ID   GALT9_HUMAN             Reviewed;         603 AA.
AC   Q9HCQ5; Q52LR8; Q6NT54; Q8NFR1;
DT   16-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT   03-APR-2007, sequence version 3.
DT   24-JAN-2024, entry version 166.
DE   RecName: Full=Polypeptide N-acetylgalactosaminyltransferase 9;
DE            EC=2.4.1.41 {ECO:0000269|PubMed:12407114};
DE   AltName: Full=Polypeptide GalNAc transferase 9;
DE            Short=GalNAc-T9;
DE            Short=pp-GaNTase 9;
DE   AltName: Full=Protein-UDP acetylgalactosaminyltransferase 9;
DE   AltName: Full=UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase 9;
GN   Name=GALNT9;
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), FUNCTION, AND TISSUE SPECIFICITY.
RC   TISSUE=Brain;
RX   PubMed=10978536; DOI=10.1016/s0167-4781(00)00180-9;
RA   Toba S., Tenno M., Konishi M., Mikami T., Itoh N., Kurosaka A.;
RT   "Brain-specific expression of a novel human UDP-GalNAc:polypeptide N-
RT   acetylgalactosaminyltransferase (GalNAc-T9).";
RL   Biochim. Biophys. Acta 1493:264-268(2000).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC   TISSUE=Kidney;
RA   Guo J.H., Zan Q., Yu L.;
RL   Submitted (DEC-2001) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC   TISSUE=Colon;
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   [4]
RP   FUNCTION, CATALYTIC ACTIVITY, AND PATHWAY.
RX   PubMed=12407114; DOI=10.1074/jbc.m203094200;
RA   Zhang Y., Iwasaki H., Wang H., Kudo T., Kalka T.B., Hennet T., Kubota T.,
RA   Cheng L., Inaba N., Gotoh M., Togayachi A., Guo J.-M., Hisatomi H.,
RA   Nakajima K., Nishihara S., Nakamura M., Marth J.D., Narimatsu H.;
RT   "Cloning and characterization of a new human UDP-N-acetyl-alpha-D-
RT   galactosamine:polypeptide N-acetylgalactosaminyltransferase, designated pp-
RT   GalNAc-T13, that is specifically expressed in neurons and synthesizes
RT   GalNAc alpha-serine/threonine antigen.";
RL   J. Biol. Chem. 278:573-584(2003).
CC   -!- FUNCTION: Catalyzes the initial reaction in O-linked oligosaccharide
CC       biosynthesis, the transfer of an N-acetyl-D-galactosamine residue to a
CC       serine or threonine residue on the protein receptor. Does not
CC       glycosylate apomucin or SDC3. {ECO:0000269|PubMed:10978536,
CC       ECO:0000269|PubMed:12407114}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=L-seryl-[protein] + UDP-N-acetyl-alpha-D-galactosamine = 3-O-
CC         [N-acetyl-alpha-D-galactosaminyl]-L-seryl-[protein] + H(+) + UDP;
CC         Xref=Rhea:RHEA:23956, Rhea:RHEA-COMP:9863, Rhea:RHEA-COMP:12788,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:53604,
CC         ChEBI:CHEBI:58223, ChEBI:CHEBI:67138; EC=2.4.1.41;
CC         Evidence={ECO:0000269|PubMed:12407114};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=L-threonyl-[protein] + UDP-N-acetyl-alpha-D-galactosamine = 3-
CC         O-[N-acetyl-alpha-D-galactosaminyl]-L-threonyl-[protein] + H(+) +
CC         UDP; Xref=Rhea:RHEA:52424, Rhea:RHEA-COMP:11060, Rhea:RHEA-
CC         COMP:11689, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013, ChEBI:CHEBI:58223,
CC         ChEBI:CHEBI:67138, ChEBI:CHEBI:87075; EC=2.4.1.41;
CC         Evidence={ECO:0000269|PubMed:12407114};
CC   -!- COFACTOR:
CC       Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250};
CC   -!- PATHWAY: Protein modification; protein glycosylation.
