BNP2_BOTJA
ID BNP2_BOTJA Reviewed; 265 AA.
AC Q9PW56; P85167;
DT 03-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 2.
DT 25-MAY-2022, entry version 69.
DE RecName: Full=Bradykinin-potentiating and C-type natriuretic peptides;
DE AltName: Full=Brain BPP-CNP;
DE Short=bBPP-CNP;
DE AltName: Full=Evasin-CNP;
DE Contains:
DE RecName: Full=Bradykinin-potentiating peptide 13a+QQWA {ECO:0000303|PubMed:20146532};
DE Short=BPP-13a+QQWA {ECO:0000303|PubMed:20146532};
DE Contains:
DE RecName: Full=Bradykinin-potentiating peptide 13a+QWA {ECO:0000303|PubMed:20146532};
DE Short=BPP-13a+QWA {ECO:0000303|PubMed:20146532};
DE Contains:
DE RecName: Full=Bradykinin-potentiating peptide 13a {ECO:0000303|PubMed:15245866, ECO:0000303|PubMed:20146532, ECO:0000303|PubMed:22869554};
DE Short=BPP-13a {ECO:0000303|PubMed:15245866, ECO:0000303|PubMed:20146532, ECO:0000303|PubMed:22869554};
DE Contains:
DE RecName: Full=Bradykinin-potentiating peptide 10c+QQWA {ECO:0000303|PubMed:20146532};
DE Short=BPP-10c+QQWA {ECO:0000303|PubMed:20146532};
DE Contains:
DE RecName: Full=Bradykinin-potentiating peptide 10c {ECO:0000303|PubMed:15245866, ECO:0000303|PubMed:22869554};
DE Short=BPP-10c {ECO:0000303|PubMed:15245866, ECO:0000303|PubMed:22869554};
DE Short=BPP-2 {ECO:0000303|PubMed:11994001};
DE AltName: Full=Evasin-10c {ECO:0000303|PubMed:15922781};
DE Contains:
DE RecName: Full=Bradykinin-potentiating peptide 12b {ECO:0000303|PubMed:15245866, ECO:0000303|PubMed:22869554};
DE Short=BPP-12b {ECO:0000303|PubMed:15245866, ECO:0000303|PubMed:22869554};
DE AltName: Full=Evasin-12b {ECO:0000303|PubMed:15922781};
DE Contains:
DE RecName: Full=Bradykinin-potentiating peptide AP {ECO:0000303|PubMed:20146532, ECO:0000303|PubMed:22869554};
DE Contains:
DE RecName: Full=Bradykinin-potentiating peptide APL {ECO:0000303|PubMed:20146532};
DE Short=BPP-APL;
DE Contains:
DE RecName: Full=Bradykinin-potentiating peptide 11e {ECO:0000303|PubMed:15245866, ECO:0000303|PubMed:22869554};
DE Short=BPP-11e {ECO:0000303|PubMed:15245866, ECO:0000303|PubMed:22869554};
DE AltName: Full=Evasin-11e {ECO:0000303|PubMed:15922781};
DE Contains:
DE RecName: Full=Bradykinin-potentiating peptide 5a {ECO:0000303|PubMed:15245866};
DE Short=BPP-5a {ECO:0000303|PubMed:15245866};
DE AltName: Full=Bradykinin-potentiating peptide Va {ECO:0000250|UniProtKB:Q6LEM5};
DE Short=BPPVa {ECO:0000250|UniProtKB:Q6LEM5};
DE AltName: Full=Evasin-5a {ECO:0000303|PubMed:15922781};
DE AltName: Full=Proline-rich peptide 5a {ECO:0000303|PubMed:21185808};
DE Short=Bj-PRO-5a {ECO:0000303|PubMed:21185808};
DE Short=PRO-5a {ECO:0000303|PubMed:21185808};
DE Contains:
DE RecName: Full=Poly-His-poly-Gly peptide 1 {ECO:0000303|PubMed:22869554};
DE Short=pHpG-1 {ECO:0000303|PubMed:22869554};
DE Contains:
DE RecName: Full=C-type natriuretic peptide;
DE AltName: Full=Bj-CNP;
DE Flags: Precursor;
OS Bothrops jararaca (Jararaca) (Bothrops jajaraca).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC Serpentes; Colubroidea; Viperidae; Crotalinae; Bothrops.
