CARDA_CYNCA
ID CARDA_CYNCA Reviewed; 504 AA.
AC Q9XFX3;
DT 15-JUN-2010, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1999, sequence version 1.
DT 03-AUG-2022, entry version 101.
DE RecName: Full=Procardosin-A {ECO:0000303|PubMed:10497243, ECO:0000303|PubMed:8654427, ECO:0000303|PubMed:9692911};
DE EC=3.4.23.-;
DE Contains:
DE RecName: Full=Cardosin-A intermediate form 35 kDa subunit {ECO:0000303|PubMed:9692911};
DE Contains:
DE RecName: Full=Cardosin-A heavy chain {ECO:0000303|PubMed:9692911};
DE AltName: Full=Cardosin-A 31 kDa subunit {ECO:0000303|PubMed:9692911};
DE Contains:
DE RecName: Full=Cardosin-A intermediate form 30 kDa subunit {ECO:0000303|PubMed:9692911};
DE Contains:
DE RecName: Full=Cardosin-A light chain {ECO:0000303|PubMed:9692911};
DE AltName: Full=Cardosin-A 15 kDa subunit {ECO:0000303|PubMed:9692911};
DE Flags: Precursor;
GN Name=cardA {ECO:0000312|EMBL:CAB40134.1};
OS Cynara cardunculus (Cardoon).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC asterids; campanulids; Asterales; Asteraceae; Carduoideae; Cardueae;
OC Carduinae; Cynara.
OX NCBI_TaxID=4265;
RN [1] {ECO:0000312|EMBL:CAB40134.1}
RP NUCLEOTIDE SEQUENCE [MRNA], SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND
RP DEVELOPMENTAL STAGE.
RC TISSUE=Flower bud {ECO:0000269|PubMed:10497243};
RX PubMed=10497243; DOI=10.1074/jbc.274.40.28724;
RA Faro C., Ramalho-Santos M., Vieira M., Mendes A., Simoes I., Andrade R.,
RA Verissimo P., Lin X., Tang J., Pires E.;
RT "Cloning and characterization of cDNA encoding cardosin A, an RGD-
RT containing plant aspartic proteinase.";
RL J. Biol. Chem. 274:28724-28729(1999).
RN [2] {ECO:0000305}
RP PROTEIN SEQUENCE OF 69-93; 129-136; 157-164; 170-185; 208-222; 238-256 AND
RP 415-450, FUNCTION, ACTIVITY REGULATION, BIOPHYSICOCHEMICAL PROPERTIES, AND
RP SUBUNIT.
RC TISSUE=Stigma {ECO:0000269|PubMed:8654427};
RX PubMed=8654427; DOI=10.1111/j.1432-1033.1996.00762.x;
RA Verissimo P., Faro C., Moir A.J., Lin Y., Tang J., Pires E.;
RT "Purification, characterization and partial amino acid sequencing of two
RT new aspartic proteinases from fresh flowers of Cynara cardunculus L.";
RL Eur. J. Biochem. 235:762-768(1996).
RN [3] {ECO:0000305}
RP PROTEIN SEQUENCE OF 69-73; 307-313; 415-419 AND 498-505, AND PROTEOLYTIC
RP PROCESSING.
RC TISSUE=Pistil {ECO:0000269|PubMed:9692911};
RX PubMed=9692911; DOI=10.1046/j.1432-1327.1998.2550133.x;
RA Ramalho-Santos M., Verissimo P., Cortes L., Samyn B., Van Beeumen J.,
RA Pires E., Faro C.;
RT "Identification and proteolytic processing of procardosin A.";
RL Eur. J. Biochem. 255:133-138(1998).
RN [4] {ECO:0000305}
RP GLYCOSYLATION AT ASN-139 AND ASN-432.
