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Heparan sulfate glucosamine 3-O-sulfotransferase 5 (EC 2.8.2.23) (Heparan sulfate D-glucosaminyl 3-O-sulfotransferase 5) (3-OST-5) (Heparan sulfate 3-O-sulfotransferase 5) (h3-OST-5)

 HS3S5_HUMAN             Reviewed;         346 AA.
Q8IZT8; A8K1J2; Q52LI2; Q8N285;
15-MAR-2005, integrated into UniProtKB/Swiss-Prot.
01-MAR-2003, sequence version 1.
28-FEB-2018, entry version 132.
RecName: Full=Heparan sulfate glucosamine 3-O-sulfotransferase 5;
EC=2.8.2.23;
AltName: Full=Heparan sulfate D-glucosaminyl 3-O-sulfotransferase 5;
Short=3-OST-5;
Short=Heparan sulfate 3-O-sulfotransferase 5;
Short=h3-OST-5;
Name=HS3ST5; Synonyms=3OST5, HS3OST5;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, CHARACTERIZATION, AND
FUNCTION IN HSV-1 ENTRY.
TISSUE=Placenta;
PubMed=12138164; DOI=10.1074/jbc.M204209200;
Xia G., Chen J., Tiwari V., Ju W., Li J.-P., Malmstroem A., Shukla D.,
Liu J.;
"Heparan sulfate 3-O-sulfotransferase isoform 5 generates both an
antithrombin-binding site and an entry receptor for herpes simplex
virus, type 1.";
J. Biol. Chem. 277:37912-37919(2002).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Caudate nucleus, and Corpus callosum;
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Brain;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[5]
CHARACTERIZATION, AND TISSUE SPECIFICITY.
PubMed=12740361; DOI=10.1074/jbc.M301861200;
Mochizuki H., Yoshida K., Gotoh M., Sugioka S., Kikuchi N.,
Kwon Y.-D., Tawada A., Maeyama K., Inaba N., Hiruma T., Kimata K.,
Narimatsu H.;
"Characterization of a heparan sulfate 3-O-sulfotransferase-5, an
enzyme synthesizing a tetrasulfated disaccharide.";
J. Biol. Chem. 278:26780-26787(2003).
[6]
CHARACTERIZATION.
PubMed=15026143; DOI=10.1016/j.bbagen.2003.12.010;
Duncan M.B., Chen J., Krise J.P., Liu J.;
"The biosynthesis of anticoagulant heparan sulfate by the heparan
sulfate 3-O-sulfotransferase isoform 5.";
Biochim. Biophys. Acta 1671:34-43(2004).
[7]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21406692; DOI=10.1126/scisignal.2001570;
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
Blagoev B.;
"System-wide temporal characterization of the proteome and
phosphoproteome of human embryonic stem cell differentiation.";
Sci. Signal. 4:RS3-RS3(2011).
[8]
X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 88-346 IN COMPLEX WITH
ADENOSINE-3'-5'-DIPHOSPHATE, CATALYTIC ACTIVITY, AND MUTAGENESIS OF
ARG-99; ARG-104; LYS-155; GLN-195; LYS-309 AND ARG-311.
PubMed=18223645; DOI=10.1038/nchembio.66;
Xu D., Moon A.F., Song D., Pedersen L.C., Liu J.;
"Engineering sulfotransferases to modify heparan sulfate.";
Nat. Chem. Biol. 4:200-202(2008).
-!- FUNCTION: Sulfotransferase that utilizes 3'-phospho-5'-adenylyl
sulfate (PAPS) to catalyze the transfer of a sulfo group to
position 3 of glucosamine residues in heparan. Catalyzes the rate
limiting step in the biosynthesis of heparan sulfate (HSact). This
modification is a crucial step in the biosynthesis of
anticoagulant heparan sulfate as it completes the structure of the
antithrombin pentasaccharide binding site. Also generates GlcUA-
GlcNS or IdoUA-GlcNS and IdoUA2S-GlcNH2. The substrate-specific O-
sulfation generates an enzyme-modified heparan sulfate which acts
as a binding receptor to Herpes simplex virus-1 (HSV-1) and
permits its entry. {ECO:0000269|PubMed:12138164}.
-!- CATALYTIC ACTIVITY: 3'-phosphoadenylyl sulfate + [heparan
sulfate]-glucosamine = adenosine 3',5'-bisphosphate + [heparan
sulfate]-glucosamine 3-sulfate. {ECO:0000269|PubMed:18223645}.
-!- SUBCELLULAR LOCATION: Golgi apparatus membrane {ECO:0000305};
Single-pass type II membrane protein {ECO:0000305}.
