GLT10_HUMAN
ID GLT10_HUMAN Reviewed; 603 AA.
AC Q86SR1; B3KXC9; Q6IN56; Q86VP8; Q8IXJ2; Q8TEJ2; Q96IV2; Q9H8E1; Q9Y4M4;
DT 16-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT 16-AUG-2004, sequence version 2.
DT 03-AUG-2022, entry version 167.
DE RecName: Full=Polypeptide N-acetylgalactosaminyltransferase 10;
DE EC=2.4.1.41;
DE AltName: Full=Polypeptide GalNAc transferase 10;
DE Short=GalNAc-T10;
DE Short=pp-GaNTase 10;
DE AltName: Full=Protein-UDP acetylgalactosaminyltransferase 10;
DE AltName: Full=UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase 10;
GN Name=GALNT10;
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, AND TISSUE
RP SPECIFICITY.
RC TISSUE=Colon cancer;
RX PubMed=12417297; DOI=10.1016/s0014-5793(02)03399-9;
RA Cheng L., Tachibana K., Zhang Y., Guo J.-M., Tachibana K.K., Kameyama A.,
RA Wang H., Hiruma T., Iwasaki H., Togayachi A., Kudo T., Narimatsu H.;
RT "Characterization of a novel human UDP-GalNAc transferase, pp-GalNAc-T10.";
RL FEBS Lett. 531:115-121(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RA Bennett E.P.;
RL Submitted (AUG-2002) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND NUCLEOTIDE SEQUENCE
RP [LARGE SCALE MRNA] OF 117-603 (ISOFORM 2).
RC TISSUE=Brain, and Placenta;
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4).
RC TISSUE=Uterus;
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 8-366 (ISOFORM 3).
RC TISSUE=Spleen;
RX PubMed=12693554; DOI=10.1093/dnares/10.1.49;
RA Jikuya H., Takano J., Kikuno R., Hirosawa M., Nagase T., Nomura N.,
RA Ohara O.;
RT "Characterization of long cDNA clones from human adult spleen. II. The
RT complete sequences of 81 cDNA clones.";
RL DNA Res. 10:49-57(2003).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 191-603 (ISOFORM 1).
RC TISSUE=Kidney, and Skin;
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 [7]
RP X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 40-603 IN COMPLEX WITH UDP-GALNAC
RP AND GALNAC-SERINE, DISULFIDE BOND, MANGANESE-BINDING SITES, AND
RP GLYCOSYLATION AT ASN-124; ASN-146 AND ASN-593.
RX PubMed=16650853; DOI=10.1016/j.jmb.2006.03.061;
RA Kubota T., Shiba T., Sugioka S., Furukawa S., Sawaki H., Kato R.,
RA Wakatsuki S., Narimatsu H.;
RT "Structural basis of carbohydrate transfer activity by human UDP-GalNAc:
RT polypeptide alpha-N-acetylgalactosaminyltransferase (pp-GalNAc-T10).";
RL J. Mol. Biol. 359:708-727(2006).
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. Has activity
CC toward Muc5Ac and EA2 peptide substrates.
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:12417297};
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:12417297};
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=Q86SR1-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q86SR1-2; Sequence=VSP_011209;
CC Name=3;
CC IsoId=Q86SR1-3; Sequence=VSP_011212, VSP_011213;
CC Name=4;
CC IsoId=Q86SR1-4; Sequence=VSP_011207, VSP_011208, VSP_011214;
CC -!- TISSUE SPECIFICITY: Widely expressed. Expressed at high level in small
CC intestine, and at intermediate levels in stomach, pancreas, ovary,
CC thyroid gland and spleen. Weakly expressed in other tissues.
CC {ECO:0000269|PubMed:12417297}.
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: According to experiments made in rat, this enzyme is unable to
CC transfer GalNAc onto serine or threonine residue on the protein
CC receptor, but instead requires the prior addition of a GalNAc on a
CC peptide before adding additional GalNAc moieties, thereby acting as a
CC glycopeptide transferase. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAB14676.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC -!- WEB RESOURCE: Name=Functional Glycomics Gateway - GTase;
CC Note=Polypeptide N-acetylgalactosaminyltransferase 10;
CC URL="http://www.functionalglycomics.org/glycomics/molecule/jsp/glycoEnzyme/viewGlycoEnzyme.jsp?gbpId=gt_hum_492";
CC -!- WEB RESOURCE: Name=Functional Glycomics Gateway - GTase;
CC Note=Polypeptide N-acetylgalactosaminyltransferase 10;
CC URL="http://www.functionalglycomics.org/glycomics/molecule/jsp/glycoEnzyme/viewGlycoEnzyme.jsp?gbpId=gt_hum_493";
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DR EMBL; AB078145; BAC56890.1; -; mRNA.
