TX9A_URTGR
ID TX9A_URTGR Reviewed; 162 AA.
AC R4ZCU1; S4S1V7;
DT 16-SEP-2015, integrated into UniProtKB/Swiss-Prot.
DT 24-JUL-2013, sequence version 1.
DT 25-MAY-2022, entry version 22.
DE RecName: Full=Precursor protein UG {ECO:0000303|PubMed:23801332};
DE Contains:
DE RecName: Full=U-actitoxin-Ugr1c {ECO:0000305};
DE Short=U-AITX-Ugr1c {ECO:0000305};
DE AltName: Full=AnmTX Ugr 9a-3 {ECO:0000303|PubMed:23801332};
DE Short=Ugr 9-3 {ECO:0000303|PubMed:23801332};
DE Contains:
DE RecName: Full=U-actitoxin-Ugr1b {ECO:0000305};
DE Short=U-AITX-Ugr1b {ECO:0000305};
DE AltName: Full=AnmTX Ugr 9a-2 {ECO:0000303|PubMed:23801332};
DE Short=Ugr 9-2 {ECO:0000303|PubMed:23801332};
DE Contains:
DE RecName: Full=Pi-actitoxin-Ugr1a {ECO:0000305};
DE Short=Pi-AITX-Ugr1a {ECO:0000305};
DE AltName: Full=Pi-AnmTX Ugr 9a-1 {ECO:0000303|PubMed:23801332};
DE Short=Ugr 9-1 {ECO:0000303|PubMed:23801332};
DE Flags: Precursor;
OS Urticina grebelnyi (Painted anemone).
OC Eukaryota; Metazoa; Cnidaria; Anthozoa; Hexacorallia; Actiniaria;
OC Actiniidae; Urticina.
OX NCBI_TaxID=1264739;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE, FUNCTION, STRUCTURE
RP BY NMR OF 132-160, SUBCELLULAR LOCATION, AND MASS SPECTROMETRY.
RC TISSUE=Nematoblast;
RX PubMed=23801332; DOI=10.1074/jbc.m113.485516;
RA Osmakov D.I., Kozlov S.A., Andreev Y.A., Koshelev S.G., Sanamyan N.P.,
RA Sanamyan K.E., Dyachenko I.A., Bondarenko D.A., Murashev A.N., Mineev K.S.,
RA Arseniev A.S., Grishin E.V.;
RT "Sea anemone peptide with uncommon beta-hairpin structure inhibits acid-
RT sensing ion channel 3 (ASIC3) and reveals analgesic activity.";
RL J. Biol. Chem. 288:23116-23127(2013).
CC -!- FUNCTION: [Pi-actitoxin-Ugr1a]: Affects the ASIC3 channel (ACCN3) and
CC produces analgesic effects. It produces a reversible inhibition effect
CC on both the transient and the sustained current of human ASIC3 channels
CC expressed in X.laevis oocytes. It completely blocks the transient
CC component (IC(50)=10 uM) and partially (48%) inhibits the amplitude of
CC the sustained component (IC(50)=1.44 uM). Using in vivo tests in mice,
CC it reverses inflammatory and acid-induced pain.
CC {ECO:0000269|PubMed:23801332}.
CC -!- FUNCTION: [U-actitoxin-Ugr1b]: Does not affect the ASIC3 channel. Does
CC not cause lethality or paralysis of noble crayfish (A.astacus) at a
CC dose of 1 mg/kg. {ECO:0000269|PubMed:23801332}.
CC -!- FUNCTION: [U-actitoxin-Ugr1c]: Does not affect the ASIC3 channel. Does
CC not cause lethality or paralysis of noble crayfish (A.astacus) at a
CC dose of 1 mg/kg. {ECO:0000269|PubMed:23801332}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:23801332}.
CC Nematocyst {ECO:0000269|PubMed:23801332}.
CC -!- DOMAIN: Pi-AnmTX Ugr 9a-1, AnmTX Ugr 9a-2 and AnmTX Ugr 9a-3 have a
CC structural fold called the boundless beta-hairpin since its beta-
CC hairpin is not stabilized by disulfide bonds.
CC {ECO:0000305|PubMed:23801332}.
