ARSI_RAT
ID ARSI_RAT Reviewed; 573 AA.
AC Q32KJ8;
DT 16-DEC-2008, integrated into UniProtKB/Swiss-Prot.
DT 06-DEC-2005, sequence version 1.
DT 03-AUG-2022, entry version 99.
DE RecName: Full=Arylsulfatase I;
DE Short=ASI;
DE EC=3.1.6.-;
DE Flags: Precursor;
GN Name=Arsi;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Brown Norway;
RX PubMed=15057822; DOI=10.1038/nature02426;
RA Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J.,
RA Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G.,
RA Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G.,
RA Morgan M., Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G.,
RA Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S.,
RA Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T.,
RA Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T., Smith D.,
RA Lee H.-M., Gustafson E., Cahill P., Kana A., Doucette-Stamm L.,
RA Weinstock K., Fechtel K., Weiss R.B., Dunn D.M., Green E.D.,
RA Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K., Zhu B., Marra M.,
RA Schein J., Bosdet I., Fjell C., Jones S., Krzywinski M., Mathewson C.,
RA Siddiqui A., Wye N., McPherson J., Zhao S., Fraser C.M., Shetty J.,
RA Shatsman S., Geer K., Chen Y., Abramzon S., Nierman W.C., Havlak P.H.,
RA Chen R., Durbin K.J., Egan A., Ren Y., Song X.-Z., Li B., Liu Y., Qin X.,
RA Cawley S., Cooney A.J., D'Souza L.M., Martin K., Wu J.Q.,
RA Gonzalez-Garay M.L., Jackson A.R., Kalafus K.J., McLeod M.P.,
RA Milosavljevic A., Virk D., Volkov A., Wheeler D.A., Zhang Z., Bailey J.A.,
RA Eichler E.E., Tuzun E., Birney E., Mongin E., Ureta-Vidal A., Woodwark C.,
RA Zdobnov E., Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J.,
RA Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D., Schmidt J.,
RA Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M., Abril J.F.,
RA Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O., Poliakov A.,
RA Huebner N., Ganten D., Goesele C., Hummel O., Kreitler T., Lee Y.-A.,
RA Monti J., Schulz H., Zimdahl H., Himmelbauer H., Lehrach H., Jacob H.J.,
RA Bromberg S., Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E.,
RA Lazar J., Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M.,
RA Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E., Webber C.,
RA Brandt P., Nyakatura G., Adetobi M., Chiaromonte F., Elnitski L.,
RA Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K., Miller W.,
RA Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S., Zhang Y.,
RA Lindpaintner K., Andrews T.D., Caccamo M., Clamp M., Clarke L., Curwen V.,
RA Durbin R.M., Eyras E., Searle S.M., Cooper G.M., Batzoglou S., Brudno M.,
RA Sidow A., Stone E.A., Payseur B.A., Bourque G., Lopez-Otin C., Puente X.S.,
RA Chakrabarti K., Chatterji S., Dewey C., Pachter L., Bray N., Yap V.B.,
RA Caspi A., Tesler G., Pevzner P.A., Haussler D., Roskin K.M., Baertsch R.,
RA Clawson H., Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J.,
RA Rosenbloom K.R., Trumbower H., Weirauch M., Cooper D.N., Stenson P.D.,
RA Ma B., Brent M., Arumugam M., Shteynberg D., Copley R.R., Taylor M.S.,
RA Riethman H., Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S.,
RA Mockrin S., Collins F.S.;
RT "Genome sequence of the Brown Norway rat yields insights into mammalian
RT evolution.";
RL Nature 428:493-521(2004).
RN [2]
RP IDENTIFICATION.
RX PubMed=16174644; DOI=10.1093/hmg/ddi351;
RA Sardiello M., Annunziata I., Roma G., Ballabio A.;
RT "Sulfatases and sulfatase modifying factors: an exclusive and promiscuous
RT relationship.";
RL Hum. Mol. Genet. 14:3203-3217(2005).
CC -!- FUNCTION: Displays arylsulfatase activity at neutral pH, when co-
CC expressed with SUMF1; arylsulfatase activity is measured in the
CC secretion medium of retinal cell line, but no activity is recorded when
CC measured in cell extracts. {ECO:0000250|UniProtKB:Q5FYB1}.
CC -!- COFACTOR:
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC Evidence={ECO:0000250|UniProtKB:P15289};
CC Note=Binds 1 Ca(2+) ion per subunit. {ECO:0000250|UniProtKB:P15289};
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:Q5FYB1}.
CC Endoplasmic reticulum {ECO:0000250|UniProtKB:Q5FYB1}. Note=Localized in
CC the intracellular granular structures. {ECO:0000250|UniProtKB:Q5FYB1}.
CC -!- PTM: The oxidation of Cys-93 residue to 3-oxoalanine (also known as
CC C(alpha)-formylglycine) by SUMF1/Sulfatase-modifying factor 1, seems
CC critical for catalytic activity. {ECO:0000250|UniProtKB:Q5FYB1}.
CC -!- SIMILARITY: Belongs to the sulfatase family. {ECO:0000305}.
