ID A0A2K6D412_MACNE Unreviewed; 609 AA.
AC A0A2K6D412;
DT 28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT 28-MAR-2018, sequence version 1.
DT 24-JAN-2024, entry version 27.
DE RecName: Full=Heparan-sulfate 6-O-sulfotransferase {ECO:0000256|RuleBase:RU364122};
DE EC=2.8.2.- {ECO:0000256|RuleBase:RU364122};
GN Name=HS6ST2 {ECO:0000313|Ensembl:ENSMNEP00000030647.1};
OS Macaca nemestrina (Pig-tailed macaque).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Cercopithecinae; Macaca.
OX NCBI_TaxID=9545 {ECO:0000313|Ensembl:ENSMNEP00000030647.1, ECO:0000313|Proteomes:UP000233120};
RN [1] {ECO:0000313|Ensembl:ENSMNEP00000030647.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) 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|ARBA:ARBA00004606,
CC ECO:0000256|RuleBase:RU364122}; Single-pass type II membrane protein
CC {ECO:0000256|ARBA:ARBA00004606, ECO:0000256|RuleBase:RU364122}.
CC -!- SIMILARITY: Belongs to the sulfotransferase 6 family.
CC {ECO:0000256|ARBA:ARBA00010109, ECO:0000256|RuleBase:RU364122}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR RefSeq; XP_011739329.1; XM_011741027.1.
DR AlphaFoldDB; A0A2K6D412; -.
DR Ensembl; ENSMNET00000055065.1; ENSMNEP00000030647.1; ENSMNEG00000038761.1.
DR GeneID; 105481428; -.
DR CTD; 90161; -.
DR GeneTree; ENSGT00950000183071; -.
DR OrthoDB; 2896660at2759; -.
DR Proteomes; UP000233120; Unplaced.
DR Bgee; ENSMNEG00000038761; Expressed in adult mammalian kidney and 3 other cell types or tissues.
DR GO; GO:0005794; C:Golgi apparatus; IEA:UniProt.
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:SF6; HEPARAN-SULFATE 6-O-SULFOTRANSFERASE 2; 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:UP000233120};
KW Signal-anchor {ECO:0000256|ARBA:ARBA00022968,
KW 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 154..172
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU364122"
FT REGION 12..66
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 530..557
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 570..609
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 570..602
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 609 AA; 69586 MW; 102EB5A3BCFB510B CRC64;
MALPACAVRA FEPPRQPERG APARTTCPRR HSRVEAELAA SRPGSVAASV RADPPRGVSH
GFHSRPLLDK PRKASSSLAG AACAPLFALL SRGRRRRMHV LRRRWDLGSL CRVLLTRGLA
ALGHSLKHVL GAIFSKIFGP LASVGNMDEK SNKLLLALVM LFLFAVIVLQ YVCPGTECQL
LRLQAFSSPV RDPYRSEDES SARFVPRYNF TRGDLLRKVD FDIKGDDLIV FLHIQKTGGT
TFGRHLVRNI QLEQPCECRV GQKKCTCHRP GKRETWLFSR FSTGWSCGLH ADWTELTSCV
PSVVDGKRDA RLRPSRNFHY ITILRDPVSR YLSEWRHVQR GATWKASLHV CDGRPPTSEE
LPSCYTGDDW SGCPLKEFMD CPYNLANNRQ VRMLSDLTLV GCYNLSVMPE KQRNKVLLES
AKSNLKHMAF FGLTEFQRKT QYLFEKTFNM NFISPFTQYN TTRASSVEIN EEIQKRIEGL
NFLDMELYSY AKDLFLQRYQ FMRQKEHQEA RRKRQEQRKF LKGRLLQTHF QSQGQGQSQN
PNQNQSQNPN PNANQNLTQN LTQNLMQNLT QSSRQKENQE SLKQNSGKEQ NGNTSNGTND
YIGSVEKWR
//