CHST9_HUMAN
ID CHST9_HUMAN Reviewed; 443 AA.
AC Q7L1S5; Q6UX69; Q9BXH3; Q9BXH4; Q9BZW9;
DT 15-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 05-MAY-2009, sequence version 2.
DT 03-AUG-2022, entry version 146.
DE RecName: Full=Carbohydrate sulfotransferase 9;
DE EC=2.8.2.-;
DE AltName: Full=GalNAc-4-O-sulfotransferase 2;
DE Short=GalNAc-4-ST2;
DE Short=GalNAc4ST-2;
DE AltName: Full=N-acetylgalactosamine-4-O-sulfotransferase 2;
GN Name=CHST9; ORFNames=UNQ2549/PRO6175;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), ENZYME ACTIVITY, AND TISSUE
RP SPECIFICITY.
RX PubMed=11445554; DOI=10.1093/glycob/11.6.495;
RA Hiraoka N., Misra A., Belot F., Hindsgaul O., Fukuda M.;
RT "Molecular cloning and expression of two distinct human N-
RT acetylgalactosamine 4-O-sulfotransferases that transfer sulfate to GalNAc
RT beta 1->4GlcNAc beta 1->R in both N- and O-glycans.";
RL Glycobiology 11:495-504(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), ENZYME ACTIVITY, AND TISSUE
RP SPECIFICITY.
RX PubMed=11139592; DOI=10.1074/jbc.m011560200;
RA Kang H.-G., Evers M.R., Xia G., Baenziger J.U., Schachner M.;
RT "Molecular cloning and expression of an N-acetylgalactosamine-4-O-
RT sulfotransferase that transfers sulfate to terminal and non-terminal beta
RT 1,4-linked N-acetylgalactosamine.";
RL J. Biol. Chem. 276:10861-10869(2001).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RX PubMed=12975309; DOI=10.1101/gr.1293003;
RA Clark H.F., Gurney A.L., Abaya E., Baker K., Baldwin D.T., Brush J.,
RA Chen J., Chow B., Chui C., Crowley C., Currell B., Deuel B., Dowd P.,
RA Eaton D., Foster J.S., Grimaldi C., Gu Q., Hass P.E., Heldens S., Huang A.,
RA Kim H.S., Klimowski L., Jin Y., Johnson S., Lee J., Lewis L., Liao D.,
RA Mark M.R., Robbie E., Sanchez C., Schoenfeld J., Seshagiri S., Simmons L.,
RA Singh J., Smith V., Stinson J., Vagts A., Vandlen R.L., Watanabe C.,
RA Wieand D., Woods K., Xie M.-H., Yansura D.G., Yi S., Yu G., Yuan J.,
RA Zhang M., Zhang Z., Goddard A.D., Wood W.I., Godowski P.J., Gray A.M.;
RT "The secreted protein discovery initiative (SPDI), a large-scale effort to
RT identify novel human secreted and transmembrane proteins: a bioinformatics
RT assessment.";
RL Genome Res. 13:2265-2270(2003).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Testis;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16177791; DOI=10.1038/nature03983;
RA Nusbaum C., Zody M.C., Borowsky M.L., Kamal M., Kodira C.D., Taylor T.D.,
RA Whittaker C.A., Chang J.L., Cuomo C.A., Dewar K., FitzGerald M.G., Yang X.,
RA Abouelleil A., Allen N.R., Anderson S., Bloom T., Bugalter B., Butler J.,
RA Cook A., DeCaprio D., Engels R., Garber M., Gnirke A., Hafez N., Hall J.L.,
RA Norman C.H., Itoh T., Jaffe D.B., Kuroki Y., Lehoczky J., Lui A.,
RA Macdonald P., Mauceli E., Mikkelsen T.S., Naylor J.W., Nicol R., Nguyen C.,
RA Noguchi H., O'Leary S.B., Piqani B., Smith C.L., Talamas J.A., Topham K.,
RA Totoki Y., Toyoda A., Wain H.M., Young S.K., Zeng Q., Zimmer A.R.,
RA Fujiyama A., Hattori M., Birren B.W., Sakaki Y., Lander E.S.;
RT "DNA sequence and analysis of human chromosome 18.";
RL Nature 437:551-555(2005).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Lung;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [7]
RP VARIANT SER-378.