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DR EMBL; AABR03109797; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BN000739; CAI84985.1; -; mRNA.
DR RefSeq; NP_001041346.1; NM_001047881.1.
DR AlphaFoldDB; Q32KJ8; -.
DR SMR; Q32KJ8; -.
DR STRING; 10116.ENSRNOP00000033542; -.
DR GlyGen; Q32KJ8; 4 sites.
DR iPTMnet; Q32KJ8; -.
DR PhosphoSitePlus; Q32KJ8; -.
DR PaxDb; Q32KJ8; -.
DR PRIDE; Q32KJ8; -.
DR Ensembl; ENSRNOT00000030966; ENSRNOP00000033542; ENSRNOG00000026060.
DR GeneID; 307404; -.
DR KEGG; rno:307404; -.
DR UCSC; RGD:1310242; rat.
DR CTD; 340075; -.
DR RGD; 1310242; Arsi.
DR eggNOG; KOG3867; Eukaryota.
DR GeneTree; ENSGT00940000157656; -.
DR HOGENOM; CLU_006332_10_1_1; -.
DR InParanoid; Q32KJ8; -.
DR OMA; WGPWASE; -.
DR OrthoDB; 515367at2759; -.
DR PhylomeDB; Q32KJ8; -.
DR TreeFam; TF314186; -.
DR Reactome; R-RNO-1660662; Glycosphingolipid metabolism.
DR Reactome; R-RNO-1663150; The activation of arylsulfatases.
DR PRO; PR:Q32KJ8; -.
DR Proteomes; UP000002494; Chromosome 18.
DR Bgee; ENSRNOG00000026060; Expressed in esophagus and 15 other tissues.
DR Genevisible; Q32KJ8; RN.
DR GO; GO:0005783; C:endoplasmic reticulum; IEA:UniProtKB-SubCell.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0008484; F:sulfuric ester hydrolase activity; IEA:InterPro.
DR Gene3D; 3.40.720.10; -; 1.
DR InterPro; IPR017850; Alkaline_phosphatase_core_sf.
DR InterPro; IPR024607; Sulfatase_CS.
DR InterPro; IPR000917; Sulfatase_N.
DR Pfam; PF00884; Sulfatase; 1.
DR SUPFAM; SSF53649; SSF53649; 1.
DR PROSITE; PS00523; SULFATASE_1; 1.
DR PROSITE; PS00149; SULFATASE_2; 1.
PE 2: Evidence at transcript level;
KW Calcium; Endoplasmic reticulum; Glycoprotein; Hydrolase; Metal-binding;
KW Reference proteome; Secreted; Signal.
FT SIGNAL 1..23
FT /evidence="ECO:0000255"
FT CHAIN 24..573
FT /note="Arylsulfatase I"
FT /id="PRO_0000356285"
FT REGION 506..550
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 93
FT /note="Nucleophile"
FT /evidence="ECO:0000250|UniProtKB:P15289"
FT ACT_SITE 149
FT /evidence="ECO:0000250|UniProtKB:P15289"
FT BINDING 55
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:P15289"
FT BINDING 56
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:P15289"
FT BINDING 93
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /note="via 3-oxoalanine"
FT /evidence="ECO:0000250|UniProtKB:P15289"
FT BINDING 147
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P15289"
FT BINDING 239
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P15289"
FT BINDING 297
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:P15289"
FT BINDING 298
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:P15289"
FT BINDING 315
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P15289"
FT MOD_RES 93
FT /note="3-oxoalanine (Cys)"
FT /evidence="ECO:0000250|UniProtKB:Q5FYB1"
FT CARBOHYD 276
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 288
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 466
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 496
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 573 AA; 64424 MW; EEC97A0D8A57D367 CRC64;
MHALSGFSLV SLLSLGYLSW DWAKPGLVAD GPAEAEDQPS AAPPQPPHII FILTDDQGYH
DVGYHGSDIE TPTLDRLAAE GVKLENYYIQ PICTPSRSQL LTGRYQIHTG LQHSIIRPRQ
PNCLPLDQVT LPQKLQEAGY STHMVGKWHL GFYRKECLPT RRGFDTFLGS LTGNVDYYTY
DNCDGPGVCG FDLHEGESVA WGLSGQYSTM LYAQRASHIL ASHSPQKPLF LYVAFQAVHT
PLQSPREYLY RYRTMGNVAR RKYAAMVTCM DEAVRNITWA LKRYGFYNNS VIIFSSDNGG
QTFSGGSNWP LRGRKGTYWE GGVRGLGFVH SPLLKKKRRT SRALVHITDW YPTLVGLAGG
TTSAADGLDG YDVWPAISEG RASPRTEILH NIDPLYNHAR HGSLEGGFGI WNTAVQAAIR
VGEWKLLTGD PGYGDWIPPQ TLASFPGSWW NLERMASIRQ AVWLFNISAD PYEREDLADQ
RPDVVRTLLA RLADYNRTAI PVRYPAANPR AHPDFNGGAW GPWASDEDEE EEDEEEEGRA
RSFPRGRRKK KCKICKLRSF FRKLNTRLMS HRI
