ID CARP1_CANAL Reviewed; 391 AA. AC P0CY27; A0A1D8PQ68; P28872; Q5A8N4; DT 19-OCT-2011, integrated into UniProtKB/Swiss-Prot. DT 19-OCT-2011, sequence version 1. DT 27-MAR-2024, entry version 73. DE RecName: Full=Secreted aspartic protease 1 {ECO:0000303|PubMed:8335356}; DE Short=ACP 1 {ECO:0000305}; DE Short=Aspartate protease 1 {ECO:0000305}; DE EC=3.4.23.24 {ECO:0000269|PubMed:21646240, ECO:0000269|PubMed:27390786, ECO:0000269|PubMed:9043112, ECO:0000269|PubMed:9841840}; DE AltName: Full=Candidapepsin-1 {ECO:0000305}; DE AltName: Full=Pepsinogen-1 {ECO:0000303|PubMed:1620110}; DE AltName: Full=Pepsinogen-10 {ECO:0000303|PubMed:8478090}; DE Flags: Precursor; GN Name=SAP1 {ECO:0000303|PubMed:8335356}; GN Synonyms=PEP1 {ECO:0000303|PubMed:1620110}, PEP10 GN {ECO:0000303|PubMed:8478090}, PRA10 {ECO:0000303|PubMed:1447155}; GN OrderedLocusNames=CAALFM_C603490CA; ORFNames=CaO19.13137, CaO19.5714; OS Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast). OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes; OC Saccharomycetales; Debaryomycetaceae; Candida/Lodderomyces clade; Candida. OX NCBI_TaxID=237561; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=SC5314 / ATCC MYA-2876; RX PubMed=15123810; DOI=10.1073/pnas.0401648101; RA Jones T., Federspiel N.A., Chibana H., Dungan J., Kalman S., Magee B.B., RA Newport G., Thorstenson Y.R., Agabian N., Magee P.T., Davis R.W., RA Scherer S.; RT "The diploid genome sequence of Candida albicans."; RL Proc. Natl. Acad. Sci. U.S.A. 101:7329-7334(2004). RN [2] RP GENOME REANNOTATION. RC STRAIN=SC5314 / ATCC MYA-2876; RX PubMed=17419877; DOI=10.1186/gb-2007-8-4-r52; RA van het Hoog M., Rast T.J., Martchenko M., Grindle S., Dignard D., RA Hogues H., Cuomo C., Berriman M., Scherer S., Magee B.B., Whiteway M., RA Chibana H., Nantel A., Magee P.T.; RT "Assembly of the Candida albicans genome into sixteen supercontigs aligned RT on the eight chromosomes."; RL Genome Biol. 8:RESEARCH52.1-RESEARCH52.12(2007). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND GENOME REANNOTATION. RC STRAIN=SC5314 / ATCC MYA-2876; RX PubMed=24025428; DOI=10.1186/gb-2013-14-9-r97; RA Muzzey D., Schwartz K., Weissman J.S., Sherlock G.; RT "Assembly of a phased diploid Candida albicans genome facilitates allele- RT specific measurements and provides a simple model for repeat and indel RT structure."; RL Genome Biol. 14:RESEARCH97.1-RESEARCH97.14(2013). RN [4] RP FUNCTION. RX PubMed=1447155; DOI=10.1128/jb.174.23.7848-7853.1992; RA Wright R.J., Carne A., Hieber A.D., Lamont I.L., Emerson G.W., RA Sullivan P.A.; RT "A second gene for a secreted aspartate proteinase in Candida albicans."; RL J. Bacteriol. 