CC       {ECO:0000269|PubMed:12407114}.
CC   -!- SUBCELLULAR LOCATION: Golgi apparatus membrane {ECO:0000250}; Single-
CC       pass type II membrane protein {ECO:0000250}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q9HCQ5-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q9HCQ5-2; Sequence=VSP_011206;
CC   -!- TISSUE SPECIFICITY: Specifically expressed in brain. Not expressed in
CC       heart, placenta, lung, liver, skeletal muscle, kidney, pancreas,
CC       spleen, thymus, prostate, testis, ovary, small intestine, colon and
CC       leukocyte. In brain, it is expressed in cerebellum, frontal lobe,
CC       temporal lobe, putamen and spinal cord, weakly expressed in cerebral
CC       cortex. Not expressed in medulla and occipital pole.
CC       {ECO:0000269|PubMed:10978536}.
CC   -!- DOMAIN: There are two conserved domains in the glycosyltransferase
CC       region: the N-terminal domain (domain A, also called GT1 motif), which
CC       is probably involved in manganese coordination and substrate binding
CC       and the C-terminal domain (domain B, also called Gal/GalNAc-T motif),
CC       which is probably involved in catalytic reaction and UDP-Gal binding.
CC       {ECO:0000250}.
CC   -!- DOMAIN: The ricin B-type lectin domain binds to GalNAc and contributes
CC       to the glycopeptide specificity. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the glycosyltransferase 2 family. GalNAc-T
CC       subfamily. {ECO:0000305}.
CC   -!- WEB RESOURCE: Name=Functional Glycomics Gateway - GTase;
CC       Note=Polypeptide N-acetylgalactosaminyltransferase 9;
CC       URL="http://www.functionalglycomics.org/glycomics/molecule/jsp/glycoEnzyme/viewGlycoEnzyme.jsp?gbpId=gt_hum_491";
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DR   EMBL; AB040672; BAB13699.2; -; mRNA.
DR   EMBL; AF458594; AAM49722.1; -; mRNA.
DR   EMBL; BC093817; AAH93817.2; -; mRNA.
DR   EMBL; BC093819; AAH93819.2; -; mRNA.
DR   CCDS; CCDS41866.1; -. [Q9HCQ5-2]
DR   CCDS; CCDS81755.1; -. [Q9HCQ5-1]
DR   RefSeq; NP_001116108.1; NM_001122636.1.
DR   RefSeq; NP_068580.2; NM_021808.3. [Q9HCQ5-2]
DR   AlphaFoldDB; Q9HCQ5; -.
DR   SMR; Q9HCQ5; -.
DR   BioGRID; 119094; 53.
DR   IntAct; Q9HCQ5; 1.
DR   STRING; 9606.ENSP00000329846; -.
DR   CAZy; CBM13; Carbohydrate-Binding Module Family 13.
DR   CAZy; GT27; Glycosyltransferase Family 27.
DR   GlyCosmos; Q9HCQ5; 1 site, No reported glycans.
DR   GlyGen; Q9HCQ5; 1 site.
DR   iPTMnet; Q9HCQ5; -.
DR   PhosphoSitePlus; Q9HCQ5; -.
DR   BioMuta; GALNT9; -.
DR   DMDM; 143811393; -.
DR   MassIVE; Q9HCQ5; -.
DR   PaxDb; 9606-ENSP00000380488; -.
DR   PeptideAtlas; Q9HCQ5; -.
DR   ProteomicsDB; 81785; -. [Q9HCQ5-1]
DR   ProteomicsDB; 81786; -. [Q9HCQ5-2]
DR   Antibodypedia; 32061; 162 antibodies from 21 providers.
DR   DNASU; 50614; -.
