HS3SA_HUMAN
ID HS3SA_HUMAN Reviewed; 406 AA.
AC Q9Y663; A8K7N2;
DT 15-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1999, sequence version 1.
DT 03-AUG-2022, entry version 159.
DE RecName: Full=Heparan sulfate glucosamine 3-O-sulfotransferase 3A1;
DE EC=2.8.2.30 {ECO:0000269|PubMed:9988768};
DE AltName: Full=Heparan sulfate D-glucosaminyl 3-O-sulfotransferase 3A1 {ECO:0000303|PubMed:9988768};
DE Short=3-OST-3A {ECO:0000303|PubMed:9988768};
DE Short=Heparan sulfate 3-O-sulfotransferase 3A1;
DE Short=h3-OST-3A;
GN Name=HS3ST3A1; Synonyms=3OST3A1, HS3ST3A; ORFNames=UNQ2551/PRO6180;
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], AND TISSUE SPECIFICITY.
RC TISSUE=Liver;
RX PubMed=9988767; DOI=10.1074/jbc.274.8.5170;
RA Shworak N.W., Liu J., Petros L.M., Zhang L., Kobayashi M., Copeland N.G.,
RA Jenkins N.A., Rosenberg R.D.;
RT "Multiple isoforms of heparan sulfate D-glucosaminyl 3-O-sulfotransferase.
RT Isolation, characterization, and expression of human cDNAs and
RT identification of distinct genomic loci.";
RL J. Biol. Chem. 274:5170-5184(1999).
RN [2]
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Spleen;
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 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 (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain;
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 [6]
RP FUNCTION IN HSV-1 ENTRY, AND MUTAGENESIS OF LYS-162.
RX PubMed=10520990; DOI=10.1016/s0092-8674(00)80058-6;
RA Shukla D., Liu J., Blaiklock P., Shworak N.W., Bai X., Esko J.D.,
RA Cohen G.H., Eisenberg R.J., Rosenberg R.D., Spear P.G.;
RT "A novel role for 3-O-sulfated heparan sulfate in herpes simplex virus 1
RT entry.";
RL Cell 99:13-22(1999).
RN [7]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=9988768; DOI=10.1074/jbc.274.8.5185;
RA Liu J., Shworak N.W., Sinay P., Schwartz J.J., Zhang L., Fritze L.M.S.,
RA Rosenberg R.D.;
RT "Expression of heparan sulfate D-glucosaminyl 3-O-sulfotransferase isoforms
RT reveals novel substrate specificities.";
RL J. Biol. Chem. 274:5185-5192(1999).
RN [8]
RP FUNCTION.
RX PubMed=10608887; DOI=10.1074/jbc.274.53.38155;
RA Liu J., Shriver Z., Blaiklock P., Yoshida K., Sasisekharan R.,
RA Rosenberg R.D.;
RT "Heparan sulfate D-glucosaminyl 3-O-sulfotransferase-3A sulfates N-
RT unsubstituted glucosamine residues.";
RL J. Biol. Chem. 274:38155-38162(1999).
RN [9]
RP X-RAY CRYSTALLOGRAPHY (1.85 ANGSTROMS) OF 139-406 IN A TERNARY COMPLEX WITH
RP PAPS AND A TETRASACCHARIDE, DISULFIDE BOND, FUNCTION, CATALYTIC ACTIVITY,
RP BINDING SITES, AND MUTAGENESIS OF LYS-161; LYS-162; ARG-166; GLU-170;
RP ARG-173; GLY-182; GLU-184; HIS-186; ASP-189; ARG-190; LYS-194; LYS-215;
RP SER-218; GLU-224; GLN-255; LYS-259; ILE-288; LYS-293; HIS-362; GLY-365;
RP LYS-366; LYS-368 AND ARG-370.
RX PubMed=15304505; DOI=10.1074/jbc.m405013200;
RA Moon A.F., Edavettal S.C., Krahn J.M., Munoz E.M., Negishi M.,
RA Linhardt R.J., Liu J., Pedersen L.C.;
RT "Structural analysis of the sulfotransferase (3-o-sulfotransferase isoform
RT 3) involved in the biosynthesis of an entry receptor for herpes simplex
RT virus 1.";
RL J. Biol. Chem. 279:45185-45193(2004).