OX NCBI_TaxID=8724;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND TISSUE SPECIFICITY.
RC TISSUE=Brain;
RX PubMed=12716428; DOI=10.1046/j.1471-4159.2003.01743.x;
RA Hayashi M.A.F., Murbach A.F., Ianzer D., Portaro F.C.V., Prezoto B.C.,
RA Fernandes B.L., Silveira P.F., Silva C.A., Pires R.S., Britto L.R.G.,
RA Dive V., Camargo A.C.M.;
RT "The C-type natriuretic peptide precursor of snake brain contains highly
RT specific inhibitors of the angiotensin-converting enzyme.";
RL J. Neurochem. 85:969-977(2003).
RN [2]
RP PROTEIN SEQUENCE OF 31-43; 51-63; 71-80; 88-99; 107-117; 107-119 AND
RP 216-234 (BPP-10C; BPP-11E; BPP-12B; BPP-13A; BPP-AP AND PHPG-1), SYNTHESIS
RP OF 71-80 (BPP-10C), FUNCTION, PYROGLUTAMATE FORMATION AT GLN-31; GLN-51;
RP GLN-71; GLN-88 AND GLN-107, AND MASS SPECTROMETRY.
RC TISSUE=Venom;
RX PubMed=22869554; DOI=10.1074/mcp.m112.019331;
RA Tashima A.K., Zelanis A., Kitano E.S., Ianzer D., Melo R.L., Rioli V.,
RA Sant'anna S.S., Schenberg A.C., Camargo A.C., Serrano S.M.T.;
RT "Peptidomics of three Bothrops snake venoms: insights into the molecular
RT diversification of proteomes and peptidomes.";
RL Mol. Cell. Proteomics 11:1245-1262(2012).
RN [3]
RP PROTEIN SEQUENCE OF 27-43; 28-43; 31-43; 47-63; 48-63; 51-63; 67-80;
RP 107-119 AND 107-120 (BPP-13A+QQWA; BPP-13A+QWA; BPP-13A; BPP-10C+QQWA;
RP BPP-AP AND BPP-APL), PYROGLUTAMATE FORMATION AT GLN-27; GLN-28; GLN-31;
RP GLN-47; GLN-48; GLN-51; GLN-67 AND GLN-107, DEVELOPMENTAL STAGE, AND
RP IDENTIFICATION BY MASS SPECTROMETRY.
RC TISSUE=Venom;
RX PubMed=20146532; DOI=10.1021/pr901027r;
RA Zelanis A., Tashima A.K., Rocha M.M., Furtado M.F., Camargo A.C., Ho P.L.,
RA Serrano S.M.;
RT "Analysis of the ontogenetic variation in the venom proteome/peptidome of
RT Bothrops jararaca reveals different strategies to deal with prey.";
RL J. Proteome Res. 9:2278-2291(2010).
RN [4]
RP PROTEIN SEQUENCE OF 31-43; 51-63; 71-80; 88-99; 107-117; 121-125 AND
RP 127-131 (BPP-13A; BPP-10C; BPP-12B; BPP11E AND BPP-5A), FUNCTION,
RP SUBCELLULAR LOCATION, TISSUE SPECIFICITY, MASS SPECTROMETRY, AND
RP PYROGLUTAMATE FORMATION AT GLN-31; GLN-51; GLN-71; GLN-88; GLN-107; GLN-121
RP AND GLN-127.