174:7848-7853(1992). RN [5] RP INDUCTION. RX PubMed=1620110; DOI=10.1128/mcb.12.7.2997-3005.1992; RA Morrow B., Srikantha T., Soll D.R.; RT "Transcription of the gene for a pepsinogen, PEP1, is regulated by white- RT opaque switching in Candida albicans."; RL Mol. Cell. Biol. 12:2997-3005(1992). RN [6] RP SUBCELLULAR LOCATION. RX PubMed=8478090; DOI=10.1128/iai.61.5.2030-2036.1993; RA Morrison C.J., Hurst S.F., Bragg S.L., Kuykendall R.J., Diaz H., Pohl J., RA Reiss E.; RT "Heterogeneity of the purified extracellular aspartyl proteinase from RT Candida albicans: characterization with monoclonal antibodies and N- RT terminal amino acid sequence analysis."; RL Infect. Immun. 61:2030-2036(1993). RN [7] RP IDENTIFICATION. RX PubMed=8335356; DOI=10.1128/iai.61.8.3240-3243.1993; RA Magee B.B., Hube B., Wright R.J., Sullivan P.J., Magee P.T.; RT "The genes encoding the secreted aspartyl proteinases of Candida albicans RT constitute a family with at least three members."; RL Infect. Immun. 61:3240-3243(1993). RN [8] RP CATALYTIC ACTIVITY, AND BIOPHYSICOCHEMICAL PROPERTIES. RX PubMed=9043112; DOI=10.1099/00221287-143-2-349; RA Smolenski G., Sullivan P.A., Cutfield S.M., Cutfield J.F.; RT "Analysis of secreted aspartic proteinases from Candida albicans: RT purification and characterization of individual Sap1, Sap2 and Sap3 RT isoenzymes."; RL Microbiology 143:349-356(1997). RN [9] RP INDUCTION, AND FUNCTION. RX PubMed=10569787; DOI=10.1128/iai.67.12.6652-6662.1999; RA Kvaal C., Lachke S.A., Srikantha T., Daniels K., McCoy J., Soll D.R.; RT "Misexpression of the opaque-phase-specific gene PEP1 (SAP1) in the white RT phase of Candida albicans confers increased virulence in a mouse model of RT cutaneous infection."; RL Infect. Immun. 67:6652-6662(1999). RN [10] RP SUBCELLULAR LOCATION, AND CATALYTIC ACTIVITY. RX PubMed=9841840; DOI=10.1086/314546; RA De Bernardis F., Arancia S., Morelli L., Hube B., Sanglard D., Schafer W., RA Cassone A.; RT "Evidence that members of the secretory aspartyl proteinase gene family, in RT particular SAP2, are virulence factors for Candida vaginitis."; RL J. Infect. Dis. 179:201-208(1999). RN [11] RP SUBCELLULAR LOCATION, AND PROPEPTIDE. RX PubMed=11065355; DOI=10.1099/00221287-146-11-2765; RA Beggah S., Lechenne B., Reichard U., Foundling S., Monod M.; RT "Intra- and intermolecular events direct the propeptide-mediated maturation RT of the Candida albicans secreted aspartic proteinase Sap1p."; RL Microbiology 146:2765-2773(2000). RN [12] RP FUNCTION. RX PubMed=11478679; DOI=10.1099/0022-1317-50-8-743; RA Schaller M., Januschke E., Schackert C., Woerle B., Korting H.C.; RT "Different isoforms of secreted aspartyl proteinases (Sap) are expressed by RT Candida albicans during oral and cutaneous candidosis in vivo."; RL J. Med. Microbiol. 50:743-747(2001). RN [13] RP ACTIVITY REGULATION. RX PubMed=12203839; DOI=10.1002/jmr.568; RA Farley P.C., Christeller J.T., Sullivan M.E., Sullivan P.A., Laing W.A.; RT "Analysis of the interaction between the aspartic peptidase inhibitor SQAPI RT and aspartic peptidases using surface plasmon resonance."; RL J. Mol. Recognit. 