CC -!- FUNCTION: Sulfotransferase that utilizes 3'-phospho-5'-adenylyl sulfate
CC (PAPS) to catalyze the transfer of a sulfo group to an N-unsubstituted
CC glucosamine linked to a 2-O-sulfo iduronic acid unit on heparan sulfate
CC (PubMed:10520990, PubMed:9988768, PubMed:10608887, PubMed:15304505).
CC Catalyzes the O-sulfation of glucosamine in IdoUA2S-GlcNS and also in
CC IdoUA2S-GlcNH2 (PubMed:10520990, PubMed:9988768, PubMed:15304505). The
CC substrate-specific O-sulfation generates an enzyme-modified heparan
CC sulfate which acts as a binding receptor to Herpes simplex virus-1
CC (HSV-1) and permits its entry (PubMed:10520990). Unlike HS3ST1/3-OST-1,
CC does not convert non-anticoagulant heparan sulfate to anticoagulant
CC heparan sulfate (PubMed:10520990). {ECO:0000269|PubMed:10520990,
CC ECO:0000269|PubMed:10608887, ECO:0000269|PubMed:15304505,
CC ECO:0000269|PubMed:9988768}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=3'-phosphoadenylyl sulfate + alpha-D-glucosaminyl-[heparan
CC sulfate](n) = 3-sulfo-alpha-D-glucosaminyl-[heparan sulfate](n) +
CC adenosine 3',5'-bisphosphate + H(+); Xref=Rhea:RHEA:15461, Rhea:RHEA-
CC COMP:9830, Rhea:RHEA-COMP:9831, ChEBI:CHEBI:15378, ChEBI:CHEBI:58339,
CC ChEBI:CHEBI:58343, ChEBI:CHEBI:58388, ChEBI:CHEBI:70975; EC=2.8.2.30;
CC Evidence={ECO:0000269|PubMed:15304505, ECO:0000269|PubMed:9988768};
CC -!- SUBCELLULAR LOCATION: Golgi apparatus membrane {ECO:0000305}; Single-
CC pass type II membrane protein {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Ubiquitous. Most abundant in heart and placenta,
CC followed by liver and kidney. {ECO:0000269|PubMed:9988767}.
CC -!- SIMILARITY: Belongs to the sulfotransferase 1 family. {ECO:0000305}.
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DR EMBL; AF105376; AAD30208.1; -; mRNA.
DR EMBL; AY358838; AAQ89197.1; -; mRNA.
DR EMBL; AK292047; BAF84736.1; -; mRNA.
DR EMBL; CH471108; EAW89959.1; -; Genomic_DNA.
DR EMBL; BC044647; AAH44647.1; -; mRNA.
DR CCDS; CCDS11165.1; -.
DR RefSeq; NP_006033.1; NM_006042.2.
DR PDB; 1T8T; X-ray; 1.85 A; A/B=139-406.
DR PDB; 1T8U; X-ray; 1.95 A; A/B=139-406.
DR PDB; 6XKG; X-ray; 1.55 A; A/B=139-406.
DR PDB; 6XL8; X-ray; 2.34 A; A/B=139-406.
DR PDBsum; 1T8T; -.
DR PDBsum; 1T8U; -.
DR PDBsum; 6XKG; -.
DR PDBsum; 6XL8; -.
DR AlphaFoldDB; Q9Y663; -.
DR SMR; Q9Y663; -.
DR BioGRID; 115280; 3.
DR STRING; 9606.ENSP00000284110; -.
DR DrugBank; DB03981; 1,4-Dideoxy-5-Dehydro-O2-Sulfo-Glucuronic Acid.
DR DrugBank; DB01812; Adenosine 3',5'-diphosphate.
DR DrugBank; DB03959; N,O6-Disulfo-Glucosamine.
DR DrugBank; DB02264; O2-Sulfo-Glucuronic Acid.
DR GlyGen; Q9Y663; 2 sites.
DR iPTMnet; Q9Y663; -.
DR PhosphoSitePlus; Q9Y663; -.
