RANSP_LEPVA
ID RANSP_LEPVA Reviewed; 217 AA.
AC P85507;
DT 25-NOV-2008, integrated into UniProtKB/Swiss-Prot.
DT 10-OCT-2018, sequence version 3.
DT 25-MAY-2022, entry version 20.
DE RecName: Full=Ranaspumin {ECO:0000303|PubMed:18689424};
DE AltName: Full=Lv-RSN-1 {ECO:0000303|PubMed:24442854};
OS Leptodactylus vastus (Northeastern pepper frog).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Neobatrachia; Hyloidea; Leptodactylidae; Leptodactylinae;
OC Leptodactylus.
OX NCBI_TaxID=326589;
RN [1]
RP PROTEIN SEQUENCE, X-RAY CRYSTALLOGRAPHY (1.60 ANGSTROMS), FUNCTION, SUUNIT,
RP SUBCELLULAR LOCATION, DISULFIDE BONDS, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RC TISSUE=Foam nest {ECO:0000303|PubMed:24442854};
RX PubMed=24442854; DOI=10.1002/cbic.201300726;
RA Cavalcante Hissa D., Arruda Bezerra G., Birner-Gruenberger R.,
RA Paulino Silva L., Uson I., Gruber K., Maciel Melo V.M.;
RT "Unique crystal structure of a novel surfactant protein from the foam nest
RT of the frog Leptodactylus vastus.";
RL ChemBioChem 15:393-398(2014).
RN [2] {ECO:0000305}
RP PROTEIN SEQUENCE OF 1-25, FUNCTION, SUBUNIT, AND SUBCELLULAR LOCATION.
RC TISSUE=Foam nest {ECO:0000269|PubMed:18689424};
RX PubMed=18689424; DOI=10.1242/jeb.019315;
RA Hissa D.C., Vasconcelos I.M., Carvalho A.F.U., Nogueira V.L.R., Cascon P.,
RA Antunes A.S.L., de Macedo G.R., Melo V.M.M.;
RT "Novel surfactant proteins are involved in the structure and stability of
RT foam nests from the frog Leptodactylus vastus.";
RL J. Exp. Biol. 211:2707-2711(2008).
RN [3]
RP FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, SUBCELLULAR LOCATION,
RP IDENTIFICATION BY MASS SPECTROMETRY, AND TISSUE SPECIFICITY.
RC TISSUE=Foam nest {ECO:0000303|PubMed:27460953};
RX PubMed=27460953; DOI=10.1002/jez.2027;
RA Hissa D.C., Bezerra W.M., Freitas C.D., Ramos M.V., Lopes J.L.,
RA Beltramini L.M., Roberto I.J., Cascon P., Melo V.M.;
RT "Frog Foam Nest Protein Diversity and Synthesis.";
RL J. Exp. Zool. Part A Ecol. Genet. Physiol. 325:425-433(2016).
CC -!- FUNCTION: Acts as a surfactant (PubMed:24442854, PubMed:18689424). Is
CC the major protein constituent (45%) of foam nests (PubMed:27460953).
CC Has no antimicrobial activity, no larvicidal activity, and is not toxic
CC to mice (PubMed:18689424). {ECO:0000269|PubMed:18689424,
CC ECO:0000269|PubMed:24442854, ECO:0000269|PubMed:27460953}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Temperature dependence:
CC Stable between 25 and 95 degrees Celsius.
CC {ECO:0000269|PubMed:27460953};
CC -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:18689424,
CC ECO:0000269|PubMed:24442854}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:18689424,
CC ECO:0000269|PubMed:24442854, ECO:0000269|PubMed:27460953}.
CC -!- TISSUE SPECIFICITY: Exclusively expressed in females in the early
CC oviduct, the glandular part of the oviduct (pars convoluta dilata) and
CC in the cloaca. {ECO:0000269|PubMed:27460953}.
CC -!- MISCELLANEOUS: Mass spectrometry data suggest sequence
CC microheterogeneity hinting at the existence of several isoforms.