-!- TISSUE SPECIFICITY: Highly expressed in skeletal muscle and fetal
brain, and also found in adult brain, spinal cord, cerebellum and
colon. {ECO:0000269|PubMed:12138164, ECO:0000269|PubMed:12740361}.
-!- SIMILARITY: Belongs to the sulfotransferase 1 family.
{ECO:0000305}.
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EMBL; AF503292; AAN37737.1; -; mRNA.
EMBL; AK091074; -; NOT_ANNOTATED_CDS; mRNA.
EMBL; AK289907; BAF82596.1; -; mRNA.
EMBL; CH471051; EAW48251.1; -; Genomic_DNA.
EMBL; BC093911; AAH93911.1; -; mRNA.
EMBL; BC093913; AAH93913.1; -; mRNA.
CCDS; CCDS34517.1; -.
RefSeq; NP_705840.2; NM_153612.3.
RefSeq; XP_006715442.1; XM_006715379.2.
RefSeq; XP_011533890.1; XM_011535588.2.
RefSeq; XP_016865959.1; XM_017010470.1.
RefSeq; XP_016865960.1; XM_017010471.1.
RefSeq; XP_016865961.1; XM_017010472.1.
RefSeq; XP_016865962.1; XM_017010473.1.
RefSeq; XP_016865963.1; XM_017010474.1.
UniGene; Hs.645477; -.
PDB; 3BD9; X-ray; 2.30 A; A=88-346.
PDBsum; 3BD9; -.
ProteinModelPortal; Q8IZT8; -.
SMR; Q8IZT8; -.
STRING; 9606.ENSP00000427888; -.
iPTMnet; Q8IZT8; -.
PhosphoSitePlus; Q8IZT8; -.
BioMuta; HS3ST5; -.
DMDM; 61214369; -.
PaxDb; Q8IZT8; -.
PRIDE; Q8IZT8; -.
Ensembl; ENST00000312719; ENSP00000427888; ENSG00000249853.
Ensembl; ENST00000411826; ENSP00000440332; ENSG00000249853.
GeneID; 222537; -.
KEGG; hsa:222537; -.
UCSC; uc003pwg.4; human.
CTD; 222537; -.
DisGeNET; 222537; -.
EuPathDB; HostDB:ENSG00000249853.7; -.
GeneCards; HS3ST5; -.
HGNC; HGNC:19419; HS3ST5.
HPA; HPA021823; -.
HPA; HPA064677; -.
MIM; 609407; gene.
neXtProt; NX_Q8IZT8; -.
OpenTargets; ENSG00000249853; -.
PharmGKB; PA164741639; -.
eggNOG; KOG3704; Eukaryota.
eggNOG; ENOG410XS59; LUCA.
GeneTree; ENSGT00760000119023; -.
HOGENOM; HOG000036663; -.
HOVERGEN; HBG053377; -.
InParanoid; Q8IZT8; -.
KO; K08104; -.
OMA; FDRDDNY; -.
OrthoDB; EOG091G0CS5; -.
PhylomeDB; Q8IZT8; -.
TreeFam; TF350755; -.
Reactome; R-HSA-2022928; HS-GAG biosynthesis.
ChiTaRS; HS3ST5; human.
EvolutionaryTrace; Q8IZT8; -.
GenomeRNAi; 222537; -.
PRO; PR:Q8IZT8; -.
Proteomes; UP000005640; Chromosome 6.
Bgee; ENSG00000249853; -.
CleanEx; HS_HS3ST5; -.
Genevisible; Q8IZT8; HS.
GO; GO:0000139; C:Golgi membrane; TAS:Reactome.
GO; GO:0016021; C:integral component of membrane; NAS:UniProtKB.
GO; GO:0050656; F:3'-phosphoadenosine 5'-phosphosulfate binding; NAS:UniProtKB.
GO; GO:0008467; F:[heparan sulfate]-glucosamine 3-sulfotransferase 1 activity; IDA:UniProtKB.
GO; GO:0006024; P:glycosaminoglycan biosynthetic process; TAS:Reactome.
GO; GO:0015015; P:heparan sulfate proteoglycan biosynthetic process, enzymatic modification; IDA:UniProtKB.
GO; GO:0050819; P:negative regulation of coagulation; IDA:UniProtKB.
GO; GO:0006477; P:protein sulfation; IDA:UniProtKB.
GO; GO:0046596; P:regulation of viral entry into host cell; IDA:UniProtKB.
InterPro; IPR037359; NST/OST.
InterPro; IPR027417; P-loop_NTPase.
InterPro; IPR000863; Sulfotransferase_dom.
PANTHER; PTHR10605; PTHR10605; 1.
Pfam; PF00685; Sulfotransfer_1; 1.
SUPFAM; SSF52540; SSF52540; 1.