15:135-144(2002). RN [14] RP INDUCTION. RX PubMed=14555467; DOI=10.1128/ec.2.5.847-855.2003; RA Lockhart S.R., Zhao R., Daniels K.J., Soll D.R.; RT "Alpha-pheromone-induced 'shmooing' and gene regulation require white- RT opaque switching during Candida albicans mating."; RL Eukaryot. Cell 2:847-855(2003). RN [15] RP FUNCTION. RX PubMed=12761103; DOI=10.1128/iai.71.6.3227-3234.2003; RA Schaller M., Bein M., Korting H.C., Baur S., Hamm G., Monod M., RA Beinhauer S., Hube B.; RT "The secreted aspartyl proteinases Sap1 and Sap2 cause tissue damage in an RT in vitro model of vaginal candidiasis based on reconstituted human vaginal RT epithelium."; RL Infect. Immun. 71:3227-3234(2003). RN [16] RP FUNCTION. RX PubMed=15845479; DOI=10.1128/iai.73.5.2758-2765.2005; RA Schaller M., Korting H.C., Borelli C., Hamm G., Hube B.; RT "Candida albicans-secreted aspartic proteinases modify the epithelial RT cytokine response in an in vitro model of vaginal candidiasis."; RL Infect. Immun. 73:2758-2765(2005). RN [17] RP FUNCTION. RX PubMed=19880183; DOI=10.1016/j.molimm.2009.08.019; RA Gropp K., Schild L., Schindler S., Hube B., Zipfel P.F., Skerka C.; RT "The yeast Candida albicans evades human complement attack by secretion of RT aspartic proteases."; RL Mol. Immunol. 47:465-475(2009). RN [18] RP FUNCTION. RX PubMed=20713630; DOI=10.1128/iai.00789-10; RA Pietrella D., Rachini A., Pandey N., Schild L., Netea M., Bistoni F., RA Hube B., Vecchiarelli A.; RT "The inflammatory response induced by aspartic proteases of Candida RT albicans is independent of proteolytic activity."; RL Infect. Immun. 78:4754-4762(2010). RN [19] RP CATALYTIC ACTIVITY, AND BIOPHYSICOCHEMICAL PROPERTIES. RX PubMed=21646240; DOI=10.1093/jb/mvr073; RA Aoki W., Kitahara N., Miura N., Morisaka H., Yamamoto Y., Kuroda K., RA Ueda M.; RT "Comprehensive characterization of secreted aspartic proteases encoded by a RT virulence gene family in Candida albicans."; RL J. Biochem. 150:431-438(2011). RN [20] RP FUNCTION, AND INDUCTION. RX PubMed=22302440; DOI=10.1007/s11046-012-9522-2; RA Ramage G., Coco B., Sherry L., Bagg J., Lappin D.F.; RT "In vitro Candida albicans biofilm induced proteinase activity and SAP8 RT expression correlates with in vivo denture stomatitis severity."; RL Mycopathologia 174:11-19(2012). RN [21] RP INDUCTION. RX PubMed=23484407; RA Staniszewska M., Bondaryk M., Siennicka K., Kurek A., Orlowski J., RA Schaller M., Kurzatkowski W.; RT "In vitro study of secreted aspartyl proteinases Sap1 to Sap3 and Sap4 to RT Sap6 expression in Candida albicans pleomorphic forms."; RL Pol. J. Microbiol. 