GALT1_MOUSE
ID GALT1_MOUSE Reviewed; 559 AA.
AC O08912; Q5BKS3; Q7TND1;
DT 27-APR-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1997, sequence version 1.
DT 03-AUG-2022, entry version 184.
DE RecName: Full=Polypeptide N-acetylgalactosaminyltransferase 1 {ECO:0000305};
DE EC=2.4.1.41 {ECO:0000269|PubMed:9153242};
DE AltName: Full=Polypeptide GalNAc transferase 1;
DE Short=GalNAc-T1;
DE Short=pp-GaNTase 1;
DE AltName: Full=Protein-UDP acetylgalactosaminyltransferase 1;
DE AltName: Full=UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase 1;
DE Contains:
DE RecName: Full=Polypeptide N-acetylgalactosaminyltransferase 1 soluble form;
GN Name=Galnt1 {ECO:0000312|MGI:MGI:894693};
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY, COFACTOR,
RP PATHWAY, AND TISSUE SPECIFICITY.
RX PubMed=9153242; DOI=10.1074/jbc.272.21.13843;
RA Hagen F.K., Ten Hagen K.G., Beres T.M., Balys M.M., VanWuyckhuyse B.C.,
RA Tabak L.A.;
RT "cDNA cloning and expression of a novel UDP-N-acetyl-D-
RT galactosamine:polypeptide N-acetylgalactosaminyltransferase.";
RL J. Biol. Chem. 272:13843-13848(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Brain, and Embryo;
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 [3]
RP FUNCTION, CATALYTIC ACTIVITY, PATHWAY, DOMAIN, AND MUTAGENESIS OF HIS-125;
RP GLU-127; GLU-150; ASP-155; ASP-156; ASP-209; HIS-211; GLU-213; ASP-310;
RP GLU-319; ASN-320; GLU-322; HIS-341; ASP-375; GLU-376; ASP-444; GLY-455;
RP PHE-457; HIS-460; GLY-464; ASN-465 AND GLN-466.
RX PubMed=10037781; DOI=10.1074/jbc.274.10.6797;
RA Hagen F.K., Hazes B., Raffo R., deSa D., Tabak L.A.;
RT "Structure-function analysis of the UDP-N-acetyl-D-
RT galactosamine:polypeptide N-acetylgalactosaminyltransferase. Essential
RT residues lie in a predicted active site cleft resembling a lactose
RT repressor fold.";
RL J. Biol. Chem. 274:6797-6803(1999).
RN [4]
RP TISSUE SPECIFICITY.
RX PubMed=12651884; DOI=10.1093/glycob/cwg062;
RA Young W.W. Jr., Holcomb D.R., Ten Hagen K.G., Tabak L.A.;
RT "Expression of UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase
RT isoforms in murine tissues determined by real-time PCR: a new view of a
RT large family.";
RL Glycobiology 13:549-557(2003).
RN [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Kidney, Pancreas, Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [6]
RP X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 88-559 IN COMPLEX WITH MANGANESE,
RP GLYCOSYLATION AT ASN-552, AND DISULFIDE BONDS.
RX PubMed=15486088; DOI=10.1073/pnas.0405657101;
RA Fritz T.A., Hurley J.H., Trinh L.B., Shiloach J., Tabak L.A.;
RT "The beginnings of mucin biosynthesis: the crystal structure of UDP-
RT GalNAc:polypeptide alpha-N-acetylgalactosaminyltransferase-T1.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:15307-15312(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 (PubMed:9153242,
CC PubMed:10037781). Has a broad spectrum of substrates such as apomucin-,
CC MUC5AC-, MUC1- and MUC2-derived peptides (By similarity).
CC {ECO:0000250|UniProtKB:Q10472, ECO:0000269|PubMed:10037781,
CC ECO:0000269|PubMed:9153242}.
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:10037781, ECO:0000269|PubMed:9153242};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:23957;
CC Evidence={ECO:0000305|PubMed:10037781, ECO:0000305|PubMed:9153242};
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:10037781, ECO:0000269|PubMed:9153242};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:52425;
CC Evidence={ECO:0000305|PubMed:10037781, ECO:0000305|PubMed:9153242};
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000269|PubMed:9153242};
CC -!- PATHWAY: Protein modification; protein glycosylation.
