ID A0A2I2Z9A8_GORGO Unreviewed; 607 AA.
AC A0A2I2Z9A8;
DT 28-FEB-2018, integrated into UniProtKB/TrEMBL.
DT 28-FEB-2018, sequence version 1.
DT 27-MAR-2024, entry version 29.
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:ENSGGOP00000043686.1};
OS Gorilla gorilla gorilla (Western lowland gorilla).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Gorilla.
OX NCBI_TaxID=9595 {ECO:0000313|Ensembl:ENSGGOP00000043686.1, ECO:0000313|Proteomes:UP000001519};
RN [1] {ECO:0000313|Ensembl:ENSGGOP00000043686.1, ECO:0000313|Proteomes:UP000001519}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Scally A.;
RT "Insights into the evolution of the great apes provided by the gorilla
RT genome.";
RL Submitted (MAY-2011) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSGGOP00000043686.1, ECO:0000313|Proteomes:UP000001519}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=22398555; DOI=10.1038/nature10842;
RA Scally A., Dutheil J.Y., Hillier L.W., Jordan G.E., Goodhead I.,
RA Herrero J., Hobolth A., Lappalainen T., Mailund T., Marques-Bonet T.,
RA McCarthy S., Montgomery S.H., Schwalie P.C., Tang Y.A., Ward M.C., Xue Y.,
RA Yngvadottir B., Alkan C., Andersen L.N., Ayub Q., Ball E.V., Beal K.,
RA Bradley B.J., Chen Y., Clee C.M., Fitzgerald S., Graves T.A., Gu Y.,
RA Heath P., Heger A., Karakoc E., Kolb-Kokocinski A., Laird G.K., Lunter G.,
RA Meader S., Mort M., Mullikin J.C., Munch K., O'Connor T.D., Phillips A.D.,
RA Prado-Martinez J., Rogers A.S., Sajjadian S., Schmidt D., Shaw K.,
RA Simpson J.T., Stenson P.D., Turner D.J., Vigilant L., Vilella A.J.,
RA Whitener W., Zhu B., Cooper D.N., de Jong P., Dermitzakis E.T.,
RA Eichler E.E., Flicek P., Goldman N., Mundy N.I., Ning Z., Odom D.T.,
RA Ponting C.P., Quail M.A., Ryder O.A., Searle S.M., Warren W.C.,
RA Wilson R.K., Schierup M.H., Rogers J., Tyler-Smith C., Durbin R.;
RT "Insights into hominid evolution from the gorilla genome sequence.";
RL Nature 483:169-175(2012).
RN [3] {ECO:0000313|Ensembl:ENSGGOP00000043686.1}
RP IDENTIFICATION.
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}.
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DR EMBL; CABD030128380; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CABD030128381; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CABD030128382; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CABD030128383; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CABD030128384; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CABD030128385; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CABD030128386; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CABD030128387; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CABD030128388; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; XP_004064951.2; XM_004064903.2.
DR AlphaFoldDB; A0A2I2Z9A8; -.
DR Ensembl; ENSGGOT00000049816.1; ENSGGOP00000043686.1; ENSGGOG00000014140.4.
DR GeneID; 101135929; -.
DR KEGG; ggo:101135929; -.
DR CTD; 90161; -.
DR GeneTree; ENSGT00950000183071; -.
DR OrthoDB; 2896660at2759; -.
DR Proteomes; UP000001519; Chromosome X.
DR Bgee; ENSGGOG00000014140; Expressed in prefrontal cortex 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:UP000001519};
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..66
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 530..607
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 530..578
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 585..600
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 607 AA; 69298 MW; 0C76905DC7D6E3DB CRC64;
MALPACAVRA FQPPRQPERG APARTTCPRR HSRVEAELAA SRPGSVAASV RAGPPRGVSH
GFHTRPLLDK PRKASSSLAG AACAPLFALL SRGRRRRMHV LRRRWDLGSL CRALLTRGLA
ALGHSLKHVL GAIFSKIFGP LASVGNMDEK SNKLLLALVM LFLFAVIVLQ YVCPGTECQL
LRLQAFSSPV PDPYRSEDES 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
QNQNQNQSQN PNPNANQNLT QNLMQNLTQS LSQKENRESP KQNSGKEQND NTSNGTNDYI
GSVEKWR
//
