B4GT7_HUMAN
ID B4GT7_HUMAN Reviewed; 327 AA.
AC Q9UBV7; B3KN39; Q9UHN2;
DT 21-FEB-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 197.
DE RecName: Full=Beta-1,4-galactosyltransferase 7;
DE Short=Beta-1,4-GalTase 7;
DE Short=Beta4Gal-T7;
DE Short=b4Gal-T7;
DE EC=2.4.1.-;
DE AltName: Full=Proteoglycan UDP-galactose:beta-xylose beta1,4-galactosyltransferase I;
DE AltName: Full=UDP-Gal:beta-GlcNAc beta-1,4-galactosyltransferase 7;
DE AltName: Full=UDP-galactose:beta-N-acetylglucosamine beta-1,4-galactosyltransferase 7;
DE AltName: Full=UDP-galactose:beta-xylose beta-1,4-galactosyltransferase;
DE AltName: Full=XGPT;
DE AltName: Full=XGalT-1;
DE AltName: Full=Xylosylprotein 4-beta-galactosyltransferase;
DE EC=2.4.1.133;
DE AltName: Full=Xylosylprotein beta-1,4-galactosyltransferase;
GN Name=B4GALT7; Synonyms=XGALT1; ORFNames=UNQ748/PRO1478;
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].
RX PubMed=10473568; DOI=10.1074/jbc.274.37.26165;
RA Almeida R., Levery S.B., Mandel U., Kresse H., Schwientek T., Bennett E.P.,
RA Clausen H.;
RT "Cloning and expression of a proteoglycan UDP-galactose:beta-xylose
RT beta1,4-galactosyltransferase I. A seventh member of the human beta4-
RT galactosyltransferase gene family.";
RL J. Biol. Chem. 274:26165-26171(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Melanoma;
RX PubMed=10438455; DOI=10.1074/jbc.274.33.22915;
RA Okajima T., Yoshida K., Kondo T., Furukawa K.;
RT "Human homolog of Caenorhabditis elegans sqv-3 gene is
RT galactosyltransferase I involved in the biosynthesis of the
RT glycosaminoglycan-protein linkage region of proteoglycans.";
RL J. Biol. Chem. 274:22915-22918(1999).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Lo N.-W., Shaper N.L., Shaper J.H.;
RT "Human beta-1,4-galactosyltransferase VII.";
RL Submitted (APR-1999) to the EMBL/GenBank/DDBJ databases.
RN [4]
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=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 [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].
RC TISSUE=Pancreas, 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 [8]
RP X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 81-327 IN COMPLEX WITH UDP AND
RP MANGANESE IONS, CATALYTIC ACTIVITY, FUNCTION, AND COFACTOR.
RX PubMed=24052259; DOI=10.1074/jbc.m113.509984;
RA Tsutsui Y., Ramakrishnan B., Qasba P.K.;
RT "Crystal structures of beta-1,4-galactosyltransferase 7 enzyme reveal
RT conformational changes and substrate Binding.";
RL J. Biol. Chem. 288:31963-31970(2013).
RN [9]
RP VARIANTS EDSSPD1 ASP-186 AND PRO-206.
RX PubMed=10506123; DOI=10.1074/jbc.274.41.28841;
RA Okajima T., Fukumoto S., Furukawa K., Urano T.;
RT "Molecular basis for the progeroid variant of Ehlers-Danlos syndrome.
RT Identification and characterization of two mutations in
RT galactosyltransferase I gene.";
RL J. Biol. Chem. 274:28841-28844(1999).
RN [10]
RP REVIEW.
RX PubMed=10580128; DOI=10.1016/s0304-4165(99)00168-3;
RA Amado M., Almeida R., Schwientek T., Clausen H.;
RT "Identification and characterization of large galactosyltransferase gene
RT families: galactosyltransferases for all functions.";
RL Biochim. Biophys. Acta 1473:35-53(1999).