CC {ECO:0000269|PubMed:10037781, ECO:0000269|PubMed:9153242}.
CC -!- SUBCELLULAR LOCATION: [Polypeptide N-acetylgalactosaminyltransferase
CC 1]: Golgi apparatus, Golgi stack membrane {ECO:0000250}; Single-pass
CC type II membrane protein {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: [Polypeptide N-acetylgalactosaminyltransferase 1
CC soluble form]: Secreted {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Widely expressed at high level. Higher expression
CC in kidney, heart, small intestine and cervix and to a lesser extent in
CC all the other tissues tested. {ECO:0000269|PubMed:12651884,
CC ECO:0000269|PubMed:9153242}.
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:0000269|PubMed:10037781}.
CC -!- DOMAIN: The ricin B-type lectin domain directs the glycopeptide
CC specificity. It is required in the glycopeptide specificity of enzyme
CC activity but not for activity with naked peptide substrates, suggesting
CC that it triggers the catalytic domain to act on GalNAc-glycopeptide
CC substrates (By similarity). {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the glycosyltransferase 2 family. GalNAc-T
CC subfamily. {ECO:0000305}.
CC -!- WEB RESOURCE: Name=Functional Glycomics Gateway - GTase;
CC Note=Polypeptide N-acetylgalactosaminyltransferase 1;
CC URL="http://www.functionalglycomics.org/glycomics/molecule/jsp/glycoEnzyme/viewGlycoEnzyme.jsp?gbpId=gt_mou_510";
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DR EMBL; U73820; AAB58477.1; -; mRNA.
DR EMBL; BC056215; AAH56215.1; -; mRNA.
DR EMBL; BC090962; AAH90962.1; -; mRNA.
DR CCDS; CCDS29100.1; -.
DR RefSeq; NP_001153876.1; NM_001160404.1.
DR RefSeq; NP_038842.3; NM_013814.3.
DR RefSeq; XP_006525713.1; XM_006525650.2.
DR PDB; 1XHB; X-ray; 2.50 A; A=88-559.
DR PDBsum; 1XHB; -.
DR AlphaFoldDB; O08912; -.
DR SMR; O08912; -.
DR BioGRID; 199820; 3.
DR STRING; 10090.ENSMUSP00000000430; -.
DR CAZy; CBM13; Carbohydrate-Binding Module Family 13.
DR CAZy; GT27; Glycosyltransferase Family 27.
DR UniLectin; O08912; -.
DR GlyGen; O08912; 2 sites.
DR iPTMnet; O08912; -.
DR PhosphoSitePlus; O08912; -.
DR SwissPalm; O08912; -.
DR EPD; O08912; -.
DR MaxQB; O08912; -.
DR PaxDb; O08912; -.
DR PeptideAtlas; O08912; -.
DR PRIDE; O08912; -.
DR ProteomicsDB; 268840; -.
DR Antibodypedia; 2480; 69 antibodies from 13 providers.
DR DNASU; 14423; -.
DR Ensembl; ENSMUST00000000430; ENSMUSP00000000430; ENSMUSG00000000420.
DR Ensembl; ENSMUST00000170243; ENSMUSP00000132142; ENSMUSG00000000420.
DR Ensembl; ENSMUST00000178605; ENSMUSP00000137427; ENSMUSG00000000420.
DR GeneID; 14423; -.
DR KEGG; mmu:14423; -.
DR UCSC; uc008egq.2; mouse.
DR CTD; 2589; -.
DR MGI; MGI:894693; Galnt1.
DR VEuPathDB; HostDB:ENSMUSG00000000420; -.
DR eggNOG; KOG3736; Eukaryota.
DR GeneTree; ENSGT00940000154732; -.
DR HOGENOM; CLU_013477_0_1_1; -.
DR InParanoid; O08912; -.
DR OMA; VAEVWMC; -.
DR OrthoDB; 606683at2759; -.
DR PhylomeDB; O08912; -.
DR TreeFam; TF313267; -.
DR BRENDA; 2.4.1.41; 3474.