DR BioMuta; HS3ST3A1; -.
DR DMDM; 61214551; -.
DR MassIVE; Q9Y663; -.
DR PaxDb; Q9Y663; -.
DR PeptideAtlas; Q9Y663; -.
DR PRIDE; Q9Y663; -.
DR ProteomicsDB; 86606; -.
DR Antibodypedia; 25095; 42 antibodies from 11 providers.
DR DNASU; 9955; -.
DR Ensembl; ENST00000284110.2; ENSP00000284110.1; ENSG00000153976.3.
DR GeneID; 9955; -.
DR KEGG; hsa:9955; -.
DR MANE-Select; ENST00000284110.2; ENSP00000284110.1; NM_006042.3; NP_006033.1.
DR UCSC; uc002gob.1; human.
DR CTD; 9955; -.
DR DisGeNET; 9955; -.
DR GeneCards; HS3ST3A1; -.
DR HGNC; HGNC:5196; HS3ST3A1.
DR HPA; ENSG00000153976; Tissue enhanced (ovary).
DR MIM; 604057; gene.
DR neXtProt; NX_Q9Y663; -.
DR OpenTargets; ENSG00000153976; -.
DR PharmGKB; PA29469; -.
DR VEuPathDB; HostDB:ENSG00000153976; -.
DR eggNOG; KOG3704; Eukaryota.
DR GeneTree; ENSGT00940000162249; -.
DR HOGENOM; CLU_017703_0_1_1; -.
DR InParanoid; Q9Y663; -.
DR OMA; TMPGLVM; -.
DR OrthoDB; 712400at2759; -.
DR PhylomeDB; Q9Y663; -.
DR TreeFam; TF350755; -.
DR BioCyc; MetaCyc:HS07937-MON; -.
DR BRENDA; 2.8.2.30; 2681.
DR PathwayCommons; Q9Y663; -.
DR Reactome; R-HSA-2022928; HS-GAG biosynthesis.
DR BioGRID-ORCS; 9955; 11 hits in 1078 CRISPR screens.
DR ChiTaRS; HS3ST3A1; human.
DR EvolutionaryTrace; Q9Y663; -.
DR GeneWiki; HS3ST3A1; -.
DR GenomeRNAi; 9955; -.
DR Pharos; Q9Y663; Tbio.
DR PRO; PR:Q9Y663; -.
DR Proteomes; UP000005640; Chromosome 17.
DR RNAct; Q9Y663; protein.
DR Bgee; ENSG00000153976; Expressed in cartilage tissue and 115 other tissues.
DR ExpressionAtlas; Q9Y663; baseline and differential.
DR Genevisible; Q9Y663; HS.
DR GO; GO:0000139; C:Golgi membrane; TAS:Reactome.
DR GO; GO:0016021; C:integral component of membrane; TAS:ProtInc.
DR GO; GO:0008467; F:[heparan sulfate]-glucosamine 3-sulfotransferase 1 activity; IDA:UniProtKB.
DR GO; GO:0033872; F:[heparan sulfate]-glucosamine 3-sulfotransferase 3 activity; IEA:UniProtKB-EC.
DR GO; GO:0008146; F:sulfotransferase activity; TAS:ProtInc.
DR GO; GO:0001658; P:branching involved in ureteric bud morphogenesis; IEA:Ensembl.
DR GO; GO:0006024; P:glycosaminoglycan biosynthetic process; IDA:UniProtKB.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR037359; NST/OST.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR000863; Sulfotransferase_dom.
DR PANTHER; PTHR10605; PTHR10605; 1.