CC -!- FUNCTION: Required for the biosynthesis of the tetrasaccharide linkage
CC region of proteoglycans, especially for small proteoglycans in skin
CC fibroblasts. {ECO:0000269|PubMed:24052259}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=3-O-(beta-D-xylosyl)-L-seryl-[protein] + UDP-alpha-D-galactose
CC = 3-O-(beta-D-galactosyl-(1->4)-beta-D-xylosyl)-L-seryl-[protein] +
CC H(+) + UDP; Xref=Rhea:RHEA:15297, Rhea:RHEA-COMP:12567, Rhea:RHEA-
CC COMP:12570, ChEBI:CHEBI:15378, ChEBI:CHEBI:58223, ChEBI:CHEBI:66914,
CC ChEBI:CHEBI:132085, ChEBI:CHEBI:132088; EC=2.4.1.133;
CC Evidence={ECO:0000269|PubMed:24052259};
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000269|PubMed:24052259};
CC -!- PATHWAY: Protein modification; protein glycosylation.
CC -!- INTERACTION:
CC Q9UBV7; A8MQ03: CYSRT1; NbExp=3; IntAct=EBI-10319970, EBI-3867333;
CC Q9UBV7; Q15323: KRT31; NbExp=3; IntAct=EBI-10319970, EBI-948001;
CC Q9UBV7; P60409: KRTAP10-7; NbExp=3; IntAct=EBI-10319970, EBI-10172290;
CC Q9UBV7; P53611: RABGGTB; NbExp=6; IntAct=EBI-10319970, EBI-536715;
CC Q9UBV7; Q9NUH8: TMEM14B; NbExp=3; IntAct=EBI-10319970, EBI-8638294;
CC -!- SUBCELLULAR LOCATION: Golgi apparatus, Golgi stack membrane; Single-
CC pass type II membrane protein. Note=Cis cisternae of Golgi stack.
CC -!- TISSUE SPECIFICITY: High expression in heart, pancreas and liver,
CC medium in placenta and kidney, low in brain, skeletal muscle and lung.
CC -!- DISEASE: Ehlers-Danlos syndrome, spondylodysplastic type, 1 (EDSSPD1)
CC [MIM:130070]: A form of Ehlers-Danlos syndrome, a group of connective
CC tissue disorders characterized by skin hyperextensibility, articular
CC hypermobility, and tissue fragility. EDSSPD1 is an autosomal recessive
CC form characterized by short stature, developmental anomalies of the
CC forearm bones and elbow, and bowing of extremities, in addition to the
CC classic features of Ehlers-Danlos syndrome.
CC {ECO:0000269|PubMed:10506123}. Note=The disease is caused by variants
CC affecting the gene represented in this entry.
CC -!- SIMILARITY: Belongs to the glycosyltransferase 7 family. {ECO:0000305}.
CC -!- WEB RESOURCE: Name=Functional Glycomics Gateway - GTase; Note=Beta-1,4-
CC galactosyltransferase 7;
CC URL="http://www.functionalglycomics.org/glycomics/molecule/jsp/glycoEnzyme/viewGlycoEnzyme.jsp?gbpId=gt_hum_442";
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DR EMBL; AJ005382; CAB56424.1; -; mRNA.
DR EMBL; AB028600; BAA83414.1; -; mRNA.
DR EMBL; AF142675; AAF22225.1; -; mRNA.
DR EMBL; AY358578; AAQ88941.1; -; mRNA.
DR EMBL; AK023506; BAG51201.1; -; mRNA.
DR EMBL; CH471195; EAW84965.1; -; Genomic_DNA.
DR EMBL; BC007317; AAH07317.1; -; mRNA.
DR EMBL; BC062983; AAH62983.1; -; mRNA.
DR EMBL; BC072403; AAH72403.1; -; mRNA.
DR CCDS; CCDS4429.1; -.
DR RefSeq; NP_009186.1; NM_007255.2.
DR PDB; 4IRP; X-ray; 2.10 A; A/B=81-327.
DR PDB; 4IRQ; X-ray; 2.30 A; A/B/C/D=81-327.
DR PDBsum; 4IRP; -.
DR PDBsum; 4IRQ; -.
DR AlphaFoldDB; Q9UBV7; -.
DR SMR; Q9UBV7; -.
DR BioGRID; 116441; 73.
DR IntAct; Q9UBV7; 31.
DR STRING; 9606.ENSP00000029410; -.