DR   Ensembl; ENST00000397325.6; ENSP00000380488.2; ENSG00000182870.13. [Q9HCQ5-2]
DR   Ensembl; ENST00000541995.5; ENSP00000440544.1; ENSG00000182870.13. [Q9HCQ5-2]
DR   Ensembl; ENST00000671997.1; ENSP00000500654.1; ENSG00000288490.1. [Q9HCQ5-2]
DR   Ensembl; ENST00000673376.1; ENSP00000500593.1; ENSG00000288490.1. [Q9HCQ5-2]
DR   GeneID; 50614; -.
DR   KEGG; hsa:50614; -.
DR   UCSC; uc001uka.3; human. [Q9HCQ5-1]
DR   AGR; HGNC:4131; -.
DR   CTD; 50614; -.
DR   DisGeNET; 50614; -.
DR   GeneCards; GALNT9; -.
DR   HGNC; HGNC:4131; GALNT9.
DR   HPA; ENSG00000182870; Tissue enriched (brain).
DR   MIM; 606251; gene.
DR   neXtProt; NX_Q9HCQ5; -.
DR   OpenTargets; ENSG00000182870; -.
DR   PharmGKB; PA28544; -.
DR   VEuPathDB; HostDB:ENSG00000182870; -.
DR   eggNOG; KOG3736; Eukaryota.
DR   GeneTree; ENSGT00940000156599; -.
DR   HOGENOM; CLU_013477_2_2_1; -.
DR   InParanoid; Q9HCQ5; -.
DR   OMA; QYVHRRY; -.
DR   OrthoDB; 202750at2759; -.
DR   PhylomeDB; Q9HCQ5; -.
DR   TreeFam; TF313267; -.
DR   BRENDA; 2.4.1.41; 2681.
DR   PathwayCommons; Q9HCQ5; -.
DR   Reactome; R-HSA-913709; O-linked glycosylation of mucins.
DR   SignaLink; Q9HCQ5; -.
DR   UniPathway; UPA00378; -.
DR   BioGRID-ORCS; 50614; 16 hits in 1139 CRISPR screens.
DR   ChiTaRS; GALNT9; human.
DR   GenomeRNAi; 50614; -.
DR   Pharos; Q9HCQ5; Tbio.
DR   PRO; PR:Q9HCQ5; -.
DR   Proteomes; UP000005640; Chromosome 12.
DR   RNAct; Q9HCQ5; Protein.
DR   Bgee; ENSG00000182870; Expressed in right hemisphere of cerebellum and 88 other cell types or tissues.
DR   ExpressionAtlas; Q9HCQ5; baseline and differential.
DR   Genevisible; Q9HCQ5; HS.
DR   GO; GO:0005794; C:Golgi apparatus; IBA:GO_Central.
DR   GO; GO:0000139; C:Golgi membrane; TAS:Reactome.
DR   GO; GO:0030246; F:carbohydrate binding; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0004653; F:polypeptide N-acetylgalactosaminyltransferase activity; IBA:GO_Central.
DR   GO; GO:0016266; P:O-glycan processing; TAS:Reactome.
DR   GO; GO:0006493; P:protein O-linked glycosylation; IBA:GO_Central.
DR   CDD; cd02510; pp-GalNAc-T; 1.
DR   CDD; cd00161; RICIN; 1.
DR   Gene3D; 2.80.10.50; -; 1.
DR   InterPro; IPR045885; GalNAc-T.
DR   InterPro; IPR001173; Glyco_trans_2-like.
DR   InterPro; IPR029044; Nucleotide-diphossugar_trans.
DR   InterPro; IPR035992; Ricin_B-like_lectins.
DR   InterPro; IPR000772; Ricin_B_lectin.
DR   PANTHER; PTHR11675; N-ACETYLGALACTOSAMINYLTRANSFERASE; 1.