RX PubMed=28132690; DOI=10.1016/j.ajhg.2017.01.013;
RA Oud M.M., Tuijnenburg P., Hempel M., van Vlies N., Ren Z.,
RA Ferdinandusse S., Jansen M.H., Santer R., Johannsen J., Bacchelli C.,
RA Alders M., Li R., Davies R., Dupuis L., Cale C.M., Wanders R.J., Pals S.T.,
RA Ocaka L., James C., Mueller I., Lehmberg K., Strom T., Engels H.,
RA Williams H.J., Beales P., Roepman R., Dias P., Brunner H.G., Cobben J.M.,
RA Hall C., Hartley T., Le Quesne Stabej P., Mendoza-Londono R., Davies E.G.,
RA de Sousa S.B., Lessel D., Arts H.H., Kuijpers T.W.;
RT "Mutations in EXTL3 cause neuro-immuno-skeletal dysplasia syndrome.";
RL Am. J. Hum. Genet. 100:281-296(2017).
CC -!- FUNCTION: Catalyzes the transfer of sulfate to position 4 of non-
CC reducing N-acetylgalactosamine (GalNAc) residues in both N-glycans and
CC O-glycans. Participates in biosynthesis of glycoprotein hormones
CC lutropin and thyrotropin, by mediating sulfation of their carbohydrate
CC structures. Has a higher activity toward carbonic anhydrase VI than
CC toward lutropin. Only active against terminal GalNAcbeta1,GalNAcbeta.
CC Isoform 2, but not isoform 1, is active toward chondroitin.
CC -!- SUBCELLULAR LOCATION: [Isoform 1]: Golgi apparatus membrane
CC {ECO:0000250}; Single-pass type II membrane protein {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: [Isoform 2]: Secreted {ECO:0000305}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q7L1S5-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q7L1S5-2; Sequence=VSP_043865, VSP_043866;
CC -!- TISSUE SPECIFICITY: Highly expressed in trachea. Also expressed in
CC fetal lung, adult pancreas, testis and salivary gland. Expressed at low
CC level in pituitary gland, apex of the heart, adult lung, prostate and
CC mammary gland. Weakly or not expressed in heart, liver and spinal cord.
CC {ECO:0000269|PubMed:11139592, ECO:0000269|PubMed:11445554}.
CC -!- SIMILARITY: Belongs to the sulfotransferase 2 family. {ECO:0000305}.
CC -!- CAUTION: It is uncertain whether Met-1 or Met-8 is the initiator.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH25764.2; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=AAK01862.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=AAK30370.1; Type=Erroneous translation; Note=Wrong choice of CDS.; Evidence={ECO:0000305};
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DR EMBL; AF239821; AAK01862.1; ALT_INIT; mRNA.
DR EMBL; AF332472; AAK30369.1; -; mRNA.
DR EMBL; AF332473; AAK30370.1; ALT_SEQ; mRNA.
DR EMBL; AY358488; AAQ88852.1; -; mRNA.
DR EMBL; AK093349; BAC04141.1; -; mRNA.
DR EMBL; AC010854; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC023575; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC116017; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC025764; AAH25764.2; ALT_INIT; mRNA.
DR CCDS; CCDS42422.1; -. [Q7L1S5-1]
DR CCDS; CCDS58618.1; -. [Q7L1S5-2]
DR RefSeq; NP_001243245.1; NM_001256316.1. [Q7L1S5-2]
DR RefSeq; NP_113610.2; NM_031422.5. [Q7L1S5-1]
DR RefSeq; XP_016881522.1; XM_017026033.1. [Q7L1S5-1]
DR AlphaFoldDB; Q7L1S5; -.