RX PubMed=9057834; DOI=10.1111/j.1432-1033.1997.t01-1-00695.x;
RA Costa J., Ashford D.A., Nimtz M., Bento I., Frazao C., Esteves C.L.,
RA Faro C.J., Kervinen J., Pires E., Verissimo P., Wlodawer A., Carrondo M.A.;
RT "The glycosylation of the aspartic proteinases from barley (Hordeum vulgare
RT L.) and cardoon (Cynara cardunculus L.).";
RL Eur. J. Biochem. 243:695-700(1997).
RN [5] {ECO:0000305}
RP SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=9362566; DOI=10.1007/s004250050183;
RA Ramalho-Santos M., Pissarra J., Verissimo P., Pereira S., Salema R.,
RA Pires E., Faro C.J.;
RT "Cardosin A, an abundant aspartic proteinase, accumulates in protein
RT storage vacuoles in the stigmatic papillae of Cynara cardunculus L.";
RL Planta 203:204-212(1997).
RN [6] {ECO:0000305}
RP INTERACTION WITH PLD1.
RX PubMed=16279943; DOI=10.1111/j.1742-4658.2005.04967.x;
RA Simoes I., Mueller E.C., Otto A., Bur D., Cheung A.Y., Faro C., Pires E.;
RT "Molecular analysis of the interaction between cardosin A and phospholipase
RT D(alpha). Identification of RGD/KGE sequences as binding motifs for C2
RT domains.";
RL FEBS J. 272:5786-5798(2005).
RN [7] {ECO:0000305}
RP FUNCTION.
RX PubMed=16428617; DOI=10.3168/jds.s0022-0302(06)72111-7;
RA Barros R.M., Malcata F.X.;
RT "Molecular characterization of peptides released from beta-lactoglobulin
RT and alpha-lactalbumin via cardosins A and B.";
RL J. Dairy Sci. 89:483-494(2006).
RN [8] {ECO:0000305}
RP SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RX PubMed=18767217; DOI=10.1007/s00709-008-0288-9;
RA Pereira C.S., da Costa D.S., Pereira S., Nogueira Fde M., Albuquerque P.M.,
RA Teixeira J., Faro C., Pissarra J.;
RT "Cardosins in postembryonic development of cardoon: towards an elucidation
RT of the biological function of plant aspartic proteinases.";
RL Protoplasma 232:203-213(2008).
RN [9] {ECO:0000305}
RP MASS SPECTROMETRY.
RX PubMed=19488781; DOI=10.1007/s00425-009-0948-9;
RA Sarmento A.C., Lopes H., Oliveira C.S., Vitorino R., Samyn B., Sergeant K.,
RA Debyser G., Van Beeumen J., Domingues P., Amado F., Pires E.,
RA Domingues M.R., Barros M.T.;
RT "Multiplicity of aspartic proteinases from Cynara cardunculus L.";
RL Planta 230:429-439(2009).
RN [10] {ECO:0000305, ECO:0000312|PDB:1B5F}
RP X-RAY CRYSTALLOGRAPHY (1.72 ANGSTROMS) OF 71-309 AND 418-504, DISULFIDE
RP BONDS, AND GLYCOSYLATION AT ASN-139 AND ASN-432.
RX PubMed=10488111; DOI=10.1074/jbc.274.39.27694;
RA Frazao C., Bento I., Costa J., Soares C.M., Verissimo P., Faro C.,
RA Pires E., Cooper J., Carrondo M.A.;
RT "Crystal structure of cardosin A, a glycosylated and Arg-Gly-Asp-containing
RT aspartic proteinase from the flowers of Cynara cardunculus L.";
RL J. Biol. Chem. 274:27694-27701(1999).
CC -!- FUNCTION: Aspartic proteinase with a high preference for bonds between
CC hydrophobic residues. Cleaves alpha-lactalbumin but not beta-
CC lactoglobulin. {ECO:0000250|UniProtKB:P85136,
CC ECO:0000269|PubMed:16428617, ECO:0000269|PubMed:8654427}.