RC TISSUE=Venom;
RX PubMed=15245866; DOI=10.1016/j.peptides.2004.04.006;
RA Ianzer D., Konno K., Marques-Porto R., Portaro F.C.V., Stoecklin R.,
RA de Camargo A.C.M., Pimenta D.C.;
RT "Identification of five new bradykinin potentiating peptides (BPPs) from
RT Bothrops jararaca crude venom by using electrospray ionization tandem mass
RT spectrometry after a two-step liquid chromatography.";
RL Peptides 25:1085-1092(2004).
RN [5]
RP SYNTHESIS OF 71-80, AND FUNCTION.
RX PubMed=11994001; DOI=10.1021/bi012121x;
RA Cotton J., Hayashi M.A., Cuniasse P., Vazeux G., Ianzer D.,
RA De Camargo A.C., Dive V.;
RT "Selective inhibition of the C-domain of angiotensin I converting enzyme by
RT bradykinin potentiating peptides.";
RL Biochemistry 41:6065-6071(2002).
RN [6]
RP FUNCTION BPP-10C.
RX PubMed=17475904; DOI=10.1124/jpet.107.120873;
RA Ianzer D., Santos R.A., Etelvino G.M., Xavier C.H., de Almeida Santos J.,
RA Mendes E.P., Machado L.T., Prezoto B.C., Dive V., de Camargo A.C.;
RT "Do the cardiovascular effects of angiotensin-converting enzyme (ACE) I
RT involve ACE-independent mechanisms? new insights from proline-rich peptides
RT of Bothrops jararaca.";
RL J. Pharmacol. Exp. Ther. 322:795-805(2007).
RN [7]
RP FUNCTION, BIOASSAY, SUBCELLULAR LOCATION, AND MUTAGENESIS OF PRO-74;
RP PRO-76; ILE-78; PRO-79 AND PRO-80.
RX PubMed=19491403; DOI=10.1074/jbc.m109.021089;
RA Guerreiro J.R., Lameu C., Oliveira E.F., Klitzke C.F., Melo R.L.,
RA Linares E., Augusto O., Fox J.W., Lebrun I., Serrano S.M., Camargo A.C.;
RT "Argininosuccinate synthetase is a functional target for a snake venom
RT anti-hypertensive peptide: role in arginine and nitric oxide production.";
RL J. Biol. Chem. 284:20022-20033(2009).
RN [8]
RP SYNTHESIS OF 121-125 AND 127-131 (BBP-5A), AND FUNCTION.
RX PubMed=21185808; DOI=10.1016/j.bcp.2010.12.016;
RA Morais K.L., Hayashi M.A., Bruni F.M., Lopes-Ferreira M., Camargo A.C.,
RA Ulrich H., Lameu C.;
RT "Bj-PRO-5a, a natural angiotensin-converting enzyme inhibitor, promotes
RT vasodilatation mediated by both bradykinin B(2)and M1 muscarinic
RT acetylcholine receptors.";
RL Biochem. Pharmacol. 81:736-742(2011).
RN [9]
RP REVIEW, AND FUNCTION.
RX PubMed=15922781; DOI=10.1016/j.toxicon.2005.02.017;
RA Hayashi M.A., Camargo A.C.;
RT "The bradykinin-potentiating peptides from venom gland and brain of
RT Bothrops jararaca contain highly site specific inhibitors of the somatic
RT angiotensin-converting enzyme.";
RL Toxicon 45:1163-1170(2005).
CC -!- FUNCTION: [Bradykinin-potentiating peptide 5a]: Modestly inhibits ACE
CC (with highest affinity for the N-site) and reveals strong bradykinin-
CC potentiating activity. Induces nitric oxide (NO) production depended on
CC muscarinic acetylcholine receptor M1 subtype (CHRM1) and bradykinin B2
CC receptor (BDKRB2) activation. Both these receptors contribute to the
CC vasodilation induced by this peptide that may have an indirect action
CC on BDKRB2 and a direct agonistic action on CHRM1.
