ID H0WDB1_CAVPO Unreviewed; 650 AA.
AC H0WDB1;
DT 22-FEB-2012, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 2.
DT 27-MAR-2024, entry version 58.
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:ENSCPOP00000020983.2};
OS Cavia porcellus (Guinea pig).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Hystricomorpha; Caviidae;
OC Cavia.
OX NCBI_TaxID=10141 {ECO:0000313|Ensembl:ENSCPOP00000020983.2, ECO:0000313|Proteomes:UP000005447};
RN [1] {ECO:0000313|Proteomes:UP000005447}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=2N {ECO:0000313|Proteomes:UP000005447};
RX PubMed=21993624; DOI=10.1038/nature10530;
RA Lindblad-Toh K., Garber M., Zuk O., Lin M.F., Parker B.J., Washietl S.,
RA Kheradpour P., Ernst J., Jordan G., Mauceli E., Ward L.D., Lowe C.B.,
RA Holloway A.K., Clamp M., Gnerre S., Alfoldi J., Beal K., Chang J.,
RA Clawson H., Cuff J., Di Palma F., Fitzgerald S., Flicek P., Guttman M.,
RA Hubisz M.J., Jaffe D.B., Jungreis I., Kent W.J., Kostka D., Lara M.,
RA Martins A.L., Massingham T., Moltke I., Raney B.J., Rasmussen M.D.,
RA Robinson J., Stark A., Vilella A.J., Wen J., Xie X., Zody M.C., Baldwin J.,
RA Bloom T., Chin C.W., Heiman D., Nicol R., Nusbaum C., Young S.,
RA Wilkinson J., Worley K.C., Kovar C.L., Muzny D.M., Gibbs R.A., Cree A.,
RA Dihn H.H., Fowler G., Jhangiani S., Joshi V., Lee S., Lewis L.R.,
RA Nazareth L.V., Okwuonu G., Santibanez J., Warren W.C., Mardis E.R.,
RA Weinstock G.M., Wilson R.K., Delehaunty K., Dooling D., Fronik C.,
RA Fulton L., Fulton B., Graves T., Minx P., Sodergren E., Birney E.,
RA Margulies E.H., Herrero J., Green E.D., Haussler D., Siepel A., Goldman N.,
RA Pollard K.S., Pedersen J.S., Lander E.S., Kellis M.;
RT "A high-resolution map of human evolutionary constraint using 29 mammals.";
RL Nature 478:476-482(2011).
RN [2] {ECO:0000313|Ensembl:ENSCPOP00000020983.2}
RP IDENTIFICATION.
RC STRAIN=2N {ECO:0000313|Ensembl:ENSCPOP00000020983.2};
RG Ensembl;
RL Submitted (NOV-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 EMBL; AAKN02053325; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AAKN02053326; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; H0WDB1; -.
DR STRING; 10141.ENSCPOP00000020983; -.
DR Ensembl; ENSCPOT00000019646.2; ENSCPOP00000020983.2; ENSCPOG00000021403.2.
DR VEuPathDB; HostDB:ENSCPOG00000021403; -.
DR eggNOG; KOG3955; Eukaryota.
DR GeneTree; ENSGT00950000183071; -.
DR HOGENOM; CLU_027877_3_0_1; -.
DR InParanoid; H0WDB1; -.
DR OMA; WWDLDEN; -.
DR TreeFam; TF312835; -.
DR Proteomes; UP000005447; Unassembled WGS sequence.
DR Bgee; ENSCPOG00000021403; Expressed in ovary and 11 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:UP000005447};
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 1..28
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 328..352
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 568..594
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 608..650
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 330..352
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 608..643
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 650 AA; 73775 MW; 49165B1C3184C010 CRC64;
MALPACAARA LGPPLQPEHG APARTTCPRR HSRVEAELAA SRPGSVSASV RAGPPRGVSH
GFNSRQLLDE PLKASASLAG ALRAPLFALL PRGRRRRMND LRRRWDLGSL CRALLTRGLA
ALGHSLKHVL SAIFSKIFGP LASVGNMDEK SNKLLLALVM FFLFAVIVLQ YVCPGTECQL
LRLQAFSSPL PDPYRSEDES SARFVPRYNF SRGDLLRKVD FDINGDDLIV FLHIQKTGGT
TFGRHLVRNI QLEQPCECRV GQKKCTCHRP GKRETWLFSR FSTGWSCGLH ADWTELTSCV
PAVVDGKRDA RLRPSRWRIF QILDAASKDR RGSPNTNPGA NSPSTKTRNT SKSGKNFHYI
TILRDPVSRY LSEWRHVQRG ATWKASLHVC DGRPPTSEEL PSCYTGDDWS GCPLKEFMDC
PYNLANNRQV RMLSDLTLVG CYNLSVMPEK QRNKVLLESA KSNLKHMAFF GLTEFQRKTQ
YLFEKTFNMN FISPFTQYNT TRASSVEINE DIQKRIERLN FLDMELYSYA KDLFLQRYQF
MRQKEHQEAR RKRQEQRKFL KGRFLQTHFQ SQSQSQSQNP SQNQSQNPNP NANQSLTQNL
IQNLTQNSSQ NLSQKENRSN QKQSPGHKQN DSSSGSSGTN DYIGSVEKWR
//