ID   GALT9_DROME             Reviewed;         650 AA.
AC   Q8MRC9; A1A6R7; A1A6V9; A8DYG1; A8DYG2; A8DYG3; Q0E950; Q9V7T0;
DT   16-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT   16-AUG-2004, sequence version 2.
DT   04-NOV-2026, entry version 170.
DE   RecName: Full=Putative polypeptide N-acetylgalactosaminyltransferase 9;
DE            Short=pp-GaNTase 9;
DE            EC=2.4.1.41 {ECO:0000269|PubMed:30158631};
DE   AltName: Full=Protein-UDP acetylgalactosaminyltransferase 9;
DE   AltName: Full=UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase 9;
GN   Name=Pgant9 {ECO:0000312|FlyBase:FBgn0050463};
GN   ORFNames=CG30463 {ECO:0000312|FlyBase:FBgn0050463};
OS   Drosophila melanogaster (Fruit fly).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Altocrustacea; Allotriocarida;
OC   Hexapoda; Insecta; Pterygota; Neoptera; Eumetabola; Endopterygota;
OC   Aparaglossata; Panorpida; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC   Drosophilidae; Drosophila; Sophophora.
OX   NCBI_TaxID=7227;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Berkeley;
RX   PubMed=10731132; DOI=10.1126/science.287.5461.2185;
RA   Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
RA   Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
RA   George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
RA   Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., Brandon R.C.,
RA   Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C.,
RA   Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A.,
RA   An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A.,
RA   Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V.,
RA   Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J.,
RA   Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E.,
RA   Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B.,
RA   Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I.,
RA   Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C.,
RA   Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S.,
RA   Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M.,
RA   Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
RA   Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D.,
RA   Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F.,
RA   Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D.,
RA   Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A.,
RA   Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C.,
RA   McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C.,
RA   Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L.,
RA   Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R.,
RA   Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V.,
RA   Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F.,
RA   Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J.,
RA   Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R.,
RA   Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y.,
RA   Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T.,
RA   Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S.,
RA   Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W.,
RA   Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M.,
RA   Venter J.C.;
RT   "The genome sequence of Drosophila melanogaster.";
RL   Science 287:2185-2195(2000).
RN   [2]
RP   GENOME REANNOTATION, AND ALTERNATIVE SPLICING.
RC   STRAIN=Berkeley;
RX   PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
RA   Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
RA   Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
RA   Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
RA   Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
RA   Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M.,
RA   Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.;
RT   "Annotation of the Drosophila melanogaster euchromatic genome: a systematic
RT   review.";
RL   Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM A).
RC   STRAIN=Berkeley; TISSUE=Embryo;
RX   PubMed=12537569; DOI=10.1186/gb-2002-3-12-research0080;
RA   Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., George R.A.,
RA   Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., Rubin G.M.,
RA   Celniker S.E.;
RT   "A Drosophila full-length cDNA resource.";
RL   Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM F).
RC   STRAIN=Berkeley;
RA   Stapleton M., Carlson J.W., Frise E., Kapadia B., Park S., Wan K.H., Yu C.,
RA   Celniker S.E.;
RL   Submitted (DEC-2006) to the EMBL/GenBank/DDBJ databases.
RN   [5]
RP   DEVELOPMENTAL STAGE.
RX   PubMed=16251381; DOI=10.1093/glycob/cwj051;
RA   Tian E., Ten Hagen K.G.;
RT   "Expression of the UDP-GalNAc: polypeptide N-
RT   acetylgalactosaminyltransferase family is spatially and temporally
RT   regulated during Drosophila development.";
RL   Glycobiology 16:83-95(2006).
RN   [6]
RP   DISRUPTION PHENOTYPE.
RX   PubMed=22157008; DOI=10.1074/jbc.m111.306159;
RA   Tran D.T., Zhang L., Zhang Y., Tian E., Earl L.A., Ten Hagen K.G.;
RT   "Multiple members of the UDP-GalNAc: polypeptide N-
RT   acetylgalactosaminyltransferase family are essential for viability in
RT   Drosophila.";
RL   J. Biol. Chem. 287:5243-5252(2012).
