ID   CXAA_CONPE              Reviewed;          16 AA.
AC   P50984;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 1.
DT   16-JUN-2009, entry version 56.
DE   RecName: Full=Alpha-conotoxin PnIA;
DE            Short=Alpha-PnIA;
OS   Conus pennaceus (Feathered cone).
OC   Eukaryota; Metazoa; Mollusca; Gastropoda; Orthogastropoda;
OC   Apogastropoda; Caenogastropoda; Sorbeoconcha; Hypsogastropoda;
OC   Neogastropoda; Conoidea; Conidae; Conus.
OX   NCBI_TaxID=37335;
RN   [1]
RP   PROTEIN SEQUENCE, AND FUNCTION.
RC   TISSUE=Venom;
RX   MEDLINE=94347719; PubMed=8068627; DOI=10.1021/bi00198a018;
RA   Fainzilber M., Hasson A., Oren R., Burlingame A.L., Gordon D.,
RA   Spira M.E., Zlotkin E.;
RT   "New mollusc-specific alpha-conotoxins block Aplysia neuronal
RT   acetylcholine receptors.";
RL   Biochemistry 33:9523-9529(1994).
RN   [2]
RP   SULFATION AT TYR-15.
RX   MEDLINE=99242956; PubMed=10226369;
RX   DOI=10.1002/(SICI)1096-9888(199904)34:4<447::AID-JMS801>3.3.CO;2-T;
RA   Wolfender J.L., Chu F., Ball H., Wolfender F., Fainzilber M.,
RA   Baldwin M.A., Burlingame A.L.;
RT   "Identification of tyrosine sulfation in Conus pennaceus conotoxins
RT   alpha-PnIA and alpha-PnIB: further investigation of labile sulfo- and
RT   phosphopeptides by electrospray, matrix-assisted laser
RT   desorption/ionization (MALDI) and atmospheric pressure MALDI mass
RT   spectrometry.";
RL   J. Mass Spectrom. 34:447-454(1999).
RN   [3]
RP   FUNCTION, SYNTHESIS, AND MUTAGENESIS OF ALA-10 AND ASN-11.
RX   PubMed=10545176; DOI=10.1021/bi991252j;
RA   Luo S., Nguyen T.A., Cartier G.E., Olivera B.M., Yoshikami D.,
RA   McIntosh J.M.;
RT   "Single-residue alteration in alpha-conotoxin PnIA switches its nAChR
RT   subtype selectivity.";
RL   Biochemistry 38:14542-14548(1999).
RN   [4]
RP   X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS), AND DISULFIDE BONDS.
RX   MEDLINE=96311277; PubMed=8740364; DOI=10.1016/S0969-2126(96)00047-0;
RA   Hu S.-H., Gehrmann J., Guddat L.W., Alewood P.F., Craik D.J.,
RA   Martin J.L.;
RT   "The 1.1 A crystal structure of the neuronal acetylcholine receptor
RT   antagonist, alpha-conotoxin PnIA from Conus pennaceus.";
RL   Structure 4:417-423(1996).
CC   -!- FUNCTION: Alpha-conotoxins act on postsynaptic membranes, they
CC       bind to the nicotinic acetylcholine receptors (nAChR) and thus
CC       inhibit them. This toxin blocks mammalian nAChRs (alpha-3/beta-2 >
CC       alpha-7 > alpha-3/beta-4).
CC   -!- SUBCELLULAR LOCATION: Secreted.
CC   -!- TISSUE SPECIFICITY: Expressed by the venom duct.
CC   -!- MISCELLANEOUS: PnIA[A10L] corresponds to PnIB[S55N], whereas
CC       PnIA[N11S] corresponds to PnIB[L54A].
CC   -!- SIMILARITY: Belongs to the conotoxin A superfamily. Alpha-type
CC       family.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   PIR; A54877; A54877.
DR   PDB; 1PEN; X-ray; 1.10 A; A=1-16.
DR   PDB; 2BR8; X-ray; 2.40 A; F/G/H/I/J=1-16.
DR   PDBsum; 1PEN; -.
DR   PDBsum; 2BR8; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0045211; C:postsynaptic membrane; IEA:UniProtKB-KW.
DR   GO; GO:0030550; F:acetylcholine receptor inhibitor activity; IEA:UniProtKB-KW.
DR   GO; GO:0009405; P:pathogenesis; IEA:UniProtKB-KW.
DR   GO; GO:0007268; P:synaptic transmission; IEA:UniProtKB-KW.
DR   InterPro; IPR018072; Conotoxin_a-typ_CS.
DR   PROSITE; PS60014; ALPHA_CONOTOXIN; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Acetylcholine receptor inhibitor; Amidation;
KW   Direct protein sequencing; Disulfide bond; Neurotoxin;
KW   Postsynaptic neurotoxin; Secreted; Sulfation; Toxin.
FT   PEPTIDE       1     16       Alpha-conotoxin PnIA.
FT                                /FTId=PRO_0000044462.
FT   MOD_RES      15     15       Sulfotyrosine.
FT   MOD_RES      16     16       Cysteine amide.
FT   DISULFID      2      8
FT   DISULFID      3     16
FT   MUTAGEN      10     10       A->L: Blocks nAChr alpha-7 subunits with
FT                                higher potency than PnIA and PnIB. Blocks
FT                                nAChR alpha-3/beta-2 subunits with a
FT                                potency range between the potency of PnIA
FT                                and PnIB.
FT   MUTAGEN      11     11       N->S: Blocks nAChR alpha-7 subunits with
FT                                lower potency than PnIA and PnIB. Blocks
FT                                nAChR alpha-3/beta-2 subunits with a
FT                                potency range between the potency of PnIA
FT                                and PnIB.
FT   HELIX         2      4
FT   HELIX         6     11
FT   TURN         13     15
SQ   SEQUENCE   16 AA;  1628 MW;  05310FF95EC99005 CRC64;
     GCCSLPPCAA NNPDYC
//