CC -!- ACTIVITY REGULATION: Inhibited by the specific aspartic proteinase
CC inhibitors diazoacetyl-noleucine methyl ester and pepstatin.
CC {ECO:0000269|PubMed:8654427}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.64 mM for Leu-Ser-Phe(NO2)-Ahx-Ala-Leu
CC {ECO:0000269|PubMed:8654427};
CC KM=0.108 mM for Lys-Pro-Ala-Glu-Phe-Phe(NO2)-Ala-Leu
CC {ECO:0000269|PubMed:8654427};
CC pH dependence:
CC Optimum pH is 5.0. Active from pH 2.0-7.0.
CC {ECO:0000269|PubMed:8654427};
CC Temperature dependence:
CC Stable at temperatures of up to 60 degrees Celsius.
CC {ECO:0000269|PubMed:8654427};
CC -!- SUBUNIT: Heterodimer of a light chain and a heavy chain. An
CC intermediate form (35 kDa and 30 kDa subunits) is produced first, and
CC undergoes proteolytic processing to remove the internal plant-specific
CC insert (PSI) and the propeptide. There is some heterogeniety at the
CC cleavage site. Interacts (via RGD or KGE motifs) with PLD1 (via C2
CC domain). {ECO:0000269|PubMed:16279943, ECO:0000269|PubMed:8654427,
CC ECO:0000269|PubMed:9692911}.
CC -!- SUBCELLULAR LOCATION: Microsome membrane {ECO:0000269|PubMed:10497243,
CC ECO:0000269|PubMed:18767217, ECO:0000269|PubMed:9362566}. Protein
CC storage vacuole {ECO:0000269|PubMed:10497243,
CC ECO:0000269|PubMed:18767217, ECO:0000269|PubMed:9362566}. Secreted,
CC cell wall {ECO:0000269|PubMed:10497243, ECO:0000269|PubMed:18767217,
CC ECO:0000269|PubMed:9362566}. Secreted, extracellular space,
CC extracellular matrix {ECO:0000269|PubMed:10497243,
CC ECO:0000269|PubMed:18767217, ECO:0000269|PubMed:9362566}.
CC Note=Procardosin-A is associated with the microsomal membranes, the
CC mature form is secreted. {ECO:0000269|PubMed:10497243,
CC ECO:0000269|PubMed:18767217, ECO:0000269|PubMed:9362566}.
CC -!- TISSUE SPECIFICITY: Detected only in pistils, not in seeds, roots,
CC midribs, bracts, stamens, pollen, vascular or supporting tissues
CC (PubMed:9362566). Detected in seeds (PubMed:18767217). High amounts are
CC detected in the broad outer region of the upper portion of the stigma,
CC towards the lower portion of the stigma it accumulates at the
CC periphery. Within the stigma, expressed mainly in the epidermic
CC papillae, lower levels are found in the cortical parenchyma. Present
CC mainly in epidermal cells within the stye (at protein level). Expressed
CC in young flower buds, and at lower levels in seeds, pollen and
CC bracteas, but not in roots or leaves. {ECO:0000269|PubMed:10497243,
CC ECO:0000269|PubMed:18767217, ECO:0000269|PubMed:9362566}.
CC -!- DEVELOPMENTAL STAGE: Expressed at the first stages of flower
CC development, and converted into its mature form as the flower matures,
CC accumulating until the later stages of flower senescence. During flower
CC development at the mRNA level, the highest expression is detected in
CC closed capitula and no mRNA was detected at later stages of floral
CC development. At the protein level, highest expression of mature
CC cardosin-A is detected in fully opened capitula. Detected at mRNA level
CC in the embryo fraction of dry seeds. Not detected in developing seeds
CC until 72-84 hours of hydration, where it is detected in the embryo and
CC remains in subsequent developmental stages. At protein level, the
CC precursor form is detected in the hydrated seed until 120 hours, an
CC intermediate form is detected at almost all stages, and the mature
CC protein is detected until 60 hours and reappears before the seedling
CC stage. {ECO:0000269|PubMed:10497243, ECO:0000269|PubMed:18767217}.