DR   PANTHER; PTHR11675:SF28; POLYPEPTIDE N-ACETYLGALACTOSAMINYLTRANSFERASE 9; 1.
DR   Pfam; PF00535; Glycos_transf_2; 1.
DR   Pfam; PF00652; Ricin_B_lectin; 1.
DR   SMART; SM00458; RICIN; 1.
DR   SUPFAM; SSF53448; Nucleotide-diphospho-sugar transferases; 1.
DR   SUPFAM; SSF50370; Ricin B-like lectins; 1.
DR   PROSITE; PS50231; RICIN_B_LECTIN; 1.
PE   1: Evidence at protein level;
KW   Alternative splicing; Disulfide bond; Glycoprotein; Glycosyltransferase;
KW   Golgi apparatus; Lectin; Manganese; Membrane; Metal-binding;
KW   Reference proteome; Signal-anchor; Transferase; Transmembrane;
KW   Transmembrane helix.
FT   CHAIN           1..603
FT                   /note="Polypeptide N-acetylgalactosaminyltransferase 9"
FT                   /id="PRO_0000059120"
FT   TOPO_DOM        1..6
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        7..29
FT                   /note="Helical; Signal-anchor for type II membrane protein"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        30..603
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          464..600
FT                   /note="Ricin B-type lectin"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00174"
FT   REGION          150..261
FT                   /note="Catalytic subdomain A"
FT   REGION          318..380
FT                   /note="Catalytic subdomain B"
FT   BINDING         191
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         222
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         245
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000250"
FT   BINDING         247
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000250"
FT   BINDING         377
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000250"
FT   BINDING         380
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         385
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        460
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        141..372
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00174"
FT   DISULFID        363..442
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00174"
FT   DISULFID        477..493
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00174"
FT   DISULFID        525..540
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00174"
FT   DISULFID        567..587
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00174"
FT   VAR_SEQ         1..366
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:15489334, ECO:0000303|Ref.2"
FT                   /id="VSP_011206"
FT   CONFLICT        539
FT                   /note="K -> R (in Ref. 1; BAB13699)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   603 AA;  68359 MW;  4B5888733D8577CF CRC64;
     MAVARKIRTL LTVNILVFVG IVLFSVYCRL QGRSQELVRI VSGDRRVRSR HAKVGTLGDR
     EAILQRLDHL EEVVYNQLNG LAKPIGLVEG PGGLGQGGLA ATLRDDGQEA EGKYEEYGYN
     AQLSDRISLD RSIPDYRPRK CRQMSYAQDL PQVSVVFIFV NEALSVILRS VHSVVNHTPS
     QLLKEVILVD DNSDNVELKF NLDQYVNKRY PGLVKIVRNS RREGLIRARL QGWKAATAPV
     VGFFDAHVEF NTGWAEPALS RIREDRRRIV LPAIDNIKYS TFEVQQYANA AHGYNWGLRC
     MYIIPPQDWL DRGDESAPIR TPAMIGCSFV VDREYFGDIG LLDPGMEVYG GENVELGMRV
     WQCGGSMEVL PCSRVAHIER TRKPYNNDID YYAKRNALRA AEVWMDDFKS HVYMAWNIPM
     SNPGVDFGDV SERLALRQRL KCRSFKWYLE NVYPEMRVYN NTLTYGEVRN SKASAYCLDQ
     GAEDGDRAIL YPCHGMSSQL VRYSADGLLQ LGPLGSTAFL PDSKCLVDDG TGRMPTLKKC
     EDVARPTQRL WDFTQSGPIV SRATGRCLEV EMSKDANFGL RLVVQRCSGQ KWMIRNWIKH
     ARH
//

ID   J3KNN1_HUMAN            Unreviewed;       603 AA.
AC   J3KNN1;
DT   03-OCT-2012, integrated into UniProtKB/TrEMBL.
DT   03-OCT-2012, sequence version 1.
DT   27-MAR-2024, entry version 78.
