SULF2_MOUSE
ID SULF2_MOUSE Reviewed; 875 AA.
AC Q8CFG0; B2RUD5; Q3TNM3; Q8BM68; Q8BUZ4; Q8BX28; Q8BZ51; Q8C169; Q9D8E2;
DT 19-JUL-2003, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 2.
DT 03-AUG-2022, entry version 143.
DE RecName: Full=Extracellular sulfatase Sulf-2;
DE Short=mSulf-2;
DE EC=3.1.6.-;
DE Flags: Precursor;
GN Name=Sulf2;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Mammary tumor;
RX PubMed=12368295; DOI=10.1074/jbc.m205131200;
RA Morimoto-Tomita M., Uchimura K., Werb Z., Hemmerich S., Rosen S.D.;
RT "Cloning and characterization of two extracellular heparin-degrading
RT endosulfatases in mice and humans.";
RL J. Biol. Chem. 277:49175-49185(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J;
RC TISSUE=Bone, Cervix squamous cell, Embryo, Embryonic stem cell, Head, Skin,
RC and Testis;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Czech II; TISSUE=Brain, and Mammary gland;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
CC -!- FUNCTION: Exhibits arylsulfatase activity and highly specific
CC endoglucosamine-6-sulfatase activity. It can remove sulfate from the C-
CC 6 position of glucosamine within specific subregions of intact heparin
CC (By similarity). {ECO:0000250}.
CC -!- COFACTOR:
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000250};
CC Note=Binds 1 Ca(2+) ion per subunit. {ECO:0000250};
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum {ECO:0000250}. Golgi
CC apparatus, Golgi stack {ECO:0000250}. Cell surface {ECO:0000250}.
CC Note=Also localized on the cell surface. {ECO:0000250}.
CC -!- PTM: The conversion to 3-oxoalanine (also known as C-formylglycine,
CC FGly), of a serine or cysteine residue in prokaryotes and of a cysteine
CC residue in eukaryotes, is critical for catalytic activity.
CC {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the sulfatase family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAB25464.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AY101177; AAM76862.1; -; mRNA.
DR EMBL; AK008108; BAB25464.1; ALT_INIT; mRNA.
DR EMBL; AK028874; BAC26165.1; -; mRNA.
DR EMBL; AK034712; BAC28804.2; -; mRNA.
DR EMBL; AK036685; BAC29534.1; -; mRNA.
DR EMBL; AK049170; BAC33584.1; -; mRNA.
DR EMBL; AK081643; BAC38279.1; -; mRNA.
DR EMBL; AK133336; BAE21607.1; -; mRNA.
DR EMBL; AK165183; BAE38065.1; -; mRNA.
DR EMBL; AL589873; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC027238; AAH27238.2; -; mRNA.
DR EMBL; BC141086; AAI41087.1; -; mRNA.
DR CCDS; CCDS17086.1; -.
DR RefSeq; NP_001239507.1; NM_001252578.1.
DR RefSeq; NP_001239508.1; NM_001252579.1.
DR RefSeq; NP_082348.2; NM_028072.5.
DR RefSeq; XP_006500272.1; XM_006500209.3.
DR RefSeq; XP_006500274.1; XM_006500211.2.
DR RefSeq; XP_017174757.1; XM_017319268.1.
DR AlphaFoldDB; Q8CFG0; -.
DR SMR; Q8CFG0; -.
DR BioGRID; 215112; 3.
DR STRING; 10090.ENSMUSP00000104872; -.
DR GlyConnect; 2308; 2 N-Linked glycans (3 sites).
DR GlyGen; Q8CFG0; 13 sites, 2 N-linked glycans (3 sites).
DR iPTMnet; Q8CFG0; -.
DR PhosphoSitePlus; Q8CFG0; -.
DR MaxQB; Q8CFG0; -.
DR PaxDb; Q8CFG0; -.
DR PRIDE; Q8CFG0; -.
DR ProteomicsDB; 254609; -.
DR Antibodypedia; 1101; 342 antibodies from 33 providers.
DR Ensembl; ENSMUST00000088086; ENSMUSP00000085405; ENSMUSG00000006800.
DR Ensembl; ENSMUST00000109249; ENSMUSP00000104872; ENSMUSG00000006800.