DR Reactome; R-MMU-6811436; COPI-independent Golgi-to-ER retrograde traffic.
DR Reactome; R-MMU-913709; O-linked glycosylation of mucins.
DR UniPathway; UPA00378; -.
DR BioGRID-ORCS; 14423; 4 hits in 74 CRISPR screens.
DR ChiTaRS; Galnt1; mouse.
DR EvolutionaryTrace; O08912; -.
DR PRO; PR:O08912; -.
DR Proteomes; UP000000589; Chromosome 18.
DR RNAct; O08912; protein.
DR Bgee; ENSMUSG00000000420; Expressed in endothelial cell of lymphatic vessel and 295 other tissues.
DR ExpressionAtlas; O08912; baseline and differential.
DR Genevisible; O08912; MM.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0005794; C:Golgi apparatus; ISO:MGI.
DR GO; GO:0032580; C:Golgi cisterna membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; ISO:MGI.
DR GO; GO:0030246; F:carbohydrate binding; IEA:UniProtKB-KW.
DR GO; GO:0030145; F:manganese ion binding; ISS:UniProtKB.
DR GO; GO:0004653; F:polypeptide N-acetylgalactosaminyltransferase activity; IDA:MGI.
DR GO; GO:0006493; P:protein O-linked glycosylation; IDA:MGI.
DR GO; GO:0018242; P:protein O-linked glycosylation via serine; ISO:MGI.
DR GO; GO:0018243; P:protein O-linked glycosylation via threonine; ISO:MGI.
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; Disulfide bond; Glycoprotein; Glycosyltransferase;
KW Golgi apparatus; Lectin; Manganese; Membrane; Metal-binding;
KW Reference proteome; Secreted; Signal-anchor; Transferase; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..559
FT /note="Polypeptide N-acetylgalactosaminyltransferase 1"
FT /id="PRO_0000223388"
FT CHAIN 41..559
FT /note="Polypeptide N-acetylgalactosaminyltransferase 1
FT soluble form"
FT /id="PRO_0000012259"
FT TOPO_DOM 1..9
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 10..28
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 29..559
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT DOMAIN 429..551
FT /note="Ricin B-type lectin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00174"
FT REGION 115..225
FT /note="Catalytic subdomain A"
FT REGION 285..347
FT /note="Catalytic subdomain B"
FT BINDING 156
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 186
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 209
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000269|PubMed:15486088"
FT BINDING 211
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000269|PubMed:15486088"
FT BINDING 316
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 344
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000269|PubMed:15486088"
FT BINDING 347
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 352
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT CARBOHYD 95
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 552
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:15486088"
FT DISULFID 106..339
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00174,
FT ECO:0000269|PubMed:15486088"
FT DISULFID 330..408
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00174,
FT ECO:0000269|PubMed:15486088"
FT DISULFID 442..459
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00174,
FT ECO:0000269|PubMed:15486088"
FT DISULFID 482..497
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00174,
FT ECO:0000269|PubMed:15486088"
FT DISULFID 523..540
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00174,
FT ECO:0000269|PubMed:15486088"
FT MUTAGEN 125
FT /note="H->F: No effect."
FT /evidence="ECO:0000269|PubMed:10037781"
FT MUTAGEN 125
FT /note="H->Q: Induces a strong decrease in activity."
FT /evidence="ECO:0000269|PubMed:10037781"
FT MUTAGEN 127
FT /note="E->Q: Loss of enzyme activity."
FT /evidence="ECO:0000269|PubMed:10037781"
FT MUTAGEN 150
FT /note="E->Q: No effect."
FT /evidence="ECO:0000269|PubMed:10037781"
FT MUTAGEN 155
FT /note="D->N: No effect; specificity not affected."
FT /evidence="ECO:0000269|PubMed:10037781"
FT MUTAGEN 156
FT /note="D->Q: Loss of enzyme activity."
FT /evidence="ECO:0000269|PubMed:10037781"
FT MUTAGEN 209
FT /note="D->N,A,E: Loss of enzyme activity."
FT /evidence="ECO:0000269|PubMed:10037781"
FT MUTAGEN 211
FT /note="H->A,D: Loss of enzyme activity."