DR EMBL; AJ505950; CAD44532.1; -; mRNA.
DR EMBL; AK023782; BAB14676.1; ALT_INIT; mRNA.
DR EMBL; AK127135; BAG54441.1; -; mRNA.
DR EMBL; AL096739; CAB46378.1; -; mRNA.
DR EMBL; AK074132; BAB84958.1; -; mRNA.
DR EMBL; BC007224; AAH07224.2; -; mRNA.
DR EMBL; BC072450; AAH72450.1; -; mRNA.
DR CCDS; CCDS4325.1; -. [Q86SR1-1]
DR PIR; T12552; T12552.
DR RefSeq; NP_938080.1; NM_198321.3. [Q86SR1-1]
DR PDB; 2D7I; X-ray; 2.50 A; A=40-603.
DR PDB; 2D7R; X-ray; 2.80 A; A=40-603.
DR PDBsum; 2D7I; -.
DR PDBsum; 2D7R; -.
DR AlphaFoldDB; Q86SR1; -.
DR SMR; Q86SR1; -.
DR BioGRID; 120723; 72.
DR IntAct; Q86SR1; 4.
DR MINT; Q86SR1; -.
DR STRING; 9606.ENSP00000297107; -.
DR BindingDB; Q86SR1; -.
DR ChEMBL; CHEMBL4523371; -.
DR CAZy; CBM13; Carbohydrate-Binding Module Family 13.
DR CAZy; GT27; Glycosyltransferase Family 27.
DR UniLectin; Q86SR1; -.
DR GlyGen; Q86SR1; 5 sites, 1 O-linked glycan (2 sites).
DR iPTMnet; Q86SR1; -.
DR PhosphoSitePlus; Q86SR1; -.
DR SwissPalm; Q86SR1; -.
DR BioMuta; GALNT10; -.
DR DMDM; 51315962; -.
DR EPD; Q86SR1; -.
DR jPOST; Q86SR1; -.
DR MassIVE; Q86SR1; -.
DR MaxQB; Q86SR1; -.
DR PaxDb; Q86SR1; -.
DR PeptideAtlas; Q86SR1; -.
DR PRIDE; Q86SR1; -.
DR ProteomicsDB; 69624; -. [Q86SR1-1]
DR ProteomicsDB; 69625; -. [Q86SR1-2]
DR ProteomicsDB; 69626; -. [Q86SR1-3]
DR ProteomicsDB; 69627; -. [Q86SR1-4]
DR Antibodypedia; 2029; 164 antibodies from 25 providers.
DR DNASU; 55568; -.
DR Ensembl; ENST00000297107.11; ENSP00000297107.6; ENSG00000164574.16. [Q86SR1-1]
DR Ensembl; ENST00000377661.2; ENSP00000366889.2; ENSG00000164574.16. [Q86SR1-2]
DR Ensembl; ENST00000425427.6; ENSP00000415210.2; ENSG00000164574.16. [Q86SR1-3]
DR GeneID; 55568; -.
DR KEGG; hsa:55568; -.
DR MANE-Select; ENST00000297107.11; ENSP00000297107.6; NM_198321.4; NP_938080.1.
DR UCSC; uc003lvg.2; human. [Q86SR1-1]
DR CTD; 55568; -.
DR DisGeNET; 55568; -.
DR GeneCards; GALNT10; -.
DR HGNC; HGNC:19873; GALNT10.
DR HPA; ENSG00000164574; Tissue enhanced (ovary).
DR MIM; 608043; gene.
DR neXtProt; NX_Q86SR1; -.
DR OpenTargets; ENSG00000164574; -.
DR PharmGKB; PA134870832; -.
DR VEuPathDB; HostDB:ENSG00000164574; -.
DR eggNOG; KOG3736; Eukaryota.
DR GeneTree; ENSGT00940000156690; -.
DR HOGENOM; CLU_013477_3_3_1; -.
DR InParanoid; Q86SR1; -.
DR OMA; DHSNFNY; -.
DR OrthoDB; 276134at2759; -.
DR PhylomeDB; Q86SR1; -.
DR TreeFam; TF313267; -.
DR PathwayCommons; Q86SR1; -.
DR Reactome; R-HSA-913709; O-linked glycosylation of mucins.
DR SignaLink; Q86SR1; -.
DR UniPathway; UPA00378; -.
DR BioGRID-ORCS; 55568; 13 hits in 1078 CRISPR screens.
DR ChiTaRS; GALNT10; human.
DR EvolutionaryTrace; Q86SR1; -.
DR GenomeRNAi; 55568; -.
DR Pharos; Q86SR1; Tchem.
DR PRO; PR:Q86SR1; -.
DR Proteomes; UP000005640; Chromosome 5.