61:247-256(2012). RN [22] RP ACTIVITY REGULATION. RX PubMed=23262278; DOI=10.1016/j.bcp.2012.12.008; RA Cadicamo C.D., Mortier J., Wolber G., Hell M., Heinrich I.E., Michel D., RA Semlin L., Berger U., Korting H.C., Holtje H.D., Koksch B., Borelli C.; RT "Design, synthesis, inhibition studies, and molecular modeling of pepstatin RT analogues addressing different secreted aspartic proteinases of Candida RT albicans."; RL Biochem. Pharmacol. 85:881-887(2013). RN [23] RP FUNCTION. RX PubMed=23927842; DOI=10.1016/j.peptides.2013.07.023; RA Bochenska O., Rapala-Kozik M., Wolak N., Bras G., Kozik A., Dubin A., RA Aoki W., Ueda M., Mak P.; RT "Secreted aspartic peptidases of Candida albicans liberate bactericidal RT hemocidins from human hemoglobin."; RL Peptides 48:49-58(2013). RN [24] RP FUNCTION, CATALYTIC ACTIVITY, AND BIOPHYSICOCHEMICAL PROPERTIES. RX PubMed=27390786; DOI=10.18388/abp.2016_1318; RA Bochenska O., Rapala-Kozik M., Wolak N., Aoki W., Ueda M., Kozik A.; RT "The action of ten secreted aspartic proteases of pathogenic yeast Candida RT albicans on major human salivary antimicrobial peptide, histatin 5."; RL Acta Biochim. Pol. 63:403-410(2016). RN [25] RP X-RAY CRYSTALLOGRAPHY (2.05 ANGSTROMS) OF 51-391, AND DISULFIDE BOND. RX PubMed=18384081; DOI=10.1002/prot.22021; RA Borelli C., Ruge E., Lee J.H., Schaller M., Vogelsang A., Monod M., RA Korting H.C., Huber R., Maskos K.; RT "X-ray structures of Sap1 and Sap5: structural comparison of the secreted RT aspartic proteinases from Candida albicans."; RL Proteins 72:1308-1319(2008). CC -!- FUNCTION: Secreted aspartic peptidases (SAPs) are a group of ten acidic CC hydrolases considered as key virulence factors (PubMed:1447155, CC PubMed:23927842, PubMed:10569787, PubMed:11478679, PubMed:12761103, CC PubMed:15845479, PubMed:19880183, PubMed:20713630, PubMed:22302440). CC These enzymes supply the fungus with nutrient amino acids as well as CC are able to degrade the selected host's proteins involved in the immune CC defense (PubMed:23927842, PubMed:10569787, PubMed:11478679, CC PubMed:12761103, PubMed:15845479, PubMed:19880183, PubMed:20713630, CC PubMed:22302440). Induces host inflammatory cytokine production in a CC proteolytic activity-independent way (PubMed:20713630). Plays a role in CC tissue damage during superficial infection (PubMed:12761103). Moreover, CC acts toward human hemoglobin though limited proteolysis to generate a CC variety of antimicrobial hemocidins, enabling to compete with the other CC microorganisms of the same physiological niche using the microbicidal CC peptides generated from the host protein (PubMed:23927842). CC {ECO:0000269|PubMed:10569787, ECO:0000269|PubMed:11478679, CC ECO:0000269|PubMed:12761103, ECO:0000269|PubMed:1447155, CC ECO:0000269|PubMed:15845479, ECO:0000269|PubMed:19880183, CC ECO:0000269|PubMed:20713630, ECO:0000269|PubMed:22302440, CC ECO:0000269|PubMed:23927842}. CC -!