CC -!- PTM: N-glycosylated. Glycans found at Asn-139 include approximately 6%
CC oligomannose, 82% oligosaccharides of the plant modified type with
CC proximal fucose but without xylose and 6% oligosaccharides of the plant
CC modified type with proximal fucose and xylose. Glycans found at Asn-432
CC include 14% oligosaccharides of the plant modified type with proximal
CC fucose but without xylose and 86% oligosaccharides of the plant
CC modified type with proximal fucose and xylose.
CC {ECO:0000269|PubMed:10488111, ECO:0000269|PubMed:9057834}.
CC -!- MASS SPECTROMETRY: [Cardosin-A heavy chain]: Mass=27203;
CC Method=Electrospray; Note=Heavy chain.;
CC Evidence={ECO:0000269|PubMed:19488781};
CC -!- MASS SPECTROMETRY: [Cardosin-A light chain]: Mass=10785;
CC Method=Electrospray; Note=Light chain.;
CC Evidence={ECO:0000269|PubMed:19488781};
CC -!- SIMILARITY: Belongs to the peptidase A1 family. {ECO:0000255}.
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DR EMBL; AJ132884; CAB40134.1; -; mRNA.
DR PDB; 1B5F; X-ray; 1.72 A; A/C=71-309, B/D=418-504.
DR PDBsum; 1B5F; -.
DR AlphaFoldDB; Q9XFX3; -.
DR SMR; Q9XFX3; -.
DR MEROPS; A01.020; -.
DR iPTMnet; Q9XFX3; -.
DR EnsemblPlants; KVI02029; KVI02029; Ccrd_019688.
DR Gramene; KVI02029; KVI02029; Ccrd_019688.
DR BRENDA; 3.4.23.40; 1789.
DR SABIO-RK; Q9XFX3; -.
DR EvolutionaryTrace; Q9XFX3; -.
DR GO; GO:0005783; C:endoplasmic reticulum; IEA:UniProtKB-KW.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0000326; C:protein storage vacuole; IEA:UniProtKB-SubCell.
DR GO; GO:0004190; F:aspartic-type endopeptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0006629; P:lipid metabolic process; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR Gene3D; 2.40.70.10; -; 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; IPR007856; SapB_1.
DR InterPro; IPR008138; SapB_2.
DR InterPro; IPR011001; Saposin-like.
DR InterPro; IPR008139; SaposinB_dom.
DR PANTHER; PTHR47966; PTHR47966; 1.
DR Pfam; PF00026; Asp; 1.
DR Pfam; PF05184; SapB_1; 1.
DR Pfam; PF03489; SapB_2; 1.
DR PRINTS; PR00792; PEPSIN.
DR SUPFAM; SSF47862; SSF47862; 1.
DR SUPFAM; SSF50630; SSF50630; 1.
DR PROSITE; PS00141; ASP_PROTEASE; 1.
DR PROSITE; PS51767; PEPTIDASE_A1; 1.
DR PROSITE; PS50015; SAP_B; 2.
PE 1: Evidence at protein level;
KW 3D-structure; Aspartyl protease; Cell wall; Direct protein sequencing;
KW Disulfide bond; Endoplasmic reticulum; Extracellular matrix; Glycoprotein;
KW Hydrolase; Membrane; Microsome; Protease; Secreted; Signal; Vacuole;
KW Zymogen.