DR RNAct; Q86SR1; protein.
DR Bgee; ENSG00000164574; Expressed in tendon of biceps brachii and 167 other tissues.
DR ExpressionAtlas; Q86SR1; baseline and differential.
DR Genevisible; Q86SR1; 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; IDA:GO_Central.
DR GO; GO:0016266; P:O-glycan processing; IDA:GO_Central.
DR GO; GO:0006493; P:protein O-linked glycosylation; IDA: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 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..603
FT /note="Polypeptide N-acetylgalactosaminyltransferase 10"
FT /id="PRO_0000059122"
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..603
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT DOMAIN 458..590
FT /note="Ricin B-type lectin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00174"
FT REGION 38..59
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 144..253
FT /note="Catalytic subdomain A"
FT REGION 311..373
FT /note="Catalytic subdomain B"
FT REGION 373..384
FT /note="Flexible loop"
FT BINDING 154
FT /ligand="substrate"
FT BINDING 156
FT /ligand="substrate"
FT BINDING 185
FT /ligand="substrate"
FT BINDING 214
FT /ligand="substrate"
FT BINDING 237
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT BINDING 238
FT /ligand="substrate"
FT BINDING 239
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT BINDING 342
FT /ligand="substrate"
FT BINDING 370
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT BINDING 373
FT /ligand="substrate"
FT BINDING 378
FT /ligand="substrate"
FT CARBOHYD 124
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:16650853"
FT CARBOHYD 146
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:16650853"
FT CARBOHYD 593
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:16650853"
FT DISULFID 135..365
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00174,
FT ECO:0000269|PubMed:16650853"
FT DISULFID 356..432
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00174,
FT ECO:0000269|PubMed:16650853"
FT DISULFID 471..488
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00174,
FT ECO:0000269|PubMed:16650853"
FT DISULFID 523..538
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00174,
FT ECO:0000269|PubMed:16650853"
FT DISULFID 563..578
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00174,
FT ECO:0000269|PubMed:16650853"
FT VAR_SEQ 1..329
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:17974005"
FT /id="VSP_011207"
FT VAR_SEQ 190..251
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_011209"
FT VAR_SEQ 330..352
FT /note="WELGGYDPGLEIWGGEQYEISFK -> MLAWRDGELEAETSSSLFLLAMQ
FT (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:17974005"
FT /id="VSP_011208"
FT VAR_SEQ 354..366
FT /note="WMCGGRMEDIPCS -> SQLSRRPVLGTAS (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:12693554"
FT /id="VSP_011212"
FT VAR_SEQ 367..603
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:12693554"
FT /id="VSP_011213"
FT VAR_SEQ 389
FT /note="N -> VRT (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:17974005"
FT /id="VSP_011214"
FT CONFLICT 518
FT /note="H -> Y (in Ref. 1; BAC56890 and 3; BAB14676)"
FT /evidence="ECO:0000305"
FT HELIX 77..84
FT /evidence="ECO:0007829|PDB:2D7I"
FT HELIX 91..93
FT /evidence="ECO:0007829|PDB:2D7I"
FT TURN 100..103
FT /evidence="ECO:0007829|PDB:2D7I"
FT HELIX 106..109
FT /evidence="ECO:0007829|PDB:2D7I"
FT HELIX 115..119
FT /evidence="ECO:0007829|PDB:2D7I"
FT HELIX 133..136
FT /evidence="ECO:0007829|PDB:2D7I"