- FUNCTION: Plays a key role in defense against host by cleaving CC histatin-5 (Hst 5), a peptide from human saliva that carries out CC fungicidal activity (PubMed:27390786). The cleavage rate decreases in CC an order of SAP2 > SAP9 > SAP3 > SAP7 > SAP4 > SAP1 > SAP8 CC (PubMed:21646240). The first cleavage occurs between residues 'Lys-17' CC and 'His-18' of Hst 5, giving DSHAKRHHGYKRKFHEK and HHSHRGY peptides CC (PubMed:27390786). Further fragmentation by SAP1 results in CC AKRHHGYKRKFHEK and AKRHHGY products (PubMed:27390786). CC {ECO:0000269|PubMed:21646240, ECO:0000269|PubMed:27390786}. CC -!- CATALYTIC ACTIVITY: CC Reaction=Preferential cleavage at the carboxyl of hydrophobic amino CC acids, but fails to cleave 15-Leu-|-Tyr-16, 16-Tyr-|-Leu-17 and 24- CC Phe-|-Phe-25 of insulin B chain. Activates trypsinogen, and degrades CC keratin.; EC=3.4.23.24; Evidence={ECO:0000269|PubMed:21646240, CC ECO:0000269|PubMed:27390786, ECO:0000269|PubMed:9043112, CC ECO:0000269|PubMed:9841840}; CC -!- ACTIVITY REGULATION: Inhibited by pepstatin A analogs and squash CC aspartic peptidase inhibitor (SQAPI). {ECO:0000269|PubMed:12203839, CC ECO:0000269|PubMed:23262278}. CC -!- BIOPHYSICOCHEMICAL PROPERTIES: CC pH dependence: CC Optimum pH is 5.0. using BSA or casein-resorufin as substrates, and CC 6.0-7.0, the pH of the saliva, for cleavage of Hst 5. CC {ECO:0000269|PubMed:21646240, ECO:0000269|PubMed:27390786, CC ECO:0000269|PubMed:9043112}; CC -!- SUBUNIT: Monomer. {ECO:0000250|UniProtKB:P0CS83}. CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:11065355, CC ECO:0000269|PubMed:8478090, ECO:0000269|PubMed:9841840}. CC -!- INDUCTION: Expressed during development of germ tubes, pseudohyphae, CC true hyphae and opaque cells (PubMed:1620110, PubMed:10569787, CC PubMed:14555467). Expressed in greater amounts in the mature biofilms CC compared to early biofilms during inflammatory disorder of the palatal CC mucosa among denture wearers (PubMed:22302440). Regulated by growth CC phase and alpha-pheromones (PubMed:23484407). CC {ECO:0000269|PubMed:10569787, ECO:0000269|PubMed:14555467, CC ECO:0000269|PubMed:1620110, ECO:0000269|PubMed:22302440, CC ECO:0000269|PubMed:23484407}. CC -!- SIMILARITY: Belongs to the peptidase A1 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; CP017628; AOW30279.1; -; Genomic_DNA. DR RefSeq; XP_718053.2; XM_712960.2. DR PDB; 2QZW; X-ray; 2.05 A; A/B=51-391. DR PDBsum; 2QZW; -. DR AlphaFoldDB; P0CY27; -. DR SMR; P0CY27; -. DR STRING; 237561.P0CY27; -. DR MEROPS; A01.014; -. DR GlyCosmos; P0CY27; 1 site, No reported glycans. DR EnsemblFungi; C6_03490C_A-T; C6_03490C_A-T-p1; C6_03490C_A. DR GeneID; 3640256; -. DR KEGG; cal:CAALFM_C603490CA; -. DR CGD; CAL0000189556; SAP1. DR VEuPathDB; FungiDB:C6_03490C_A; -. DR eggNOG; KOG1339; Eukaryota. DR HOGENOM; CLU_013253_9_1_1; -. DR InParanoid; P0CY27; -. DR OMA; APCTRCF; -. DR OrthoDB; 615305at2759; -. DR BRENDA; 3.4.23.24; 1096. DR EvolutionaryTrace; P0CY27; -. DR PHI-base; PHI:6783; -. DR PHI-base; PHI:6789; -. DR PHI-base; PHI:6811; -. DR PRO; PR:P0CY27; -. DR Proteomes; UP000000559; Chromosome 6. DR GO; GO:0005576; C:extracellular region; IDA:CGD. DR GO; GO:0009277; C:fungal-type cell wall; IBA:GO_Central. DR GO; GO:0004190; F:aspartic-type endopeptidase activity; IDA:UniProtKB. