GLT15_HUMAN
ID GLT15_HUMAN Reviewed; 639 AA.
AC Q8N3T1; A6NMN1; B2R638; F1LIP6; Q86T60; Q96C46; Q96DJ5;
DT 16-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT 16-AUG-2004, sequence version 2.
DT 03-AUG-2022, entry version 158.
DE RecName: Full=Polypeptide N-acetylgalactosaminyltransferase 15;
DE EC=2.4.1.41 {ECO:0000269|PubMed:15147861};
DE AltName: Full=Polypeptide GalNAc transferase-like protein 2;
DE Short=GalNAc-T-like protein 2;
DE Short=pp-GaNTase-like protein 2;
DE AltName: Full=Polypeptide N-acetylgalactosaminyltransferase-like protein 2;
DE AltName: Full=Protein-UDP acetylgalactosaminyltransferase-like protein 2;
DE AltName: Full=UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase-like protein 2;
GN Name=GALNT15; Synonyms=GALNTL2; ORFNames=UNQ770/PRO1564;
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], TISSUE SPECIFICITY, FUNCTION, AND CATALYTIC
RP ACTIVITY.
RX PubMed=15147861; DOI=10.1016/j.febslet.2004.03.108;
RA Cheng L., Tachibana K., Iwasaki H., Kameyama A., Zhang Y., Kubota T.,
RA Hiruma T., Tachibana K., Kudo T., Guo J.-M., Narimatsu H.;
RT "Characterization of a novel human UDP-GalNAc transferase, pp-GalNAc-T15.";
RL FEBS Lett. 566:17-24(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND TISSUE SPECIFICITY.
RC TISSUE=Osteoarthritic cartilage;
RX PubMed=11597177; DOI=10.1053/joca.2001.0421;
RA Kumar S., Connor J.R., Dodds R.A., Halsey W., Van Horn M., Mao J.,
RA Sathe G.M., Mui P., Agarwal P., Badger A.M., Lee J.C., Gowen M., Lark M.W.;
RT "Identification and initial characterization of 5000 expressed sequenced
RT tags (ESTs) each from adult human normal and osteoarthritic cartilage cDNA
RT libraries.";
RL Osteoarthritis Cartilage 9:641-653(2001).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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].
RC TISSUE=Brain;
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 MRNA], AND VARIANT THR-432.
RC TISSUE=Adipose tissue, and Spinal cord;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D.,
RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16641997; DOI=10.1038/nature04728;
RA Muzny D.M., Scherer S.E., Kaul R., Wang J., Yu J., Sudbrak R., Buhay C.J.,
RA Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P.,
RA Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J., Jackson A.,
RA Khan Z.M., Kovar-Smith C., Lewis L.R., Lozado R.J., Metzker M.L.,
RA Milosavljevic A., Miner G.R., Morgan M.B., Nazareth L.V., Scott G.,
RA Sodergren E., Song X.-Z., Steffen D., Wei S., Wheeler D.A., Wright M.W.,
RA Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M.,
RA Brown M.J., Chen G., Chen Z., Clendenning J., Clerc-Blankenburg K.P.,
RA Chen R., Chen Z., Davis C., Delgado O., Dinh H.H., Dong W., Draper H.,
RA Ernst S., Fu G., Gonzalez-Garay M.L., Garcia D.K., Gillett W., Gu J.,
RA Hao B., Haugen E., Havlak P., He X., Hennig S., Hu S., Huang W.,
RA Jackson L.R., Jacob L.S., Kelly S.H., Kube M., Levy R., Li Z., Liu B.,
RA Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O.,
RA Palmeiri A., Pasternak S., Perez L.M., Phelps K.A., Plopper F.J., Qiang B.,
RA Raymond C., Rodriguez R., Saenphimmachak C., Santibanez J., Shen H.,
RA Shen Y., Subramanian S., Tabor P.E., Verduzco D., Waldron L., Wang J.,
RA Wang J., Wang Q., Williams G.A., Wong G.K.-S., Yao Z., Zhang J., Zhang X.,
RA Zhao G., Zhou J., Zhou Y., Nelson D., Lehrach H., Reinhardt R.,
RA Naylor S.L., Yang H., Olson M., Weinstock G., Gibbs R.A.;
RT "The DNA sequence, annotation and analysis of human chromosome 3.";
RL Nature 440:1194-1198(2006).
