ID A0A1S3IZJ9_LINUN Unreviewed; 525 AA.
AC A0A1S3IZJ9;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 28.
DE RecName: Full=Heparan-sulfate 6-O-sulfotransferase {ECO:0000256|RuleBase:RU364122};
DE EC=2.8.2.- {ECO:0000256|RuleBase:RU364122};
GN Name=LOC106168908 {ECO:0000313|RefSeq:XP_013403620.1};
OS Lingula unguis.
OC Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Brachiopoda; Linguliformea;
OC Lingulata; Lingulida; Linguloidea; Lingulidae; Lingula.
OX NCBI_TaxID=7574 {ECO:0000313|Proteomes:UP000085678, ECO:0000313|RefSeq:XP_013403620.1};
RN [1] {ECO:0000313|RefSeq:XP_013403620.1}
RP IDENTIFICATION.
RC TISSUE=Gonads {ECO:0000313|RefSeq:XP_013403620.1};
RG RefSeq;
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|RuleBase:RU364122}; Single-
CC pass type II membrane protein {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_013403620.1; XM_013548166.2.
DR AlphaFoldDB; A0A1S3IZJ9; -.
DR STRING; 7574.A0A1S3IZJ9; -.
DR EnsemblMetazoa; XM_013548166.2; XP_013403620.1; LOC106168908.
DR GeneID; 106168908; -.
DR KEGG; lak:106168908; -.
DR InParanoid; A0A1S3IZJ9; -.
DR OrthoDB; 2896660at2759; -.
DR Proteomes; UP000085678; Unplaced.
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:SF0; HEPARAN-SULFATE 6-O-SULFOTRANSFERASE; 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:UP000085678};
KW Signal-anchor {ECO:0000256|RuleBase:RU364122};
KW Transferase {ECO:0000256|RuleBase:RU364122};
KW Transmembrane {ECO:0000256|RuleBase:RU364122}.
FT REGION 388..525
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 397..422
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 424..479
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 490..506
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 507..525
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 525 AA; 60537 MW; 684604814764E14B CRC64;
MKEKKIGKLV LGVLAILVLL GFLFMGYFCA DQTCALKPGS PTPGYLHFDV QAYLKGELPA
KVFEEKDLER DFQVDLEDGD VIVFHHMQKT GGTTFGRHLV NDLQLKHPCR KVDGRKRYDC
QNSDHHVWLF SRYSTGWRCG LHADWTELQE CVDREMDAFE GKHRTRRYHY ITMLRDPVKR
YLSEWMHVRR GATWKTAQLR CNGRQATLQE VPFCYNSSDW YGVTIEEFLA CPHNLGNNRQ
TRMLANLSAV GCYNRSLLPP DVRDKMLLES AKTNLRNMAY FGILEYQPEM QYLFEKTFHL
KFGVQFSLFN KTHITKLKMS NKTVEEIVKV NSLDVKLYQY AKELFLQRVN HARRKAAKAQ
ETISQYSNLE KSNIDYIVDS SKQVVPKKEV LSRSEENNDG SSRSGSINDK TERSQSTLDV
HVSETVPKKV KGDPDLEPGR FDGSRSEGID EPRKSNIEPQ IDKSEGDQAD SRLKSLHQEK
SLLTSKPGID GLHRESRSRQ VTGENYDDSE LDIDEEDNDD EDEVK
//
