PA2H_CRODU
ID PA2H_CRODU Reviewed; 138 AA.
AC P08878;
DT 01-NOV-1988, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1988, sequence version 1.
DT 25-MAY-2022, entry version 116.
DE RecName: Full=Phospholipase A2 homolog crotoxin acid subunit CA;
DE Short=CTX subunit CA;
DE AltName: Full=Crotapotin;
DE Contains:
DE RecName: Full=Crotoxin chain alpha CA1, CA2 and CA4 {ECO:0000303|PubMed:1868083};
DE Contains:
DE RecName: Full=Crotoxin chain alpha CA3 {ECO:0000303|PubMed:1868083};
DE Contains:
DE RecName: Full=Crotoxin chain beta CA2, CA3 and CA4 {ECO:0000303|PubMed:1868083};
DE Contains:
DE RecName: Full=Crotoxin chain beta CA1 {ECO:0000303|PubMed:1868083};
DE Contains:
DE RecName: Full=Crotoxin chain gamma {ECO:0000303|PubMed:1868083};
DE AltName: Full=Analgesic peptide {ECO:0000303|PubMed:18495297};
DE AltName: Full=Crotalphine {ECO:0000303|PubMed:18495297, ECO:0000303|PubMed:18703042, ECO:0000303|PubMed:24460677};
DE Flags: Precursor;
OS Crotalus durissus terrificus (South American rattlesnake).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC Serpentes; Colubroidea; Viperidae; Crotalinae; Crotalus.
OX NCBI_TaxID=8732;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Venom gland;
RX PubMed=3174444; DOI=10.1093/nar/16.18.9050;
RA Ducancel F., Guignery Frelat G., Menez A., Boulain J.-C., Bouchier C.,
RA Bon C.;
RT "Cloning and sequencing of cDNAs encoding the two subunits of Crotoxin.";
RL Nucleic Acids Res. 16:9050-9050(1988).
RN [2]
RP PROTEIN SEQUENCE OF 38-78; 83-118 AND 125-138 (CA1; CA2; CA3 AND CA4), AND
RP PYROGLUTAMATE FORMATION AT GLN-84 AND GLN-125.
RC TISSUE=Venom;
RX PubMed=1868083; DOI=10.1021/bi00246a028;
RA Faure G., Guilaume J.-L., Camoin L., Saliou B., Bon C.;
RT "Multiplicity of acidic subunit isoforms of crotoxin, the phospholipase A2
RT neurotoxin from Crotalus durissus terrificus venom, results from
RT posttranslational modifications.";
RL Biochemistry 30:8074-8084(1991).
RN [3]
RP PROTEIN SEQUENCE OF 39-76; 95-118 AND 125-138.
RC TISSUE=Venom;
RX PubMed=4084559; DOI=10.1021/bi00346a005;
RA Aird S.D., Kaiser I.I., Lewis R.V., Kruggel W.G.;
RT "Rattlesnake presynaptic neurotoxins: primary structure and evolutionary
RT origin of the acidic subunit.";
RL Biochemistry 24:7054-7058(1985).
RN [4]
RP PROTEIN SEQUENCE OF 84-118.
RC TISSUE=Venom;
RX PubMed=2400773; DOI=10.1016/0167-4838(90)90079-u;
RA Aird S.D., Yates J.R. III, Martino P.A., Shabanowitz J., Hunt D.F.,
RA Kaiser I.I.;
RT "The amino acid sequence of the acidic subunit B-chain of crotoxin.";
RL Biochim. Biophys. Acta 1040:217-224(1990).
RN [5]
RP PROTEIN SEQUENCE OF 125-138, MASS SPECTROMETRY, SYNTHESIS OF 125-138,
RP FUNCTION, MUTAGENESIS OF GLN-136, AND DISULFIDE BOND.
RC TISSUE=Venom;
RX PubMed=18495297; DOI=10.1016/j.peptides.2008.04.003;
RA Konno K., Picolo G., Gutierrez V.P., Brigatte P., Zambelli V.O.,
RA Camargo A.C., Cury Y.;
RT "Crotalphine, a novel potent analgesic peptide from the venom of the South
RT American rattlesnake Crotalus durissus terrificus.";
RL Peptides 29:1293-1304(2008).
