XXLT1_MOUSE
ID XXLT1_MOUSE Reviewed; 392 AA.
AC Q3U4G3; E9QL73; Q3TLX5; Q8K2I0;
DT 16-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 2.
DT 03-AUG-2022, entry version 109.
DE RecName: Full=Xyloside xylosyltransferase 1;
DE EC=2.4.2.62 {ECO:0000269|PubMed:26414444};
DE AltName: Full=UDP-xylose:alpha-xyloside alpha-1,3-xylosyltransferase;
GN Name=Xxylt1;
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 [LARGE SCALE MRNA].
RC STRAIN=NOD; TISSUE=Mammary gland;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=FVB/N; TISSUE=Mammary tumor;
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 [4] {ECO:0007744|PDB:4WLG, ECO:0007744|PDB:4WLM, ECO:0007744|PDB:4WLZ, ECO:0007744|PDB:4WM0, ECO:0007744|PDB:4WMA, ECO:0007744|PDB:4WMB, ECO:0007744|PDB:4WMI, ECO:0007744|PDB:4WMK, ECO:0007744|PDB:4WN2}
RP X-RAY CRYSTALLOGRAPHY (1.62 ANGSTROMS) OF 87-392 IN COMPLEXES WITH
RP MANGANESE IONS; F9 AND SUBSTRATES, CATALYTIC ACTIVITY, FUNCTION, COFACTOR,
RP DISULFIDE BONDS, TOPOLOGY, AND MUTAGENESIS OF ASP-225; GLU-255; GLN-257;
RP HIS-262; TRP-265; GLN-266; SER-289; ASP-319; ARG-324; GLY-325; HIS-326;
RP ASP-329; GLN-330; TRP-358; TRP-359 AND ASN-384.
RX PubMed=26414444; DOI=10.1038/nchembio.1927;
RA Yu H., Takeuchi M., LeBarron J., Kantharia J., London E., Bakker H.,
RA Haltiwanger R.S., Li H., Takeuchi H.;
RT "Notch-modifying xylosyltransferase structures support an SNi-like
RT retaining mechanism.";
RL Nat. Chem. Biol. 11:847-854(2015).
CC -!- FUNCTION: Alpha-1,3-xylosyltransferase, which elongates the O-linked
CC xylose-glucose disaccharide attached to EGF-like repeats in the
CC extracellular domain of target proteins by catalyzing the addition of
CC the second xylose. Known targets include Notch proteins and coagulation
CC factors, such as F9. {ECO:0000269|PubMed:26414444}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=3-O-[alpha-D-xylosyl-(1->3)-beta-D-glucosyl]-L-seryl-[EGF-like
CC domain protein] + UDP-alpha-D-xylose = 3-O-[alpha-D-xylosyl-(1->3)-
CC alpha-D-xylosyl-(1->3)-beta-D-glucosyl]-L-seryl-[EGF-like domain
CC protein] + H(+) + UDP; Xref=Rhea:RHEA:22820, Rhea:RHEA-COMP:14611,
CC Rhea:RHEA-COMP:14619, ChEBI:CHEBI:15378, ChEBI:CHEBI:57632,
CC ChEBI:CHEBI:58223, ChEBI:CHEBI:140575, ChEBI:CHEBI:140599;
CC EC=2.4.2.62; Evidence={ECO:0000269|PubMed:26414444};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000250|UniProtKB:Q8NBI6};
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000305|PubMed:26414444};
CC Note=Has the highest in vitro activity with 20 mM Mn(2+), a
CC concentration entirely out of the physiological range. Can also utilize
CC Mg(2+), suggesting this may be the physiological cofactor.
CC {ECO:0000250|UniProtKB:Q8NBI6};
CC -!- SUBUNIT: Homodimer (PubMed:26414444). Dimer formation may be essential
CC for the retention in endoplasmic reticulum (Probable).
CC {ECO:0000269|PubMed:26414444, ECO:0000305}.
CC -!- INTERACTION:
CC Q3U4G3; P00740: F9; Xeno; NbExp=3; IntAct=EBI-16178491, EBI-9640450;
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000250|UniProtKB:Q8NBI6}; Single-pass type II membrane protein
CC {ECO:0000250|UniProtKB:Q8NBI6}.
CC -!- SIMILARITY: Belongs to the glycosyltransferase 8 family. {ECO:0000305}.
CC -!- CAUTION: It is uncertain whether Met-1 or Met-14 is the initiator.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH31419.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AK154256; BAE32468.1; -; mRNA.
