GLT14_HUMAN
ID GLT14_HUMAN Reviewed; 552 AA.
AC Q96FL9; B3KV89; Q4ZG75; Q53SU1; Q53TJ0; Q8IVI4; Q9BRH1; Q9H827; Q9H9J8;
DT 16-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 167.
DE RecName: Full=Polypeptide N-acetylgalactosaminyltransferase 14;
DE EC=2.4.1.41;
DE AltName: Full=Polypeptide GalNAc transferase 14;
DE Short=GalNAc-T14;
DE Short=pp-GaNTase 14;
DE AltName: Full=Protein-UDP acetylgalactosaminyltransferase 14;
DE AltName: Full=UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase 14;
GN Name=GALNT14; ORFNames=UNQ2434/PRO4994;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), ENZYME ACTIVITY, ALTERNATIVE
RP SPLICING, AND TISSUE SPECIFICITY.
RC TISSUE=Stomach;
RX PubMed=12507512; DOI=10.1016/s0006-291x(02)02908-x;
RA Wang H., Tachibana K., Zhang Y., Iwasaki H., Kameyama A., Chen L.,
RA Guo J.-M., Hiruma T., Togayachi A., Kudo T., Kikuchi N., Narimatsu H.;
RT "Cloning and characterization of a novel UDP-GalNAc:polypeptide N-
RT acetylgalactosaminyltransferase, pp-GalNAc-T14.";
RL Biochem. Biophys. Res. Commun. 300:738-744(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RA Wandall H.H., Bennett E.P.;
RL Submitted (SEP-2011) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RX PubMed=12975309; DOI=10.1101/gr.1293003;
RA Clark H.F., Gurney A.L., Abaya E., Baker K., Baldwin D.T., Brush J.,
RA Chen J., Chow B., Chui C., Crowley C., Currell B., Deuel B., Dowd P.,
RA Eaton D., Foster J.S., Grimaldi C., Gu Q., Hass P.E., Heldens S., Huang A.,
RA Kim H.S., Klimowski L., Jin Y., Johnson S., Lee J., Lewis L., Liao D.,
RA Mark M.R., Robbie E., Sanchez C., Schoenfeld J., Seshagiri S., Simmons L.,
RA Singh J., Smith V., Stinson J., Vagts A., Vandlen R.L., Watanabe C.,
RA Wieand D., Woods K., Xie M.-H., Yansura D.G., Yi S., Yu G., Yuan J.,
RA Zhang M., Zhang Z., Goddard A.D., Wood W.I., Godowski P.J., Gray A.M.;
RT "The secreted protein discovery initiative (SPDI), a large-scale effort to
RT identify novel human secreted and transmembrane proteins: a bioinformatics
RT assessment.";
RL Genome Res. 13:2265-2270(2003).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 3 AND 4), AND
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-435 (ISOFORM 2).
RC TISSUE=Fibroblast, Retinoblastoma, and Teratocarcinoma;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15815621; DOI=10.1038/nature03466;
RA Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P.,
RA Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C.,
RA Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L.,
RA Du H., Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A.,
RA Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J.,
RA Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M.,
RA Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T.,
RA Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S.,
RA Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K.,
RA McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C.,
RA Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S.,
RA Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C.,
RA Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M.,
RA Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C.,
RA Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J.,
RA Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E.,
RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X.,
RA Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M.,
RA Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C.,
RA Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S.,
RA Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H.,
RA Wilson R.K.;
RT "Generation and annotation of the DNA sequences of human chromosomes 2 and
RT 4.";
RL Nature 434:724-731(2005).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
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 [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Eye, and Ovary;
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 [8]
RP TISSUE SPECIFICITY.
RX PubMed=20179215; DOI=10.1158/1078-0432.ccr-09-3108;
RA Stern H.M., Padilla M., Wagner K., Amler L., Ashkenazi A.;
RT "Development of immunohistochemistry assays to assess GALNT14 and FUT3/6 in
RT clinical trials of dulanermin and drozitumab.";
RL Clin. Cancer Res. 16:1587-1596(2010).
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. Displays activity
CC toward mucin-derived peptide substrates such as Muc2, Muc5AC, Muc7, and
CC Muc13 (-58). May be involved in O-glycosylation in kidney.
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:12507512};
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:12507512};
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250};
CC -!- PATHWAY: Protein modification; protein glycosylation.
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=4;
CC Name=1;
CC IsoId=Q96FL9-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q96FL9-2; Sequence=VSP_011222;
CC Name=3;
CC IsoId=Q96FL9-3; Sequence=VSP_011221;
CC Name=4;
CC IsoId=Q96FL9-4; Sequence=VSP_045121;
CC -!- TISSUE SPECIFICITY: Detected in renal tubules (at protein level).