CC -!- MASS SPECTROMETRY: [U-actitoxin-Ugr1c]: Mass=3053; Method=MALDI;
CC Note=Average mass.; Evidence={ECO:0000269|PubMed:23801332};
CC -!- MASS SPECTROMETRY: [U-actitoxin-Ugr1b]: Mass=3087; Method=MALDI;
CC Note=Average mass.; Evidence={ECO:0000269|PubMed:23801332};
CC -!- MASS SPECTROMETRY: [Pi-actitoxin-Ugr1a]: Mass=3135.5; Method=MALDI;
CC Note=Average mass.; Evidence={ECO:0000269|PubMed:23801332};
CC -!- MISCELLANEOUS: [Pi-actitoxin-Ugr1a]: Shows neither agonistic nor
CC antagonistic activity on ASIC1a/ASIC1, ASIC1b/ASIC1 and ASIC2a/ASIC2 at
CC concentrations up to 50 uM as well as on the hKv1.3/KCNA3 channel at
CC concentrations up to 1 uM. It does not cause lethality or paralysis of
CC noble crayfish (A.astacus) at a dose of 1 mg/kg.
CC {ECO:0000269|PubMed:23801332}.
CC -!- SIMILARITY: Belongs to the sea anemone structural class 9a family.
CC {ECO:0000305|PubMed:23801332}.
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DR EMBL; HF562346; CCP19153.1; -; mRNA.
DR PDB; 2LZO; NMR; -; A=132-160.
DR PDBsum; 2LZO; -.
DR AlphaFoldDB; R4ZCU1; -.
DR SMR; R4ZCU1; -.
DR TCDB; 8.B.15.1.3; the sea anemone peptide toxin class 4 (shtx) family.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0042151; C:nematocyst; IEA:UniProtKB-SubCell.
DR GO; GO:0099106; F:ion channel regulator activity; IEA:UniProtKB-KW.
DR GO; GO:0090729; F:toxin activity; IEA:UniProtKB-KW.
PE 1: Evidence at protein level;
KW 3D-structure; Cleavage on pair of basic residues;
KW Direct protein sequencing; Disulfide bond; Ion channel impairing toxin;
KW Nematocyst; Neurotoxin; Proton-gated sodium channel impairing toxin;
KW Secreted; Signal; Toxin.
FT SIGNAL 1..19
FT /evidence="ECO:0000255"
FT CHAIN 20..162
FT /note="Precursor protein UG"
FT /id="PRO_0000433732"
FT PROPEP 20..23
FT /evidence="ECO:0000269|PubMed:23801332"
FT /id="PRO_0000433733"
FT PEPTIDE 24..52
FT /note="U-actitoxin-Ugr1c"
FT /id="PRO_0000433734"
FT PROPEP 56..59
FT /evidence="ECO:0000269|PubMed:23801332"
FT /id="PRO_0000433735"
FT PEPTIDE 60..88
FT /note="U-actitoxin-Ugr1b"
FT /id="PRO_0000433736"
FT PROPEP 92..95
FT /evidence="ECO:0000269|PubMed:23801332"
FT /id="PRO_0000433737"
FT PEPTIDE 96..124
FT /note="U-actitoxin-Ugr1b"
FT /id="PRO_0000433738"
FT PROPEP 128..131
FT /evidence="ECO:0000269|PubMed:23801332"
FT /id="PRO_0000433739"
FT PEPTIDE 132..160
FT /note="Pi-actitoxin-Ugr1a"
FT /id="PRO_0000433740"
FT DISULFID 30..42
FT /evidence="ECO:0000305|PubMed:23801332"
FT DISULFID 33..49
FT /evidence="ECO:0000305|PubMed:23801332"
FT DISULFID 66..78
FT /evidence="ECO:0000305|PubMed:23801332"
FT DISULFID 69..85
FT /evidence="ECO:0000305|PubMed:23801332"
FT DISULFID 102..114
FT /evidence="ECO:0000305|PubMed:23801332"
FT DISULFID 105..121
FT /evidence="ECO:0000305|PubMed:23801332"
FT DISULFID 138..150
FT /evidence="ECO:0000269|PubMed:23801332"
FT DISULFID 141..157
FT /evidence="ECO:0000269|PubMed:23801332"
FT STRAND 142..144
FT /evidence="ECO:0007829|PDB:2LZO"
FT STRAND 150..152
FT /evidence="ECO:0007829|PDB:2LZO"
SQ SEQUENCE 162 AA; 17737 MW; 9D235318845F4640 CRC64;
MERILLCFIV ATLVAISMAN PRPISIDPPC WTCYYRDSSG NCAFDAIACG GARKRVPKPI
SIDPPCRTCY YRDSSGNCVY DAFGCGGARK RVPKPISIDP PCRTCYYRDS SGNCVYDAFG
CGGARKRVPK PISIDPPCRF CYHRDGSGNC VYDAYGCGAV RK
