SULF1_DROME
ID SULF1_DROME Reviewed; 1114 AA.
AC Q9VEX0; Q8MRG1; Q9NIH6;
DT 19-JUL-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 153.
DE RecName: Full=Extracellular sulfatase SULF-1 homolog;
DE Short=DmSulf-1;
DE EC=3.1.6.-;
DE Flags: Precursor;
GN Name=Sulf1; ORFNames=CG6725;
OS Drosophila melanogaster (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7227;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley;
RX PubMed=10731132; DOI=10.1126/science.287.5461.2185;
RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., Brandon R.C.,
RA Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C.,
RA Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A.,
RA An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A.,
RA Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V.,
RA Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J.,
RA Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E.,
RA Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B.,
RA Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I.,
RA Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C.,
RA Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S.,
RA Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M.,
RA Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D.,
RA Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F.,
RA Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D.,
RA Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A.,
RA Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C.,
RA McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C.,
RA Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L.,
RA Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R.,
RA Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V.,
RA Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F.,
RA Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J.,
RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R.,
RA Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y.,
RA Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T.,
RA Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S.,
RA Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W.,
RA Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M.,
RA Venter J.C.;
RT "The genome sequence of Drosophila melanogaster.";
RL Science 287:2185-2195(2000).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=Berkeley;
RX PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M.,
RA Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.;
RT "Annotation of the Drosophila melanogaster euchromatic genome: a systematic
RT review.";
RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Berkeley; TISSUE=Embryo;
RX PubMed=12537569; DOI=10.1186/gb-2002-3-12-research0080;
RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., George R.A.,
RA Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., Rubin G.M.,
RA Celniker S.E.;
RT "A Drosophila full-length cDNA resource.";
RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002).
RN [4]
RP NUCLEOTIDE SEQUENCE OF 104-1087.
RA Standiford D.M., Emerson C.P. Jr.;
RT "Analysis of Drosophila melanogaster Sulf1 during development.";
RL Submitted (DEC-1999) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-743, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RC STRAIN=Oregon-R; TISSUE=Head;
RX PubMed=17893096; DOI=10.1093/glycob/cwm097;
RA Koles K., Lim J.-M., Aoki K., Porterfield M., Tiemeyer M., Wells L.,
RA Panin V.;
RT "Identification of N-glycosylated proteins from the central nervous system
RT of Drosophila melanogaster.";
RL Glycobiology 17:1388-1403(2007).
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=AAF32278.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=AAM50312.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AE014297; AAF55296.1; -; Genomic_DNA.
DR EMBL; AY119658; AAM50312.1; ALT_INIT; mRNA.
DR EMBL; AF211192; AAF32278.1; ALT_FRAME; mRNA.
DR RefSeq; NP_001262626.1; NM_001275697.1.
DR RefSeq; NP_001262627.1; NM_001275698.1.
DR RefSeq; NP_524987.1; NM_080248.3.
DR AlphaFoldDB; Q9VEX0; -.
DR SMR; Q9VEX0; -.
DR BioGRID; 72725; 12.
DR DIP; DIP-21001N; -.
DR IntAct; Q9VEX0; 5.
DR STRING; 7227.FBpp0082725; -.
DR GlyGen; Q9VEX0; 13 sites.
DR iPTMnet; Q9VEX0; -.
DR PaxDb; Q9VEX0; -.
DR PRIDE; Q9VEX0; -.
DR EnsemblMetazoa; FBtr0083273; FBpp0082725; FBgn0040271.
DR EnsemblMetazoa; FBtr0334699; FBpp0306754; FBgn0040271.
DR EnsemblMetazoa; FBtr0334700; FBpp0306755; FBgn0040271.
DR GeneID; 53437; -.
DR KEGG; dme:Dmel_CG6725; -.
DR UCSC; CG6725-RA; d. melanogaster.
DR CTD; 23213; -.
DR FlyBase; FBgn0040271; Sulf1.
DR VEuPathDB; VectorBase:FBgn0040271; -.
DR eggNOG; KOG3731; Eukaryota.
DR GeneTree; ENSGT00940000169254; -.
DR HOGENOM; CLU_006332_2_1_1; -.
DR InParanoid; Q9VEX0; -.
DR OMA; QCIEDTA; -.
DR OrthoDB; 1273622at2759; -.
DR PhylomeDB; Q9VEX0; -.
DR BioGRID-ORCS; 53437; 0 hits in 3 CRISPR screens.
DR GenomeRNAi; 53437; -.
DR PRO; PR:Q9VEX0; -.
DR Proteomes; UP000000803; Chromosome 3R.
DR Bgee; FBgn0040271; Expressed in mouthpart and 86 other tissues.
DR ExpressionAtlas; Q9VEX0; baseline and differential.
DR Genevisible; Q9VEX0; DM.
DR GO; GO:0009986; C:cell surface; IEA:UniProtKB-SubCell.
DR GO; GO:0005783; C:endoplasmic reticulum; IEA:UniProtKB-SubCell.
DR GO; GO:0005615; C:extracellular space; IDA:FlyBase.
DR GO; GO:0005795; C:Golgi stack; IEA:UniProtKB-SubCell.
DR GO; GO:0005539; F:glycosaminoglycan binding; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0008449; F:N-acetylglucosamine-6-sulfatase activity; IMP:FlyBase.
DR GO; GO:0030202; P:heparin metabolic process; IGI:FlyBase.