FT /evidence="ECO:0000269|PubMed:10037781"
FT MUTAGEN 213
FT /note="E->Q: Loss of enzyme activity."
FT /evidence="ECO:0000269|PubMed:10037781"
FT MUTAGEN 310
FT /note="D->N: Loss of enzyme activity."
FT /evidence="ECO:0000269|PubMed:10037781"
FT MUTAGEN 319
FT /note="E->Q: Loss of enzyme activity."
FT /evidence="ECO:0000269|PubMed:10037781"
FT MUTAGEN 320
FT /note="N->A: No effect."
FT /evidence="ECO:0000269|PubMed:10037781"
FT MUTAGEN 322
FT /note="E->Q: Loss of enzyme activity."
FT /evidence="ECO:0000269|PubMed:10037781"
FT MUTAGEN 341
FT /note="H->A,L,V,K,R: Little or no effect."
FT /evidence="ECO:0000269|PubMed:10037781"
FT MUTAGEN 375
FT /note="D->A,N: Little or no effect."
FT /evidence="ECO:0000269|PubMed:10037781"
FT MUTAGEN 376
FT /note="E->Q: No effect."
FT /evidence="ECO:0000269|PubMed:10037781"
FT MUTAGEN 444
FT /note="D->H: Induces a decrease in activity."
FT /evidence="ECO:0000269|PubMed:10037781"
FT MUTAGEN 455
FT /note="G->V: Induces a slight decrease in activity."
FT /evidence="ECO:0000269|PubMed:10037781"
FT MUTAGEN 457
FT /note="F->H: Induces a slight decrease in activity."
FT /evidence="ECO:0000269|PubMed:10037781"
FT MUTAGEN 460
FT /note="H->K,N: Induces a slight decrease in activity."
FT /evidence="ECO:0000269|PubMed:10037781"
FT MUTAGEN 464
FT /note="G->A: Induces a slight decrease in activity."
FT /evidence="ECO:0000269|PubMed:10037781"
FT MUTAGEN 465..466
FT /note="NQ->QN: Induces a decrease in activity."
FT MUTAGEN 465
FT /note="N->A: Little or no effect. Induces a slight decrease
FT in activity; when associated with A-466."
FT /evidence="ECO:0000269|PubMed:10037781"
FT MUTAGEN 466
FT /note="Q->A: Little or no effect. Induces a slight decrease
FT in activity; when associated with A-465."
FT /evidence="ECO:0000269|PubMed:10037781"
FT CONFLICT 81
FT /note="I -> T (in Ref. 2; AAH56215)"
FT /evidence="ECO:0000305"
FT HELIX 104..107
FT /evidence="ECO:0007829|PDB:1XHB"
FT STRAND 118..126
FT /evidence="ECO:0007829|PDB:1XHB"
FT HELIX 129..141
FT /evidence="ECO:0007829|PDB:1XHB"
FT HELIX 145..147
FT /evidence="ECO:0007829|PDB:1XHB"
FT STRAND 148..155
FT /evidence="ECO:0007829|PDB:1XHB"
FT HELIX 161..163
FT /evidence="ECO:0007829|PDB:1XHB"
FT HELIX 165..172
FT /evidence="ECO:0007829|PDB:1XHB"
FT STRAND 173..176
FT /evidence="ECO:0007829|PDB:1XHB"
FT STRAND 178..182
FT /evidence="ECO:0007829|PDB:1XHB"
FT HELIX 189..199
FT /evidence="ECO:0007829|PDB:1XHB"
FT STRAND 202..214
FT /evidence="ECO:0007829|PDB:1XHB"
FT HELIX 219..228
FT /evidence="ECO:0007829|PDB:1XHB"
FT STRAND 232..241