DR Pfam; PF00685; Sulfotransfer_1; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Disulfide bond; Glycoprotein; Golgi apparatus; Membrane;
KW Reference proteome; Signal-anchor; Transferase; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..406
FT /note="Heparan sulfate glucosamine 3-O-sulfotransferase
FT 3A1"
FT /id="PRO_0000085217"
FT TOPO_DOM 1..24
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 25..43
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 44..406
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT REGION 92..134
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 162..166
FT /ligand="3'-phosphoadenylyl sulfate"
FT /ligand_id="ChEBI:CHEBI:58339"
FT /evidence="ECO:0000269|PubMed:15304505"
FT BINDING 166
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:15304505"
FT BINDING 184..190
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:15304505"
FT BINDING 215..218
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:15304505"
FT BINDING 243
FT /ligand="3'-phosphoadenylyl sulfate"
FT /ligand_id="ChEBI:CHEBI:58339"
FT /evidence="ECO:0000269|PubMed:15304505"
FT BINDING 251
FT /ligand="3'-phosphoadenylyl sulfate"
FT /ligand_id="ChEBI:CHEBI:58339"
FT /evidence="ECO:0000269|PubMed:15304505"
FT BINDING 255..259
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:15304505"
FT BINDING 283..284
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:15304505"
FT BINDING 367..370
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:15304505"
FT BINDING 368..372
FT /ligand="3'-phosphoadenylyl sulfate"
FT /ligand_id="ChEBI:CHEBI:58339"
FT /evidence="ECO:0000269|PubMed:15304505"
FT CARBOHYD 273
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 344
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 351..363
FT /evidence="ECO:0000269|PubMed:15304505"
FT MUTAGEN 161
FT /note="K->A: 99.6% loss of enzymatic activity."
FT /evidence="ECO:0000269|PubMed:15304505"
FT MUTAGEN 162
FT /note="K->A: 99.6% loss of enzymatic activity; no HSV1
FT entry activity."
FT /evidence="ECO:0000269|PubMed:10520990,
FT ECO:0000269|PubMed:15304505"
FT MUTAGEN 166
FT /note="R->E: 99.8% loss of enzymatic activity."
FT /evidence="ECO:0000269|PubMed:15304505"
FT MUTAGEN 170
FT /note="E->Q: 17% loss of enzymatic activity."
FT /evidence="ECO:0000269|PubMed:15304505"
FT MUTAGEN 173
FT /note="R->S: 44.1% loss of enzymatic activity."
FT /evidence="ECO:0000269|PubMed:15304505"
FT MUTAGEN 182
FT /note="G->A: No effect on enzymatic activity."
FT /evidence="ECO:0000269|PubMed:15304505"
FT MUTAGEN 184
FT /note="E->Q: 99.9% loss of enzymatic activity."
FT /evidence="ECO:0000269|PubMed:15304505"
FT MUTAGEN 186
FT /note="H->F: Abolishes enzymatic activity."
FT /evidence="ECO:0000269|PubMed:15304505"
FT MUTAGEN 189
FT /note="D->N: 99.1% loss of enzymatic activity."
FT /evidence="ECO:0000269|PubMed:15304505"
FT MUTAGEN 190
FT /note="R->E: 32% loss of enzymatic activity."
FT /evidence="ECO:0000269|PubMed:15304505"
FT MUTAGEN 194
FT /note="K->A: 99.5% loss of enzymatic activity."
FT /evidence="ECO:0000269|PubMed:15304505"
FT MUTAGEN 215
FT /note="K->A: 99.9% loss of enzymatic activity."
FT /evidence="ECO:0000269|PubMed:15304505"
FT MUTAGEN 218
FT /note="S->A: 23.3% loss of enzymatic activity."
FT /evidence="ECO:0000269|PubMed:15304505"
FT MUTAGEN 224
FT /note="E->Q: 47.6% loss of enzymatic activity."
FT /evidence="ECO:0000269|PubMed:15304505"
FT MUTAGEN 255
FT /note="Q->A: 99.6% loss of enzymatic activity."
FT /evidence="ECO:0000269|PubMed:15304505"
FT MUTAGEN 259
FT /note="K->A: 48.3% loss of enzymatic activity."
FT /evidence="ECO:0000269|PubMed:15304505"
FT MUTAGEN 288
FT /note="I->A: 65% loss of enzymatic activity."
FT /evidence="ECO:0000269|PubMed:15304505"
FT MUTAGEN 293
FT /note="K->A: 33.6% loss of enzymatic activity."
FT /evidence="ECO:0000269|PubMed:15304505"
FT MUTAGEN 362
FT /note="H->A: No effect on enzymatic activity."
FT /evidence="ECO:0000269|PubMed:15304505"
FT MUTAGEN 365
FT /note="G->A: 43% loss of enzymatic activity."