CC Highly expressed in fetal and adult kidney. Widely expressed at low
CC level. Weakly expressed in whole brain, cerebellum, thymus, lung,
CC mammary gland, liver, stomach, small intestine, colon, pancreas,
CC spleen, bladder, uterus, placenta, testis, ovary, skeletal muscle,
CC leukocyte, B-cell, bone marrow, fetal brain, fetal thymus, fetal lung,
CC fetal liver, fetal small intestine, fetal spleen, fetal skeletal and
CC fetus. Detected in renal tubules (at protein level).
CC {ECO:0000269|PubMed:12507512, ECO:0000269|PubMed:20179215}.
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 -!- MISCELLANEOUS: [Isoform 1]: Major isoform.
CC -!- MISCELLANEOUS: [Isoform 3]: Minor isoform. {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the glycosyltransferase 2 family. GalNAc-T
CC subfamily. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAB14795.1; Type=Miscellaneous discrepancy; Note=Chimeric at the C-terminus.; Evidence={ECO:0000305};
CC -!- WEB RESOURCE: Name=Functional Glycomics Gateway - GTase;
CC Note=Polypeptide N-acetylgalactosaminyltransferase 14;
CC URL="http://www.functionalglycomics.org/glycomics/molecule/jsp/glycoEnzyme/viewGlycoEnzyme.jsp?gbpId=gt_hum_497";
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DR EMBL; AB078144; BAC56889.1; -; mRNA.
DR EMBL; Y09324; CAA70505.4; -; mRNA.
DR EMBL; AY358758; AAQ89118.1; -; mRNA.
DR EMBL; AK022753; BAB14227.1; -; mRNA.
DR EMBL; AK024039; BAB14795.1; ALT_SEQ; mRNA.
DR EMBL; AK091313; BAC03634.1; -; mRNA.
DR EMBL; AK122747; BAG53701.1; -; mRNA.
DR EMBL; AC009301; AAX88899.1; -; Genomic_DNA.
DR EMBL; AC009305; AAX93209.1; -; Genomic_DNA.
DR EMBL; AC015980; AAY24301.1; -; Genomic_DNA.
DR EMBL; CH471053; EAX00489.1; -; Genomic_DNA.
DR EMBL; BC006269; AAH06269.2; -; mRNA.
DR EMBL; BC010659; AAH10659.1; -; mRNA.
DR CCDS; CCDS1773.2; -. [Q96FL9-1]
DR CCDS; CCDS58705.1; -. [Q96FL9-4]
DR CCDS; CCDS58706.1; -. [Q96FL9-3]
DR RefSeq; NP_001240755.1; NM_001253826.1. [Q96FL9-3]
DR RefSeq; NP_001240756.1; NM_001253827.1. [Q96FL9-4]
DR RefSeq; NP_001316024.1; NM_001329095.1.
DR RefSeq; NP_001316025.1; NM_001329096.1. [Q96FL9-4]
DR RefSeq; NP_078848.2; NM_024572.3. [Q96FL9-1]
DR AlphaFoldDB; Q96FL9; -.
DR SMR; Q96FL9; -.
DR BioGRID; 122753; 48.
DR IntAct; Q96FL9; 2.
DR BindingDB; Q96FL9; -.
DR ChEMBL; CHEMBL4523427; -.
DR CAZy; CBM13; Carbohydrate-Binding Module Family 13.
DR CAZy; GT27; Glycosyltransferase Family 27.
DR GlyGen; Q96FL9; 3 sites, 3 O-linked glycans (3 sites).
DR iPTMnet; Q96FL9; -.
DR PhosphoSitePlus; Q96FL9; -.
DR BioMuta; GALNT14; -.
DR DMDM; 51316071; -.
DR EPD; Q96FL9; -.
DR MassIVE; Q96FL9; -.
DR MaxQB; Q96FL9; -.
DR PaxDb; Q96FL9; -.
DR PeptideAtlas; Q96FL9; -.
DR PRIDE; Q96FL9; -.
DR ProteomicsDB; 3748; -.
DR ProteomicsDB; 76541; -. [Q96FL9-1]
DR ProteomicsDB; 76542; -. [Q96FL9-2]
DR ProteomicsDB; 76543; -. [Q96FL9-3]
DR Antibodypedia; 2530; 227 antibodies from 24 providers.
DR DNASU; 79623; -.
DR Ensembl; ENST00000324589.9; ENSP00000314500.5; ENSG00000158089.15. [Q96FL9-3]
DR Ensembl; ENST00000349752.10; ENSP00000288988.6; ENSG00000158089.15. [Q96FL9-1]
DR Ensembl; ENST00000406653.5; ENSP00000385435.1; ENSG00000158089.15. [Q96FL9-4]
DR GeneID; 79623; -.
DR KEGG; hsa:79623; -.
DR MANE-Select; ENST00000349752.10; ENSP00000288988.6; NM_024572.4; NP_078848.2.
DR UCSC; uc002rnq.4; human. [Q96FL9-1]
DR CTD; 79623; -.
DR DisGeNET; 79623; -.
DR GeneCards; GALNT14; -.
DR HGNC; HGNC:22946; GALNT14.