CC -!- FUNCTION: [Bradykinin-potentiating peptide 10c]: Peptide with several
CC activities. It inhibits the activity of the angiotensin-converting
CC enzyme (ACE) by a preferential interaction with its C-domain
CC (PubMed:11994001). It evokes transient hypotension (-14 mmHg) similar
CC to that evoked by 0,5 ug of bradykinin, when injected alone into rats.
CC It has a high bradykinin-potentiating effect (120%), when 60 nmol of
CC BPP-10c are coinjected with 0.5 ug of bradykinin into rats
CC (PubMed:22869554). Does not affect angiotensin-1 pressor effects. Shows
CC potent and long-lasting antihypertensive activity as well as a
CC reduction of the heart rate (PubMed:17475904). It also binds and dose-
CC dependently promotes the activation of cytosolic argininosuccinate
CC synthase (ASS1), an enzyme that catalyzes the conversion of citrulline,
CC L-aspartate and ATP to argininosuccinate, AMP and pyrophosphate. It
CC also enhances ASS1-dependent arginine production in HEK 293 cells, as
CC well as in spontaneous hypertensive rat (SHR) and Wistar rat plasma. In
CC addition, it induces the production of nitric-oxide (NO) by HUVEC cells
CC via the endothelial nitric-oxide synthase (NOS3), which use arginine as
CC a substrate and produce NO. It has been shown to be internalized by
CC ASS1-expressing endothelial (HUVEC) and kidney (HEK 293) cells, and is
CC detected homogenously distributed within the cell cytoplasm for up to 2
CC hours (PubMed:19491403). {ECO:0000269|PubMed:11994001,
CC ECO:0000269|PubMed:17475904, ECO:0000269|PubMed:19491403,
CC ECO:0000269|PubMed:22869554}.
CC -!- FUNCTION: [Poly-His-poly-Gly peptide 1]: May serve as a
CC metalloproteinase inhibitor during glandular storage. Their inhibition
CC may be instantly disengaged, by dilution or physiochemical change, when
CC venom is injected into tissue of the victim.
CC {ECO:0000250|UniProtKB:A8YPR6}.
CC -!- FUNCTION: Natriuretic peptide exhibits natriuretic and vasodepressor
CC activity. Acts by stimulating cGMP. {ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: Secreted. Cytoplasm, cytosol. Note=BPP-10c is
CC internalized in the cytosol of prey cells.
CC -!- TISSUE SPECIFICITY: Adult brain regions; ventromedial hypothalamus,
CC paraventricular nucleus, paraventricular organ, and the subcommissural
CC organ. Also expressed by the venom gland. {ECO:0000269|PubMed:12716428,
CC ECO:0000269|PubMed:15245866}.
CC -!- DEVELOPMENTAL STAGE: BPP-10a, BPP-10c+QQWA, BPP-AP, BPP-13A, BPP-
CC 13a+QWA and BPP-13a+QQWA seem to be found in both adult and newborn
CC B.jararaca venoms, whereas BPP-APL seem to be only present in newborn
CC venom. {ECO:0000269|PubMed:20146532}.