RN   [7] {ECO:0000312|PDB:6E4R, ECO:0007744|PDB:6E4Q}
RP   X-RAY CRYSTALLOGRAPHY IN COMPLEX WITH SUBSTRATE AND MAGNESIUM, FUNCTION
RP   (ISOFORMS A AND B), CATALYTIC ACTIVITY, PATHWAY, SUBUNIT, SUBCELLULAR
RP   LOCATION (ISOFORMS A AND B), DEVELOPMENTAL STAGE (ISOFORMS A AND B),
RP   DOMAIN, DISRUPTION PHENOTYPE, GLYCOSYLATION AT ASN-321, AND MUTAGENESIS OF
RP   254-PRO--LEU-650.
RX   PubMed=30158631; DOI=10.1038/s41467-018-05978-9;
RA   Ji S., Samara N.L., Revoredo L., Zhang L., Tran D.T., Muirhead K.,
RA   Tabak L.A., Ten Hagen K.G.;
RT   "A molecular switch orchestrates enzyme specificity and secretory granule
RT   morphology.";
RL   Nat. Commun. 9:3508-3508(2018).
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 (PubMed:30158631).
CC       It can both act as a peptide transferase that transfers GalNAc onto
CC       unmodified peptide substrates, and as a glycopeptide transferase that
CC       requires the prior addition of a GalNAc on a peptide before adding
CC       additional GalNAc moieties (PubMed:30158631).
CC       {ECO:0000269|PubMed:30158631}.
CC   -!- FUNCTION: [Isoform A]: N-acetylgalactosaminyltransferase which
CC       preferentially O-glycosylates negatively charge substrates. O-
CC       glycosylates mucin-like protein Sgs3 in the salivary gland but to a
CC       lesser extent than isoform B. By regulating the O-glycosylation of
CC       secretory cargo proteins plays a role in the morphology and maturation
CC       of salivary gland secretory granules. {ECO:0000269|PubMed:30158631}.
CC   -!- FUNCTION: [Isoform B]: N-acetylgalactosaminyltransferase which
CC       preferentially O-glycosylates positively charge substrates. O-
CC       glycosylates mucin-like protein Sgs3 in the salivary gland. By
CC       regulating the O-glycosylation of secretory cargo proteins, plays a
CC       role in the morphology and maturation of salivary gland secretory
CC       granules. {ECO:0000269|PubMed:30158631}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=L-seryl-[protein] + UDP-N-acetyl-alpha-D-galactosamine = a 3-
CC         O-[N-acetyl-alpha-D-galactosaminyl]-L-seryl-[protein] + UDP + H(+);
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:30158631};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=L-threonyl-[protein] + UDP-N-acetyl-alpha-D-galactosamine = a
CC         3-O-[N-acetyl-alpha-D-galactosaminyl]-L-threonyl-[protein] + UDP +
CC         H(+); 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:30158631};
CC   -!- COFACTOR:
CC       Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC         Evidence={ECO:0000269|PubMed:30158631};
CC   -!- PATHWAY: Protein modification; protein glycosylation.
CC       {ECO:0000305|PubMed:30158631}.
CC   -!- SUBUNIT: Isoform A forms homotetramer. Isoform B forms homodimer.
CC       {ECO:0000269|PubMed:30158631}.
CC   -!- SUBCELLULAR LOCATION: [Isoform A]: Golgi apparatus membrane
CC       {ECO:0000269|PubMed:30158631}; Single-pass type II membrane protein
CC       {ECO:0000269|PubMed:30158631}.
