ID A0A158NAY9_ATTCE Unreviewed; 475 AA.
AC A0A158NAY9;
DT 08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT 08-JUN-2016, sequence version 1.
DT 24-JAN-2024, entry version 30.
DE RecName: Full=Heparan-sulfate 6-O-sulfotransferase {ECO:0000256|RuleBase:RU364122};
DE EC=2.8.2.- {ECO:0000256|RuleBase:RU364122};
GN Name=105617753 {ECO:0000313|EnsemblMetazoa:XP_012054697.1};
OS Atta cephalotes (Leafcutter ant).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Hymenoptera; Apocrita; Aculeata; Formicoidea;
OC Formicidae; Myrmicinae; Atta.
OX NCBI_TaxID=12957 {ECO:0000313|EnsemblMetazoa:XP_012054697.1, ECO:0000313|Proteomes:UP000005205};
RN [1] {ECO:0000313|Proteomes:UP000005205}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=21347285; DOI=10.1371/journal.pgen.1002007;
RA Suen G., Teiling C., Li L., Holt C., Abouheif E., Bornberg-Bauer E.,
RA Bouffard P., Caldera E.J., Cash E., Cavanaugh A., Denas O., Elhaik E.,
RA Fave M.J., Gadau J., Gibson J.D., Graur D., Grubbs K.J., Hagen D.E.,
RA Harkins T.T., Helmkampf M., Hu H., Johnson B.R., Kim J., Marsh S.E.,
RA Moeller J.A., Munoz-Torres M.C., Murphy M.C., Naughton M.C., Nigam S.,
RA Overson R., Rajakumar R., Reese J.T., Scott J.J., Smith C.R., Tao S.,
RA Tsutsui N.D., Viljakainen L., Wissler L., Yandell M.D., Zimmer F.,
RA Taylor J., Slater S.C., Clifton S.W., Warren W.C., Elsik C.G., Smith C.D.,
RA Weinstock G.M., Gerardo N.M., Currie C.R.;
RT "The genome sequence of the leaf-cutter ant Atta cephalotes reveals
RT insights into its obligate symbiotic lifestyle.";
RL PLoS Genet. 7:e1002007-e1002007(2011).
RN [2] {ECO:0000313|EnsemblMetazoa:XP_012054697.1}
RP IDENTIFICATION.
RG EnsemblMetazoa;
RL Submitted (APR-2016) to UniProtKB.
CC -!- FUNCTION: 6-O-sulfation enzyme which catalyzes the transfer of sulfate
CC from 3'-phosphoadenosine 5'-phosphosulfate (PAPS) to position 6 of the
CC N-sulfoglucosamine residue (GlcNS) of heparan sulfate.
CC {ECO:0000256|RuleBase:RU364122}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=3'-phosphoadenylyl sulfate + alpha-D-glucosaminyl-[heparan
CC sulfate](n) = 6-sulfo-alpha-D-glucosaminyl-[heparan sulfate](n) +
CC adenosine 3',5'-bisphosphate + H(+); Xref=Rhea:RHEA:56604, Rhea:RHEA-
CC COMP:9830, Rhea:RHEA-COMP:14621, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:58339, ChEBI:CHEBI:58343, ChEBI:CHEBI:58388,
CC ChEBI:CHEBI:140604; Evidence={ECO:0000256|RuleBase:RU364122};
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|RuleBase:RU364122}; Single-
CC pass type II membrane protein {ECO:0000256|RuleBase:RU364122}.
CC -!- SIMILARITY: Belongs to the sulfotransferase 6 family.
CC {ECO:0000256|ARBA:ARBA00010109, ECO:0000256|RuleBase:RU364122}.
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DR EMBL; ADTU01010515; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; ADTU01010516; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; ADTU01010517; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; ADTU01010518; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; ADTU01010519; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; ADTU01010520; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; XP_012054697.1; XM_012199307.1.
DR AlphaFoldDB; A0A158NAY9; -.
DR STRING; 12957.A0A158NAY9; -.
DR EnsemblMetazoa; XM_012199307.1; XP_012054697.1; LOC105617753.
DR GeneID; 105617753; -.
DR KEGG; acep:105617753; -.
DR InParanoid; A0A158NAY9; -.
DR OrthoDB; 2896660at2759; -.
DR Proteomes; UP000005205; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0008146; F:sulfotransferase activity; IEA:InterPro.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR InterPro; IPR010635; Heparan_SO4-6-sulfoTrfase.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR005331; Sulfotransferase.
DR PANTHER; PTHR12812; HEPARAN SULFATE 6-O-SULFOTRANSFERASE 3; 1.
DR PANTHER; PTHR12812:SF0; HEPARAN-SULFATE 6-O-SULFOTRANSFERASE; 1.
DR Pfam; PF03567; Sulfotransfer_2; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
PE 3: Inferred from homology;
KW Membrane {ECO:0000256|RuleBase:RU364122};
KW Reference proteome {ECO:0000313|Proteomes:UP000005205};
KW Signal-anchor {ECO:0000256|RuleBase:RU364122};
KW Transferase {ECO:0000256|RuleBase:RU364122};
KW Transmembrane {ECO:0000256|RuleBase:RU364122};
KW Transmembrane helix {ECO:0000256|RuleBase:RU364122}.
FT TRANSMEM 60..80
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU364122"
FT REGION 25..54
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 26..53
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 475 AA; 54609 MW; 145E488A8E42349E CRC64;
MGRRTGIDAE IDATISELEV LVASETQQGE KEDEGEGKEN IYDGRSTTRM ESRHPRKNRL
RSIVGICLFL ALTGIIYLGY FCPDHVCALT NREIRESIGL SESLSIAHGS PVAGSVALSS
VSIELDRNGL LSVHPAFKLQ SIQGSLGYDD IFANDTFQFD INAHDVMVFL HIQKTGGTLF
GKHLVRDLEL QRPCSCQRRR KRCFCFRPNH NENWLFSRYS TGWKCGLHAD WTELTNCVDT
ELNKIEGDEI KRRYFYITII RDPVARYLSE FRHVQRGATW RGARHWCGGT QANIPQCYDG
PNWKGVTLEE FMECPYNLAR NRQTRMLADL SIVGCYNSTL SKTDKERLIL ASAKHNLQFM
PFFMLTEYQK VGQYTFEETF KMRFAVAFEQ HNATLSAATM ATLSTEQLDA VRKLNSLDLE
LYEFAKNLAF QRFKRLRDRD PHFVQRFQHL GELPLRQSAT EFNWDSVIED TTDNE
//