FT SIGNAL 1..24
FT /evidence="ECO:0000255"
FT CHAIN 25..504
FT /note="Procardosin-A"
FT /evidence="ECO:0000255"
FT /id="PRO_5000064832"
FT CHAIN 25..309
FT /note="Cardosin-A intermediate form 35 kDa subunit"
FT /evidence="ECO:0000269|PubMed:9692911"
FT /id="PRO_0000394444"
FT PROPEP 25..68
FT /evidence="ECO:0000269|PubMed:9692911"
FT /id="PRO_0000394445"
FT CHAIN 69..309
FT /note="Cardosin-A heavy chain"
FT /evidence="ECO:0000269|PubMed:9692911"
FT /id="PRO_5000064833"
FT CHAIN 310..504
FT /note="Cardosin-A intermediate form 30 kDa subunit"
FT /evidence="ECO:0000269|PubMed:9692911"
FT /id="PRO_0000394446"
FT PROPEP 310..414
FT /note="Plant-specific insert"
FT /evidence="ECO:0000269|PubMed:9692911"
FT /id="PRO_0000394447"
FT CHAIN 415..504
FT /note="Cardosin-A light chain"
FT /evidence="ECO:0000269|PubMed:9692911"
FT /id="PRO_5000064834"
FT DOMAIN 85..501
FT /note="Peptidase A1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01103"
FT DOMAIN 311..416
FT /note="Saposin B-type"
FT /evidence="ECO:0000250|UniProtKB:P42210,
FT ECO:0000255|PROSITE-ProRule:PRU00415"
FT MOTIF 246..248
FT /note="RGD motif"
FT /evidence="ECO:0000269|PubMed:16279943"
FT MOTIF 455..457
FT /note="KGE motif"
FT /evidence="ECO:0000269|PubMed:16279943"
FT ACT_SITE 103
FT /evidence="ECO:0000250|UniProtKB:P42210,
FT ECO:0000255|PROSITE-ProRule:PRU10094"
FT ACT_SITE 286
FT /evidence="ECO:0000250|UniProtKB:P42210,
FT ECO:0000255|PROSITE-ProRule:PRU10094"
FT SITE 68..69
FT /note="Cleavage"
FT /evidence="ECO:0000269|PubMed:9692911"
FT SITE 309..310
FT /note="Cleavage"
FT /evidence="ECO:0000269|PubMed:9692911"
FT SITE 414..415
FT /note="Cleavage"
FT /evidence="ECO:0000269|PubMed:9692911"
FT CARBOHYD 139
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00415,
FT ECO:0000269|PubMed:10488111, ECO:0000269|PubMed:9057834"
FT CARBOHYD 432
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00415,
FT ECO:0000269|PubMed:10488111, ECO:0000269|PubMed:9057834"
FT DISULFID 116..122
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00415,
FT ECO:0000269|PubMed:10488111"
FT DISULFID 277..281
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00415,
FT ECO:0000269|PubMed:10488111"
FT DISULFID 316..410
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00415"
FT DISULFID 341..382
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00415"
FT DISULFID 347..379
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00415"
FT DISULFID 424..461
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00415,
FT ECO:0000269|PubMed:10488111"
FT CONFLICT 84
FT /note="S -> D (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 90..92
FT /note="GIG -> PTQ (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 129
FT /note="E -> R (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 159..160
FT /note="DS -> SF (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 163
FT /note="I -> K (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 180