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND VARIANT THR-432.
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain;
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).
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. Although it
CC displays a much weaker activity toward all substrates tested compared
CC to GALNT2, it is able to transfer up to seven GalNAc residues to the
CC Muc5AC peptide, suggesting that it can fill vicinal Thr/Ser residues in
CC cooperation with other GALNT proteins. Prefers Muc1a as substrate.
CC {ECO:0000269|PubMed:15147861}.
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:15147861};
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:15147861};
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250};
CC -!- PATHWAY: Protein modification; protein glycosylation.
CC -!- INTERACTION:
CC Q8N3T1; Q8TD46-4: CD200R1; NbExp=3; IntAct=EBI-3925203, EBI-12824513;
CC Q8N3T1; P11912: CD79A; NbExp=3; IntAct=EBI-3925203, EBI-7797864;
CC Q8N3T1; Q8N5K1: CISD2; NbExp=3; IntAct=EBI-3925203, EBI-1045797;
CC Q8N3T1; P34910-2: EVI2B; NbExp=3; IntAct=EBI-3925203, EBI-17640610;
CC Q8N3T1; Q6DN72: FCRL6; NbExp=3; IntAct=EBI-3925203, EBI-23889796;
CC Q8N3T1; O15552: FFAR2; NbExp=3; IntAct=EBI-3925203, EBI-2833872;
CC Q8N3T1; Q8TBE3: FNDC9; NbExp=3; IntAct=EBI-3925203, EBI-12142257;
CC Q8N3T1; Q8NBJ4: GOLM1; NbExp=3; IntAct=EBI-3925203, EBI-712073;
CC Q8N3T1; Q6UWB1: IL27RA; NbExp=3; IntAct=EBI-3925203, EBI-19045531;
CC Q8N3T1; Q95460-2: MR1; NbExp=3; IntAct=EBI-3925203, EBI-12201447;
CC Q8N3T1; Q9BQ51: PDCD1LG2; NbExp=3; IntAct=EBI-3925203, EBI-16427978;
CC Q8N3T1; Q13113: PDZK1IP1; NbExp=3; IntAct=EBI-3925203, EBI-716063;
CC Q8N3T1; Q9BRI3: SLC30A2; NbExp=5; IntAct=EBI-3925203, EBI-8644112;
CC Q8N3T1; P30825: SLC7A1; NbExp=3; IntAct=EBI-3925203, EBI-4289564;
CC Q8N3T1; Q8TBG9: SYNPR; NbExp=3; IntAct=EBI-3925203, EBI-10273251;
CC Q8N3T1; Q7Z7N9: TMEM179B; NbExp=3; IntAct=EBI-3925203, EBI-11724423;
CC -!- SUBCELLULAR LOCATION: Golgi apparatus membrane {ECO:0000250}; Single-
CC pass type II membrane protein {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Widely expressed. Highly expressed in small
CC intestine, placenta, spleen, cerebral cortex and ovary. Expressed at
CC intermediate level in uterus, mammary gland, stomach, cerebellum and
CC whole brain. Weakly expressed in fetal brain, bone marrow, thyroid
CC gland, thymus, heart, skeletal muscle, lung, liver, colon, pancreas,
CC kidney and testis. Not expressed in leukocyte. Expressed in both normal
CC and osteoarthritic cartilage. Expressed at low level in chondrocytes in
CC all zones of both normal and osteoarthritic cartilage.
CC {ECO:0000269|PubMed:11597177, ECO:0000269|PubMed:15147861}.
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 -!- CAUTION: Was originally termed Galnt15/pp-GaNTase 15.