DR EMBL; AK166259; BAE38667.1; -; mRNA.
DR EMBL; AC090430; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC126280; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC031419; AAH31419.1; ALT_INIT; mRNA.
DR CCDS; CCDS49822.1; -.
DR RefSeq; NP_941028.2; NM_198626.2.
DR PDB; 4WLG; X-ray; 3.00 A; A/B=87-392.
DR PDB; 4WLM; X-ray; 3.00 A; A/B=87-392.
DR PDB; 4WLZ; X-ray; 3.03 A; A/B=87-392.
DR PDB; 4WM0; X-ray; 2.37 A; A=87-392.
DR PDB; 4WMA; X-ray; 1.62 A; A=87-392.
DR PDB; 4WMB; X-ray; 2.05 A; A=87-392.
DR PDB; 4WMI; X-ray; 1.87 A; A=87-392.
DR PDB; 4WMK; X-ray; 2.08 A; A=87-392.
DR PDB; 4WN2; X-ray; 1.95 A; A=87-392.
DR PDB; 4WNH; X-ray; 1.95 A; A=87-392.
DR PDBsum; 4WLG; -.
DR PDBsum; 4WLM; -.
DR PDBsum; 4WLZ; -.
DR PDBsum; 4WM0; -.
DR PDBsum; 4WMA; -.
DR PDBsum; 4WMB; -.
DR PDBsum; 4WMI; -.
DR PDBsum; 4WMK; -.
DR PDBsum; 4WN2; -.
DR PDBsum; 4WNH; -.
DR AlphaFoldDB; Q3U4G3; -.
DR SMR; Q3U4G3; -.
DR BioGRID; 234571; 3.
DR DIP; DIP-61862N; -.
DR IntAct; Q3U4G3; 1.
DR STRING; 10090.ENSMUSP00000050246; -.
DR CAZy; GT8; Glycosyltransferase Family 8.
DR iPTMnet; Q3U4G3; -.
DR PhosphoSitePlus; Q3U4G3; -.
DR EPD; Q3U4G3; -.
DR MaxQB; Q3U4G3; -.
DR PaxDb; Q3U4G3; -.
DR PeptideAtlas; Q3U4G3; -.
DR PRIDE; Q3U4G3; -.
DR ProteomicsDB; 300016; -.
DR Antibodypedia; 53804; 52 antibodies from 12 providers.
DR DNASU; 268880; -.
DR Ensembl; ENSMUST00000055389; ENSMUSP00000050246; ENSMUSG00000047434.
DR GeneID; 268880; -.
DR KEGG; mmu:268880; -.
DR UCSC; uc007yxa.2; mouse.
DR CTD; 152002; -.
DR MGI; MGI:2146443; Xxylt1.
DR VEuPathDB; HostDB:ENSMUSG00000047434; -.
DR eggNOG; KOG3765; Eukaryota.
DR GeneTree; ENSGT00940000158154; -.
DR HOGENOM; CLU_048175_0_0_1; -.
DR InParanoid; Q3U4G3; -.
DR OMA; TIYDVKV; -.
DR OrthoDB; 830935at2759; -.
DR PhylomeDB; Q3U4G3; -.
DR TreeFam; TF323210; -.
DR BRENDA; 2.4.2.62; 3474.
DR BioGRID-ORCS; 268880; 1 hit in 73 CRISPR screens.
DR ChiTaRS; Xxylt1; mouse.
DR PRO; PR:Q3U4G3; -.
DR Proteomes; UP000000589; Chromosome 16.
DR RNAct; Q3U4G3; protein.
DR Bgee; ENSMUSG00000047434; Expressed in embryonic post-anal tail and 140 other tissues.
DR Genevisible; Q3U4G3; MM.
DR GO; GO:0030176; C:integral component of endoplasmic reticulum membrane; ISS:UniProtKB.
DR GO; GO:0000287; F:magnesium ion binding; ISS:UniProtKB.
DR GO; GO:0030145; F:manganese ion binding; IDA:UniProtKB.
DR GO; GO:0035252; F:UDP-xylosyltransferase activity; IDA:UniProtKB.
DR GO; GO:0140560; F:xylosyl alpha-1,3-xylosyltransferase activity; ISS:UniProtKB.
DR GO; GO:0016266; P:O-glycan processing; IDA:UniProtKB.
DR Gene3D; 3.90.550.10; -; 1.