CC   -!- SUBCELLULAR LOCATION: [Isoform B]: Golgi apparatus membrane
CC       {ECO:0000269|PubMed:30158631}; Single-pass type II membrane protein
CC       {ECO:0000269|PubMed:30158631}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=4;
CC       Name=A; Synonyms=D;
CC         IsoId=Q8MRC9-1; Sequence=Displayed;
CC       Name=B; Synonyms=C;
CC         IsoId=Q8MRC9-2; Sequence=VSP_034635;
CC       Name=E;
CC         IsoId=Q8MRC9-3; Sequence=VSP_034632, VSP_034635;
CC       Name=F;
CC         IsoId=Q8MRC9-4; Sequence=VSP_034633, VSP_034634, VSP_034635;
CC   -!- DEVELOPMENTAL STAGE: Expressed both maternally and zygotically
CC       (PubMed:16251381). Expressed through embryonic and larval stages
CC       (PubMed:16251381). During embryonic stages 9-11, expressed in the
CC       developing anterior midgut and amnioserosa (PubMed:16251381). Expressed
CC       in the salivary glands from embryonic stage 12 onwards
CC       (PubMed:16251381). During embryonic stages 12-13, still expressed in
CC       the amnioserosa region (PubMed:16251381). In third instar larvae,
CC       expressed ubiquitously in wing, with increased expression in the notum
CC       and ventral wing pouch, leg and haltere imaginal disks
CC       (PubMed:16251381). In eye-antennal imaginal disk, expressed in the
CC       presumptive eye region only (PubMed:16251381). Isoform A: Expressed in
CC       trachea, midgut, salivary gland, hindgut, central nervous system and
CC       Malpighian tubules (PubMed:30158631). Isoform B: Specifically expressed
CC       in the salivary gland (PubMed:30158631). {ECO:0000269|PubMed:16251381,
CC       ECO:0000269|PubMed:30158631}.
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 involved in manganese coordination and substrate binding and the C-
CC       terminal domain (domain B, also called Gal/GalNAc-T motif), which is
CC       involved in catalytic reaction and UDP-Gal binding.
CC       {ECO:0000269|PubMed:30158631}.
CC   -!- DOMAIN: The alpha subunit loop in the ricin B-type lectin domain
CC       regulates substrate specificity and modulates the substrate access to
CC       the active site. In isoform A, the alpha subunit loop is composed of
CC       positively charged residues and acts on negatively charged substrates.
CC       In isoform B, the alpha subunit loop is composed of negatively charged
CC       residues and acts on positively charged substrates.
CC       {ECO:0000269|PubMed:30158631}.
CC   -!- DISRUPTION PHENOTYPE: RNAi-mediated knockdown in the whole body, in the
CC       mesoderm, the respiratory system or the amnioserosa results in
CC       lethality (PubMed:22157008). RNAi-mediated knockdown in the epidermis
CC       or the digestive system and reproductive tract results in a reduction
CC       in viability (PubMed:22157008). RNAi-mediated knockdown in salivary
CC       glands results in aberrant secretory granule morphology showing
CC       angular, shard-like morphology (PubMed:30158631).
CC       {ECO:0000269|PubMed:22157008, ECO:0000269|PubMed:30158631}.
CC   -!- SIMILARITY: Belongs to the glycosyltransferase 2 family. GalNAc-T
CC       subfamily. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=ABL75647.1; Type=Miscellaneous discrepancy; Note=Intron retention.; Evidence={ECO:0000305};
CC       Sequence=ABL75689.1; Type=Miscellaneous discrepancy; Note=Intron retention.; Evidence={ECO:0000305};
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DR   EMBL; AE013599; AAF57964.3; -; Genomic_DNA.
DR   EMBL; AE013599; AAF57966.2; -; Genomic_DNA.
DR   EMBL; AE013599; ABV53822.1; -; Genomic_DNA.
DR   EMBL; AE013599; ABV53823.1; -; Genomic_DNA.
DR   EMBL; AE013599; ABV53824.1; -; Genomic_DNA.
DR   EMBL; AY121661; AAM51988.1; -; mRNA.
DR   EMBL; BT029588; ABL75647.1; ALT_SEQ; mRNA.
DR   EMBL; BT029630; ABL75689.1; ALT_SEQ; mRNA.
