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 24-JAN-2024, entry version 167. 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}. 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; 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 GlyCosmos; Q9Y663; 2 sites, No reported glycans. DR GlyGen; Q9Y663; 2 sites. DR iPTMnet; Q9Y663; -. DR PhosphoSitePlus; Q9Y663; -. DR BioMuta; HS3ST3A1; -. DR DMDM; 61214551; -. DR MassIVE; Q9Y663; -. DR PaxDb; 9606-ENSP00000284110; -. DR PeptideAtlas; Q9Y663; -. DR ProteomicsDB; 86606; -. DR Antibodypedia; 25095; 57 antibodies from 12 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 AGR; HGNC:5196; -. 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; ELSHYMP; -. DR OrthoDB; 10019at2759; -. DR PhylomeDB; Q9Y663; -. DR TreeFam; TF350755; -. DR BioCyc; MetaCyc:HS07937-MONOMER; -. DR BRENDA; 2.8.2.30; 2681. DR PathwayCommons; Q9Y663; -. DR Reactome; R-HSA-2022928; HS-GAG biosynthesis. DR BioGRID-ORCS; 9955; 13 hits in 1155 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 117 other cell types or tissues. DR ExpressionAtlas; Q9Y663; baseline and differential. DR GO; GO:0000139; C:Golgi membrane; TAS:Reactome. DR GO; GO:0016020; C: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 GO; GO:0015015; P:heparan sulfate proteoglycan biosynthetic process, enzymatic modification; TAS:Reactome. DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1. DR InterPro; IPR037359; NST/OST. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR000863; Sulfotransferase_dom. DR PANTHER; PTHR10605:SF64; HEPARAN SULFATE GLUCOSAMINE 3-O-SULFOTRANSFERASE 3A1; 1. DR PANTHER; PTHR10605; HEPARAN SULFATE SULFOTRANSFERASE; 1. DR Pfam; PF00685; Sulfotransfer_1; 1. DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1. DR Genevisible; Q9Y663; HS. 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 //