CC {ECO:0000305|PubMed:27460953}.
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DR PDB; 4K82; X-ray; 1.60 A; A=1-217.
DR PDB; 4K83; X-ray; 1.75 A; A=1-217.
DR PDBsum; 4K82; -.
DR PDBsum; 4K83; -.
DR AlphaFoldDB; P85507; -.
DR SMR; P85507; -.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
PE 1: Evidence at protein level;
KW 3D-structure; Direct protein sequencing; Disulfide bond; Secreted.
FT CHAIN 1..217
FT /note="Ranaspumin"
FT /evidence="ECO:0000269|PubMed:24442854"
FT /id="PRO_0000445589"
FT DISULFID 18..67
FT /evidence="ECO:0000269|PubMed:24442854,
FT ECO:0007744|PDB:4K82"
FT DISULFID 38..114
FT /evidence="ECO:0000269|PubMed:24442854,
FT ECO:0007744|PDB:4K82"
FT DISULFID 125..168
FT /evidence="ECO:0000269|PubMed:24442854,
FT ECO:0007744|PDB:4K82"
FT DISULFID 146..207
FT /evidence="ECO:0000269|PubMed:24442854,
FT ECO:0007744|PDB:4K82"
FT UNSURE 42
FT /note="N or D"
FT /evidence="ECO:0000303|PubMed:24442854"
FT UNSURE 120
FT /note="M or T"
FT /evidence="ECO:0000303|PubMed:24442854"
FT UNSURE 123
FT /note="N or Q"
FT /evidence="ECO:0000303|PubMed:24442854"
FT HELIX 14..24
FT /evidence="ECO:0007829|PDB:4K82"
FT STRAND 25..28
FT /evidence="ECO:0007829|PDB:4K82"
FT HELIX 29..42
FT /evidence="ECO:0007829|PDB:4K82"
FT HELIX 48..64
FT /evidence="ECO:0007829|PDB:4K82"
FT HELIX 69..76
FT /evidence="ECO:0007829|PDB:4K82"
FT TURN 77..79
FT /evidence="ECO:0007829|PDB:4K82"
FT STRAND 84..86
FT /evidence="ECO:0007829|PDB:4K82"
FT HELIX 89..102
FT /evidence="ECO:0007829|PDB:4K82"
FT HELIX 107..121
FT /evidence="ECO:0007829|PDB:4K82"
FT TURN 122..124
FT /evidence="ECO:0007829|PDB:4K82"
FT HELIX 126..129
FT /evidence="ECO:0007829|PDB:4K82"
FT TURN 130..132
FT /evidence="ECO:0007829|PDB:4K82"
FT HELIX 133..144
FT /evidence="ECO:0007829|PDB:4K82"
FT HELIX 152..165
FT /evidence="ECO:0007829|PDB:4K82"
FT HELIX 167..170
FT /evidence="ECO:0007829|PDB:4K82"
FT HELIX 175..180
FT /evidence="ECO:0007829|PDB:4K82"
FT STRAND 182..185
FT /evidence="ECO:0007829|PDB:4K82"
FT STRAND 188..191
FT /evidence="ECO:0007829|PDB:4K82"
FT HELIX 193..195
FT /evidence="ECO:0007829|PDB:4K82"
FT HELIX 196..204
FT /evidence="ECO:0007829|PDB:4K82"
FT HELIX 206..212
FT /evidence="ECO:0007829|PDB:4K82"
SQ SEQUENCE 217 AA; 23468 MW; 6D6F2F26F6C8EE4E CRC64;
LLEGFLVGGG VPGPGTACLT KALKDSGDLL VELAVIICAY QNGKDLQEQD FKELKELLER
TLERAGCALD DIVADLGLEE LLGSIGVSTG DIIQGLYKLL KELKIDETVF NAVCDVTKKM
LDNKCLPKIL QGDLVKFLKD LKYKVCIEGG DPELIIKDLK IILERLPCVL GGVGLDDLFK
NIFVKDGILS FEGIAKPLGD LLILVLCPNV KNINVSS