RN [6]
RP BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, AND LETHAL DOSES.
RX PubMed=8513799; DOI=10.1111/j.1432-1033.1993.tb17946.x;
RA Faure G., Harvey A.L., Thomson E., Saliou B., Radvanyi F., Bon C.;
RT "Comparison of crotoxin isoforms reveals that stability of the complex
RT plays a major role in its pharmacological action.";
RL Eur. J. Biochem. 214:491-496(1993).
RN [7]
RP INHIBITION OF CROTOXIN BY CICS.
RX PubMed=10903514; DOI=10.1046/j.1432-1327.2000.01532.x;
RA Faure G., Villela C., Perales J., Bon C.;
RT "Interaction of the neurotoxic and nontoxic secretory phospholipases A2
RT with the crotoxin inhibitor from Crotalus serum.";
RL Eur. J. Biochem. 267:4799-4808(2000).
RN [8]
RP PHARMACEUTICAL.
RX PubMed=11948110;
RA Cura J.E., Blanzaco D.P., Brisson C., Cura M.A., Cabrol R., Larrateguy L.,
RA Mendez C., Sechi J.C., Silveira J.S., Theiller E., de Roodt A.R.,
RA Vidal J.C.;
RT "Phase I and pharmacokinetics study of crotoxin (cytotoxic PLA(2), NSC-
RT 624244) in patients with advanced cancer.";
RL Clin. Cancer Res. 8:1033-1041(2002).
RN [9]
RP FUNCTION.
RX PubMed=12657321; DOI=10.1016/s0041-0101(02)00394-x;
RA Faure G., Copic A., Le Porrier S., Gubensek F., Bon C., Krizaj I.;
RT "Crotoxin acceptor protein isolated from Torpedo electric organ: binding
RT properties to crotoxin by surface plasmon resonance.";
RL Toxicon 41:509-517(2003).
RN [10]
RP FUNCTION (CROTOXIN CHAIN GAMMA).
RX PubMed=18703042; DOI=10.1016/j.ejphar.2008.07.053;
RA Gutierrez V.P., Konno K., Chacur M., Sampaio S.C., Picolo G., Brigatte P.,
RA Zambelli V.O., Cury Y.;
RT "Crotalphine induces potent antinociception in neuropathic pain by acting
RT at peripheral opioid receptors.";
RL Eur. J. Pharmacol. 594:84-92(2008).
RN [11]
RP REVIEW.
RX PubMed=20109480; DOI=10.1016/j.toxicon.2010.01.011;
RA Sampaio S.C., Hyslop S., Fontes M.R., Prado-Franceschi J., Zambelli V.O.,
RA Magro A.J., Brigatte P., Gutierrez V.P., Cury Y.;
RT "Crotoxin: novel activities for a classic beta-neurotoxin.";
RL Toxicon 55:1045-1060(2010).
RN [12]
RP FUNCTION (CROTOXIN CHAIN GAMMA), AND SYNTHESIS OF 125-138.
RX PubMed=24460677; DOI=10.1111/bph.12488;
RA Machado F.C., Zambelli V.O., Fernandes A.C., Heimann A.S., Cury Y.,
RA Picolo G.;
RT "Peripheral interactions between cannabinoid and opioid systems contribute
RT to the antinociceptive effect of crotalphine.";
RL Br. J. Pharmacol. 171:961-972(2014).
RN [13]
RP X-RAY CRYSTALLOGRAPHY (1.35 ANGSTROMS) OF 38-118 IN COMPLEX WITH CROTOXIN
RP CBB SUBUNIT, SITES, AND DISULFIDE BONDS.
RC TISSUE=Venom;
RX PubMed=21787789; DOI=10.1016/j.jmb.2011.07.027;
RA Faure G., Xu H., Saul F.A.;
RT "Crystal structure of crotoxin reveals key residues involved in the
RT stability and toxicity of this potent heterodimeric beta-neurotoxin.";
RL J. Mol. Biol. 412:176-191(2011).