FT /evidence="ECO:0000269|PubMed:15304505"
FT MUTAGEN 366
FT /note="K->A: 99.8% loss of enzymatic activity."
FT /evidence="ECO:0000269|PubMed:15304505"
FT MUTAGEN 368
FT /note="K->A: 99.9% loss of enzymatic activity."
FT /evidence="ECO:0000269|PubMed:15304505"
FT MUTAGEN 370
FT /note="R->E: 99.2% loss of enzymatic activity."
FT /evidence="ECO:0000269|PubMed:15304505"
FT HELIX 139..147
FT /evidence="ECO:0007829|PDB:1T8T"
FT STRAND 154..159
FT /evidence="ECO:0007829|PDB:6XKG"
FT HELIX 165..172
FT /evidence="ECO:0007829|PDB:6XKG"
FT STRAND 178..180
FT /evidence="ECO:0007829|PDB:6XKG"
FT HELIX 187..191
FT /evidence="ECO:0007829|PDB:6XKG"
FT HELIX 192..194
FT /evidence="ECO:0007829|PDB:6XKG"
FT HELIX 195..202
FT /evidence="ECO:0007829|PDB:6XKG"
FT STRAND 211..215
FT /evidence="ECO:0007829|PDB:6XKG"
FT HELIX 217..221
FT /evidence="ECO:0007829|PDB:6XKG"
FT HELIX 225..232
FT /evidence="ECO:0007829|PDB:6XKG"
FT STRAND 237..242
FT /evidence="ECO:0007829|PDB:6XKG"
FT HELIX 245..259
FT /evidence="ECO:0007829|PDB:6XKG"
FT HELIX 266..270
FT /evidence="ECO:0007829|PDB:6XKG"
FT STRAND 271..273
FT /evidence="ECO:0007829|PDB:6XL8"
FT STRAND 274..279
FT /evidence="ECO:0007829|PDB:6XKG"
FT HELIX 284..287
FT /evidence="ECO:0007829|PDB:6XKG"
FT HELIX 291..299
FT /evidence="ECO:0007829|PDB:6XKG"
FT HELIX 304..306
FT /evidence="ECO:0007829|PDB:6XKG"
FT STRAND 307..311
FT /evidence="ECO:0007829|PDB:6XKG"
FT HELIX 312..317
FT /evidence="ECO:0007829|PDB:6XKG"
FT HELIX 319..330
FT /evidence="ECO:0007829|PDB:6XKG"
FT HELIX 338..340
FT /evidence="ECO:0007829|PDB:6XKG"
FT STRAND 341..344
FT /evidence="ECO:0007829|PDB:6XKG"
FT TURN 345..348
FT /evidence="ECO:0007829|PDB:6XKG"
FT STRAND 349..355
FT /evidence="ECO:0007829|PDB:6XKG"
FT STRAND 358..360
FT /evidence="ECO:0007829|PDB:6XKG"
FT HELIX 377..398
FT /evidence="ECO:0007829|PDB:6XKG"
SQ SEQUENCE 406 AA; 44900 MW; 57B6A0ABC897577A CRC64;
MAPPGPASAL STSAEPLSRS IFRKFLLMLC SLLTSLYVFY CLAERCQTLS GPVVGLSGGG
EEAGAPGGGV LAGGPRELAV WPAAAQRKRL LQLPQWRRRR PPAPRDDGEE AAWEEESPGL
SGGPGGSGAG STVAEAPPGT LALLLDEGSK QLPQAIIIGV KKGGTRALLE FLRVHPDVRA
VGAEPHFFDR SYDKGLAWYR DLMPRTLDGQ ITMEKTPSYF VTREAPARIS AMSKDTKLIV
VVRDPVTRAI SDYTQTLSKR PDIPTFESLT FKNRTAGLID TSWSAIQIGI YAKHLEHWLR
HFPIRQMLFV SGERLISDPA GELGRVQDFL GLKRIITDKH FYFNKTKGFP CLKKAEGSSR
PHCLGKTKGR THPEIDREVV RRLREFYRPF NLKFYQMTGH DFGWDG