DR Ensembl; ENSMUST00000146497; ENSMUSP00000154557; ENSMUSG00000006800.
DR GeneID; 72043; -.
DR KEGG; mmu:72043; -.
DR UCSC; uc008nyk.2; mouse.
DR CTD; 55959; -.
DR MGI; MGI:1919293; Sulf2.
DR VEuPathDB; HostDB:ENSMUSG00000006800; -.
DR eggNOG; KOG3731; Eukaryota.
DR GeneTree; ENSGT00940000159151; -.
DR HOGENOM; CLU_006332_2_0_1; -.
DR InParanoid; Q8CFG0; -.
DR OMA; PQMDGRS; -.
DR OrthoDB; 1273622at2759; -.
DR PhylomeDB; Q8CFG0; -.
DR TreeFam; TF313545; -.
DR BioGRID-ORCS; 72043; 3 hits in 75 CRISPR screens.
DR ChiTaRS; Sulf2; mouse.
DR PRO; PR:Q8CFG0; -.
DR Proteomes; UP000000589; Chromosome 2.
DR RNAct; Q8CFG0; protein.
DR Bgee; ENSMUSG00000006800; Expressed in embryonic post-anal tail and 278 other tissues.
DR ExpressionAtlas; Q8CFG0; baseline and differential.
DR Genevisible; Q8CFG0; MM.
DR GO; GO:0009986; C:cell surface; ISS:UniProtKB.
DR GO; GO:0005783; C:endoplasmic reticulum; ISO:MGI.
DR GO; GO:0005615; C:extracellular space; ISO:MGI.
DR GO; GO:0005795; C:Golgi stack; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR GO; GO:0004065; F:arylsulfatase activity; ISS:UniProtKB.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0005539; F:glycosaminoglycan binding; IBA:GO_Central.
DR GO; GO:0008449; F:N-acetylglucosamine-6-sulfatase activity; IMP:UniProtKB.
DR GO; GO:0060348; P:bone development; IGI:BHF-UCL.
DR GO; GO:0051216; P:cartilage development; IMP:UniProtKB.
DR GO; GO:0002063; P:chondrocyte development; IMP:UniProtKB.
DR GO; GO:0048706; P:embryonic skeletal system development; IGI:UniProtKB.
DR GO; GO:0014846; P:esophagus smooth muscle contraction; IGI:UniProtKB.
DR GO; GO:0035860; P:glial cell-derived neurotrophic factor receptor signaling pathway; IDA:UniProtKB.
DR GO; GO:0032836; P:glomerular basement membrane development; IGI:UniProtKB.
DR GO; GO:0003094; P:glomerular filtration; IGI:UniProtKB.
DR GO; GO:0030201; P:heparan sulfate proteoglycan metabolic process; IMP:UniProtKB.
DR GO; GO:0060384; P:innervation; IGI:UniProtKB.
DR GO; GO:0001822; P:kidney development; IGI:BHF-UCL.
DR GO; GO:0097421; P:liver regeneration; IMP:MGI.
DR GO; GO:0040037; P:negative regulation of fibroblast growth factor receptor signaling pathway; IGI:UniProtKB.
DR GO; GO:0090263; P:positive regulation of canonical Wnt signaling pathway; IMP:MGI.
DR GO; GO:0010575; P:positive regulation of vascular endothelial growth factor production; IGI:UniProtKB.
DR GO; GO:0030177; P:positive regulation of Wnt signaling pathway; ISO:MGI.
DR GO; GO:2000345; P:regulation of hepatocyte proliferation; IMP:MGI.
DR GO; GO:0009611; P:response to wounding; IMP:MGI.
DR GO; GO:0006790; P:sulfur compound metabolic process; ISO:MGI.
DR Gene3D; 3.40.720.10; -; 1.
DR InterPro; IPR017850; Alkaline_phosphatase_core_sf.
DR InterPro; IPR014615; Extracellular_sulfatase.
DR InterPro; IPR024609; Extracellular_sulfatase_C.
DR InterPro; IPR024607; Sulfatase_CS.
DR InterPro; IPR000917; Sulfatase_N.
DR Pfam; PF12548; DUF3740; 1.