CC {ECO:0000305|PubMed:15147861}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAD89983.1; Type=Frameshift; Evidence={ECO:0000305};
CC -!- WEB RESOURCE: Name=Functional Glycomics Gateway - GTase;
CC Note=Polypeptide N-acetylgalactosaminyltransferase-like protein 2;
CC URL="http://www.functionalglycomics.org/glycomics/molecule/jsp/glycoEnzyme/viewGlycoEnzyme.jsp?gbpId=gt_hum_501";
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DR EMBL; AB078149; BAD29961.1; -; mRNA.
DR EMBL; AY035399; AAK63127.1; -; mRNA.
DR EMBL; AY358443; AAQ88808.1; -; mRNA.
DR EMBL; AK312425; BAG35335.1; -; mRNA.
DR EMBL; AL831925; CAD38585.1; -; mRNA.
DR EMBL; AL832575; CAD89983.1; ALT_FRAME; mRNA.
DR EMBL; AC087858; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471055; EAW64266.1; -; Genomic_DNA.
DR EMBL; BC014789; AAH14789.1; -; mRNA.
DR CCDS; CCDS33711.1; -.
DR RefSeq; NP_473451.3; NM_054110.4.
DR AlphaFoldDB; Q8N3T1; -.
DR SMR; Q8N3T1; -.
DR BioGRID; 125583; 18.
DR IntAct; Q8N3T1; 17.
DR STRING; 9606.ENSP00000344260; -.
DR CAZy; CBM13; Carbohydrate-Binding Module Family 13.
DR CAZy; GT27; Glycosyltransferase Family 27.
DR GlyGen; Q8N3T1; 2 sites.
DR PhosphoSitePlus; Q8N3T1; -.
DR BioMuta; GALNT15; -.
DR DMDM; 51316023; -.
DR EPD; Q8N3T1; -.
DR MassIVE; Q8N3T1; -.
DR PaxDb; Q8N3T1; -.
DR PeptideAtlas; Q8N3T1; -.
DR PRIDE; Q8N3T1; -.
DR ProteomicsDB; 71833; -.
DR Antibodypedia; 2430; 71 antibodies from 18 providers.
DR DNASU; 117248; -.
DR Ensembl; ENST00000339732.10; ENSP00000344260.5; ENSG00000131386.20.
DR GeneID; 117248; -.
DR KEGG; hsa:117248; -.
DR MANE-Select; ENST00000339732.10; ENSP00000344260.5; NM_054110.5; NP_473451.3.
DR UCSC; uc003car.5; human.
DR CTD; 117248; -.
DR DisGeNET; 117248; -.
DR GeneCards; GALNT15; -.
DR HGNC; HGNC:21531; GALNT15.
DR HPA; ENSG00000131386; Tissue enhanced (adipose tissue, brain).
DR MIM; 615131; gene.
DR neXtProt; NX_Q8N3T1; -.
DR OpenTargets; ENSG00000131386; -.
DR PharmGKB; PA134936170; -.
DR VEuPathDB; HostDB:ENSG00000131386; -.
DR eggNOG; KOG3736; Eukaryota.
DR GeneTree; ENSGT00940000160808; -.
DR HOGENOM; CLU_013477_0_3_1; -.
DR InParanoid; Q8N3T1; -.
DR OMA; APERDWG; -.
DR OrthoDB; 606683at2759; -.
DR PhylomeDB; Q8N3T1; -.
DR TreeFam; TF313267; -.
DR PathwayCommons; Q8N3T1; -.
DR Reactome; R-HSA-913709; O-linked glycosylation of mucins.
DR SignaLink; Q8N3T1; -.
DR UniPathway; UPA00378; -.
DR BioGRID-ORCS; 117248; 6 hits in 1066 CRISPR screens.
DR ChiTaRS; GALNT15; human.
DR GeneWiki; GALNTL2; -.
DR GenomeRNAi; 117248; -.
DR Pharos; Q8N3T1; Tbio.
DR PRO; PR:Q8N3T1; -.
DR Proteomes; UP000005640; Chromosome 3.
DR RNAct; Q8N3T1; protein.
DR Bgee; ENSG00000131386; Expressed in mucosa of stomach and 167 other tissues.