DR InterPro; IPR002495; Glyco_trans_8.
DR InterPro; IPR029044; Nucleotide-diphossugar_trans.
DR InterPro; IPR042465; XXLT1.
DR PANTHER; PTHR46612; PTHR46612; 1.
DR Pfam; PF01501; Glyco_transf_8; 1.
DR SUPFAM; SSF53448; SSF53448; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Disulfide bond; Endoplasmic reticulum; Glycosyltransferase;
KW Magnesium; Manganese; Membrane; Metal-binding; Reference proteome;
KW Signal-anchor; Transferase; Transmembrane; Transmembrane helix.
FT CHAIN 1..392
FT /note="Xyloside xylosyltransferase 1"
FT /id="PRO_0000234428"
FT TOPO_DOM 1..19
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305|PubMed:26414444"
FT TRANSMEM 20..42
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 43..392
FT /note="Lumenal"
FT /evidence="ECO:0000305|PubMed:26414444"
FT REGION 262..265
FT /note="Interaction with target proteins"
FT /evidence="ECO:0000269|PubMed:26414444"
FT BINDING 103..105
FT /ligand="UDP-alpha-D-xylose"
FT /ligand_id="ChEBI:CHEBI:57632"
FT /evidence="ECO:0000269|PubMed:26414444,
FT ECO:0007744|PDB:4WNH"
FT BINDING 225
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000269|PubMed:26414444,
FT ECO:0007744|PDB:4WLM, ECO:0007744|PDB:4WLZ,
FT ECO:0007744|PDB:4WMA, ECO:0007744|PDB:4WMB,
FT ECO:0007744|PDB:4WMI, ECO:0007744|PDB:4WMK,
FT ECO:0007744|PDB:4WN2, ECO:0007744|PDB:4WNH"
FT BINDING 226
FT /ligand="UDP-alpha-D-xylose"
FT /ligand_id="ChEBI:CHEBI:57632"
FT /evidence="ECO:0000269|PubMed:26414444,
FT ECO:0007744|PDB:4WNH"
FT BINDING 227
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000269|PubMed:26414444,
FT ECO:0007744|PDB:4WLM, ECO:0007744|PDB:4WLZ,
FT ECO:0007744|PDB:4WMA, ECO:0007744|PDB:4WMB,
FT ECO:0007744|PDB:4WMI, ECO:0007744|PDB:4WMK,
FT ECO:0007744|PDB:4WN2, ECO:0007744|PDB:4WNH"
FT BINDING 289
FT /ligand="UDP-alpha-D-xylose"
FT /ligand_id="ChEBI:CHEBI:57632"
FT /evidence="ECO:0000269|PubMed:26414444,
FT ECO:0007744|PDB:4WNH"
FT BINDING 327
FT /ligand="UDP-alpha-D-xylose"
FT /ligand_id="ChEBI:CHEBI:57632"
FT /evidence="ECO:0000269|PubMed:26414444,
FT ECO:0007744|PDB:4WNH"
FT BINDING 330
FT /ligand="a glycoprotein"
FT /ligand_id="ChEBI:CHEBI:17089"
FT /ligand_note="substrate"
FT /ligand_part="3-O-[alpha-D-xylosyl-(1->3)-beta-D-glucosyl]-
FT L-seryl residue"
FT /ligand_part_id="ChEBI:CHEBI:140575"
FT /evidence="ECO:0000269|PubMed:26414444,
FT ECO:0007744|PDB:4WM0, ECO:0007744|PDB:4WNH"
FT BINDING 330
FT /ligand="UDP-alpha-D-xylose"
FT /ligand_id="ChEBI:CHEBI:57632"
FT /evidence="ECO:0000269|PubMed:26414444,
FT ECO:0007744|PDB:4WNH"
FT BINDING 359
FT /ligand="a glycoprotein"
FT /ligand_id="ChEBI:CHEBI:17089"
FT /ligand_note="substrate"
FT /ligand_part="3-O-[alpha-D-xylosyl-(1->3)-beta-D-glucosyl]-
FT L-seryl residue"
FT /ligand_part_id="ChEBI:CHEBI:140575"
FT /evidence="ECO:0000269|PubMed:26414444,