DR   RefSeq; NP_001097341.1; NM_001103871.1. [Q8MRC9-2]
DR   RefSeq; NP_001097342.1; NM_001103872.1. [Q8MRC9-1]
DR   RefSeq; NP_001097343.1; NM_001103873.1. [Q8MRC9-3]
DR   RefSeq; NP_725602.1; NM_166188.2. [Q8MRC9-1]
DR   RefSeq; NP_725603.2; NM_166189.2. [Q8MRC9-2]
DR   PDB; 6E4Q; X-ray; 2.80 A; A/B/C/D=146-650.
DR   PDB; 6E4R; X-ray; 2.06 A; A/B=146-650.
DR   AlphaFoldDB; Q8MRC9; -.
DR   SMR; Q8MRC9; -.
DR   BioGRID; 73174; 2.
DR   FunCoup; Q8MRC9; 383.
DR   IntAct; Q8MRC9; 2.
DR   STRING; 7227.FBpp0086258; -.
DR   CAZy; CBM13; Carbohydrate-Binding Module Family 13.
DR   CAZy; GT27; Glycosyltransferase Family 27.
DR   UniLectin; Q8MRC9; -.
DR   GlyCosmos; Q8MRC9; 3 sites, No reported glycans.
DR   GlyGen; Q8MRC9; 3 sites.
DR   iPTMnet; Q8MRC9; -.
DR   PaxDb; 7227-FBpp0086258; -.
DR   PeptideAtlas; Q8MRC9; -.
DR   EnsemblMetazoa; FBtr0087112; FBpp0086258; FBgn0050463.
DR   EnsemblMetazoa; FBtr0113380; FBpp0112292; FBgn0050463.
DR   GeneID; 246627; -.
DR   KEGG; dme:Dmel_CG30463; -.
DR   UCSC; CG30463-RA; d. melanogaster. [Q8MRC9-1]
DR   UCSC; CG30463-RC; d. melanogaster.
DR   UCSC; CG30463-RD; d. melanogaster.
DR   UCSC; CG30463-RE; d. melanogaster.
DR   AGR; FB:FBgn0050463; -.
DR   CTD; 246627; -.
DR   FlyBase; FBgn0050463; Pgant9.
DR   VEuPathDB; VectorBase:FBgn0050463; -.
DR   eggNOG; KOG3736; Eukaryota.
DR   HOGENOM; CLU_013477_0_1_1; -.
DR   InParanoid; Q8MRC9; -.
DR   OMA; AAHHKPV; -.
DR   OrthoDB; 6119243at2759; -.
DR   PhylomeDB; Q8MRC9; -.
DR   UniPathway; UPA00378; -.
DR   BioGRID-ORCS; 246627; 0 hits in 3 CRISPR screens.
DR   GenomeRNAi; 246627; -.
DR   PRO; PR:Q8MRC9; -.
DR   Proteomes; UP000000803; Chromosome 2R.
DR   Bgee; FBgn0050463; Expressed in dorsal appendage forming follicle cell in ovary and 269 other cell types or tissues.
DR   GO; GO:0005794; C:Golgi apparatus; ISS:FlyBase.
DR   GO; GO:0031985; C:Golgi cisterna; IDA:FlyBase.
DR   GO; GO:0000139; C:Golgi membrane; IDA:FlyBase.
DR   GO; GO:0016020; C:membrane; ISM:FlyBase.
DR   GO; GO:0004653; F:polypeptide N-acetylgalactosaminyltransferase activity; IDA:FlyBase.
DR   GO; GO:0006493; P:protein O-linked glycosylation; IBA:GO_Central.
DR   GO; GO:0016266; P:protein O-linked glycosylation via N-acetylgalactosamine; IDA:FlyBase.
DR   CDD; cd23462; beta-trefoil_Ricin_Pgant9-like; 1.
DR   CDD; cd02510; pp-GalNAc-T; 1.
DR   FunFam; 2.80.10.50:FF:000047; Polypeptide N-acetylgalactosaminyltransferase; 1.
DR   FunFam; 3.90.550.10:FF:000021; Polypeptide N-acetylgalactosaminyltransferase; 1.
DR   Gene3D; 2.80.10.50; -; 1.