FT STRAND 140..143
FT /evidence="ECO:0007829|PDB:2D7I"
FT STRAND 147..155
FT /evidence="ECO:0007829|PDB:2D7I"
FT HELIX 158..171
FT /evidence="ECO:0007829|PDB:2D7I"
FT HELIX 174..176
FT /evidence="ECO:0007829|PDB:2D7I"
FT STRAND 177..184
FT /evidence="ECO:0007829|PDB:2D7I"
FT HELIX 190..192
FT /evidence="ECO:0007829|PDB:2D7I"
FT HELIX 194..200
FT /evidence="ECO:0007829|PDB:2D7I"
FT STRAND 206..210
FT /evidence="ECO:0007829|PDB:2D7I"
FT HELIX 217..227
FT /evidence="ECO:0007829|PDB:2D7I"
FT STRAND 230..235
FT /evidence="ECO:0007829|PDB:2D7I"
FT STRAND 238..242
FT /evidence="ECO:0007829|PDB:2D7I"
FT HELIX 248..256
FT /evidence="ECO:0007829|PDB:2D7I"
FT STRAND 260..269
FT /evidence="ECO:0007829|PDB:2D7I"
FT TURN 271..273
FT /evidence="ECO:0007829|PDB:2D7I"
FT STRAND 285..288
FT /evidence="ECO:0007829|PDB:2D7I"
FT STRAND 294..297
FT /evidence="ECO:0007829|PDB:2D7I"
FT TURN 301..303
FT /evidence="ECO:0007829|PDB:2D7I"
FT STRAND 319..325
FT /evidence="ECO:0007829|PDB:2D7I"
FT HELIX 326..331
FT /evidence="ECO:0007829|PDB:2D7I"
FT STRAND 341..344
FT /evidence="ECO:0007829|PDB:2D7I"
FT HELIX 345..355
FT /evidence="ECO:0007829|PDB:2D7I"
FT STRAND 359..370
FT /evidence="ECO:0007829|PDB:2D7I"
FT HELIX 386..397
FT /evidence="ECO:0007829|PDB:2D7I"
FT HELIX 399..401
FT /evidence="ECO:0007829|PDB:2D7I"
FT HELIX 402..406
FT /evidence="ECO:0007829|PDB:2D7I"
FT HELIX 410..412
FT /evidence="ECO:0007829|PDB:2D7I"
FT HELIX 421..430
FT /evidence="ECO:0007829|PDB:2D7I"
FT HELIX 435..441
FT /evidence="ECO:0007829|PDB:2D7I"
FT HELIX 446..449
FT /evidence="ECO:0007829|PDB:2D7I"
FT STRAND 458..465
FT /evidence="ECO:0007829|PDB:2D7I"
FT TURN 466..468
FT /evidence="ECO:0007829|PDB:2D7I"
FT TURN 478..480
FT /evidence="ECO:0007829|PDB:2D7I"
FT HELIX 495..497
FT /evidence="ECO:0007829|PDB:2D7I"
FT STRAND 503..505
FT /evidence="ECO:0007829|PDB:2D7I"
FT TURN 507..509
FT /evidence="ECO:0007829|PDB:2D7R"
FT STRAND 511..514
FT /evidence="ECO:0007829|PDB:2D7I"
FT STRAND 521..525
FT /evidence="ECO:0007829|PDB:2D7R"
FT STRAND 528..532
FT /evidence="ECO:0007829|PDB:2D7I"
FT STRAND 534..537
FT /evidence="ECO:0007829|PDB:2D7R"
FT STRAND 540..543
FT /evidence="ECO:0007829|PDB:2D7I"
FT STRAND 548..550
FT /evidence="ECO:0007829|PDB:2D7R"
FT TURN 551..553
FT /evidence="ECO:0007829|PDB:2D7R"
FT STRAND 554..556
FT /evidence="ECO:0007829|PDB:2D7R"
FT TURN 558..560
FT /evidence="ECO:0007829|PDB:2D7I"
FT STRAND 563..566
FT /evidence="ECO:0007829|PDB:2D7I"
FT TURN 568..570
FT /evidence="ECO:0007829|PDB:2D7I"
FT STRAND 573..576
FT /evidence="ECO:0007829|PDB:2D7I"
FT STRAND 587..591
FT /evidence="ECO:0007829|PDB:2D7I"
FT HELIX 594..597
FT /evidence="ECO:0007829|PDB:2D7I"
FT TURN 598..601
FT /evidence="ECO:0007829|PDB:2D7I"
SQ SEQUENCE 603 AA; 68992 MW; EE176F6139B92573 CRC64;
MRRKEKRLLQ AVALVLAALV LLPNVGLWAL YRERQPDGTP GGSGAAVAPA AGQGSHSRQK
KTFFLGDGQK LKDWHDKEAI RRDAQRVGNG EQGRPYPMTD AERVDQAYRE NGFNIYVSDK
ISLNRSLPDI RHPNCNSKRY LETLPNTSII IPFHNEGWSS LLRTVHSVLN RSPPELVAEI
VLVDDFSDRE HLKKPLEDYM ALFPSVRILR TKKREGLIRT RMLGASVATG DVITFLDSHC
EANVNWLPPL LDRIARNRKT IVCPMIDVID HDDFRYETQA GDAMRGAFDW EMYYKRIPIP
PELQKADPSD PFESPVMAGG LFAVDRKWFW ELGGYDPGLE IWGGEQYEIS FKVWMCGGRM
EDIPCSRVGH IYRKYVPYKV PAGVSLARNL KRVAEVWMDE YAEYIYQRRP EYRHLSAGDV
AVQKKLRSSL NCKSFKWFMT KIAWDLPKFY PPVEPPAAAW GEIRNVGTGL CADTKHGALG
SPLRLEGCVR GRGEAAWNNM QVFTFTWRED IRPGDPQHTK KFCFDAISHT SPVTLYDCHS
MKGNQLWKYR KDKTLYHPVS GSCMDCSESD HRIFMNTCNP SSLTQQWLFE HTNSTVLEKF
NRN
