MIT1_DENPO
ID MIT1_DENPO Reviewed; 81 AA.
AC P25687;
DT 01-MAY-1992, integrated into UniProtKB/Swiss-Prot.
DT 19-JUL-2005, sequence version 3.
DT 25-MAY-2022, entry version 88.
DE RecName: Full=Toxin MIT1 {ECO:0000303|PubMed:10567694};
DE Short=MIT 1 {ECO:0000303|PubMed:10567694};
DE AltName: Full=Black mamba intestinal toxin 1 {ECO:0000303|PubMed:10567694};
DE AltName: Full=Black mamba venom protein A {ECO:0000303|PubMed:7461607};
OS Dendroaspis polylepis polylepis (Black mamba).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC Serpentes; Colubroidea; Elapidae; Elapinae; Dendroaspis.
OX NCBI_TaxID=8620;
RN [1]
RP PROTEIN SEQUENCE, SEQUENCE REVISION TO 18; 22 AND 54, FUNCTION, AND
RP SUBCELLULAR LOCATION.
RC TISSUE=Venom;
RX PubMed=10567694; DOI=10.1016/s0014-5793(99)01459-3;
RA Schweitz H., Pascaud P., Diochot S., Moinier D., Lazdunski M.;
RT "MIT1, a black mamba toxin with a new and highly potent activity on
RT intestinal contraction.";
RL FEBS Lett. 461:183-188(1999).
RN [2]
RP PROTEIN SEQUENCE OF 1-80.
RC TISSUE=Venom;
RX PubMed=7461607; DOI=10.1515/bchm2.1980.361.2.1787;
RA Joubert F.J., Strydom D.J.;
RT "Snake venom. The amino acid sequence of protein A from Dendroaspis
RT polylepis polylepis (black mamba) venom.";
RL Hoppe-Seyler's Z. Physiol. Chem. 361:1787-1794(1980).
RN [3]
RP PARTIAL PROTEIN SEQUENCE, FUNCTION, AND ACTIVITY PROFILE.
RC TISSUE=Venom;
RX PubMed=12054613; DOI=10.1016/s0006-291x(02)00239-5;
RA Masuda Y., Takatsu Y., Terao Y., Kumano S., Ishibashi Y., Suenaga M.,
RA Abe M., Fukusumi S., Watanabe T., Shintani Y., Yamada T., Hinuma S.,
RA Inatomi N., Ohtaki T., Onda H., Fujino M.;
RT "Isolation and identification of EG-VEGF/prokineticins as cognate ligands
RT for two orphan G-protein-coupled receptors.";
RL Biochem. Biophys. Res. Commun. 293:396-402(2002).
RN [4]
RP STRUCTURE BY NMR OF 1-80, AND DISULFIDE BONDS.
RC TISSUE=Venom;
RX PubMed=9761684; DOI=10.1006/jmbi.1998.2057;
RA Boisbouvier J., Albrand J.-P., Blackledge M., Jaquinod M., Schweitz H.,
RA Lazdunski M., Marion D.;
RT "A structural homologue of colipase in black mamba venom revealed by NMR
RT floating disulphide bridge analysis.";
RL J. Mol. Biol. 283:205-219(1998).
CC -!- FUNCTION: Potent agonist for both PKR1/PROKR1 and PKR2/PROKR2
CC (PubMed:12054613). Potently contracts gastrointestinal (GI) smooth
CC muscle (PubMed:10567694). {ECO:0000269|PubMed:10567694,
CC ECO:0000269|PubMed:12054613}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:10567694}.
CC -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC {ECO:0000305|PubMed:10567694}.
CC -!- MISCELLANEOUS: This toxin does not inhibit Kv1.1/KCNA1, Kv1.2/KCNA2,
CC Kv1.3/KCNA3, Kv1.4/KCNA4, Kv1.5/KCNA5, Kv2.1/KCNB1, Kv3.4/KCNC4,
CC Kv4.2/KCND2, K2P2.1/KCNK2, Kv11/KCNH, Kv7.1/KCNQ1, Kv7.2/KCNQ2,
CC Kv7.3/KCNQ3, Kir1.1/KCNJ1, Kir2.1/KCNJ2, Kir2.2/KCNJ12, Kir3.1/KCNJ3-
CC Kir3.2/KCNJ6 (GIRK1,2) and Kir3.1/KCNJ3-Kir3.4/KCNJ5 (GIRK1,4).
CC {ECO:0000269|PubMed:10567694}.
CC -!- SIMILARITY: Belongs to the AVIT (prokineticin) family. {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 PDB; 1IMT; NMR; -; A=1-80.
DR PDBsum; 1IMT; -.
DR AlphaFoldDB; P25687; -.
DR SMR; P25687; -.
DR EvolutionaryTrace; P25687; -.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0090729; F:toxin activity; IEA:UniProtKB-KW.
DR InterPro; IPR009523; Prokineticin.
DR InterPro; IPR023569; Prokineticin_domain.
DR PANTHER; PTHR18821; PTHR18821; 1.
DR Pfam; PF06607; Prokineticin; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Direct protein sequencing; Disulfide bond;
KW G-protein coupled receptor impairing toxin; Secreted; Toxin.
FT CHAIN 1..81
FT /note="Toxin MIT1"
FT /evidence="ECO:0000303|PubMed:10567694"
FT /id="PRO_0000165469"
FT DISULFID 7..19
FT /evidence="ECO:0000269|PubMed:9761684"
FT DISULFID 13..31
FT /evidence="ECO:0000269|PubMed:9761684"
FT DISULFID 18..59
FT /evidence="ECO:0000269|PubMed:9761684"
FT DISULFID 41..67
FT /evidence="ECO:0000269|PubMed:9761684"
FT DISULFID 61..77
FT /evidence="ECO:0000269|PubMed:9761684"
FT VARIANT 72
FT /note="P -> Q (in protein A')"
FT HELIX 10..12
FT /evidence="ECO:0007829|PDB:1IMT"
FT STRAND 17..21
FT /evidence="ECO:0007829|PDB:1IMT"
FT STRAND 29..33
FT /evidence="ECO:0007829|PDB:1IMT"
FT STRAND 66..71
FT /evidence="ECO:0007829|PDB:1IMT"
FT STRAND 74..78
FT /evidence="ECO:0007829|PDB:1IMT"
SQ SEQUENCE 81 AA; 8604 MW; 5F6B703434338B03 CRC64;
AVITGACERD LQCGKGTCCA VSLWIKSVRV CTPVGTSGED CHPASHKIPF SGQRMHHTCP
CAPNLACVQT SPKKFKCLSK S