DE   RecName: Full=Polypeptide N-acetylgalactosaminyltransferase {ECO:0000256|ARBA:ARBA00012644, ECO:0000256|RuleBase:RU361242};
DE            EC=2.4.1.- {ECO:0000256|RuleBase:RU361242};
DE   AltName: Full=Protein-UDP acetylgalactosaminyltransferase {ECO:0000256|RuleBase:RU361242};
GN   Name=GALNT9 {ECO:0000313|Ensembl:ENSP00000329846.8};
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 {ECO:0000313|Ensembl:ENSP00000329846.8, ECO:0000313|Proteomes:UP000005640};
RN   [1] {ECO:0000313|Ensembl:ENSP00000329846.8, ECO:0000313|Proteomes:UP000005640}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16541075; DOI=10.1038/nature04569;
RG   Baylor College of Medicine Human Genome Sequencing Center Sequence Production Team;
RA   Scherer S.E., Muzny D.M., Buhay C.J., Chen R., Cree A., Ding Y.,
RA   Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C.,
RA   Hernandez J., Hodgson A.V., Hume J., Jackson A., Khan Z.M., Kovar-Smith C.,
RA   Lewis L.R., Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R.,
RA   Montgomery K.T., Morgan M.B., Nazareth L.V., Scott G., Sodergren E.,
RA   Song X.Z., Steffen D., Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y.,
RA   Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G.,
RA   Chen Z., Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H.,
RA   Draper H., Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S.,
RA   Kelly S.H., Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M.,
RA   Nguyen B.V., Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.,
RA   Santibanez J., Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q.,
RA   Williams G.A., Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V.,
RA   Bailey M., Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E.,
RA   Burkett C.E., Burrell K.L., Calderon E., Cardenas V., Carter K., Casias K.,
RA   Cavazos I., Cavazos S.R., Ceasar H., Chacko J., Chan S.N., Chavez D.,
RA   Christopoulos C., Chu J., Cockrell R., Cox C.D., Dang M., Dathorne S.R.,
RA   David R., Davis C.M., Davy-Carroll L., Deshazo D.R., Donlin J.E.,
RA   D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J., Escotto M., Flagg N.,
RA   Forbes L.D., Gabisi A.M., Garza M., Hamilton C., Henderson N.,
RA   Hernandez O., Hines S., Hogues M.E., Huang M., Idlebird D.G., Johnson R.,
RA   Jolivet A., Jones S., Kagan R., King L.M., Leal B., Lebow H., Lee S.,
RA   LeVan J.M., Lewis L.C., London P., Lorensuhewa L.M., Loulseged H.,
RA   Lovett D.A., Lucier A., Lucier R.L., Ma J., Madu R.C., Mapua P.,
RA   Martindale A.D., Martinez E., Massey E., Mawhiney S., Meador M.G.,
RA   Mendez S., Mercado C., Mercado I.C., Merritt C.E., Miner Z.L., Minja E.,
RA   Mitchell T., Mohabbat F., Mohabbat K., Montgomery B., Moore N., Morris S.,
RA   Munidasa M., Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O.,
RA   Nwokenkwo S., Obregon M., Oguh M., Oragunye N., Oviedo R.J., Parish B.J.,
RA   Parker D.N., Parrish J., Parks K.L., Paul H.A., Payton B.A., Perez A.,
RA   Perrin W., Pickens A., Primus E.L., Pu L.L., Puazo M., Quiles M.M.,
RA   Quiroz J.B., Rabata D., Reeves K., Ruiz S.J., Shao H., Sisson I.,
RA   Sonaike T., Sorelle R.P., Sutton A.E., Svatek A.F., Svetz L.A.,
RA   Tamerisa K.S., Taylor T.R., Teague B., Thomas N., Thorn R.D., Trejos Z.Y.,
RA   Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I., Vera V.A.,
RA   Villasana D.M., Wang L., Ward-Moore S., Warren J.T., Wei X., White F.,
RA   Williamson A.L., Wleczyk R., Wooden H.S., Wooden S.H., Yen J., Yoon L.,
RA   Yoon V., Zorrilla S.E., Nelson D., Kucherlapati R., Weinstock G.,
RA   Gibbs R.A., null.;
RT   "The finished DNA sequence of human chromosome 12.";
RL   Nature 440:346-351(2006).
