ID   AMPS1_LITPI             Reviewed;         114 AA.
AC   P85072;
DT   12-JUN-2007, integrated into UniProtKB/Swiss-Prot.
DT   12-JUN-2007, sequence version 1.
DT   03-AUG-2022, entry version 43.
DE   RecName: Full=Amphinase-1;
DE            EC=3.1.27.-;
OS   Lithobates pipiens (Northern leopard frog) (Rana pipiens).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC   Batrachia; Anura; Neobatrachia; Ranoidea; Ranidae; Lithobates.
OX   NCBI_TaxID=8404;
RN   [1]
RP   PROTEIN SEQUENCE, FUNCTION, SUBUNIT, AND MASS SPECTROMETRY.
RC   TISSUE=Oocyte;
RX   PubMed=17560606; DOI=10.1016/j.jmb.2007.04.071;
RA   Singh U.P., Ardelt W., Saxena S.K., Holloway D.E., Vidunas E., Lee H.-S.,
RA   Saxena A., Shogen K., Acharya K.R.;
RT   "Enzymatic and structural characterisation of amphinase, a novel cytotoxic
RT   ribonuclease from Rana pipiens oocytes.";
RL   J. Mol. Biol. 371:93-111(2007).
CC   -!- FUNCTION: Endonuclease, hydrolyzes highly polymerized RNA, poly(U) and
CC       poly(C), and the dinucleotides CpA and UpA. More active towards rCA
CC       than rUA or rUG. Has cytotoxic activity against cultured human
CC       submaxillary gland carcinoma cells. {ECO:0000269|PubMed:17560606}.
CC   -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:17560606}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305}.
CC   -!- PTM: There are at least five different forms arising from glycan
CC       heterogeneity. {ECO:0000269|PubMed:17560606}.
CC   -!- MASS SPECTROMETRY: Mass=14932; Mass_error=1; Method=Electrospray;
CC       Note=Major (most represented) glycoform 1.;
CC       Evidence={ECO:0000269|PubMed:17560606};
CC   -!- MASS SPECTROMETRY: Mass=14729; Mass_error=1; Method=Electrospray;
CC       Note=Major (second-most represented) glycoform 2.;
CC       Evidence={ECO:0000269|PubMed:17560606};
CC   -!- MASS SPECTROMETRY: Mass=15298; Mass_error=1; Method=Electrospray;
CC       Note=Minor glycoform 3.; Evidence={ECO:0000269|PubMed:17560606};
CC   -!- MASS SPECTROMETRY: Mass=14568; Mass_error=1; Method=Electrospray;
CC       Note=Minor glycoform 4.; Evidence={ECO:0000269|PubMed:17560606};
CC   -!- MASS SPECTROMETRY: Mass=15095; Mass_error=1; Method=Electrospray;
CC       Note=Minor (least represented) glycoform 5.;
CC       Evidence={ECO:0000269|PubMed:17560606};
CC   -!- SIMILARITY: Belongs to the pancreatic ribonuclease family.
CC       {ECO:0000255}.
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DR   AlphaFoldDB; P85072; -.
DR   SMR; P85072; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0004519; F:endonuclease activity; IEA:UniProtKB-KW.
DR   GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR   Gene3D; 3.10.130.10; -; 1.
DR   InterPro; IPR001427; RNaseA.
DR   InterPro; IPR036816; RNaseA-like_dom_sf.
DR   InterPro; IPR023411; RNaseA_AS.
DR   InterPro; IPR023412; RNaseA_domain.
DR   PANTHER; PTHR11437; PTHR11437; 1.
DR   Pfam; PF00074; RnaseA; 1.
DR   SMART; SM00092; RNAse_Pc; 1.
DR   SUPFAM; SSF54076; SSF54076; 1.
DR   PROSITE; PS00127; RNASE_PANCREATIC; 1.
PE   1: Evidence at protein level;
KW   Direct protein sequencing; Disulfide bond; Endonuclease; Glycoprotein;
KW   Hydrolase; Nuclease; Secreted.
FT   CHAIN           1..114
FT                   /note="Amphinase-1"
FT                   /id="PRO_0000291307"
FT   ACT_SITE        15
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000250|UniProtKB:P11916"
FT   ACT_SITE        107
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250|UniProtKB:P11916"
FT   BINDING         42..46
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:P11916"
FT   CARBOHYD        27
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        67
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        91
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        26..79
FT                   /evidence="ECO:0000250|UniProtKB:P11916"
FT   DISULFID        41..85
FT                   /evidence="ECO:0000250|UniProtKB:P11916"
FT   DISULFID        59..100
FT                   /evidence="ECO:0000250|UniProtKB:P11916"
FT   DISULFID        97..114
FT                   /evidence="ECO:0000250|UniProtKB:P11916"
SQ   SEQUENCE   114 AA;  13071 MW;  9E1E2743B38178DA CRC64;
     KPKEDREWEK FKTKHITSQS VADFNCNRTM NDPAYTPDGQ CKPVNTFIHS TTGPVKEICR
     RATGRVNKSS TQQFTLTTCK NPIRCKYSQS NTTNFICITC RDNYPVHFVK TGKC