FT /evidence="ECO:0007829|PDB:1XHB"
FT STRAND 243..245
FT /evidence="ECO:0007829|PDB:1XHB"
FT STRAND 255..259
FT /evidence="ECO:0007829|PDB:1XHB"
FT STRAND 265..269
FT /evidence="ECO:0007829|PDB:1XHB"
FT HELIX 272..277
FT /evidence="ECO:0007829|PDB:1XHB"
FT TURN 278..280
FT /evidence="ECO:0007829|PDB:1XHB"
FT STRAND 293..299
FT /evidence="ECO:0007829|PDB:1XHB"
FT HELIX 300..305
FT /evidence="ECO:0007829|PDB:1XHB"
FT HELIX 322..329
FT /evidence="ECO:0007829|PDB:1XHB"
FT STRAND 333..345
FT /evidence="ECO:0007829|PDB:1XHB"
FT HELIX 360..373
FT /evidence="ECO:0007829|PDB:1XHB"
FT HELIX 375..378
FT /evidence="ECO:0007829|PDB:1XHB"
FT HELIX 379..383
FT /evidence="ECO:0007829|PDB:1XHB"
FT HELIX 388..390
FT /evidence="ECO:0007829|PDB:1XHB"
FT HELIX 397..405
FT /evidence="ECO:0007829|PDB:1XHB"
FT HELIX 411..417
FT /evidence="ECO:0007829|PDB:1XHB"
FT STRAND 426..432
FT /evidence="ECO:0007829|PDB:1XHB"
FT STRAND 434..436
FT /evidence="ECO:0007829|PDB:1XHB"
FT TURN 437..439
FT /evidence="ECO:0007829|PDB:1XHB"
FT STRAND 441..444
FT /evidence="ECO:0007829|PDB:1XHB"
FT STRAND 455..458
FT /evidence="ECO:0007829|PDB:1XHB"
FT HELIX 464..466
FT /evidence="ECO:0007829|PDB:1XHB"
FT STRAND 468..471
FT /evidence="ECO:0007829|PDB:1XHB"
FT STRAND 476..478
FT /evidence="ECO:0007829|PDB:1XHB"
FT STRAND 481..484
FT /evidence="ECO:0007829|PDB:1XHB"
FT STRAND 493..496
FT /evidence="ECO:0007829|PDB:1XHB"
FT HELIX 502..504
FT /evidence="ECO:0007829|PDB:1XHB"
FT STRAND 506..509
FT /evidence="ECO:0007829|PDB:1XHB"
FT TURN 510..513
FT /evidence="ECO:0007829|PDB:1XHB"
FT STRAND 514..520
FT /evidence="ECO:0007829|PDB:1XHB"
FT STRAND 522..526
FT /evidence="ECO:0007829|PDB:1XHB"
FT STRAND 529..531
FT /evidence="ECO:0007829|PDB:1XHB"
FT STRAND 536..539
FT /evidence="ECO:0007829|PDB:1XHB"
FT HELIX 544..546
FT /evidence="ECO:0007829|PDB:1XHB"
FT STRAND 548..550
FT /evidence="ECO:0007829|PDB:1XHB"
SQ SEQUENCE 559 AA; 64255 MW; AC5AB655D91F83E4 CRC64;
MRKFAYCKVV LATSLVWVLL DMFLLLYFSE CNKCEEKQER GLPAGDVLEL VQKPHEGPGE
MGKPVVIPKE DQEKMKEMFK INQFNLMASE MIALNRSLPD VRLEGCKTKV YPDNLPTTSV
VIVFHNEAWS TLLRTVHSVI NRSPRHMIEE IVLVDDASER DFLKRPLESY VKKLKVPVHV
IRMEQRSGLI RARLKGAAVS RGQVITFLDA HCECTAGWLE PLLARIKHDR RTVVCPIIDV
ISDDTFEYMA GSDMTYGGFN WKLNFRWYPV PQREMDRRKG DRTLPVRTPT MAGGLFSIDR
DYFQEIGTYD AGMDIWGGEN LEISFRIWQC GGTLEIVTCS HVGHVFRKAT PYTFPGGTGQ
IINKNNRRLA EVWMDEFKNF FYIISPGVTK VDYGDISSRL GLRRKLQCKP FSWYLENIYP
DSQIPRHYFS LGEIRNVETN QCLDNMARKE NEKVGIFNCH GMGGNQVFSY TANKEIRTDD
LCLDVSKLNG PVTMLKCHHL KGNQLWEYDP VKLTLQHVNS NQCLDKATEE DSQVPSIRDC
TGSRSQQWLL RNVTLPEIF