RN   [2] {ECO:0000313|Ensembl:ENSP00000329846.8}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (NOV-2023) to UniProtKB.
CC   -!- COFACTOR:
CC       Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC         Evidence={ECO:0000256|ARBA:ARBA00001936,
CC         ECO:0000256|RuleBase:RU361242};
CC   -!- PATHWAY: Protein modification; protein glycosylation.
CC       {ECO:0000256|ARBA:ARBA00004922, ECO:0000256|RuleBase:RU361242}.
CC   -!- SUBCELLULAR LOCATION: Golgi apparatus membrane
CC       {ECO:0000256|RuleBase:RU361242}; Single-pass type II membrane protein
CC       {ECO:0000256|RuleBase:RU361242}. Membrane
CC       {ECO:0000256|ARBA:ARBA00004606}; Single-pass type II membrane protein
CC       {ECO:0000256|ARBA:ARBA00004606}.
CC   -!- SIMILARITY: Belongs to the glycosyltransferase 2 family. GalNAc-T
CC       subfamily. {ECO:0000256|ARBA:ARBA00005680,
CC       ECO:0000256|RuleBase:RU361242}.
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DR   EMBL; AC138466; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC148477; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC232989; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC233270; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AEKP01194575; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AEKP01194576; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   RefSeq; NP_001116108.1; NM_001122636.1.
DR   AlphaFoldDB; J3KNN1; -.
DR   SMR; J3KNN1; -.
DR   MassIVE; J3KNN1; -.
DR   PeptideAtlas; J3KNN1; -.
DR   Antibodypedia; 32061; 162 antibodies from 21 providers.
DR   DNASU; 50614; -.
DR   Ensembl; ENST00000328957.13; ENSP00000329846.8; ENSG00000182870.13.
DR   GeneID; 50614; -.
DR   KEGG; hsa:50614; -.
DR   MANE-Select; ENST00000328957.13; ENSP00000329846.8; NM_001122636.2; NP_001116108.1.
DR   UCSC; uc001ukc.5; human.
DR   CTD; 50614; -.
DR   HGNC; HGNC:4131; GALNT9.
DR   VEuPathDB; HostDB:ENSG00000182870; -.
DR   GeneTree; ENSGT00940000156599; -.
DR   HOGENOM; CLU_013477_4_0_1; -.
DR   OMA; QYVHRRY; -.
DR   OrthoDB; 202750at2759; -.
DR   PhylomeDB; J3KNN1; -.
DR   UniPathway; UPA00378; -.
DR   BioGRID-ORCS; 50614; 16 hits in 1139 CRISPR screens.
DR   ChiTaRS; GALNT9; human.
DR   GenomeRNAi; 50614; -.
DR   Proteomes; UP000005640; Chromosome 12.
DR   Bgee; ENSG00000182870; Expressed in right hemisphere of cerebellum and 88 other cell types or tissues.
DR   ExpressionAtlas; J3KNN1; baseline and differential.
DR   GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0030246; F:carbohydrate binding; IEA:UniProtKB-KW.
DR   GO; GO:0004653; F:polypeptide N-acetylgalactosaminyltransferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0006493; P:protein O-linked glycosylation; IEA:UniProt.
DR   CDD; cd02510; pp-GalNAc-T; 1.
DR   CDD; cd00161; RICIN; 1.
DR   Gene3D; 2.80.10.50; -; 1.
DR   InterPro; IPR045885; GalNAc-T.