DR CAZy; GT7; Glycosyltransferase Family 7.
DR GlyGen; Q9UBV7; 1 site.
DR iPTMnet; Q9UBV7; -.
DR PhosphoSitePlus; Q9UBV7; -.
DR SwissPalm; Q9UBV7; -.
DR BioMuta; B4GALT7; -.
DR DMDM; 13123990; -.
DR EPD; Q9UBV7; -.
DR jPOST; Q9UBV7; -.
DR MassIVE; Q9UBV7; -.
DR MaxQB; Q9UBV7; -.
DR PaxDb; Q9UBV7; -.
DR PeptideAtlas; Q9UBV7; -.
DR PRIDE; Q9UBV7; -.
DR ProteomicsDB; 84081; -.
DR Antibodypedia; 29347; 125 antibodies from 21 providers.
DR DNASU; 11285; -.
DR Ensembl; ENST00000029410.10; ENSP00000029410.5; ENSG00000027847.14.
DR GeneID; 11285; -.
DR KEGG; hsa:11285; -.
DR MANE-Select; ENST00000029410.10; ENSP00000029410.5; NM_007255.3; NP_009186.1.
DR UCSC; uc003mhy.4; human.
DR CTD; 11285; -.
DR DisGeNET; 11285; -.
DR GeneCards; B4GALT7; -.
DR HGNC; HGNC:930; B4GALT7.
DR HPA; ENSG00000027847; Low tissue specificity.
DR MalaCards; B4GALT7; -.
DR MIM; 130070; phenotype.
DR MIM; 604327; gene.
DR neXtProt; NX_Q9UBV7; -.
DR OpenTargets; ENSG00000027847; -.
DR Orphanet; 75496; B4GALT7-related spondylodysplastic Ehlers-Danlos syndrome.
DR PharmGKB; PA25229; -.
DR VEuPathDB; HostDB:ENSG00000027847; -.
DR eggNOG; KOG3917; Eukaryota.
DR GeneTree; ENSGT00940000157712; -.
DR HOGENOM; CLU_044391_5_1_1; -.
DR InParanoid; Q9UBV7; -.
DR OMA; QMNGMSN; -.
DR OrthoDB; 1201618at2759; -.
DR PhylomeDB; Q9UBV7; -.
DR TreeFam; TF312834; -.
DR BioCyc; MetaCyc:HS00459-MON; -.
DR BRENDA; 2.4.1.133; 2681.
DR BRENDA; 2.4.1.38; 2681.
DR PathwayCommons; Q9UBV7; -.
DR Reactome; R-HSA-1971475; A tetrasaccharide linker sequence is required for GAG synthesis.
DR Reactome; R-HSA-3560783; Defective B4GALT7 causes EDS, progeroid type.
DR SignaLink; Q9UBV7; -.
DR UniPathway; UPA00378; -.
DR BioGRID-ORCS; 11285; 46 hits in 1078 CRISPR screens.
DR GeneWiki; B4GALT7; -.
DR GenomeRNAi; 11285; -.
DR Pharos; Q9UBV7; Tbio.
DR PRO; PR:Q9UBV7; -.
DR Proteomes; UP000005640; Chromosome 5.
DR RNAct; Q9UBV7; protein.
DR Bgee; ENSG00000027847; Expressed in tendon of biceps brachii and 175 other tissues.
DR ExpressionAtlas; Q9UBV7; baseline and differential.
DR Genevisible; Q9UBV7; HS.
DR GO; GO:0005794; C:Golgi apparatus; IDA:UniProtKB.
DR GO; GO:0032580; C:Golgi cisterna membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0000139; C:Golgi membrane; TAS:Reactome.
DR GO; GO:0016021; C:integral component of membrane; IDA:UniProtKB.
DR GO; GO:0003831; F:beta-N-acetylglucosaminylglycopeptide beta-1,4-galactosyltransferase activity; IDA:UniProtKB.
DR GO; GO:0008378; F:galactosyltransferase activity; IDA:UniProtKB.
DR GO; GO:0030145; F:manganese ion binding; IDA:UniProtKB.
