ProteinModelPortaliQ5FYB1.
SMRiQ5FYB1. Positions 45-523.

Family & Domainsi

Compositional bias

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

Sequence similaritiesi

Belongs to the sulfatase family.

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiCOG3119.
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

MHTLTGFSLV SLLSFGYLSW DWAKPSFVAD GPGEAGEQPS AAPPQPPHII    50
FILTDDQGYH DVGYHGSDIE TPTLDRLAAK GVKLENYYIQ PICTPSRSQL 100
LTGRYQIHTG LQHSIIRPQQ PNCLPLDQVT LPQKLQEAGY STHMVGKWHL 150
GFYRKECLPT RRGFDTFLGS LTGNVDYYTY DNCDGPGVCG FDLHEGENVA 200
WGLSGQYSTM LYAQRASHIL ASHSPQRPLF LYVAFQAVHT PLQSPREYLY 250
RYRTMGNVAR RKYAAMVTCM DEAVRNITWA LKRYGFYNNS VIIFSSDNGG 300
QTFSGGSNWP LRGRKGTYWE GGVRGLGFVH SPLLKRKQRT SRALMHITDW 350
YPTLVGLAGG TTSAADGLDG YDVWPAISEG RASPRTEILH NIDPLYNHAQ 400
HGSLEGGFGI WNTAVQAAIR VGEWKLLTGD PGYGDWIPPQ TLATFPGSWW 450
NLERMASVRQ AVWLFNISAD PYEREDLAGQ RPDVVRTLLA RLAEYNRTAI 500
PVRYPAENPR AHPDFNGGAW GPWASDEEEE EEEGRARSFS RGRRKKKCKI 550
CKLRSFFRKL NTRLMSQRI 569
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

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 143143Missing in isoform 2. VSP_036022Add
BLAST

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti171 – 1711L → F in BAG53634. 1 Publication
Sequence conflicti211 – 2111L → P in BAG53634. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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:
EMBL
GenBank
DDBJ
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.
PharmGKBi PA143485309.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG3119.
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

ArrayExpressi Q5FYB1.
Bgeei Q5FYB1.
CleanExi HS_ARSI.
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, 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.
    , 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: September 3, 2014
This is version 88 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 1 Publication, has no arylsulfatase activity.

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

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