GALT9_DROME
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 03-AUG-2022, entry version 155.
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; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; 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 (2.06 ANGSTROMS) OF 146-650 IN COMPLEX WITH SUBSTRATE
RP AND MAGNESIUM, FUNCTION (ISOFORMS A AND B), CATALYTIC ACTIVITY, PATHWAY,
RP SUBUNIT, SUBCELLULAR LOCATION (ISOFORMS A AND B), DEVELOPMENTAL STAGE
RP (ISOFORMS A AND B), DOMAIN, DISRUPTION PHENOTYPE, GLYCOSYLATION AT ASN-321,
RP AND MUTAGENESIS OF 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 = 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:30158631};
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: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 PDBsum; 6E4Q; -.
DR PDBsum; 6E4R; -.
DR AlphaFoldDB; Q8MRC9; -.
DR SMR; Q8MRC9; -.
DR BioGRID; 73174; 2.
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 GlyGen; Q8MRC9; 2 sites.
DR iPTMnet; Q8MRC9; -.
DR PaxDb; Q8MRC9; -.
DR PRIDE; Q8MRC9; -.
DR EnsemblMetazoa; FBtr0087112; FBpp0086258; FBgn0050463. [Q8MRC9-1]
DR EnsemblMetazoa; FBtr0087113; FBpp0086259; FBgn0050463. [Q8MRC9-2]
DR EnsemblMetazoa; FBtr0113379; FBpp0112291; FBgn0050463. [Q8MRC9-2]
DR EnsemblMetazoa; FBtr0113380; FBpp0112292; FBgn0050463. [Q8MRC9-1]
DR EnsemblMetazoa; FBtr0113381; FBpp0112293; FBgn0050463. [Q8MRC9-3]
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 CTD; 246627; -.
DR FlyBase; FBgn0050463; Pgant9.
DR VEuPathDB; VectorBase:FBgn0050463; -.
DR eggNOG; KOG3736; Eukaryota.
DR GeneTree; ENSGT00940000170662; -.
DR HOGENOM; CLU_013477_0_1_1; -.
DR InParanoid; Q8MRC9; -.
DR OMA; QFNWHAV; -.
DR PhylomeDB; Q8MRC9; -.
DR Reactome; R-DME-913709; O-linked glycosylation of mucins.
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 seminal fluid secreting gland and 27 other tissues.
DR Genevisible; Q8MRC9; DM.
DR GO; GO:0005829; C:cytosol; HDA:FlyBase.
DR GO; GO:0005794; C:Golgi apparatus; IDA:FlyBase.
DR GO; GO:0031985; C:Golgi cisterna; IDA:FlyBase.
DR GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; ISM:FlyBase.
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; ISS:FlyBase.
DR GO; GO:0006493; P:protein O-linked glycosylation; IDA:FlyBase.
DR GO; GO:0019953; P:sexual reproduction; IEP:FlyBase.
DR CDD; cd02510; pp-GalNAc-T; 1.
DR CDD; cd00161; RICIN; 1.
DR Gene3D; 3.90.550.10; -; 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 Pfam; PF00535; Glycos_transf_2; 1.
DR Pfam; PF00652; Ricin_B_lectin; 1.
DR SMART; SM00458; RICIN; 1.
DR SUPFAM; SSF50370; SSF50370; 1.
DR SUPFAM; SSF53448; SSF53448; 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 99..138
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