CC -!- FUNCTION: CAalpha-CAbeta-CAgamma: The acidic subunit of crotoxin (CA)
CC is a heterotrimer of three disulfide-linked chains generated by post-
CC translational maturation of a PLA2-like precursor. CA has no PLA2
CC activity and is not neurotoxic by itself, but plays several important
CC functions in the crotoxin complex by increasing the lethal potency of
CC the uncomplexed CB subunit. It acts by physically occluding the
CC hydrophobic interfacial binding surface (IBS) of CB (PubMed:21787789
CC and PubMed:21787789). This effect decreases the adsorption of CB to
CC phospholipid membranes, targeting the crotoxin complex to reach the
CC specific presynaptic receptor (R48) at the neuromuscular junction. It
CC also prevents the formation of the reactive CB dimer. Moreover, the CA
CC subunit inhibits the catalytic activity by partially masking the
CC catalytic site of CB (PubMed:21787789) and inhibits its anticoagulant
CC activity. {ECO:0000269|PubMed:21787789}.
CC -!- FUNCTION: Heterodimer CA-CB: Crotoxin is a potent presynaptic
CC neurotoxin that possesses phospholipase A2 (PLA2) activity and exerts a
CC lethal action by blocking neuromuscular transmission. It consists of a
CC non-covalent association of a basic and weakly toxic PLA2 subunit
CC (CBa2, CBb, CBc, or CBd), with a small acidic, non-enzymatic and non-
CC toxic subunit (CA1, CA2, CA3 or CA4). The complex acts by binding to a
CC specific 48-kDa protein (R48/CAPT) receptor located on presynaptic
CC membranes, forming a transient ternary complex CA-CB-R48, followed by
CC dissociation of the CA-CB complex and release of the CA subunit
CC (PubMed:12657321). At equilibrium, only the CB subunits remain
CC associated with the specific crotoxin receptor. In addition to
CC neurotoxicity, crotoxin has been found to exert myotoxicity,
CC nephrotoxicity, and cardiovascular toxicity (PubMed:20109480).
CC Moreover, anti-inflammatory, immunomodulatory, anti-tumor and analgesic
CC effects of crotoxin have also been reported (PubMed:20109480).
CC {ECO:0000269|PubMed:12657321, ECO:0000269|PubMed:20109480}.
CC -!- FUNCTION: [Crotoxin chain gamma]: Found in the venom as a monomer and
CC stabilized by one disulfide bond (Cys-131 and Cys-138)
CC (PubMed:18495297). This peptide induces potent antinociceptive effects
CC in acute and chronic pain models (PubMed:18495297, PubMed:18703042).
CC This effect is mediated by the release of peripheral dynorphin A, an
CC endogenous agonist of kappa-opioid receptors, and this release is
CC dependent on cannabinoid receptor CB2 activation (PubMed:24460677).
CC {ECO:0000269|PubMed:18495297, ECO:0000269|PubMed:18703042,
CC ECO:0000269|PubMed:24460677}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.05 uM for 1-palmitoyl-2-(10-pyrenyldecanoyl)-sn-glycero-3-
CC monomethyl phosphatidic acid (class 2 heterodimer CA2-CBa2)
CC {ECO:0000269|PubMed:8513799};
CC KM=0.05 uM for 1-palmitoyl-2-(10-pyrenyldecanoyl)-sn-glycero-3-
CC monomethyl phosphatidic acid (class 2 heterodimer CA3-CBa2)
CC {ECO:0000269|PubMed:8513799};
CC KM=0.3 uM for 1-palmitoyl-2-(10-pyrenyldecanoyl)-sn-glycero-3-
CC monomethyl phosphatidic acid (class 2 heterodimer CA2-CBb)
CC {ECO:0000269|PubMed:8513799};
CC KM=0.2 uM for 1-palmitoyl-2-(10-pyrenyldecanoyl)-sn-glycero-3-