DR GO; GO:0046525; F:xylosylprotein 4-beta-galactosyltransferase activity; IDA:UniProtKB.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR GO; GO:0006024; P:glycosaminoglycan biosynthetic process; IDA:UniProtKB.
DR GO; GO:0030203; P:glycosaminoglycan metabolic process; TAS:Reactome.
DR GO; GO:0070085; P:glycosylation; IBA:GO_Central.
DR GO; GO:0048147; P:negative regulation of fibroblast proliferation; IMP:UniProtKB.
DR GO; GO:0036211; P:protein modification process; TAS:ProtInc.
DR GO; GO:0006487; P:protein N-linked glycosylation; IDA:UniProtKB.
DR GO; GO:0030166; P:proteoglycan biosynthetic process; IBA:GO_Central.
DR GO; GO:0006029; P:proteoglycan metabolic process; IMP:UniProtKB.
DR GO; GO:0097435; P:supramolecular fiber organization; IMP:UniProtKB.
DR DisProt; DP02634; -.
DR Gene3D; 3.90.550.10; -; 1.
DR InterPro; IPR003859; Galactosyl_T.
DR InterPro; IPR027791; Galactosyl_T_C.
DR InterPro; IPR027995; Galactosyl_T_N.
DR InterPro; IPR029044; Nucleotide-diphossugar_trans.
DR PANTHER; PTHR19300; PTHR19300; 1.
DR Pfam; PF02709; Glyco_transf_7C; 1.
DR Pfam; PF13733; Glyco_transf_7N; 1.
DR PRINTS; PR02050; B14GALTRFASE.
DR SUPFAM; SSF53448; SSF53448; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Disease variant; Disulfide bond; Dwarfism;
KW Ehlers-Danlos syndrome; Glycoprotein; Glycosyltransferase; Golgi apparatus;
KW Manganese; Membrane; Metal-binding; Reference proteome; Signal-anchor;
KW Transferase; Transmembrane; Transmembrane helix.
FT CHAIN 1..327
FT /note="Beta-1,4-galactosyltransferase 7"
FT /id="PRO_0000080550"
FT TOPO_DOM 1..30
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 31..51
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 52..327
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT REGION 63..87
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 100..104
FT /ligand="UDP-alpha-D-galactose"
FT /ligand_id="ChEBI:CHEBI:66914"
FT /evidence="ECO:0000269|PubMed:24052259,
FT ECO:0007744|PDB:4IRP, ECO:0007744|PDB:4IRQ"
FT BINDING 139..141
FT /ligand="UDP-alpha-D-galactose"
FT /ligand_id="ChEBI:CHEBI:66914"
FT /evidence="ECO:0000303|PubMed:24052259"
FT BINDING 164..165
FT /ligand="UDP-alpha-D-galactose"
FT /ligand_id="ChEBI:CHEBI:66914"
FT /evidence="ECO:0000269|PubMed:24052259,
FT ECO:0007744|PDB:4IRP, ECO:0007744|PDB:4IRQ"
FT BINDING 165
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000269|PubMed:24052259,
FT ECO:0007744|PDB:4IRP, ECO:0007744|PDB:4IRQ"
FT BINDING 194
FT /ligand="UDP-alpha-D-galactose"
FT /ligand_id="ChEBI:CHEBI:66914"
FT /evidence="ECO:0000269|PubMed:24052259,
FT ECO:0007744|PDB:4IRP, ECO:0007744|PDB:4IRQ"
FT BINDING 224
FT /ligand="UDP-alpha-D-galactose"
FT /ligand_id="ChEBI:CHEBI:66914"
FT /evidence="ECO:0000269|PubMed:24052259,
FT ECO:0007744|PDB:4IRQ"