DR BioGRID; 123672; 10.
DR IntAct; Q7L1S5; 3.
DR STRING; 9606.ENSP00000480991; -.
DR GlyGen; Q7L1S5; 4 sites.
DR iPTMnet; Q7L1S5; -.
DR PhosphoSitePlus; Q7L1S5; -.
DR BioMuta; CHST9; -.
DR DMDM; 229462829; -.
DR EPD; Q7L1S5; -.
DR jPOST; Q7L1S5; -.
DR MassIVE; Q7L1S5; -.
DR PaxDb; Q7L1S5; -.
DR PeptideAtlas; Q7L1S5; -.
DR PRIDE; Q7L1S5; -.
DR ProteomicsDB; 68748; -. [Q7L1S5-1]
DR Antibodypedia; 2549; 144 antibodies from 23 providers.
DR DNASU; 83539; -.
DR Ensembl; ENST00000580774.2; ENSP00000464655.1; ENSG00000154080.14. [Q7L1S5-2]
DR Ensembl; ENST00000581714.5; ENSP00000462852.1; ENSG00000154080.14. [Q7L1S5-1]
DR Ensembl; ENST00000618847.5; ENSP00000480991.1; ENSG00000154080.14. [Q7L1S5-1]
DR GeneID; 83539; -.
DR KEGG; hsa:83539; -.
DR MANE-Select; ENST00000618847.5; ENSP00000480991.1; NM_031422.6; NP_113610.2.
DR UCSC; uc002kwd.5; human. [Q7L1S5-1]
DR CTD; 83539; -.
DR DisGeNET; 83539; -.
DR GeneCards; CHST9; -.
DR HGNC; HGNC:19898; CHST9.
DR HPA; ENSG00000154080; Tissue enhanced (salivary).
DR MIM; 610191; gene.
DR neXtProt; NX_Q7L1S5; -.
DR OpenTargets; ENSG00000154080; -.
DR PharmGKB; PA134888782; -.
DR VEuPathDB; HostDB:ENSG00000154080; -.
DR eggNOG; KOG4651; Eukaryota.
DR GeneTree; ENSGT00940000160563; -.
DR HOGENOM; CLU_2687119_0_0_1; -.
DR InParanoid; Q7L1S5; -.
DR OMA; NWPLDIR; -.
DR PhylomeDB; Q7L1S5; -.
DR TreeFam; TF325581; -.
DR PathwayCommons; Q7L1S5; -.
DR Reactome; R-HSA-2022870; Chondroitin sulfate biosynthesis. [Q7L1S5-2]
DR SignaLink; Q7L1S5; -.
DR BioGRID-ORCS; 83539; 7 hits in 1061 CRISPR screens.
DR ChiTaRS; CHST9; human.
DR GenomeRNAi; 83539; -.
DR Pharos; Q7L1S5; Tbio.
DR PRO; PR:Q7L1S5; -.
DR Proteomes; UP000005640; Chromosome 18.
DR RNAct; Q7L1S5; protein.
DR Bgee; ENSG00000154080; Expressed in bronchial epithelial cell and 102 other tissues.
DR ExpressionAtlas; Q7L1S5; baseline and differential.
DR Genevisible; Q7L1S5; HS.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0000139; C:Golgi membrane; TAS:Reactome.
DR GO; GO:0016021; C:integral component of membrane; NAS:UniProtKB.
DR GO; GO:0047756; F:chondroitin 4-sulfotransferase activity; TAS:Reactome.
DR GO; GO:0001537; F:N-acetylgalactosamine 4-O-sulfotransferase activity; IDA:UniProtKB.
DR GO; GO:0008146; F:sulfotransferase activity; IBA:GO_Central.
DR GO; GO:0016051; P:carbohydrate biosynthetic process; IEA:InterPro.