DR   Gene3D; 3.90.550.10; Spore Coat Polysaccharide Biosynthesis Protein SpsA, Chain A; 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:SF131; POLYPEPTIDE N-ACETYLGALACTOSAMINYLTRANSFERASE 9-RELATED; 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   3D-structure; Alternative splicing; Disulfide bond; Glycoprotein;
KW   Glycosyltransferase; Golgi apparatus; Lectin; Manganese; Membrane;
KW   Metal-binding; Reference proteome; Signal-anchor; Transferase;
KW   Transmembrane; Transmembrane helix.
FT   CHAIN           1..650
FT                   /note="Putative polypeptide N-
FT                   acetylgalactosaminyltransferase 9"
FT                   /id="PRO_0000059163"
FT   TOPO_DOM        1..11
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        12..31
FT                   /note="Helical; Signal-anchor for type II membrane protein"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        32..650
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          521..643
FT                   /note="Ricin B-type lectin"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00174"
FT   REGION          84..154
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          208..317
FT                   /note="Catalytic subdomain A"
FT                   /evidence="ECO:0000305|PubMed:30158631"
FT   REGION          378..440
FT                   /note="Catalytic subdomain B"
FT                   /evidence="ECO:0000305|PubMed:30158631"
FT   COMPBIAS        107..136
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         216
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000269|PubMed:30158631,
FT                   ECO:0000312|PDB:6E4Q"
FT   BINDING         249
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000269|PubMed:30158631,
FT                   ECO:0000312|PDB:6E4Q"
FT   BINDING         278
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000269|PubMed:30158631,
FT                   ECO:0000312|PDB:6E4Q"
FT   BINDING         301
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000269|PubMed:30158631,
FT                   ECO:0000312|PDB:6E4Q"
FT   BINDING         302
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000269|PubMed:30158631,
FT                   ECO:0000312|PDB:6E4Q"
FT   BINDING         303
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000269|PubMed:30158631,
FT                   ECO:0000312|PDB:6E4Q"
FT   BINDING         303
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000269|PubMed:30158631,
FT                   ECO:0000312|PDB:6E4Q"
FT   BINDING         437
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000269|PubMed:30158631,
FT                   ECO:0000312|PDB:6E4Q"
FT   BINDING         440
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000269|PubMed:30158631,
FT                   ECO:0000312|PDB:6E4Q"
FT   BINDING         445
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000269|PubMed:30158631,
FT                   ECO:0000312|PDB:6E4Q"
FT   CARBOHYD        321
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000269|PubMed:30158631,
FT                   ECO:0007744|PDB:6E4Q"
FT   CARBOHYD        373
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        198..432
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00174,
FT                   ECO:0000269|PubMed:30158631, ECO:0000312|PDB:6E4Q"
FT   DISULFID        423..499
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00174,
FT                   ECO:0000269|PubMed:30158631, ECO:0000312|PDB:6E4Q"
FT   DISULFID        535..554
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00174,
FT                   ECO:0000269|PubMed:30158631, ECO:0000312|PDB:6E4Q"
FT   DISULFID        577..590
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00174,
FT                   ECO:0000269|PubMed:30158631, ECO:0000312|PDB:6E4Q"
FT   DISULFID        616..631
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00174,
FT                   ECO:0000269|PubMed:30158631, ECO:0000312|PDB:6E4Q"
FT   VAR_SEQ         1..383
FT                   /note="Missing (in isoform E)"
FT                   /evidence="ECO:0000305"
FT                   /id="VSP_034632"
FT   VAR_SEQ         2..22
FT                   /note="AFIWRRRSTTIVKLVAFALAI -> NFYLSSWHCQVTQSGLVAGLE (in
FT                   isoform F)"
FT                   /evidence="ECO:0000303|Ref.4"
FT                   /id="VSP_034633"
FT   VAR_SEQ         23..273
FT                   /note="Missing (in isoform F)"
FT                   /evidence="ECO:0000303|Ref.4"
FT                   /id="VSP_034634"
FT   VAR_SEQ         526..556
FT                   /note="RNLGYGGRTCLDAPAGKKHQKKAVGTYPCHR -> ANVPNGMCLDAKEKSEE
FT                   ETPVSIYECHG (in isoform B, isoform E and isoform F)"
FT                   /evidence="ECO:0000303|Ref.4"
FT                   /id="VSP_034635"
FT   MUTAGEN         254..650
FT                   /note="Missing: Results in secretory granule defects
FT                   including an angular and shard-like morphology."