CC -!- MASS SPECTROMETRY: [Bradykinin-potentiating peptide 10c]: Mass=1195.6;
CC Method=Electrospray; Note=BPP-10c.;
CC Evidence={ECO:0000269|PubMed:22869554};
CC -!- MASS SPECTROMETRY: [Bradykinin-potentiating peptide 11e]: Mass=1189.4;
CC Method=Electrospray; Evidence={ECO:0000269|PubMed:15245866};
CC -!- MASS SPECTROMETRY: [Bradykinin-potentiating peptide 11e]: Mass=1188.7;
CC Method=Electrospray; Note=BPP-11e.;
CC Evidence={ECO:0000269|PubMed:22869554};
CC -!- MASS SPECTROMETRY: [Bradykinin-potentiating peptide AP]: Mass=1356.5;
CC Method=Electrospray; Note=BPP-AP.;
CC Evidence={ECO:0000269|PubMed:22869554};
CC -!- MASS SPECTROMETRY: [Bradykinin-potentiating peptide 12b]: Mass=1280.7;
CC Method=Electrospray; Note=BPP-12b.;
CC Evidence={ECO:0000269|PubMed:22869554};
CC -!- MASS SPECTROMETRY: [Poly-His-poly-Gly peptide 1]: Mass=1563.7;
CC Method=Electrospray; Note=pHpG-1.;
CC Evidence={ECO:0000269|PubMed:22869554};
CC -!- MISCELLANEOUS: The name evasin stands for 'Endogenous VASopeptidase
CC INhibitors' and is given to endogenous brain proteins in order to
CC distinguish them from venom proteins. {ECO:0000305|PubMed:15922781}.
CC -!- MISCELLANEOUS: A BPP-13a without the two first amino acids has been
CC detected. {ECO:0000305|PubMed:20146532}.
CC -!- SIMILARITY: In the N-terminal section; belongs to the bradykinin-
CC potentiating peptide family. {ECO:0000305}.
CC -!- SIMILARITY: In the central section; belongs to the pHpG family.
CC {ECO:0000305}.
CC -!- SIMILARITY: In the C-terminal section; belongs to the natriuretic
CC peptide family. {ECO:0000255}.
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DR EMBL; AF171670; AAD51326.2; -; mRNA.
DR AlphaFoldDB; Q9PW56; -.
DR TCDB; 1.C.46.1.2; the c-type natriuretic peptide (cnp) family.
DR GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0005179; F:hormone activity; IEA:InterPro.
DR GO; GO:0008191; F:metalloendopeptidase inhibitor activity; IEA:UniProtKB-KW.
DR GO; GO:0060422; F:peptidyl-dipeptidase inhibitor activity; IDA:UniProtKB.
DR GO; GO:0090729; F:toxin activity; IEA:UniProtKB-KW.
DR GO; GO:0097746; P:blood vessel diameter maintenance; IDA:UniProtKB.
DR GO; GO:0045776; P:negative regulation of blood pressure; IDA:UniProtKB.
DR GO; GO:0006469; P:negative regulation of protein kinase activity; NAS:UniProtKB.
DR GO; GO:0042311; P:vasodilation; IEA:UniProtKB-KW.
DR InterPro; IPR000663; Natr_peptide.
DR InterPro; IPR030480; Natr_peptide_CS.
DR Pfam; PF00212; ANP; 1.
DR SMART; SM00183; NAT_PEP; 1.
DR PROSITE; PS00263; NATRIURETIC_PEPTIDE; 1.
PE 1: Evidence at protein level;
KW Cleavage on pair of basic residues; Cytoplasm; Direct protein sequencing;
KW Disulfide bond; G-protein coupled receptor impairing toxin;
KW Hypotensive agent; Metalloenzyme inhibitor; Metalloprotease inhibitor;
KW Protease inhibitor; Pyrrolidone carboxylic acid; Secreted; Signal; Toxin;
KW Vasoactive; Vasodilator.
