HS2ST_DROME
ID HS2ST_DROME Reviewed; 349 AA.
AC P25722; Q9VIW4;
DT 01-MAY-1992, integrated into UniProtKB/Swiss-Prot.
DT 02-MAY-2002, sequence version 2.
DT 03-AUG-2022, entry version 155.
DE RecName: Full=Heparin sulfate O-sulfotransferase;
DE EC=2.8.2.-;
GN Name=Hs2st; ORFNames=CG10234;
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 [MRNA], AND ALTERNATIVE SPLICING.
RC STRAIN=Oregon-R;
RX PubMed=1936954; DOI=10.1093/genetics/129.1.133;
RA Powers P.A., Ganetzky B.;
RT "On the components of segregation distortion in Drosophila melanogaster. V.
RT Molecular analysis of the Sd locus.";
RL Genetics 129:133-144(1991).
RN [2]
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 [3]
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM S1).
RC STRAIN=Berkeley; TISSUE=Head;
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).
CC -!- SUBUNIT: Homotrimer. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Golgi apparatus membrane {ECO:0000250}; Single-
CC pass type II membrane protein {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Comment=Additional isoforms seem to exist.;
CC Name=S1;
CC IsoId=P25722-1; Sequence=Displayed;
CC Name=S2;
CC IsoId=P25722-2; Sequence=VSP_004382;
CC Name=S4;
CC IsoId=P25722-3; Sequence=VSP_004383;
CC -!- SIMILARITY: Belongs to the sulfotransferase 3 family. {ECO:0000305}.
CC -!- CAUTION: Was originally thought to be SD. {ECO:0000305|PubMed:1936954}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAA42779.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; X60218; CAA42779.1; ALT_FRAME; mRNA.
DR EMBL; AE014134; AAF53800.1; -; Genomic_DNA.
DR EMBL; AY058422; AAL13651.1; -; mRNA.
DR PIR; S18765; S18765.
DR RefSeq; NP_477339.1; NM_057991.5. [P25722-1]
DR AlphaFoldDB; P25722; -.
DR SMR; P25722; -.
DR BioGRID; 69059; 4.
DR IntAct; P25722; 1.
DR STRING; 7227.FBpp0080826; -.
DR GlyGen; P25722; 3 sites.
DR PaxDb; P25722; -.
DR PRIDE; P25722; -.
DR DNASU; 44433; -.
DR EnsemblMetazoa; FBtr0081288; FBpp0080826; FBgn0024230. [P25722-1]
DR GeneID; 44433; -.
DR KEGG; dme:Dmel_CG10234; -.
DR CTD; 44433; -.
DR FlyBase; FBgn0024230; Hs2st.
DR VEuPathDB; VectorBase:FBgn0024230; -.
DR eggNOG; KOG3922; Eukaryota.
DR GeneTree; ENSGT00530000063408; -.
DR HOGENOM; CLU_045310_1_1_1; -.
DR InParanoid; P25722; -.
DR OMA; KWHEMKP; -.
DR PhylomeDB; P25722; -.
DR Reactome; R-DME-2022928; HS-GAG biosynthesis.
DR SignaLink; P25722; -.
DR BioGRID-ORCS; 44433; 0 hits in 1 CRISPR screen.
DR GenomeRNAi; 44433; -.
DR PRO; PR:P25722; -.
DR Proteomes; UP000000803; Chromosome 2L.
DR Bgee; FBgn0024230; Expressed in saliva-secreting gland and 12 other tissues.
DR Genevisible; P25722; DM.
DR GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0004394; F:heparan sulfate 2-O-sulfotransferase activity; IDA:FlyBase.
DR GO; GO:0008146; F:sulfotransferase activity; IBA:GO_Central.
DR GO; GO:0015012; P:heparan sulfate proteoglycan biosynthetic process; IMP:FlyBase.
DR GO; GO:0015015; P:heparan sulfate proteoglycan biosynthetic process, enzymatic modification; IBA:GO_Central.
DR GO; GO:0015014; P:heparan sulfate proteoglycan biosynthetic process, polysaccharide chain biosynthetic process; IBA:GO_Central.
DR GO; GO:0007424; P:open tracheal system development; IMP:FlyBase.
DR GO; GO:0007165; P:signal transduction; NAS:FlyBase.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR007734; Heparan_SO4_2-O-STrfase.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR005331; Sulfotransferase.
DR PANTHER; PTHR12129; PTHR12129; 1.
DR Pfam; PF03567; Sulfotransfer_2; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
PE 2: Evidence at transcript level;
KW Alternative splicing; Disulfide bond; Glycoprotein; Golgi apparatus;
KW Membrane; Reference proteome; Signal-anchor; Transferase; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..349
FT /note="Heparin sulfate O-sulfotransferase"
FT /id="PRO_0000207680"
FT TOPO_DOM 1..17
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 18..38
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 39..349
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT ACT_SITE 139
FT /evidence="ECO:0000250"
FT CARBOHYD 107
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 126
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 282
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 200..208
FT /evidence="ECO:0000250"
FT DISULFID 221..227
FT /evidence="ECO:0000250"
FT VAR_SEQ 1..255
FT /note="Missing (in isoform S4)"
FT /evidence="ECO:0000305"
FT /id="VSP_004383"
FT VAR_SEQ 1..24
FT /note="MFRKLLKMWILLRPTHWLILIALC -> MKRSAECSEWQAFFESDDGFRQPG
FT IIITIDEAFEAII (in isoform S2)"
FT /evidence="ECO:0000305"
FT /id="VSP_004382"
FT CONFLICT 28
FT /note="C -> S (in Ref. 1; CAA42779)"
FT /evidence="ECO:0000305"
FT CONFLICT 180..181
FT /note="DN -> EH (in Ref. 1; CAA42779)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 349 AA; 41273 MW; E4655D92D7615C41 CRC64;
MFRKLLKMWI LLRPTHWLIL IALCAVTCAG YWLLWSEIRL EHAFKPLSKL GDSLSPDQHA
SSTTDDFDFE EHLVVLYNRV PKTGSTSFVN IAYDLCKPNK FHVLHINVTA NMHVLSLPNQ
IQFVRNVSRW HEMKPALYHG HMAFLDFSKF QIAHKPIYIN LVRKPLDRLV SYYYFLRFGD
NYRPNLVRKK AGNKITFDEC VVQKQPDCDP KNMWLQIPFF CGHAAECWEP GSSWALDQAK
RNLVNEYFLV GVTEQMYEFV DLLERSLPRI FHGFREHYHN SNKSHLRVTS SKLPPSESTI
KSIQKTKIWQ MENDLYDFAL AQFEFNKKKL MQPDNKHVQK FMYEKIRPK