CC monomethyl phosphatidic acid (class 2 heterodimer CA3-CBb)
CC {ECO:0000269|PubMed:8513799};
CC KM=0.22 uM for 1-palmitoyl-2-(10-pyrenyldecanoyl)-sn-glycero-3-
CC monomethyl phosphatidic acid (class 2 heterodimer CA2-CBc)
CC {ECO:0000269|PubMed:8513799};
CC KM=0.2 uM for 1-palmitoyl-2-(10-pyrenyldecanoyl)-sn-glycero-3-
CC monomethyl phosphatidic acid (class 2 heterodimer CA3-CBc)
CC {ECO:0000269|PubMed:8513799};
CC KM=0.35 uM for 1-palmitoyl-2-(10-pyrenyldecanoyl)-sn-glycero-3-
CC monomethyl phosphatidic acid (class 2 heterodimer CA2-CBd)
CC {ECO:0000269|PubMed:8513799};
CC KM=0.3 uM for 1-palmitoyl-2-(10-pyrenyldecanoyl)-sn-glycero-3-
CC monomethyl phosphatidic acid (class 2 heterodimer CA3-CBd)
CC {ECO:0000269|PubMed:8513799};
CC Vmax=25 umol/min/mg enzyme (class 2 heterodimer CA2-CBa2)
CC {ECO:0000269|PubMed:8513799};
CC Vmax=24 umol/min/mg enzyme (class 2 heterodimer CA3-CBa2)
CC {ECO:0000269|PubMed:8513799};
CC Vmax=10 umol/min/mg enzyme (class 2 heterodimer CA2-CBb)
CC {ECO:0000269|PubMed:8513799};
CC Vmax=9 umol/min/mg enzyme (class 2 heterodimer CA3-CBb)
CC {ECO:0000269|PubMed:8513799};
CC Vmax=7 umol/min/mg enzyme (class 2 heterodimer CA2-CBc)
CC {ECO:0000269|PubMed:8513799};
CC Vmax=6.6 umol/min/mg enzyme (class 2 heterodimer CA3-CBc)
CC {ECO:0000269|PubMed:8513799};
CC Vmax=4.6 umol/min/mg enzyme (class 2 heterodimer CA2-CBd)
CC {ECO:0000269|PubMed:8513799};
CC Vmax=4 umol/min/mg enzyme (class 2 heterodimer CA3-CBd)
CC {ECO:0000269|PubMed:8513799};
CC -!- SUBUNIT: Heterodimer of one of the acidic (CA1, CA2, CA3 or CA4) and
CC one of the basic (CBa1, CBa2, CBb, CBc or CBd) subunits; non-covalently
CC linked. The acidic subunit is non-toxic, without enzymatic activity and
CC comprises 3 peptides that are cross-linked by 5 disulfide bridges. The
CC basic subunit is toxic, has phospholipase A2 activity and is composed
CC of a single chain. Multiple variants of each subunit give different
CC crotoxin complexes that can be subdivided into 2 classes: (1) those of
CC high toxicity, low PLA2 activity (CBb, CBc and CBd linked with high
CC affinity to any CA) and high stability (K(d)=4.5 nM) and (2) those of
CC moderate toxicity, high PLA2 activity (CBa2 linked with low affinity to
CC any CA) and low stability (K(d)=25 nM). {ECO:0000269|PubMed:21787789,
CC ECO:0000269|PubMed:8513799}.
CC -!- SUBCELLULAR LOCATION: Secreted.
CC -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC -!- MASS SPECTROMETRY: [Crotoxin chain gamma]: Mass=1534.6; Method=MALDI;
CC Note=Monoisotopic mass.; Evidence={ECO:0000269|PubMed:18495297};
CC -!- TOXIC DOSE: In class 2 heterodimer CA2-CBa2, LD(50) is 420 ug/kg by
CC intravenous injection into mice. {ECO:0000269|PubMed:8513799}.
CC -!- TOXIC DOSE: In class 2 heterodimer CA2-CBa2, LD(50) is 650 ug/kg by
CC subcutaneous injection into mice. {ECO:0000269|PubMed:8513799}.
CC -!- TOXIC DOSE: In class 2 heterodimer CA3-CBa2, LD(50) is 450 ug/kg by
CC intravenous injection into mice. {ECO:0000269|PubMed:8513799}.
CC -!- TOXIC DOSE: In class 1 heterodimer CA2-CBb, LD(50) is 110 ug/kg by
CC intravenous injection into mice. {ECO:0000269|PubMed:8513799}.
CC -!- TOXIC DOSE: In class 1 heterodimer CA3-CBb, LD(50) is 95 ug/kg by
CC intravenous injection into mice. {ECO:0000269|PubMed:8513799}.