FT SIGNAL 1..23
FT /evidence="ECO:0000255"
FT PROPEP 24..26
FT /evidence="ECO:0000269|PubMed:20146532"
FT /id="PRO_0000252066"
FT PEPTIDE 27..43
FT /note="Bradykinin-potentiating peptide 13a+QQWA"
FT /evidence="ECO:0000269|PubMed:20146532"
FT /id="PRO_0000422964"
FT PEPTIDE 28..43
FT /note="Bradykinin-potentiating peptide 13a+QWA"
FT /evidence="ECO:0000269|PubMed:20146532"
FT /id="PRO_0000422965"
FT PEPTIDE 31..43
FT /note="Bradykinin-potentiating peptide 13a"
FT /evidence="ECO:0000269|PubMed:15245866,
FT ECO:0000269|PubMed:20146532, ECO:0000269|PubMed:22869554"
FT /id="PRO_0000252067"
FT PROPEP 44..46
FT /evidence="ECO:0000305"
FT /id="PRO_0000252068"
FT PEPTIDE 47..63
FT /note="Bradykinin-potentiating peptide 13a+QQWA"
FT /evidence="ECO:0000269|PubMed:20146532"
FT /id="PRO_0000422966"
FT PEPTIDE 48..63
FT /note="Bradykinin-potentiating peptide 13a+QWA"
FT /evidence="ECO:0000269|PubMed:20146532"
FT /id="PRO_0000422967"
FT PEPTIDE 51..63
FT /note="Bradykinin-potentiating peptide 13a"
FT /evidence="ECO:0000269|PubMed:15245866,
FT ECO:0000269|PubMed:20146532, ECO:0000269|PubMed:22869554"
FT /id="PRO_0000252069"
FT PROPEP 64..66
FT /evidence="ECO:0000305"
FT /id="PRO_0000252070"
FT PEPTIDE 67..80
FT /note="Bradykinin-potentiating peptide 10c+QQWA"
FT /evidence="ECO:0000269|PubMed:20146532"
FT /id="PRO_0000422968"
FT PEPTIDE 71..80
FT /note="Bradykinin-potentiating peptide 10c"
FT /evidence="ECO:0000269|PubMed:15245866,
FT ECO:0000269|PubMed:22869554"
FT /id="PRO_0000252071"
FT PROPEP 81..87
FT /evidence="ECO:0000305"
FT /id="PRO_0000252072"
FT PEPTIDE 88..99
FT /note="Bradykinin-potentiating peptide 12b"
FT /evidence="ECO:0000269|PubMed:15245866,
FT ECO:0000269|PubMed:22869554"
FT /id="PRO_0000252073"
FT PROPEP 100..106
FT /evidence="ECO:0000305"
FT /id="PRO_0000252074"
FT PEPTIDE 107..120
FT /note="Bradykinin-potentiating peptide APL"
FT /evidence="ECO:0000269|PubMed:20146532,
FT ECO:0000269|PubMed:22869554"
FT /id="PRO_0000422969"
FT PEPTIDE 107..119
FT /note="Bradykinin-potentiating peptide AP"
FT /evidence="ECO:0000269|PubMed:20146532"
FT /id="PRO_0000421889"
FT PEPTIDE 107..117
FT /note="Bradykinin-potentiating peptide 11e"
FT /evidence="ECO:0000269|PubMed:15245866,
FT ECO:0000269|PubMed:22869554"
FT /id="PRO_0000252075"
FT PROPEP 118..120
FT /evidence="ECO:0000305"
FT /id="PRO_0000252076"
FT PEPTIDE 121..125
FT /note="Bradykinin-potentiating peptide 5a"
FT /evidence="ECO:0000269|PubMed:15245866"
FT /id="PRO_0000252077"
FT PROPEP 126
FT /evidence="ECO:0000305"
FT /id="PRO_0000252078"
FT PEPTIDE 127..131
FT /note="Bradykinin-potentiating peptide 5a"
FT /evidence="ECO:0000269|PubMed:15245866"
FT /id="PRO_0000252079"
FT PROPEP 132..215
FT /evidence="ECO:0000305"
FT /id="PRO_0000252080"
FT PEPTIDE 216..234
