GenomeNet

Database: UniProt
Entry: A0A2K5KXF2_CERAT
LinkDB: A0A2K5KXF2_CERAT
Original site: A0A2K5KXF2_CERAT 
ID   A0A2K5KXF2_CERAT        Unreviewed;       645 AA.
AC   A0A2K5KXF2;
DT   28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT   28-MAR-2018, sequence version 1.
DT   27-MAR-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=HS6ST2 {ECO:0000313|Ensembl:ENSCATP00000005376.1};
OS   Cercocebus atys (Sooty mangabey) (Cercocebus torquatus atys).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC   Cercopithecidae; Cercopithecinae; Cercocebus.
OX   NCBI_TaxID=9531 {ECO:0000313|Ensembl:ENSCATP00000005376.1, ECO:0000313|Proteomes:UP000233060};
RN   [1] {ECO:0000313|Ensembl:ENSCATP00000005376.1}
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_011916421.1; XM_012061031.1.
DR   AlphaFoldDB; A0A2K5KXF2; -.
DR   STRING; 9531.ENSCATP00000005376; -.
DR   Ensembl; ENSCATT00000020261.1; ENSCATP00000005376.1; ENSCATG00000017649.1.
DR   GeneID; 105586246; -.
DR   KEGG; caty:105586246; -.
DR   CTD; 90161; -.
DR   GeneTree; ENSGT00950000183071; -.
DR   OMA; WWDLDEN; -.
DR   OrthoDB; 2896660at2759; -.
DR   Proteomes; UP000233060; Unplaced.
DR   Bgee; ENSCATG00000017649; Expressed in frontal cortex and 5 other cell types or tissues.
DR   GO; GO:0005794; C:Golgi apparatus; IEA:Ensembl.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0017095; F:heparan sulfate 6-O-sulfotransferase activity; IEA:Ensembl.
DR   GO; GO:0015012; P:heparan sulfate proteoglycan biosynthetic process; IEA:Ensembl.
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:UP000233060};
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        154..172
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU364122"
FT   REGION          9..66
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          328..353
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          570..645
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        330..353
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        570..611
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        621..638
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   645 AA;  73361 MW;  60C6F75EA4E924AE CRC64;
     MALPACAVRA FEPPRQPERG APARTTCPRR HSRVEAELAA SRPGSVAASV RAGPPRGVSH
     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 RLRPSRWRIF QILDAASKDK RGSPNTNAGA NSPSSTKTRN TSKSGKNFHY
     ITILRDPVSR YLSEWRHVQR GATWKASLHV CDGRPPTSEE LPSCYTGDDW SGCPLKEFMD
     CPYNLANNRQ VRMLSDLTLV GCYNLSVMPE KQRNKVLLES AKSNLKHMAF FGLTEFQRKT
     QYLFEKTFNM NFISPFTQYN TTRASSVEIN EEIQKRIEGL NFLDMELYSY AKDLFLQRYQ
     FMRQKEHQEA RRKRQEQRKF LKGRLLQTHF QSQGQGQSQN PNQNQSQNPN PNANQNLTQN
     LMQNLTQSSR QKENRESLKQ NSGKEQNGNT SNGTNDYIGS VEKWR
//
DBGET integrated database retrieval system