1: Evidence at protein level;
3D-structure; Complete proteome; Disulfide bond; Glycoprotein;
Golgi apparatus; Membrane; Polymorphism; Reference proteome;
Signal-anchor; Transferase; Transmembrane; Transmembrane helix.
CHAIN 1 346 Heparan sulfate glucosamine 3-O-
sulfotransferase 5.
/FTId=PRO_0000085222.
TOPO_DOM 1 12 Cytoplasmic. {ECO:0000255}.
TRANSMEM 13 32 Helical; Signal-anchor for type II
membrane protein. {ECO:0000255}.
TOPO_DOM 33 346 Lumenal. {ECO:0000255}.
NP_BIND 100 104 PAPS. {ECO:0000250}.
NP_BIND 309 313 PAPS. {ECO:0000250}.
REGION 122 128 Substrate binding. {ECO:0000250}.
REGION 155 158 Substrate binding. {ECO:0000250}.
REGION 226 227 Substrate binding. {ECO:0000250}.
BINDING 183 183 PAPS. {ECO:0000250}.
BINDING 191 191 PAPS. {ECO:0000250}.
BINDING 293 293 PAPS. {ECO:0000250}.
CARBOHYD 287 287 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 294 304 {ECO:0000250}.
VARIANT 247 247 I -> N (in dbSNP:rs17793043).
/FTId=VAR_052531.
MUTAGEN 99 99 R->A: Reduces enzyme activity by over
99%. {ECO:0000269|PubMed:18223645}.
MUTAGEN 104 104 R->A: Reduces enzyme activity by 93%,.
{ECO:0000269|PubMed:18223645}.
MUTAGEN 155 155 K->A: Reduces enzyme activity by over
99%. {ECO:0000269|PubMed:18223645}.
MUTAGEN 195 195 Q->A: Reduces enzyme activity by over
99%. {ECO:0000269|PubMed:18223645}.
MUTAGEN 309 309 K->A: Loss of enzyme activity.
{ECO:0000269|PubMed:18223645}.
MUTAGEN 311 311 R->A: Reduces enzyme activity by 98%.
{ECO:0000269|PubMed:18223645}.
STRAND 92 97 {ECO:0000244|PDB:3BD9}.
HELIX 103 110 {ECO:0000244|PDB:3BD9}.
STRAND 116 118 {ECO:0000244|PDB:3BD9}.
HELIX 129 133 {ECO:0000244|PDB:3BD9}.
HELIX 136 140 {ECO:0000244|PDB:3BD9}.
STRAND 151 155 {ECO:0000244|PDB:3BD9}.
HELIX 157 160 {ECO:0000244|PDB:3BD9}.
HELIX 165 172 {ECO:0000244|PDB:3BD9}.
STRAND 177 182 {ECO:0000244|PDB:3BD9}.
HELIX 185 202 {ECO:0000244|PDB:3BD9}.
HELIX 210 214 {ECO:0000244|PDB:3BD9}.
TURN 217 219 {ECO:0000244|PDB:3BD9}.
HELIX 227 231 {ECO:0000244|PDB:3BD9}.
HELIX 234 242 {ECO:0000244|PDB:3BD9}.
HELIX 247 249 {ECO:0000244|PDB:3BD9}.
STRAND 250 254 {ECO:0000244|PDB:3BD9}.
HELIX 255 260 {ECO:0000244|PDB:3BD9}.
HELIX 262 272 {ECO:0000244|PDB:3BD9}.
HELIX 281 283 {ECO:0000244|PDB:3BD9}.
STRAND 284 287 {ECO:0000244|PDB:3BD9}.
TURN 288 291 {ECO:0000244|PDB:3BD9}.
STRAND 292 296 {ECO:0000244|PDB:3BD9}.
STRAND 298 300 {ECO:0000244|PDB:3BD9}.
HELIX 318 339 {ECO:0000244|PDB:3BD9}.
SEQUENCE 346 AA; 40408 MW; C763F70793FDB156 CRC64;
MLFKQQAWLR QKLLVLGSLA VGSLLYLVAR VGSLDRLQPI CPIEGRLGGA RTQAEFPLRA
LQFKRGLLHE FRKGNASKEQ VRLHDLVQQL PKAIIIGVRK GGTRALLEML NLHPAVVKAS
QEIHFFDNDE NYGKGIEWYR KKMPFSYPQQ ITIEKSPAYF ITEEVPERIY KMNSSIKLLI
IVREPTTRAI SDYTQVLEGK ERKNKTYYKF EKLAIDPNTC EVNTKYKAVR TSIYTKHLER
WLKYFPIEQF HVVDGDRLIT EPLPELQLVE KFLNLPPRIS QYNLYFNATR GFYCLRFNII
FNKCLAGSKG RIHPEVDPSV ITKLRKFFHP FNQKFYQITG RTLNWP


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