FT /note="Poly-His-poly-Gly peptide 1"
FT /evidence="ECO:0000269|PubMed:22869554"
FT /id="PRO_0000421890"
FT PROPEP 235..243
FT /evidence="ECO:0000305"
FT /id="PRO_0000421891"
FT PEPTIDE 244..265
FT /note="C-type natriuretic peptide"
FT /id="PRO_0000252081"
FT REGION 153..211
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 27
FT /note="Pyrrolidone carboxylic acid"
FT /evidence="ECO:0000269|PubMed:20146532"
FT MOD_RES 28
FT /note="Pyrrolidone carboxylic acid"
FT /evidence="ECO:0000269|PubMed:20146532"
FT MOD_RES 31
FT /note="Pyrrolidone carboxylic acid"
FT /evidence="ECO:0000269|PubMed:15245866,
FT ECO:0000269|PubMed:20146532, ECO:0000269|PubMed:22869554"
FT MOD_RES 47
FT /note="Pyrrolidone carboxylic acid"
FT /evidence="ECO:0000269|PubMed:20146532"
FT MOD_RES 48
FT /note="Pyrrolidone carboxylic acid"
FT /evidence="ECO:0000269|PubMed:20146532"
FT MOD_RES 51
FT /note="Pyrrolidone carboxylic acid"
FT /evidence="ECO:0000269|PubMed:15245866,
FT ECO:0000269|PubMed:20146532, ECO:0000269|PubMed:22869554"
FT MOD_RES 67
FT /note="Pyrrolidone carboxylic acid"
FT /evidence="ECO:0000269|PubMed:20146532"
FT MOD_RES 71
FT /note="Pyrrolidone carboxylic acid"
FT /evidence="ECO:0000269|PubMed:15245866,
FT ECO:0000269|PubMed:22869554"
FT MOD_RES 88
FT /note="Pyrrolidone carboxylic acid"
FT /evidence="ECO:0000269|PubMed:15245866,
FT ECO:0000269|PubMed:22869554"
FT MOD_RES 107
FT /note="Pyrrolidone carboxylic acid"
FT /evidence="ECO:0000269|PubMed:15245866,
FT ECO:0000269|PubMed:20146532, ECO:0000269|PubMed:22869554"
FT MOD_RES 121
FT /note="Pyrrolidone carboxylic acid"
FT /evidence="ECO:0000269|PubMed:15245866"
FT MOD_RES 127
FT /note="Pyrrolidone carboxylic acid"
FT /evidence="ECO:0000269|PubMed:15245866"
FT DISULFID 249..265
FT /evidence="ECO:0000250|UniProtKB:P23582"
FT MUTAGEN 74
FT /note="P->A: Low decrease in ability to enhance AsS
FT activity."
FT /evidence="ECO:0000269|PubMed:19491403"
FT MUTAGEN 76
FT /note="P->A: Low decrease in ability to enhance AsS
FT activity."
FT /evidence="ECO:0000269|PubMed:19491403"
FT MUTAGEN 78
FT /note="I->A: Low decrease in ability to enhance AsS
FT activity."
FT /evidence="ECO:0000269|PubMed:19491403"
FT MUTAGEN 79
FT /note="P->A: Important decrease in ability to enhance AsS
FT activity."
FT /evidence="ECO:0000269|PubMed:19491403"
FT MUTAGEN 80
FT /note="P->A: Important decrease in ability to enhance AsS
FT activity."
FT /evidence="ECO:0000269|PubMed:19491403"
SQ SEQUENCE 265 AA; 27763 MW; 8E99AEC976CCD439 CRC64;
MVLSRLAASG LLLLALLALS VDGKPVQQWA QGGWPRPGPE IPPLKVQQWA QGGWPRPGPE
IPPLTVQQWA QNWPHPQIPP LTVQQWAQWG RPPGPPIPPL TVQQWAQARP PHPPIPPAPL
QKWAPVQKWA PLLQPHESPA SGTTALREEL SLGPEAASGV PSAGAEVGRS GSKAPAAPHR
LSKSKGAAAT SAASRPMRDL RPDGKQARQN WGRMVHHDHH AAVGGGGGGG GGGARRLKGL
AKKGAAKGCF GLKVDRIGTM SGLGC