CC -!- TOXIC DOSE: In class 1 heterodimer CA2-CBc, LD(50) is 80 ug/kg by
CC intravenous injection into mice. {ECO:0000269|PubMed:8513799}.
CC -!- TOXIC DOSE: In class 1 heterodimer CA3-CBc, LD(50) is 110 ug/kg by
CC intravenous injection into mice. {ECO:0000269|PubMed:8513799}.
CC -!- TOXIC DOSE: In class 1 heterodimer CA2-CBd, LD(50) is 70 ug/kg by
CC intravenous injection into mice. {ECO:0000269|PubMed:8513799}.
CC -!- TOXIC DOSE: In class 1 heterodimer CA2-CBd, LD(50) is 150 ug/kg by
CC subcutaneous injection into mice. {ECO:0000269|PubMed:8513799}.
CC -!- TOXIC DOSE: In class 1 heterodimer CA3-CBd, LD(50) is 90 ug/kg by
CC intravenous injection into mice. {ECO:0000269|PubMed:8513799}.
CC -!- PHARMACEUTICAL: Crotoxin (CA-CBc) is under phase II clinical trial as
CC an anti-tumor drug.
CC -!- MISCELLANEOUS: The crotoxin heterodimer is inhibited by the crotoxin
CC inhibitor from Crotalus serum (CICS). CICS neutralizes the lethal
CC potency of crotoxin and inhibits its PLA2 activity. CICS only binds
CC tightly to the CB subunit and induces the dissociation of the
CC heterodimer (By similarity). Tested on the CA2-CBd heterodimer
CC (PubMed:10903514). {ECO:0000250, ECO:0000305|PubMed:10903514}.
CC -!- SIMILARITY: Belongs to the phospholipase A2 family. Group II subfamily.
CC D49 sub-subfamily. {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; X12606; CAA31126.1; -; mRNA.
DR PIR; S01392; PSRSAT.
DR PDB; 3R0L; X-ray; 1.35 A; A=38-76, B=84-118, C=125-138.
DR PDBsum; 3R0L; -.
DR AlphaFoldDB; P08878; -.
DR SMR; P08878; -.
DR ABCD; P08878; 1 sequenced antibody.
DR SABIO-RK; P08878; -.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0004623; F:phospholipase A2 activity; IEA:InterPro.
DR GO; GO:0090729; F:toxin activity; IEA:UniProtKB-KW.
DR GO; GO:0050482; P:arachidonic acid secretion; IEA:InterPro.
DR GO; GO:0016042; P:lipid catabolic process; IEA:InterPro.
DR GO; GO:0006644; P:phospholipid metabolic process; IEA:InterPro.
DR CDD; cd00125; PLA2c; 1.
DR Gene3D; 1.20.90.10; -; 1.
DR InterPro; IPR001211; PLipase_A2.
DR InterPro; IPR033112; PLipase_A2_Asp_AS.
DR InterPro; IPR016090; PLipase_A2_dom.
DR InterPro; IPR036444; PLipase_A2_dom_sf.
DR InterPro; IPR033113; PLipase_A2_His_AS.
DR PANTHER; PTHR11716; PTHR11716; 1.
DR Pfam; PF00068; Phospholip_A2_1; 1.
DR PRINTS; PR00389; PHPHLIPASEA2.
DR SMART; SM00085; PA2c; 1.
DR SUPFAM; SSF48619; SSF48619; 1.
DR PROSITE; PS00119; PA2_ASP; 1.
DR PROSITE; PS00118; PA2_HIS; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Direct protein sequencing; Disulfide bond;
KW G-protein coupled receptor impairing toxin; Neurotoxin; Pharmaceutical;
KW Presynaptic neurotoxin; Pyrrolidone carboxylic acid; Secreted; Signal;
KW Toxin.
