ID   AMPS3_LITPI             Reviewed;         114 AA.
AC   P85074;
DT   12-JUN-2007, integrated into UniProtKB/Swiss-Prot.
DT   12-JUN-2007, sequence version 1.
DT   03-AUG-2022, entry version 46.
DE   RecName: Full=Amphinase-3;
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=13993; Mass_error=1; Method=Electrospray;
CC       Note=Major (most represented) glycoform 1.;
CC       Evidence={ECO:0000269|PubMed:17560606};
CC   -!- MASS SPECTROMETRY: Mass=14358; Mass_error=1; Method=Electrospray;
CC       Note=Minor glycoform 2.; Evidence={ECO:0000269|PubMed:17560606};
CC   -!- MASS SPECTROMETRY: Mass=14155; Mass_error=1; Method=Electrospray;
CC       Note=Minor glycoform 3.; Evidence={ECO:0000269|PubMed:17560606};
CC   -!- MASS SPECTROMETRY: Mass=14520; Mass_error=1; Method=Electrospray;
CC       Note=Minor glycoform 4.; Evidence={ECO:0000269|PubMed:17560606};
CC   -!- MASS SPECTROMETRY: Mass=13790; Mass_error=1; Method=Electrospray;
CC       Note=Minor glycoform 5.; Evidence={ECO:0000269|PubMed:17560606};
CC   -!- SIMILARITY: Belongs to the pancreatic ribonuclease family.
CC       {ECO:0000255}.
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DR   AlphaFoldDB; P85074; -.
DR   SMR; P85074; -.
DR   PRIDE; P85074; -.
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-3"
FT                   /id="PRO_0000291309"
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        25
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;  13066 MW;  7391969850820409 CRC64;
     KPKEDKEWEK FKVKHITSQS VADFNCTSTM NNPDFTPDGQ CKPINTFIHS NTGPVKEICR
     RASGRVNKSS TQQFPLTTCK NPKRCKYSQS NETNYICITC RDNYPVHFVK IGKC