FT ECO:0007744|PDB:4WM0, ECO:0007744|PDB:4WNH"
FT BINDING 382
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000269|PubMed:26414444,
FT ECO:0007744|PDB:4WLM, ECO:0007744|PDB:4WLZ,
FT ECO:0007744|PDB:4WMA, ECO:0007744|PDB:4WMB,
FT ECO:0007744|PDB:4WMI, ECO:0007744|PDB:4WMK,
FT ECO:0007744|PDB:4WN2, ECO:0007744|PDB:4WNH"
FT BINDING 384
FT /ligand="a glycoprotein"
FT /ligand_id="ChEBI:CHEBI:17089"
FT /ligand_note="substrate"
FT /ligand_part="3-O-[alpha-D-xylosyl-(1->3)-beta-D-glucosyl]-
FT L-seryl residue"
FT /ligand_part_id="ChEBI:CHEBI:140575"
FT /evidence="ECO:0000269|PubMed:26414444,
FT ECO:0007744|PDB:4WM0, ECO:0007744|PDB:4WNH"
FT DISULFID 349..374
FT /evidence="ECO:0007744|PDB:4WLG, ECO:0007744|PDB:4WLM,
FT ECO:0007744|PDB:4WLZ, ECO:0007744|PDB:4WM0,
FT ECO:0007744|PDB:4WMA, ECO:0007744|PDB:4WMB,
FT ECO:0007744|PDB:4WMI, ECO:0007744|PDB:4WMK,
FT ECO:0007744|PDB:4WN2, ECO:0007744|PDB:4WNH"
FT DISULFID 356..385
FT /evidence="ECO:0007744|PDB:4WLG, ECO:0007744|PDB:4WLM,
FT ECO:0007744|PDB:4WLZ, ECO:0007744|PDB:4WM0,
FT ECO:0007744|PDB:4WMA, ECO:0007744|PDB:4WMB,
FT ECO:0007744|PDB:4WMI, ECO:0007744|PDB:4WMK,
FT ECO:0007744|PDB:4WN2, ECO:0007744|PDB:4WNH"
FT MUTAGEN 225
FT /note="D->N: No effect on enzyme activity."
FT /evidence="ECO:0000269|PubMed:26414444"
FT MUTAGEN 255
FT /note="E->A: Abolishes enzyme activity."
FT /evidence="ECO:0000269|PubMed:26414444"
FT MUTAGEN 257
FT /note="Q->A: Reduces enzyme activity."
FT /evidence="ECO:0000269|PubMed:26414444"
FT MUTAGEN 262
FT /note="H->A: Reduces enzyme activity."
FT /evidence="ECO:0000269|PubMed:26414444"
FT MUTAGEN 265
FT /note="W->A: Slightly reduces enzyme activity."
FT /evidence="ECO:0000269|PubMed:26414444"
FT MUTAGEN 266
FT /note="Q->K: No effect on enzyme activity."
FT /evidence="ECO:0000269|PubMed:26414444"
FT MUTAGEN 289
FT /note="S->A: Slightly reduces enzyme activity."
FT /evidence="ECO:0000269|PubMed:26414444"
FT MUTAGEN 319
FT /note="D->N: No significant effect on enzyme activity."
FT /evidence="ECO:0000269|PubMed:26414444"
FT MUTAGEN 324
FT /note="R->S: Reduces enzyme activity."
FT /evidence="ECO:0000269|PubMed:26414444"
FT MUTAGEN 325
FT /note="G->S: Strongly reduces enzyme activity."
FT /evidence="ECO:0000269|PubMed:26414444"
FT MUTAGEN 326
FT /note="H->A: Abolishes enzyme activity."
FT /evidence="ECO:0000269|PubMed:26414444"
FT MUTAGEN 329
FT /note="D->A: Increases enzyme activity."
FT /evidence="ECO:0000269|PubMed:26414444"
FT MUTAGEN 330
FT /note="Q->A: Abolishes enzyme activity."
FT /evidence="ECO:0000269|PubMed:26414444"
FT MUTAGEN 358
FT /note="W->A: Abolishes enzyme activity."
FT /evidence="ECO:0000269|PubMed:26414444"
FT MUTAGEN 359
FT /note="W->A: Abolishes enzyme activity."
FT /evidence="ECO:0000269|PubMed:26414444"
FT MUTAGEN 384
FT /note="N->A: Abolishes enzyme activity."