FT /note="A -> T (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 449..450
FT /note="YI -> SY (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT STRAND 73..80
FT /evidence="ECO:0007829|PDB:1B5F"
FT TURN 81..83
FT /evidence="ECO:0007829|PDB:1B5F"
FT STRAND 84..91
FT /evidence="ECO:0007829|PDB:1B5F"
FT TURN 92..95
FT /evidence="ECO:0007829|PDB:1B5F"
FT STRAND 96..103
FT /evidence="ECO:0007829|PDB:1B5F"
FT STRAND 109..113
FT /evidence="ECO:0007829|PDB:1B5F"
FT HELIX 120..123
FT /evidence="ECO:0007829|PDB:1B5F"
FT HELIX 130..132
FT /evidence="ECO:0007829|PDB:1B5F"
FT STRAND 137..146
FT /evidence="ECO:0007829|PDB:1B5F"
FT STRAND 151..163
FT /evidence="ECO:0007829|PDB:1B5F"
FT STRAND 166..179
FT /evidence="ECO:0007829|PDB:1B5F"
FT HELIX 181..184
FT /evidence="ECO:0007829|PDB:1B5F"
FT STRAND 191..194
FT /evidence="ECO:0007829|PDB:1B5F"
FT STRAND 199..201
FT /evidence="ECO:0007829|PDB:1B5F"
FT HELIX 204..210
FT /evidence="ECO:0007829|PDB:1B5F"
FT STRAND 215..223
FT /evidence="ECO:0007829|PDB:1B5F"
FT STRAND 228..230
FT /evidence="ECO:0007829|PDB:1B5F"
FT STRAND 233..237
FT /evidence="ECO:0007829|PDB:1B5F"
FT HELIX 242..244
FT /evidence="ECO:0007829|PDB:1B5F"
FT STRAND 245..256
FT /evidence="ECO:0007829|PDB:1B5F"
FT TURN 257..260
FT /evidence="ECO:0007829|PDB:1B5F"
FT STRAND 261..264
FT /evidence="ECO:0007829|PDB:1B5F"
FT STRAND 267..269
FT /evidence="ECO:0007829|PDB:1B5F"
FT TURN 276..279
FT /evidence="ECO:0007829|PDB:1B5F"
FT STRAND 281..285
FT /evidence="ECO:0007829|PDB:1B5F"
FT STRAND 290..294
FT /evidence="ECO:0007829|PDB:1B5F"
FT HELIX 296..305
FT /evidence="ECO:0007829|PDB:1B5F"
FT HELIX 424..429
FT /evidence="ECO:0007829|PDB:1B5F"
FT STRAND 433..437
FT /evidence="ECO:0007829|PDB:1B5F"
FT STRAND 440..444
FT /evidence="ECO:0007829|PDB:1B5F"
FT HELIX 446..449
FT /evidence="ECO:0007829|PDB:1B5F"
FT STRAND 450..454
FT /evidence="ECO:0007829|PDB:1B5F"
FT TURN 456..458
FT /evidence="ECO:0007829|PDB:1B5F"
FT STRAND 460..467
FT /evidence="ECO:0007829|PDB:1B5F"
FT STRAND 471..479
FT /evidence="ECO:0007829|PDB:1B5F"
FT HELIX 481..484
FT /evidence="ECO:0007829|PDB:1B5F"
FT STRAND 487..492
FT /evidence="ECO:0007829|PDB:1B5F"
FT TURN 493..496
FT /evidence="ECO:0007829|PDB:1B5F"
FT STRAND 497..503
FT /evidence="ECO:0007829|PDB:1B5F"
SQ SEQUENCE 504 AA; 55504 MW; 4753F3EDA161171C CRC64;
MGTSIKANVL ALFLFYLLSP TVFSVSDDGL IRIGLKKRKV DRIDQLRGRR ALMEGNARKD
FGFRGTVRDS GSAVVALTND RDTSYFGEIG IGTPPQKFTV IFDTGSSVLW VPSSKCINSK
ACRAHSMYES SDSSTYKENG TFGAIIYGTG SITGFFSQDS VTIGDLVVKE QDFIEATDEA
DNVFLHRLFD GILGLSFQTI SVPVWYNMLN QGLVKERRFS FWLNRNVDEE EGGELVFGGL
DPNHFRGDHT YVPVTYQYYW QFGIGDVLIG DKSTGFCAPG CQAFADSGTS LLSGPTAIVT
QINHAIGANG VMNQQCKTVV SRYGRDIIEM LRSKIQPDKI CSHMKLCTFD GARDVSSIIE
SVVDKNNDKS SGGIHDEMCT FCEMAVVWMQ NEIKQSETED NIINYANELC EHLSTSSEEL
QVDCNTLSSM PNVSFTIGGK KFGLTPEQYI LKVGKGEATQ CISGFTAMDA TLLGPLWILG
DVFMRPYHTV FDYGNLLVGF AEAA