FT                   /evidence="ECO:0000269|PubMed:30158631"
FT   CONFLICT        145
FT                   /note="N -> D (in Ref. 3; AAM51988)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        454
FT                   /note="L -> P (in Ref. 3; AAM51988)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        472
FT                   /note="Y -> C (in Ref. 3; AAM51988)"
FT                   /evidence="ECO:0000305"
FT   HELIX           148..150
FT                   /evidence="ECO:0007829|PDB:6E4R"
FT   HELIX           161..174
FT                   /evidence="ECO:0007829|PDB:6E4R"
FT   HELIX           178..183
FT                   /evidence="ECO:0007829|PDB:6E4R"
FT   HELIX           196..200
FT                   /evidence="ECO:0007829|PDB:6E4R"
FT   STRAND          211..219
FT                   /evidence="ECO:0007829|PDB:6E4R"
FT   HELIX           222..235
FT                   /evidence="ECO:0007829|PDB:6E4R"
FT   HELIX           238..240
FT                   /evidence="ECO:0007829|PDB:6E4R"
FT   STRAND          241..248
FT                   /evidence="ECO:0007829|PDB:6E4R"
FT   HELIX           254..256
FT                   /evidence="ECO:0007829|PDB:6E4R"
FT   HELIX           258..263
FT                   /evidence="ECO:0007829|PDB:6E4R"
FT   HELIX           264..266
FT                   /evidence="ECO:0007829|PDB:6E4R"
FT   STRAND          270..274
FT                   /evidence="ECO:0007829|PDB:6E4R"
FT   HELIX           281..291
FT                   /evidence="ECO:0007829|PDB:6E4R"
FT   STRAND          294..301
FT                   /evidence="ECO:0007829|PDB:6E4R"
FT   STRAND          304..306
FT                   /evidence="ECO:0007829|PDB:6E4R"
FT   HELIX           311..320
FT                   /evidence="ECO:0007829|PDB:6E4R"
FT   STRAND          324..334
FT                   /evidence="ECO:0007829|PDB:6E4R"
FT   TURN            335..337
FT                   /evidence="ECO:0007829|PDB:6E4R"
FT   HELIX           345..347
FT                   /evidence="ECO:0007829|PDB:6E4R"
FT   STRAND          349..353
FT                   /evidence="ECO:0007829|PDB:6E4R"
FT   TURN            355..357
FT                   /evidence="ECO:0007829|PDB:6E4Q"
FT   STRAND          359..363
FT                   /evidence="ECO:0007829|PDB:6E4R"
FT   HELIX           366..369
FT                   /evidence="ECO:0007829|PDB:6E4R"
FT   STRAND          386..392
FT                   /evidence="ECO:0007829|PDB:6E4R"
FT   HELIX           393..398
FT                   /evidence="ECO:0007829|PDB:6E4R"
FT   HELIX           412..422
FT                   /evidence="ECO:0007829|PDB:6E4R"
FT   STRAND          426..439
FT                   /evidence="ECO:0007829|PDB:6E4R"
FT   HELIX           445..448
FT                   /evidence="ECO:0007829|PDB:6E4R"
FT   HELIX           455..465
FT                   /evidence="ECO:0007829|PDB:6E4R"
FT   HELIX           467..469
FT                   /evidence="ECO:0007829|PDB:6E4R"