DR   InterPro; IPR001173; Glyco_trans_2-like.
DR   InterPro; IPR029044; Nucleotide-diphossugar_trans.
DR   InterPro; IPR035992; Ricin_B-like_lectins.
DR   InterPro; IPR000772; Ricin_B_lectin.
DR   PANTHER; PTHR11675; N-ACETYLGALACTOSAMINYLTRANSFERASE; 1.
DR   PANTHER; PTHR11675:SF28; POLYPEPTIDE N-ACETYLGALACTOSAMINYLTRANSFERASE 9; 1.
DR   Pfam; PF00535; Glycos_transf_2; 1.
DR   Pfam; PF00652; Ricin_B_lectin; 1.
DR   SMART; SM00458; RICIN; 1.
DR   SUPFAM; SSF53448; Nucleotide-diphospho-sugar transferases; 1.
DR   SUPFAM; SSF50370; Ricin B-like lectins; 1.
DR   PROSITE; PS50231; RICIN_B_LECTIN; 1.
PE   1: Evidence at protein level;
KW   Disulfide bond {ECO:0000256|ARBA:ARBA00023157,
KW   ECO:0000256|RuleBase:RU361242};
KW   Glycosyltransferase {ECO:0000256|ARBA:ARBA00022676,
KW   ECO:0000256|RuleBase:RU361242};
KW   Golgi apparatus {ECO:0000256|ARBA:ARBA00023034,
KW   ECO:0000256|RuleBase:RU361242};
KW   Lectin {ECO:0000256|ARBA:ARBA00022734, ECO:0000256|RuleBase:RU361242};
KW   Manganese {ECO:0000256|ARBA:ARBA00023211, ECO:0000256|RuleBase:RU361242};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|RuleBase:RU361242};
KW   Proteomics identification {ECO:0007829|PeptideAtlas:J3KNN1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000005640};
KW   Signal-anchor {ECO:0000256|ARBA:ARBA00022968};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU361242};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692,
KW   ECO:0000256|RuleBase:RU361242};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|RuleBase:RU361242}.
FT   TRANSMEM        7..27
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU361242"
FT   DOMAIN          465..595
FT                   /note="Ricin B lectin"
FT                   /evidence="ECO:0000259|SMART:SM00458"
SQ   SEQUENCE   603 AA;  68389 MW;  B8824EA9F92DC117 CRC64;
     MAVARKIRTL LTVNILVFVG IVLFSVYCRL QGRSQELVRI VSGDRRVRSR HAKVGTLGDR
     EAILQRLDHL EEVVYNQLNG LAKPIGLVEG PGGLGQGGLA ATLRDDGQEA EGKYEEYGYN
     AQLSDRISLD RSIPDYRPRK CRQMSYAQDL PQVSVVFIFV NEALSVILRS VHSVVNHTPS
     QLLKEVILVD DNSDNVELKF NLDQYVNKRY PGLVKIVRNS RREGLIRARL QGWKAATAPV
     VGFFDAHVEF NTGWAEPALS RIREDRRRIV LPAIDNIKYS TFEVQQYANA AHGYNWGLWC
     MYIIPPQDWL DRGDESAPIR TPAMIGCSFV VDREYFGDIG LLDPGMEVYG GENVELGMRV
     WQCGGSMEVL PCSRVAHIER TRKPYNNDID YYAKRNALRA AEVWMDDFKS HVYMAWNIPM
     SNPGVDFGDV SERLALRQRL KCRSFKWYLE NVYPEMRVYN NTLTYGEVRN SKASAYCLDQ
     GAEDGDRAIL YPCHGMSSQL VRYSADGLLQ LGPLGSTAFL PDSKCLVDDG TGRMPTLKKC
     EDVARPTQRL WDFTQSGPIV SRATGRCLEV EMSKDANFGL RLVVQRCSGQ KWMIRNWIKH
     ARH
//