FT /evidence="ECO:0000269|PubMed:26414444"
FT CONFLICT 46..47
FT /note="ET -> LP (in Ref. 3; AAH31419)"
FT /evidence="ECO:0000305"
FT CONFLICT 80..81
FT /note="AS -> GF (in Ref. 1; BAE32468 and 3; AAH31419)"
FT /evidence="ECO:0000305"
FT CONFLICT 100
FT /note="L -> Q (in Ref. 1; BAE38667)"
FT /evidence="ECO:0000305"
FT CONFLICT 110
FT /note="N -> D (in Ref. 1; BAE38667)"
FT /evidence="ECO:0000305"
FT CONFLICT 312
FT /note="S -> A (in Ref. 1; BAE38667)"
FT /evidence="ECO:0000305"
FT STRAND 96..103
FT /evidence="ECO:0007829|PDB:4WMA"
FT HELIX 111..127
FT /evidence="ECO:0007829|PDB:4WMA"
FT STRAND 134..142
FT /evidence="ECO:0007829|PDB:4WMA"
FT HELIX 144..155
FT /evidence="ECO:0007829|PDB:4WMA"
FT STRAND 165..172
FT /evidence="ECO:0007829|PDB:4WMA"
FT HELIX 173..191
FT /evidence="ECO:0007829|PDB:4WMA"
FT STRAND 192..196
FT /evidence="ECO:0007829|PDB:4WMA"
FT HELIX 199..202
FT /evidence="ECO:0007829|PDB:4WMA"
FT HELIX 203..209
FT /evidence="ECO:0007829|PDB:4WMA"
FT HELIX 210..213
FT /evidence="ECO:0007829|PDB:4WMA"
FT STRAND 220..224
FT /evidence="ECO:0007829|PDB:4WMA"
FT STRAND 226..230
FT /evidence="ECO:0007829|PDB:4WMA"
FT HELIX 235..238
FT /evidence="ECO:0007829|PDB:4WMA"
FT HELIX 239..243
FT /evidence="ECO:0007829|PDB:4WMA"
FT STRAND 250..254
FT /evidence="ECO:0007829|PDB:4WMA"
FT HELIX 259..263
FT /evidence="ECO:0007829|PDB:4WMA"
FT HELIX 265..270
FT /evidence="ECO:0007829|PDB:4WMA"
FT TURN 280..282
FT /evidence="ECO:0007829|PDB:4WMA"
FT STRAND 287..295
FT /evidence="ECO:0007829|PDB:4WMA"
FT HELIX 296..301
FT /evidence="ECO:0007829|PDB:4WMA"
FT HELIX 303..308
FT /evidence="ECO:0007829|PDB:4WMA"
FT HELIX 311..321
FT /evidence="ECO:0007829|PDB:4WMA"
FT HELIX 329..339
FT /evidence="ECO:0007829|PDB:4WMA"
FT HELIX 341..343
FT /evidence="ECO:0007829|PDB:4WMA"
FT STRAND 344..347
FT /evidence="ECO:0007829|PDB:4WMA"
FT HELIX 349..351
FT /evidence="ECO:0007829|PDB:4WMA"
FT STRAND 352..354
FT /evidence="ECO:0007829|PDB:4WMA"
FT HELIX 358..362
FT /evidence="ECO:0007829|PDB:4WMA"
FT TURN 365..367
FT /evidence="ECO:0007829|PDB:4WMA"
FT HELIX 368..372
FT /evidence="ECO:0007829|PDB:4WMA"
FT STRAND 379..382
FT /evidence="ECO:0007829|PDB:4WMA"
FT TURN 384..386
FT /evidence="ECO:0007829|PDB:4WMA"
SQ SEQUENCE 392 AA; 43839 MW; 0916EB1D7E27F08E CRC64;
MGLLRGGAAC ARAMARLGAL RSHYCALLLA AALAVCAFYY LGSGRETFSS ATKRLKEARA
GAAAPTPPAP ELARGSAAPA SGAKAKSLEG GVVVPVDYHL LMMFTKAEHN APLQAKARVA
LSSLLRLAKF EAHEVLNLHF VSEEASREVA KALLRELLPP AAGFKCKVIF HDVAVLTDKL
FPVVEAMQKY FSAGSGTYYS DSIFFLSVAM HQIMPKEIPR IIQLDLDLKY KTNIRELFEE
FDNFLPGAVI GIAREMQPVY RHTFWQFRHE NPKTRVGDPP PEGLPGFNSG VMLLNLEAMR
QSPLYSHLLE PSWVQQLADK YHFRGHLGDQ DFFTMIGMEH PELFHVLDCT WNRQLCTWWR
DHGYSDVFQA YFRCEGHVKI YHGNCNTPIP ED