FT   HELIX           470..476
FT                   /evidence="ECO:0007829|PDB:6E4R"
FT   TURN            477..479
FT                   /evidence="ECO:0007829|PDB:6E4R"
FT   HELIX           488..496
FT                   /evidence="ECO:0007829|PDB:6E4R"
FT   HELIX           502..508
FT                   /evidence="ECO:0007829|PDB:6E4R"
FT   HELIX           516..518
FT                   /evidence="ECO:0007829|PDB:6E4R"
FT   STRAND          519..523
FT                   /evidence="ECO:0007829|PDB:6E4R"
FT   STRAND          525..527
FT                   /evidence="ECO:0007829|PDB:6E4R"
FT   STRAND          534..538
FT                   /evidence="ECO:0007829|PDB:6E4R"
FT   STRAND          541..544
FT                   /evidence="ECO:0007829|PDB:6E4Q"
FT   STRAND          547..553
FT                   /evidence="ECO:0007829|PDB:6E4R"
FT   HELIX           559..561
FT                   /evidence="ECO:0007829|PDB:6E4R"
FT   STRAND          563..565
FT                   /evidence="ECO:0007829|PDB:6E4R"
FT   STRAND          571..573
FT                   /evidence="ECO:0007829|PDB:6E4R"
FT   STRAND          576..583
FT                   /evidence="ECO:0007829|PDB:6E4R"
FT   STRAND          585..589
FT                   /evidence="ECO:0007829|PDB:6E4R"
FT   HELIX           595..597
FT                   /evidence="ECO:0007829|PDB:6E4R"
FT   STRAND          599..602
FT                   /evidence="ECO:0007829|PDB:6E4R"
FT   TURN            603..606
FT                   /evidence="ECO:0007829|PDB:6E4R"
FT   STRAND          607..610
FT                   /evidence="ECO:0007829|PDB:6E4R"
FT   TURN            611..613
FT                   /evidence="ECO:0007829|PDB:6E4R"
FT   STRAND          616..619
FT                   /evidence="ECO:0007829|PDB:6E4R"
FT   STRAND          626..629
FT                   /evidence="ECO:0007829|PDB:6E4R"
FT   HELIX           636..638
FT                   /evidence="ECO:0007829|PDB:6E4R"
FT   STRAND          640..642
FT                   /evidence="ECO:0007829|PDB:6E4R"
FT   HELIX           647..649
FT                   /evidence="ECO:0007829|PDB:6E4R"
SQ   SEQUENCE   650 AA;  73193 MW;  AC847736AD1C07CA CRC64;
     MAFIWRRRST TIVKLVAFAL AIWFCIAFLV YTDDTRRRAA QEGAGASGAG SAPGVGGGAG
     GLGDPIALAL RNEPAGEDFG INGNVIGGGG QKQAHDEADI PPTVGKHKAD LQAERMRKKA
     AEQPKKKPQE DSKKVIDPPA NFEENPGELG KPVRLPKEMS DEMKKAVDDG WTKNAFNQYV
     SDLISVHRTL PDPRDAWCKD EARYLTNLPK TDVIICFHNE AWTVLLRTVH SVLDRSPEHL
     IGKIILVDDY SDMPHLKRQL EDYFAAYPKV QIIRGQKREG LIRARILGAN HAKSPVLTYL
     DSHCECTEGW LEPLLDRIAR NSTTVVCPVI DVISDETLEY HYRDSGGVNV GGFDWNLQFS
     WHPVPERERK RHNSTAEPVY SPTMAGGLFS IDREFFDRLG TYDSGFDIWG GENLELSFKT
     WMCGGTLEIV PCSHVGHIFR KRSPYKWRSG VNVLKKNSVR LAEVWMDEYS QYYYHRIGND
     KGDWGDVSDR RKLRNDLKCK SFKWYLDNIY PELFIPGDSV AHGEIRNLGY GGRTCLDAPA
     GKKHQKKAVG TYPCHRQGGN QYWMLSKAGE IRRDDSCLDY AGKDVTLFGC HGGKGNQFWT
     YRENTKQLHH GTSGKCLAIS ESKDKLLMEE CSASLSRQQW TLENYDSSKL
//