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 24-JAN-2024, entry version 154. 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}; 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 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. DR AlphaFoldDB; Q7L1S5; -. DR BioGRID; 123672; 10. DR IntAct; Q7L1S5; 3. DR STRING; 9606.ENSP00000480991; -. DR GlyCosmos; Q7L1S5; 4 sites, No reported glycans. DR GlyGen; Q7L1S5; 6 sites, 1 O-linked glycan (2 sites). DR iPTMnet; Q7L1S5; -. DR PhosphoSitePlus; Q7L1S5; -. DR BioMuta; CHST9; -. DR DMDM; 229462829; -. DR EPD; Q7L1S5; -. DR jPOST; Q7L1S5; -. DR MassIVE; Q7L1S5; -. DR PaxDb; 9606-ENSP00000480991; -. DR PeptideAtlas; Q7L1S5; -. DR ProteomicsDB; 68748; -. [Q7L1S5-1] DR Antibodypedia; 2549; 162 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 AGR; HGNC:19898; -. 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; YRHNANE; -. DR OrthoDB; 2907043at2759; -. 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 1137 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 cell types or tissues. DR ExpressionAtlas; Q7L1S5; baseline and differential. DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell. DR GO; GO:0000139; C:Golgi membrane; TAS:Reactome. DR GO; GO:0016020; C: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; CARBOHYDRATE SULFOTRANSFERASE; 1. DR PANTHER; PTHR12137:SF6; CARBOHYDRATE SULFOTRANSFERASE 9; 1. DR Pfam; PF03567; Sulfotransfer_2; 1. DR Genevisible; Q7L1S5; HS. 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 //