DR GO; GO:0008045; P:motor neuron axon guidance; IMP:FlyBase.
DR GO; GO:0090090; P:negative regulation of canonical Wnt signaling pathway; IMP:FlyBase.
DR GO; GO:0042059; P:negative regulation of epidermal growth factor receptor signaling pathway; IGI:FlyBase.
DR GO; GO:0045879; P:negative regulation of smoothened signaling pathway; IMP:FlyBase.
DR GO; GO:0045880; P:positive regulation of smoothened signaling pathway; IMP:FlyBase.
DR GO; GO:0016201; P:synaptic target inhibition; IMP:FlyBase.
DR GO; GO:0048100; P:wing disc anterior/posterior pattern formation; IMP:FlyBase.
DR GO; GO:0048190; P:wing disc dorsal/ventral pattern formation; IMP:FlyBase.
DR Gene3D; 3.40.720.10; -; 1.
DR InterPro; IPR017850; Alkaline_phosphatase_core_sf.
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 SUPFAM; SSF53649; SSF53649; 2.
DR PROSITE; PS00523; SULFATASE_1; 1.
PE 1: Evidence at protein level;
KW Calcium; Endoplasmic reticulum; Glycoprotein; Golgi apparatus; Hydrolase;
KW Metal-binding; Reference proteome; Signal.
FT SIGNAL 1..25
FT /evidence="ECO:0000255"
FT CHAIN 26..1114
FT /note="Extracellular sulfatase SULF-1 homolog"
FT /id="PRO_0000033439"
FT REGION 466..504
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 781..812
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 876..901
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1073..1114
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 466..482
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 483..504
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 876..891
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1077..1114
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 98
FT /note="Nucleophile"
FT /evidence="ECO:0000250|UniProtKB:P15289"
FT BINDING 62
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 63
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 98
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /note="via 3-oxoalanine"
FT /evidence="ECO:0000250"
FT BINDING 327
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 328
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT MOD_RES 98
FT /note="3-oxoalanine (Cys)"
FT /evidence="ECO:0000250|UniProtKB:P15289"
FT CARBOHYD 122
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 159
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 181
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 208
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 251
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 447
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 683
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 713
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 743
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:17893096"
FT CARBOHYD 817
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 945
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 955
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 974
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CONFLICT 104..105
FT /note="SL -> TR (in Ref. 4; AAF32278)"
FT /evidence="ECO:0000305"
FT CONFLICT 655
FT /note="E -> A (in Ref. 3; AAM50312)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1114 AA; 127303 MW; FC14DD0975B3A096 CRC64;
MMRHSSLRLI IGGLILLLFV LNVFSKEQGS HSHKRSHSAK RFSRDSNSAR ERRPNIILIL
TDDQDVELGS LNFMPRTLRL LRDGGAEFRH AYTTTPMCCP ARSSLLTGMY VHNHMVFTNN
DNCSSPQWQA THETRSYATY LSNAGYRTGY FGKYLNKYNG SYIPPGWREW GGLIMNSKYY
NYSINLNGQK IKHGFDYAKD YYPDLIANDS IAFLRSSKQQ NQRKPVLLTM SFPAPHGPED
SAPQYSHLFF NVTTHHTPSY DHAPNPDKQW ILRVTEPMQP VHKRFTNLLM TKRLQTLQSV
DVAVERVYNE LKELGELDNT YIVYTSDHGY HLGQFGLIKG KSFPFEFDVR VPFLIRGPGI
QASKVVNEIV LNVDLAPTFL DMGGVPTPQH MDGRSILPLL LSRNRAVRDN WPDSFLIESS
GRRETAEQIA ESRARLQIER RNMKLANSSL LEDFLEGAGE STTIVSSSST AATLMSSTAQ
QPEDGEEEVE TDNEEDDVDG DGAMDSSAAA LEEDDLDDAA FEEGDEELDQ EFQQNNDLPL
APYITKMMRL NSECSDPALL KNCLPGQKWK CVNEEGRWRK HKCKFHLQLE HQLAAMPRKQ
YQRNCACFTP DGVVYTKIRA PSAGLHRVNK RTHNGPGRRR NKREVFHTEL PDEMEELLDL
HQVVDQLVDH THRSKRDLPA SSNETIAQVI QQIQSTLEIL ELKFNEHELH ASNSSGNSYE
RGEKYTKSGG HRCFVDATTA KVNCSNVIYD DEKTWRTSRT QIDMLIKLLK DKIGKLKEMK
KQLRESNKQA LAAGRRNDNR RRNDQSVLDS GAGPEFNMSY FTEISSTPRS NVVGQTEVFQ
GYGSASAFDS LEQTQSHRFT PRAECYCEPD VGENHADSKE MAREARRKLK EERQRKKERK
RIKKARLEKE CLSEKMNCFS HDNQHWRTAP LWNDSPFCFC MNANNNTYSC LRTINGTHNF
LYCEFTTGLI TFYNLTIDRF ETINRAAGLT PGERSHMHDA LDQLKSCRGR SCSIRRHQNH
LEGGSSAPLL PINQVHRNNK RKHSPLAGAV GNYAFVGPRL DMEALPPIKR RKLSKYNRLT
GSQQSHMKRR PWKQTPLQQS PRFLRTHSVT PAQA
