MAXSB_BOMMX
ID MAXSB_BOMMX Reviewed; 305 AA.
AC Q5GC92; Q5GC93;
DT 07-JUN-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2005, sequence version 1.
DT 25-MAY-2022, entry version 34.
DE RecName: Full=Maximins-S type B/C;
DE Contains:
DE RecName: Full=Maximin-S1;
DE Contains:
DE RecName: Full=Maximin-S3;
DE Contains:
DE RecName: Full=Maximin-S5;
DE Contains:
DE RecName: Full=Maximin-S2;
DE Contains:
DE RecName: Full=Maximin-S4;
DE Flags: Precursor;
OS Bombina maxima (Giant fire-bellied toad) (Chinese red belly toad).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Bombinatoridae; Bombina.
OX NCBI_TaxID=161274;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], SYNTHESIS OF MAXIMIN-S1, SYNTHESIS OF
RP MAXIMIN-S4, AMIDATION AT ASN-83; ASN-118; LYS-153; ASN-188; ASN-223;
RP ASN-258 AND LYS-293, AND MASS SPECTROMETRY.
RC TISSUE=Skin, and Skin secretion;
RX PubMed=15649437; DOI=10.1016/j.bbrc.2004.12.094;
RA Wang T., Zhang J., Shen J.-H., Jin Y., Lee W.-H., Zhang Y.;
RT "Maximins S, a novel group of antimicrobial peptides from toad Bombina
RT maxima.";
RL Biochem. Biophys. Res. Commun. 327:945-951(2005).
CC -!- FUNCTION: Maximin-S1 has no antimicrobial activity. Has no hemolytic
CC activity.
CC -!- FUNCTION: Maximin-S2 has an activity against mycoplasma but has no
CC activity against common Gram-positive and Gram-negative bacteria nor
CC fungi. Has no hemolytic activity (By similarity). {ECO:0000250}.
CC -!- FUNCTION: Maximin-S3 has an activity against mycoplasma but has no
CC activity against common Gram-positive and Gram-negative bacteria nor
CC fungi. Has no hemolytic activity (By similarity). {ECO:0000250}.
CC -!- FUNCTION: Maximin-S4 has an activity against mycoplasma but has no
CC activity against common Gram-positive and Gram-negative bacteria nor
CC fungi. Has no hemolytic activity.
CC -!- FUNCTION: Maximin-S5 has an activity against mycoplasma but has no
CC activity against common Gram-positive and Gram-negative bacteria nor
CC fungi. Has no hemolytic activity (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Secreted.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=B;
CC IsoId=Q5GC92-1; Sequence=Displayed;
CC Name=C;
CC IsoId=Q5GC92-2; Sequence=VSP_013916;
CC -!- TISSUE SPECIFICITY: Expressed by the skin dorsal glands.
CC -!- MASS SPECTROMETRY: [Maximin-S3]: Mass=1973.92; Method=MALDI;
CC Note=Maximin-S2.; Evidence={ECO:0000269|PubMed:15649437};
CC -!- MASS SPECTROMETRY: [Maximin-S3]: Mass=1959.22; Method=MALDI;
CC Note=Maximin-S3.; Evidence={ECO:0000269|PubMed:15649437};
CC -!- MASS SPECTROMETRY: [Maximin-S2]: Mass=2087.90; Method=MALDI;
CC Note=Maximin-S4.; Evidence={ECO:0000269|PubMed:15649437};
CC -!- MASS SPECTROMETRY: [Maximin-S3]: Mass=1987.08; Method=MALDI;
CC Note=Maximin-S5.; Evidence={ECO:0000269|PubMed:15649437};
CC -!- SIMILARITY: Belongs to the maximin-S family. {ECO:0000305}.
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DR EMBL; AY652773; AAV97981.1; -; mRNA.
DR EMBL; AY652772; AAV97980.1; -; mRNA.
DR AlphaFoldDB; Q5GC92; -.
DR SMR; Q5GC92; -.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0042742; P:defense response to bacterium; IEA:UniProtKB-KW.
PE 1: Evidence at protein level;
KW Alternative splicing; Amidation; Antibiotic; Antimicrobial;
KW Cleavage on pair of basic residues; Secreted; Signal.
FT SIGNAL 1..18
FT /evidence="ECO:0000255"
FT PROPEP 19..35
FT /id="PRO_0000010268"
FT PEPTIDE 36..49
FT /note="Maximin-S1"
FT /id="PRO_0000010269"
FT PROPEP 52..65
FT /id="PRO_0000010270"
FT PEPTIDE 66..83
FT /note="Maximin-S3"
FT /id="PRO_0000010271"
FT PROPEP 87..100
FT /id="PRO_0000010272"
FT PEPTIDE 101..118
FT /note="Maximin-S3"
FT /id="PRO_0000010273"
FT PROPEP 122..135
FT /id="PRO_0000010274"
FT PEPTIDE 136..153
FT /note="Maximin-S5"
FT /id="PRO_0000010275"
FT PROPEP 157..170
FT /id="PRO_0000010276"
FT PEPTIDE 171..188
FT /note="Maximin-S2"
FT /id="PRO_0000010277"
FT PROPEP 192..205
FT /id="PRO_0000010278"
FT PEPTIDE 206..223
FT /note="Maximin-S3"
FT /id="PRO_0000010279"
FT PROPEP 227..240
FT /id="PRO_0000010280"
FT PEPTIDE 241..258
FT /note="Maximin-S3"
FT /id="PRO_0000010281"
FT PROPEP 262..275
FT /id="PRO_0000010282"
FT PEPTIDE 276..293
FT /note="Maximin-S4"
FT /id="PRO_0000010283"
FT PROPEP 297..305
FT /id="PRO_0000010284"
FT MOD_RES 83
FT /note="Asparagine amide"
FT /evidence="ECO:0000269|PubMed:15649437"
FT MOD_RES 118
FT /note="Asparagine amide"
FT /evidence="ECO:0000269|PubMed:15649437"
FT MOD_RES 153
FT /note="Lysine amide"
FT /evidence="ECO:0000269|PubMed:15649437"
FT MOD_RES 188
FT /note="Asparagine amide"
FT /evidence="ECO:0000269|PubMed:15649437"
FT MOD_RES 223
FT /note="Asparagine amide"
FT /evidence="ECO:0000269|PubMed:15649437"
FT MOD_RES 258
FT /note="Asparagine amide"
FT /evidence="ECO:0000269|PubMed:15649437"
FT MOD_RES 293
FT /note="Lysine amide"
FT /evidence="ECO:0000269|PubMed:15649437"
FT VAR_SEQ 127..266
FT /note="Missing (in isoform C)"
FT /evidence="ECO:0000305"
FT /id="VSP_013916"
SQ SEQUENCE 305 AA; 34225 MW; 06DB61968E73BF38 CRC64;
MNFNYFILVL FFITSGHAKS ETREVHQEAE NHIKRGSNTG FNFKTLDKEK RSAEEQNLAE
HLVTRGSNKG FNFMVDMINA LSNGKRSAEE QDLAEHLVTR GSNKGFNFMV DMINALSNGK
RSAEEQDLAE DLVTRGSNKG FNFMVDMIQA LSKGKRSAED QDLAEDLVTR GSNKGFNFMV
DMIQALSNGK RSAEEQDLAE HLVTRGSNKG FNFMVDMINA LSNGKRSAEE QDLSEDLVTR
GSNKGFNFMV DMINALSNGK RSAEEQDLVE DLVTRRSNKG FNFMVDMIQA LSKGKRSAEQ
EKDMK