FT SIGNAL 1..37
FT /evidence="ECO:0000269|PubMed:1868083"
FT CHAIN 38..78
FT /note="Crotoxin chain alpha CA3"
FT /evidence="ECO:0000269|PubMed:1868083"
FT /id="PRO_0000420453"
FT CHAIN 38..76
FT /note="Crotoxin chain alpha CA1, CA2 and CA4"
FT /id="PRO_0000022854"
FT PROPEP 79..82
FT /evidence="ECO:0000269|PubMed:1868083"
FT /id="PRO_0000022855"
FT CHAIN 83..118
FT /note="Crotoxin chain beta CA1"
FT /evidence="ECO:0000269|PubMed:1868083"
FT /id="PRO_0000420454"
FT CHAIN 84..118
FT /note="Crotoxin chain beta CA2, CA3 and CA4"
FT /evidence="ECO:0000269|PubMed:2400773"
FT /id="PRO_0000022856"
FT PROPEP 119..124
FT /id="PRO_0000022857"
FT CHAIN 125..138
FT /note="Crotoxin chain gamma"
FT /evidence="ECO:0000269|PubMed:18495297,
FT ECO:0000269|PubMed:1868083, ECO:0000269|PubMed:4084559"
FT /id="PRO_0000022858"
FT SITE 43
FT /note="Binds Val-18 of CBb"
FT /evidence="ECO:0000269|PubMed:21787789"
FT SITE 45
FT /note="Binds Asn-16 of CBb"
FT /evidence="ECO:0000269|PubMed:21787789"
FT SITE 45
FT /note="Binds Val-18 of CBb"
FT /evidence="ECO:0000269|PubMed:21787789"
FT SITE 49
FT /note="Binds Arg-14 of CBb"
FT /evidence="ECO:0000269|PubMed:21787789"
FT SITE 93
FT /note="Binds Gly-31 of CBb"
FT /evidence="ECO:0000269|PubMed:21787789"
FT SITE 95
FT /note="Binds Trp-61 of CA2, important for stability (Asp-
FT 89)"
FT /evidence="ECO:0000269|PubMed:21787789"
FT SITE 105
FT /note="Binds Trp-30 of CA2, important for stability (Asp-
FT 99)"
FT /evidence="ECO:0000269|PubMed:21787789"
FT MOD_RES 84
FT /note="Pyrrolidone carboxylic acid"
FT /evidence="ECO:0000269|PubMed:1868083"
FT MOD_RES 125
FT /note="Pyrrolidone carboxylic acid"
FT /evidence="ECO:0000269|PubMed:1868083"
FT DISULFID 42..131
FT /note="Interchain (between alpha and gamma chains);
FT alternate"
FT /evidence="ECO:0000269|PubMed:21787789"
FT DISULFID 44..60
FT /evidence="ECO:0000269|PubMed:21787789"
FT DISULFID 59..111
FT /note="Interchain (between alpha and beta chains)"
FT /evidence="ECO:0000269|PubMed:21787789"
FT DISULFID 65..138
FT /note="Interchain (between alpha and gamma chains);
FT alternate"
FT /evidence="ECO:0000269|PubMed:21787789"
FT DISULFID 66..104
FT /note="Interchain (between alpha and beta chains)"
FT /evidence="ECO:0000269|PubMed:21787789"
FT DISULFID 73..97
FT /note="Interchain (between alpha and beta chains)"
FT /evidence="ECO:0000269|PubMed:21787789"
FT DISULFID 91..102
FT /evidence="ECO:0000269|PubMed:21787789"
FT DISULFID 131..138
FT /note="Intrachain; alternate"
FT /evidence="ECO:0000269|PubMed:18495297"
FT MUTAGEN 136
FT /note="Q->K: No change in analgesic activity."
FT /evidence="ECO:0000269|PubMed:18495297"
FT CONFLICT 74
FT /note="D -> N (in Ref. 3; AA sequence)"
FT /evidence="ECO:0000305"
FT TURN 48..50
FT /evidence="ECO:0007829|PDB:3R0L"
FT HELIX 53..68
FT /evidence="ECO:0007829|PDB:3R0L"
FT HELIX 96..116
FT /evidence="ECO:0007829|PDB:3R0L"
SQ SEQUENCE 138 AA; 15273 MW; F32771BE091CD888 CRC64;
MRALWIVAVL LVGVEGSLVE FETLMMKIAG RSGISYYSSY GCYCGAGGQG WPQDASDRCC
FEHDCCYAKL TGCDPTTDVY TYRQEDGEIV CGEDDPCGTQ ICECDKAAAI CFRNSMDTYD
YKYLQFSPEN CQGESQPC