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0044406; P:adhesion of symbiont to host; IMP:CGD. DR GO; GO:0031505; P:fungal-type cell wall organization; IBA:GO_Central. DR GO; GO:0052391; P:induction by symbiont of defense-related host calcium ion flux; IDA:CGD. DR GO; GO:0044416; P:induction by symbiont of host defense response; IDA:CGD. DR GO; GO:0052559; P:induction by symbiont of host immune response; IDA:CGD. DR GO; GO:0006807; P:nitrogen compound metabolic process; IMP:CGD. DR GO; GO:0030163; P:protein catabolic process; IMP:CGD. DR GO; GO:0019538; P:protein metabolic process; IDA:CGD. DR GO; GO:0006508; P:proteolysis; IDA:UniProtKB. DR GO; GO:0006465; P:signal peptide processing; IDA:CGD. DR GO; GO:0035756; P:transepithelial migration of symbiont in host; IMP:CGD. DR CDD; cd05474; SAP_like; 1. DR Gene3D; 2.40.70.10; Acid Proteases; 2. DR InterPro; IPR001461; Aspartic_peptidase_A1. DR InterPro; IPR001969; Aspartic_peptidase_AS. DR InterPro; IPR033121; PEPTIDASE_A1. DR InterPro; IPR021109; Peptidase_aspartic_dom_sf. DR InterPro; IPR033876; SAP-like. DR PANTHER; PTHR47966; BETA-SITE APP-CLEAVING ENZYME, ISOFORM A-RELATED; 1. DR PANTHER; PTHR47966:SF81; PEPTIDASE A1 DOMAIN-CONTAINING PROTEIN; 1. DR Pfam; PF00026; Asp; 1. DR PRINTS; PR00792; PEPSIN. DR SUPFAM; SSF50630; Acid proteases; 1. DR PROSITE; PS00141; ASP_PROTEASE; 2. DR PROSITE; PS51767; PEPTIDASE_A1; 1. PE 1: Evidence at protein level; KW 3D-structure; Aspartyl protease; Cleavage on pair of basic residues; KW Disulfide bond; Glycoprotein; Hydrolase; Metal-binding; Protease; KW Reference proteome; Secreted; Signal; Virulence; Zinc; Zymogen. FT SIGNAL 1..18 FT /evidence="ECO:0000255" FT PROPEP 19..50 FT /note="Activation peptide" FT /evidence="ECO:0000305" FT /id="PRO_0000413044" FT CHAIN 51..391 FT /note="Secreted aspartic protease 1" FT /id="PRO_0000413045" FT DOMAIN 64..377 FT /note="Peptidase A1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01103" FT ACT_SITE 82 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01103" FT ACT_SITE 267 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01103" FT BINDING 82..84 FT /ligand="pepstatin A" FT /ligand_id="ChEBI:CHEBI:190525" FT /ligand_note="inhibitor" FT /evidence="ECO:0000250|UniProtKB:P0CY29" FT BINDING 135..136 FT /ligand="pepstatin A" FT /ligand_id="ChEBI:CHEBI:190525" FT /ligand_note="inhibitor" FT /evidence="ECO:0000250|UniProtKB:P0CY29" FT BINDING 241 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /evidence="ECO:0000250|UniProtKB:P0CY29" FT BINDING 263 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /evidence="ECO:0000250|UniProtKB:P0CY29" FT