DR HPA; ENSG00000158089; Tissue enhanced (kidney).
DR MIM; 608225; gene.
DR neXtProt; NX_Q96FL9; -.
DR OpenTargets; ENSG00000158089; -.
DR PharmGKB; PA134920089; -.
DR VEuPathDB; HostDB:ENSG00000158089; -.
DR GeneTree; ENSGT00940000158182; -.
DR HOGENOM; CLU_013477_0_2_1; -.
DR InParanoid; Q96FL9; -.
DR OMA; QLCLSVH; -.
DR OrthoDB; 606683at2759; -.
DR PhylomeDB; Q96FL9; -.
DR TreeFam; TF313267; -.
DR BRENDA; 2.4.1.41; 2681.
DR PathwayCommons; Q96FL9; -.
DR Reactome; R-HSA-913709; O-linked glycosylation of mucins.
DR SignaLink; Q96FL9; -.
DR UniPathway; UPA00378; -.
DR BioGRID-ORCS; 79623; 7 hits in 1059 CRISPR screens.
DR ChiTaRS; GALNT14; human.
DR GeneWiki; GALNT14; -.
DR GenomeRNAi; 79623; -.
DR Pharos; Q96FL9; Tchem.
DR PRO; PR:Q96FL9; -.
DR Proteomes; UP000005640; Chromosome 2.
DR RNAct; Q96FL9; protein.
DR Bgee; ENSG00000158089; Expressed in lower esophagus mucosa and 126 other tissues.
DR ExpressionAtlas; Q96FL9; baseline and differential.
DR Genevisible; Q96FL9; 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: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 Alternative splicing; Disulfide bond; Glycosyltransferase; Golgi apparatus;
KW Lectin; Manganese; Membrane; Metal-binding; Reference proteome;
KW Signal-anchor; Transferase; Transmembrane; Transmembrane helix.
FT CHAIN 1..552
FT /note="Polypeptide N-acetylgalactosaminyltransferase 14"
FT /id="PRO_0000059133"
FT TOPO_DOM 1..6
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 7..26
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 27..552
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT DOMAIN 415..550
FT /note="Ricin B-type lectin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00174"
FT REGION 110..215
FT /note="Catalytic subdomain A"
FT REGION 274..336
FT /note="Catalytic subdomain B"
FT BINDING 151
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 176
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 199
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250"
FT BINDING 200
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 201
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250"
FT BINDING 305
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 333
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250"
FT BINDING 336
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 339
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 341
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT DISULFID 101..328
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00174"
FT DISULFID 319..397
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00174"
FT DISULFID 430..449
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00174"
FT DISULFID 476..493
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00174"
FT DISULFID 517..538
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00174"
FT VAR_SEQ 1..43
FT /note="MRRLTRRLVLPVFGVLWITVLLFFWVTKRKLEVPTGPEVQTPK -> MSFPM
FT SLARSSVPFADSGLSSSQ (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_045121"
FT VAR_SEQ 44..99
FT /note="PSDADWDDLWDQFDERRYLNAKKWRVGDDPYKLYAFNQRESERISSNRAIPD
FT TRHL -> VWSLFFKVAGMSPWAPQVPVSPTPPYQRGHLPTGGHLAVCHFPCLLQEAQF
FT HLQTQVFLQV (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_011221"
FT VAR_SEQ 100..132
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_011222"
FT VARIANT 469
FT /note="Q -> K (in dbSNP:rs2288101)"
FT /id="VAR_033948"
FT CONFLICT 368
FT /note="Q -> R (in Ref. 4; BAB14795)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 552 AA; 64321 MW; 6F2ABAA89F482696 CRC64;
MRRLTRRLVL PVFGVLWITV LLFFWVTKRK LEVPTGPEVQ TPKPSDADWD DLWDQFDERR
YLNAKKWRVG DDPYKLYAFN QRESERISSN RAIPDTRHLR CTLLVYCTDL PPTSIIITFH
NEARSTLLRT IRSVLNRTPT HLIREIILVD DFSNDPDDCK QLIKLPKVKC LRNNERQGLV
RSRIRGADIA QGTTLTFLDS HCEVNRDWLQ PLLHRVKEDY TRVVCPVIDI INLDTFTYIE
SASELRGGFD WSLHFQWEQL SPEQKARRLD PTEPIRTPII AGGLFVIDKA WFDYLGKYDM
DMDIWGGENF EISFRVWMCG GSLEIVPCSR VGHVFRKKHP YVFPDGNANT YIKNTKRTAE
VWMDEYKQYY YAARPFALER PFGNVESRLD LRKNLRCQSF KWYLENIYPE LSIPKESSIQ
KGNIRQRQKC LESQRQNNQE TPNLKLSPCA KVKGEDAKSQ VWAFTYTQQI LQEELCLSVI
TLFPGAPVVL VLCKNGDDRQ QWTKTGSHIE HIASHLCLDT DMFGDGTENG KEIVVNPCES
SLMSQHWDMV SS
