ID   A0A1W2PQ14_HUMAN        Unreviewed;       277 AA.
AC   A0A1W2PQ14;
DT   07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT   07-JUN-2017, sequence version 1.
DT   16-JAN-2019, entry version 12.
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:ENSP00000491722};
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC   Catarrhini; Hominidae; Homo.
OX   NCBI_TaxID=9606 {ECO:0000313|Ensembl:ENSP00000491722, ECO:0000313|Proteomes:UP000005640};
RN   [1] {ECO:0000313|Ensembl:ENSP00000491722, ECO:0000313|Proteomes:UP000005640}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=15772651; DOI=10.1038/nature03440;
RA   Ross M.T., Grafham D.V., Coffey A.J., Scherer S., McLay K., Muzny D.,
RA   Platzer M., Howell G.R., Burrows C., Bird C.P., Frankish A.,
RA   Lovell F.L., Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G.,
RA   Jones M.C., Hurles M.E., Andrews T.D., Scott C.E., Searle S.,
RA   Ramser J., Whittaker A., Deadman R., Carter N.P., Hunt S.E., Chen R.,
RA   Cree A., Gunaratne P., Havlak P., Hodgson A., Metzker M.L.,
RA   Richards S., Scott G., Steffen D., Sodergren E., Wheeler D.A.,
RA   Worley K.C., Ainscough R., Ambrose K.D., Ansari-Lari M.A., Aradhya S.,
RA   Ashwell R.I., Babbage A.K., Bagguley C.L., Ballabio A., Banerjee R.,
RA   Barker G.E., Barlow K.F., Barrett I.P., Bates K.N., Beare D.M.,
RA   Beasley H., Beasley O., Beck A., Bethel G., Blechschmidt K., Brady N.,
RA   Bray-Allen S., Bridgeman A.M., Brown A.J., Brown M.J., Bonnin D.,
RA   Bruford E.A., Buhay C., Burch P., Burford D., Burgess J., Burrill W.,
RA   Burton J., Bye J.M., Carder C., Carrel L., Chako J., Chapman J.C.,
RA   Chavez D., Chen E., Chen G., Chen Y., Chen Z., Chinault C.,
RA   Ciccodicola A., Clark S.Y., Clarke G., Clee C.M., Clegg S.,
RA   Clerc-Blankenburg K., Clifford K., Cobley V., Cole C.G., Conquer J.S.,
RA   Corby N., Connor R.E., David R., Davies J., Davis C., Davis J.,
RA   Delgado O., Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S.,
RA   Draper H., Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I.,
RA   Eades T., Ellwood M., Emery-Cohen A., Errington H., Evans K.L.,
RA   Faulkner L., Francis F., Frankland J., Fraser A.E., Galgoczy P.,
RA   Gilbert J., Gill R., Gloeckner G., Gregory S.G., Gribble S.,
RA   Griffiths C., Grocock R., Gu Y., Gwilliam R., Hamilton C., Hart E.A.,
RA   Hawes A., Heath P.D., Heitmann K., Hennig S., Hernandez J.,
RA   Hinzmann B., Ho S., Hoffs M., Howden P.J., Huckle E.J., Hume J.,
RA   Hunt P.J., Hunt A.R., Isherwood J., Jacob L., Johnson D., Jones S.,
RA   de Jong P.J., Joseph S.S., Keenan S., Kelly S., Kershaw J.K., Khan Z.,
RA   Kioschis P., Klages S., Knights A.J., Kosiura A., Kovar-Smith C.,
RA   Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L., Liu W.,
RA   Lloyd C., Lloyd D.M., Loulseged H., Loveland J.E., Lovell J.D.,
RA   Lozado R., Lu J., Lyne R., Ma J., Maheshwari M., Matthews L.H.,
RA   McDowall J., McLaren S., McMurray A., Meidl P., Meitinger T.,
RA   Milne S., Miner G., Mistry S.L., Morgan M., Morris S., Mueller I.,
RA   Mullikin J.C., Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N.,
RA   Okwuonu G., Palmer S., Pandian R., Parker D., Parrish J.,
RA   Pasternak S., Patel D., Pearce A.V., Pearson D.M., Pelan S.E.,
RA   Perez L., Porter K.M., Ramsey Y., Reichwald K., Rhodes S.,
RA   Ridler K.A., Schlessinger D., Schueler M.G., Sehra H.K.,
RA   Shaw-Smith C., Shen H., Sheridan E.M., Shownkeen R., Skuce C.D.,
RA   Smith M.L., Sotheran E.C., Steingruber H.E., Steward C.A., Storey R.,
RA   Swann R.M., Swarbreck D., Tabor P.E., Taudien S., Taylor T.,
RA   Teague B., Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S.,
RA   Tromans A.C., d'Urso M., Verduzco D., Villasana D., Waldron L.,
RA   Wall M., Wang Q., Warren J., Warry G.L., Wei X., West A.,
RA   Whitehead S.L., Whiteley M.N., Wilkinson J.E., Willey D.L.,
RA   Williams G., Williams L., Williamson A., Williamson H., Wilming L.,
RA   Woodmansey R.L., Wray P.W., Yen J., Zhang J., Zhou J., Zoghbi H.,
RA   Zorilla S., Buck D., Reinhardt R., Poustka A., Rosenthal A.,
RA   Lehrach H., Meindl A., Minx P.J., Hillier L.W., Willard H.F.,
RA   Wilson R.K., Waterston R.H., Rice C.M., Vaudin M., Coulson A.,
RA   Nelson D.L., Weinstock G., Sulston J.E., Durbin R.M., Hubbard T.,
RA   Gibbs R.A., Beck S., Rogers J., Bentley D.R.;
RT   "The DNA sequence of the human X chromosome.";
RL   Nature 434:325-337(2005).