DR Pfam; PF00884; Sulfatase; 1.
DR PIRSF; PIRSF036665; Sulf1; 1.
DR SUPFAM; SSF53649; SSF53649; 2.
DR PROSITE; PS00523; SULFATASE_1; 1.
PE 2: Evidence at transcript level;
KW Calcium; Endoplasmic reticulum; Glycoprotein; Golgi apparatus; Hydrolase;
KW Metal-binding; Reference proteome; Signal.
FT SIGNAL 1..24
FT /evidence="ECO:0000255"
FT CHAIN 25..875
FT /note="Extracellular sulfatase Sulf-2"
FT /id="PRO_0000033441"
FT REGION 560..595
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 88
FT /note="Nucleophile"
FT /evidence="ECO:0000250|UniProtKB:P15289"
FT BINDING 52
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 53
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 88
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /note="via 3-oxoalanine"
FT /evidence="ECO:0000250"
FT BINDING 317
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 318
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT MOD_RES 88
FT /note="3-oxoalanine (Cys)"
FT /evidence="ECO:0000250|UniProtKB:P15289"
FT CARBOHYD 65
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 112
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 132
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 149
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 171
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 198
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 241
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 539
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 566
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 613
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 722
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 759
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 769
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CONFLICT 131
FT /note="L -> F (in Ref. 2; BAC38279)"
FT /evidence="ECO:0000305"
FT CONFLICT 285
FT /note="Q -> H (in Ref. 2; BAC26165)"
FT /evidence="ECO:0000305"
FT CONFLICT 534
FT /note="T -> A (in Ref. 2; BAC26165)"
FT /evidence="ECO:0000305"
FT CONFLICT 614
FT /note="D -> G (in Ref. 2; BAC26165)"
FT /evidence="ECO:0000305"
FT CONFLICT 669
FT /note="R -> K (in Ref. 1; AAM76862 and 4; AAH27238/
FT AAI41087)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 875 AA; 100497 MW; A04AE401029FCCDC CRC64;
MAPPGLPLWL LSTALLSLLA GSSAFLSHPR LKGRFQRDRR NIRPNIILVL TDDQDVELGS
MQVMNKTRRI MEQGGAHFIN AFVTTPMCCP SRSSILTGKY VHNHNTYTNN ENCSSPSWQA
QHESRTFAVY LNSTGYRTAF FGKYLNEYNG SYVPPGWKEW VGLLKNSRFY NYTLCRNGVK
EKHGSDYSTD YLTDLITNDS VSFFRTSKKM YPHRPVLMVI SHAAPHGPED SAPQYSRLFP
NASQHITPSY NYAPNPDKHW IMRYTGPMKP IHMEFTNMLQ RKRLQTLMSV DDSMETIYDM
LVETGELDNT YILYTADHGY HIGQFGLVKG KSMPYEFDIR VPFYVRGPNV EAGSLNPHIV
LNIDLAPTIL DIAGLDIPAD MDGKSILKLL DSERPVNRFH LKKKLRVWRD SFLVERGKLL
HKREGDKVNA QEENFLPKYQ RVKDLCQRAE YQTACEQLGQ KWQCVEDASG TLKLHKCKGP
MRFGGGGGSR ALSNLVPKYD GQSSEACSCD SGGGGDYKLG LAGRRKLFKK KYKTSYARNR
SIRSVAIEVD GEIYHVGLDT VPQPRNLSKP HWPGAPEDQD DKDGGSFSGT GGLPDYSAPN
PIKVTHRCYI LENDTVQCDL DLYKSLQAWK DHKLHIDHEI ETLQNKIKNL REVRGHLKKK
RPEECDCHRI SYHSQHKGRL KHKGSSLHPF RKGLQEKDKV WLLREQKRKK KLRKLLKRLQ
NNDTCSMPGL TCFTHDNHHW QTAPLWTLGP FCACTSANNN TYWCLRTINE THNFLFCEFA
TGFIEYFDLS TDPYQLMNAV NTLDRDVLNQ LHVQLMELRS CKGYKQCNPR TRNMDLGLRD
GGSYEQYRQF QRRKWPEMKR PSSKSLGQLW EGWEG