FT BINDING 226..229
FT /ligand="N-acetyl-D-glucosamine"
FT /ligand_id="ChEBI:CHEBI:506227"
FT /evidence="ECO:0000305"
FT BINDING 257..259
FT /ligand="UDP-alpha-D-galactose"
FT /ligand_id="ChEBI:CHEBI:66914"
FT /evidence="ECO:0000269|PubMed:24052259,
FT ECO:0007744|PDB:4IRQ"
FT BINDING 257
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000269|PubMed:24052259,
FT ECO:0007744|PDB:4IRP, ECO:0007744|PDB:4IRQ"
FT BINDING 266
FT /ligand="UDP-alpha-D-galactose"
FT /ligand_id="ChEBI:CHEBI:66914"
FT /evidence="ECO:0000269|PubMed:24052259,
FT ECO:0007744|PDB:4IRQ"
FT CARBOHYD 154
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 316..324
FT VARIANT 186
FT /note="A -> D (in EDSSPD1; dbSNP:rs121917817)"
FT /evidence="ECO:0000269|PubMed:10506123"
FT /id="VAR_010293"
FT VARIANT 206
FT /note="L -> P (in EDSSPD1; dbSNP:rs121917818)"
FT /evidence="ECO:0000269|PubMed:10506123"
FT /id="VAR_010294"
FT CONFLICT 147
FT /note="V -> L (in Ref. 3; AAF22225)"
FT /evidence="ECO:0000305"
FT HELIX 82..84
FT /evidence="ECO:0007829|PDB:4IRP"
FT HELIX 88..90
FT /evidence="ECO:0007829|PDB:4IRP"
FT STRAND 95..103
FT /evidence="ECO:0007829|PDB:4IRP"
FT HELIX 105..121
FT /evidence="ECO:0007829|PDB:4IRP"
FT STRAND 126..133
FT /evidence="ECO:0007829|PDB:4IRP"
FT STRAND 135..137
FT /evidence="ECO:0007829|PDB:4IRP"
FT HELIX 141..151
FT /evidence="ECO:0007829|PDB:4IRP"
FT STRAND 158..162
FT /evidence="ECO:0007829|PDB:4IRP"
FT STRAND 166..168
FT /evidence="ECO:0007829|PDB:4IRP"
FT STRAND 183..186
FT /evidence="ECO:0007829|PDB:4IRP"
FT TURN 188..190
FT /evidence="ECO:0007829|PDB:4IRP"
FT STRAND 191..193
FT /evidence="ECO:0007829|PDB:4IRP"
FT STRAND 202..207
FT /evidence="ECO:0007829|PDB:4IRP"
FT HELIX 208..213
FT /evidence="ECO:0007829|PDB:4IRP"
FT STRAND 223..226
FT /evidence="ECO:0007829|PDB:4IRQ"
FT HELIX 227..237
FT /evidence="ECO:0007829|PDB:4IRP"
FT HELIX 251..253
FT /evidence="ECO:0007829|PDB:4IRQ"
FT STRAND 254..257
FT /evidence="ECO:0007829|PDB:4IRP"
FT TURN 261..263
FT /evidence="ECO:0007829|PDB:4IRQ"
FT HELIX 274..277
FT /evidence="ECO:0007829|PDB:4IRQ"
FT TURN 287..289
FT /evidence="ECO:0007829|PDB:4IRP"
FT STRAND 292..302
FT /evidence="ECO:0007829|PDB:4IRP"
FT STRAND 305..314
FT /evidence="ECO:0007829|PDB:4IRP"
FT TURN 318..320
FT /evidence="ECO:0007829|PDB:4IRP"
FT HELIX 322..325
FT /evidence="ECO:0007829|PDB:4IRP"
SQ SEQUENCE 327 AA; 37406 MW; 2EDF51A2F8143135 CRC64;
MFPSRRKAAQ LPWEDGRSGL LSGGLPRKCS VFHLFVACLS LGFFSLLWLQ LSCSGDVARA
VRGQGQETSG PPRACPPEPP PEHWEEDASW GPHRLAVLVP FRERFEELLV FVPHMRRFLS
RKKIRHHIYV LNQVDHFRFN RAALINVGFL ESSNSTDYIA MHDVDLLPLN EELDYGFPEA
GPFHVASPEL HPLYHYKTYV GGILLLSKQH YRLCNGMSNR FWGWGREDDE FYRRIKGAGL
QLFRPSGITT GYKTFRHLHD PAWRKRDQKR IAAQKQEQFK VDREGGLNTV KYHVASRTAL
SVGGAPCTVL NIMLDCDKTA TPWCTFS