RN   [2] {ECO:0000313|Ensembl:ENSP00000491722}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (APR-2017) to UniProtKB.
CC   -!- FUNCTION: 6-O-sulfation enzyme which catalyzes the transfer of
CC       sulfate from 3'-phosphoadenosine 5'-phosphosulfate (PAPS) to
CC       position 6 of the N-sulfoglucosamine residue (GlcNS) of heparan
CC       sulfate. {ECO:0000256|RuleBase:RU364122}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=3'-phosphoadenylyl sulfate + alpha-D-glucosaminyl-
CC         [heparan sulfate](n) = 6-sulfo-alpha-D-glucosaminyl-[heparan
CC         sulfate](n) + adenosine 3',5'-bisphosphate + H(+);
CC         Xref=Rhea:RHEA:56604, Rhea:RHEA-COMP:9830, Rhea:RHEA-COMP:14621,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:58339, ChEBI:CHEBI:58343,
CC         ChEBI:CHEBI:58388, ChEBI:CHEBI:140604;
CC         Evidence={ECO:0000256|RuleBase:RU364122};
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|RuleBase:RU364122};
CC       Single-pass type II membrane protein
CC       {ECO:0000256|RuleBase:RU364122}.
CC   -!- SIMILARITY: Belongs to the sulfotransferase 6 family.
CC       {ECO:0000256|RuleBase:RU364122}.
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DR   EMBL; AL022159; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; KF459414; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; KF459415; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; KF459420; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; KF459421; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; Z82205; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; Z86064; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   jPOST; A0A1W2PQ14; -.
DR   PeptideAtlas; A0A1W2PQ14; -.
DR   Ensembl; ENST00000640529; ENSP00000491722; ENSG00000171004.
DR   HGNC; HGNC:19133; HS6ST2.
DR   OpenTargets; ENSG00000171004; -.
DR   GeneTree; ENSGT00940000154073; -.
DR   ChiTaRS; HS6ST2; human.
DR   Proteomes; UP000005640; Chromosome X.
DR   ExpressionAtlas; A0A1W2PQ14; baseline and differential.
DR   GO; GO:0016021; C:integral component of membrane; IEA:InterPro.
DR   GO; GO:0008146; F:sulfotransferase activity; IEA:InterPro.
DR   InterPro; IPR010635; Heparan_SO4-6-sulfoTrfase.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR005331; Sulfotransferase.
DR   PANTHER; PTHR12812; PTHR12812; 1.
DR   Pfam; PF03567; Sulfotransfer_2; 1.
DR   SUPFAM; SSF52540; SSF52540; 1.
PE   1: Evidence at protein level;
KW   Complete proteome {ECO:0000313|Proteomes:UP000005640};
KW   Membrane {ECO:0000256|RuleBase:RU364122};
KW   Proteomics identification {ECO:0000213|MaxQB:A0A1W2PQ14,
KW   ECO:0000213|PeptideAtlas:A0A1W2PQ14};
KW   Reference proteome {ECO:0000313|Proteomes:UP000005640};
KW   Signal {ECO:0000256|SAM:SignalP};
KW   Signal-anchor {ECO:0000256|RuleBase:RU364122};
KW   Transferase {ECO:0000256|RuleBase:RU364122};
KW   Transmembrane {ECO:0000256|RuleBase:RU364122}.
FT   SIGNAL        1     19       {ECO:0000256|SAM:SignalP}.
FT   CHAIN        20    277       Heparan-sulfate 6-O-sulfotransferase.
FT                                {ECO:0000256|SAM:SignalP}.
FT                                /FTId=PRO_5012529238.
SQ   SEQUENCE   277 AA;  31771 MW;  EEF8E7BC15D9D79D CRC64;
     MLFLFAVIVL QYVCPGTECQ LLRLQAFSSP VPDPYRSEDE SSARFVPRYN FTRGDLLRKV
     DFDIKGDDLI VFLHIQKTGG TTFGRHLVRN IQLEQPCECR VGQKKCTCHR PGKRETWLFS
     RFSTGWSCGL HADWTELTRC VPHIWNWEQS FSISYNRWRI FQILDAASKD KRGSPNTNAG
     ANSPSSTKTR NTSKSGKNFH YITILRDPVS RYLSEWRHVQ RGATWKASLH VCDGRPPTSE
     ELPSCYTGDD WSGCPLKEFM DCPYNLANNR QCACSPT
//