BINDING 267..271 FT /ligand="pepstatin A" FT /ligand_id="ChEBI:CHEBI:190525" FT /ligand_note="inhibitor" FT /evidence="ECO:0000250|UniProtKB:P0CY29" FT CARBOHYD 40 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT DISULFID 97..109 FT /evidence="ECO:0000269|PubMed:18384081" FT DISULFID 305..343 FT /evidence="ECO:0000269|PubMed:18384081" FT STRAND 53..59 FT /evidence="ECO:0007829|PDB:2QZW" FT STRAND 64..70 FT /evidence="ECO:0007829|PDB:2QZW" FT TURN 71..74 FT /evidence="ECO:0007829|PDB:2QZW" FT STRAND 75..82 FT /evidence="ECO:0007829|PDB:2QZW" FT STRAND 88..97 FT /evidence="ECO:0007829|PDB:2QZW" FT TURN 106..109 FT /evidence="ECO:0007829|PDB:2QZW" FT HELIX 117..119 FT /evidence="ECO:0007829|PDB:2QZW" FT STRAND 124..133 FT /evidence="ECO:0007829|PDB:2QZW" FT STRAND 139..151 FT /evidence="ECO:0007829|PDB:2QZW" FT STRAND 154..171 FT /evidence="ECO:0007829|PDB:2QZW" FT STRAND 173..175 FT /evidence="ECO:0007829|PDB:2QZW" FT HELIX 179..181 FT /evidence="ECO:0007829|PDB:2QZW" FT STRAND 183..186 FT /evidence="ECO:0007829|PDB:2QZW" FT HELIX 190..196 FT /evidence="ECO:0007829|PDB:2QZW" FT STRAND 199..208 FT /evidence="ECO:0007829|PDB:2QZW" FT STRAND 215..221 FT /evidence="ECO:0007829|PDB:2QZW" FT STRAND 223..225 FT /evidence="ECO:0007829|PDB:2QZW" FT STRAND 228..231 FT /evidence="ECO:0007829|PDB:2QZW" FT STRAND 234..237 FT /evidence="ECO:0007829|PDB:2QZW" FT STRAND 241..243 FT /evidence="ECO:0007829|PDB:2QZW" FT STRAND 245..253 FT /evidence="ECO:0007829|PDB:2QZW" FT STRAND 256..266 FT /evidence="ECO:0007829|PDB:2QZW" FT STRAND 271..275 FT /evidence="ECO:0007829|PDB:2QZW" FT HELIX 277..287 FT /evidence="ECO:0007829|PDB:2QZW" FT STRAND 290..292 FT /evidence="ECO:0007829|PDB:2QZW" FT STRAND 295..297 FT /evidence="ECO:0007829|PDB:2QZW" FT STRAND 300..303 FT /evidence="ECO:0007829|PDB:2QZW" FT STRAND 310..316 FT /evidence="ECO:0007829|PDB:2QZW" FT STRAND 320..324 FT /evidence="ECO:0007829|PDB:2QZW" FT HELIX 325..328 FT /evidence="ECO:0007829|PDB:2QZW" FT STRAND 341..345 FT /evidence="ECO:0007829|PDB:2QZW" FT STRAND 347..349 FT /evidence="ECO:0007829|PDB:2QZW" FT HELIX 357..360 FT /evidence="ECO:0007829|PDB:2QZW" FT STRAND 363..368 FT /evidence="ECO:0007829|PDB:2QZW" FT TURN 369..372 FT /evidence="ECO:0007829|PDB:2QZW" FT STRAND 373..379 FT /evidence="ECO:0007829|PDB:2QZW" FT STRAND 387..389 FT /evidence="ECO:0007829|PDB:2QZW" SQ SEQUENCE 391 AA; 41602 MW; CF88C56943BCCCA9 CRC64; MFLKNIFIAL AIALLVDASP AKRSPGFVTL DFDVIKTPVN ATGQEGKVKR QAIPVTLNNE HVSYAADITI GSNKQKFNVI VDTGSSDLWV PDASVTCDKP RPGQSADFCK GKGIYTPKSS TTSQNLGTPF YIGYGDGSSS QGTLYKDTVG FGGASITKQV FADITKTSIP QGILGIGYKT NEAAGDYDNV PVTLKNQGVI AKNAYSLYLN SPNAATGQII FGGVDKAKYS GSLIAVPVTS DRELRITLNS LKAVGKNING NIDVLLDSGT TITYLQQDVA QDIIDAFQAE LKSDGQGHTF YVTDCQTSGT VDFNFDNNAK ISVPASEFTA PLSYANGQPY PKCQLLLGIS DANILGDNFL RSAYLVYDLD DDKISLAQVK YTSASNIAAL T //