DR ExpressionAtlas; Q8N3T1; baseline and differential.
DR Genevisible; Q8N3T1; HS.
DR GO; GO:0005794; C:Golgi apparatus; IBA:GO_Central.
DR GO; GO:0000139; C:Golgi membrane; TAS:Reactome.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0030133; C:transport vesicle; IDA:LIFEdb.
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; 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 Disulfide bond; Glycoprotein; Glycosyltransferase; Golgi apparatus; Lectin;
KW Manganese; Membrane; Metal-binding; Reference proteome; Signal-anchor;
KW Transferase; Transmembrane; Transmembrane helix.
FT CHAIN 1..639
FT /note="Polypeptide N-acetylgalactosaminyltransferase 15"
FT /id="PRO_0000059137"
FT TOPO_DOM 1..11
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 12..34
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 35..639
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT DOMAIN 504..631
FT /note="Ricin B-type lectin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00174"
FT REGION 106..155
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 190..299
FT /note="Catalytic subdomain A"
FT REGION 358..420
FT /note="Catalytic subdomain B"
FT COMPBIAS 120..139
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 231
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 260
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 283
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250"
FT BINDING 285
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250"
FT BINDING 417
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250"
FT CARBOHYD 107
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 574
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 181..412
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00174"
FT DISULFID 403..482
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00174"
FT DISULFID 517..536
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00174"
FT DISULFID 562..575
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00174"
FT DISULFID 603..620
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00174"
FT VARIANT 68
FT /note="V -> G (in dbSNP:rs36026882)"
FT /id="VAR_049243"
FT VARIANT 151
FT /note="P -> L (in dbSNP:rs11715981)"
FT /id="VAR_049244"
FT VARIANT 324
FT /note="P -> A (in dbSNP:rs12634179)"
FT /id="VAR_049245"
FT VARIANT 432
FT /note="A -> T (in dbSNP:rs17851238)"
FT /evidence="ECO:0000269|PubMed:17974005, ECO:0000269|Ref.7"
FT /id="VAR_049246"
FT VARIANT 510
FT /note="H -> Y (in dbSNP:rs2271077)"
FT /id="VAR_019593"
FT CONFLICT 44
FT /note="V -> D (in Ref. 5; CAD38585)"
FT /evidence="ECO:0000305"
FT CONFLICT 326
FT /note="K -> R (in Ref. 5; CAD89983)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 639 AA; 73063 MW; F5DCA523AF4965DA CRC64;
MLLRKRYRHR PCRLQFLLLL LMLGCVLMMV AMLHPPHHTL HQTVTAQASK HSPEARYRLD
FGESQDWVLE AEDEGEEYSP LEGLPPFISL REDQLLVAVA LPQARRNQSQ GRRGGSYRLI
KQPRRQDKEA PKRDWGADED GEVSEEEELT PFSLDPRGLQ EALSARIPLQ RALPEVRHPL
CLQQHPQDSL PTASVILCFH DEAWSTLLRT VHSILDTVPR AFLKEIILVD DLSQQGQLKS
ALSEYVARLE GVKLLRSNKR LGAIRARMLG ATRATGDVLV FMDAHCECHP GWLEPLLSRI
AGDRSRVVSP VIDVIDWKTF QYYPSKDLQR GVLDWKLDFH WEPLPEHVRK ALQSPISPIR
SPVVPGEVVA MDRHYFQNTG AYDSLMSLRG GENLELSFKA WLCGGSVEIL PCSRVGHIYQ
NQDSHSPLDQ EATLRNRVRI AETWLGSFKE TFYKHSPEAF SLSKAEKPDC MERLQLQRRL
GCRTFHWFLA NVYPELYPSE PRPSFSGKLH NTGLGLCADC QAEGDILGCP MVLAPCSDSR
QQQYLQHTSR KEIHFGSPQH LCFAVRQEQV ILQNCTEEGL AIHQQHWDFQ ENGMIVHILS
GKCMEAVVQE NNKDLYLRPC DGKARQQWRF DQINAVDER