DR GO; GO:0030206; P:chondroitin sulfate biosynthetic process; TAS:Reactome.
DR GO; GO:0030203; P:glycosaminoglycan metabolic process; NAS:UniProtKB.
DR GO; GO:0042446; P:hormone biosynthetic process; ISS:UniProtKB.
DR GO; GO:0030166; P:proteoglycan biosynthetic process; ISS:UniProtKB.
DR GO; GO:0006790; P:sulfur compound metabolic process; IDA:UniProtKB.
DR InterPro; IPR018011; Carb_sulfotrans_8-10.
DR InterPro; IPR005331; Sulfotransferase.
DR PANTHER; PTHR12137; PTHR12137; 1.
DR Pfam; PF03567; Sulfotransfer_2; 1.
PE 2: Evidence at transcript level;
KW Alternative splicing; Carbohydrate metabolism; Glycoprotein;
KW Golgi apparatus; Membrane; Reference proteome; Secreted; Signal-anchor;
KW Transferase; Transmembrane; Transmembrane helix.
FT CHAIN 1..443
FT /note="Carbohydrate sulfotransferase 9"
FT /id="PRO_0000189655"
FT TOPO_DOM 1..12
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 13..33
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 34..443
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT REGION 108..132
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 108..128
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 220..226
FT /ligand="3'-phosphoadenylyl sulfate"
FT /ligand_id="ChEBI:CHEBI:58339"
FT /evidence="ECO:0000250"
FT BINDING 280..288
FT /ligand="3'-phosphoadenylyl sulfate"
FT /ligand_id="ChEBI:CHEBI:58339"
FT /evidence="ECO:0000250"
FT CARBOHYD 159
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 243
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 324
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 437
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT VAR_SEQ 68..74
FT /note="MSTEKIQ -> KPQVSHA (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:11139592"
FT /id="VSP_043865"
FT VAR_SEQ 75..443
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:11139592"
FT /id="VSP_043866"
FT VARIANT 122
FT /note="S -> N (in dbSNP:rs17694469)"
FT /id="VAR_055150"
FT VARIANT 378
FT /note="N -> S (in dbSNP:rs758130927)"
FT /evidence="ECO:0000269|PubMed:28132690"
FT /id="VAR_079095"
FT CONFLICT 136
FT /note="R -> H (in Ref. 1; AAK01862)"
FT /evidence="ECO:0000305"
FT CONFLICT 150
FT /note="N -> D (in Ref. 1; AAK01862)"
FT /evidence="ECO:0000305"
FT CONFLICT 194..195
FT /note="HH -> PP (in Ref. 2; AAK30370)"
FT /evidence="ECO:0000305"
FT CONFLICT 442
FT /note="F -> L (in Ref. 3; AAQ88852)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 443 AA; 52055 MW; 5455E67D20C9F8D6 CRC64;
MQPSEMVMNP KQVFLSVLIF GVAGLLLFMY LQVWIEEQHT GRVEKRREQK VTSGWGPVKY
LRPVPRIMST EKIQEHITNQ NPKFHMPEDV REKKENLLLN SERSTRLLTK TSHSQGGDQA
LSKSTGSPTE KLIEKRQGAK TVFNKFSNMN WPVDIHPLNK SLVKDNKWKK TEETQEKRRS
FLQEFCKKYG GVSHHQSHLF HTVSRIYVED KHKILYCEVP KAGCSNWKRI LMVLNGLASS
AYNISHNAVH YGKHLKKLDS FDLKGIYTRL NTYTKAVFVR DPMERLVSAF RDKFEHPNSY
YHPVFGKAII KKYRPNACEE ALINGSGVKF KEFIHYLLDS HRPVGMDIHW EKVSKLCYPC
LINYDFVGKF ETLEEDANYF LQMIGAPKEL KFPNFKDRHS SDERTNAQVV RQYLKDLTRT
ERQLIYDFYY LDYLMFNYTT PFL
