ID   AMPS2_LITPI             Reviewed;         114 AA.
AC   P85073;
DT   12-JUN-2007, integrated into UniProtKB/Swiss-Prot.
DT   12-JUN-2007, sequence version 1.
DT   03-AUG-2022, entry version 50.
DE   RecName: Full=Amphinase-2;
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, X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS), FUNCTION, SUBUNIT,
RP   MASS SPECTROMETRY, GLYCOSYLATION AT ASN-27, AND DISULFIDE BONDS.
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. Hydrolyzes 18S and 28S
CC       ribosomal RNA. More active towards rCA than rUA or rUG. Has cytotoxic
CC       activity against cultured human submaxillary gland carcinoma cells.
CC       {ECO:0000269|PubMed:17560606}.
CC   -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:17560606}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305}.
CC   -!- PTM: There are at least four different forms arising from glycan
CC       heterogeneity. {ECO:0000269|PubMed:17560606}.
CC   -!- MASS SPECTROMETRY: Mass=14012; Mass_error=1; Method=Electrospray;
CC       Note=Major (most represented) glycoform 1.;
CC       Evidence={ECO:0000269|PubMed:17560606};
CC   -!- MASS SPECTROMETRY: Mass=14378; Mass_error=1; Method=Electrospray;
CC       Note=Major (second-most represented) glycoform 2.;
CC       Evidence={ECO:0000269|PubMed:17560606};
CC   -!- MASS SPECTROMETRY: Mass=13809; Mass_error=1; Method=Electrospray;
CC       Note=Minor glycoform 3.; Evidence={ECO:0000269|PubMed:17560606};
CC   -!- MASS SPECTROMETRY: Mass=14539; Mass_error=1; Method=Electrospray;
CC       Note=Minor glycoform 4.; Evidence={ECO:0000269|PubMed:17560606};
CC   -!- SIMILARITY: Belongs to the pancreatic ribonuclease family.
CC       {ECO:0000255}.
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DR   PDB; 2P6Z; X-ray; 1.93 A; A/B=1-114.
DR   PDB; 2P7S; X-ray; 1.80 A; A=1-114.
DR   PDBsum; 2P6Z; -.
DR   PDBsum; 2P7S; -.
DR   AlphaFoldDB; P85073; -.
DR   SMR; P85073; -.
DR   iPTMnet; P85073; -.
DR   EvolutionaryTrace; P85073; -.
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   3D-structure; Direct protein sequencing; Disulfide bond; Endonuclease;
KW   Glycoprotein; Hydrolase; Nuclease; Secreted.
FT   CHAIN           1..114
FT                   /note="Amphinase-2"
FT                   /id="PRO_0000291308"
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:0000269|PubMed:17560606"
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:0000269|PubMed:17560606"
FT   DISULFID        41..85
FT                   /evidence="ECO:0000269|PubMed:17560606"
FT   DISULFID        59..100
FT                   /evidence="ECO:0000269|PubMed:17560606"
FT   DISULFID        97..114
FT                   /evidence="ECO:0000269|PubMed:17560606"
FT   HELIX           6..15
FT                   /evidence="ECO:0007829|PDB:2P7S"
FT   TURN            21..23
FT                   /evidence="ECO:0007829|PDB:2P7S"
FT   HELIX           26..29
FT                   /evidence="ECO:0007829|PDB:2P7S"
FT   HELIX           33..35
FT                   /evidence="ECO:0007829|PDB:2P6Z"
FT   STRAND          45..50
FT                   /evidence="ECO:0007829|PDB:2P7S"
FT   HELIX           52..56
FT                   /evidence="ECO:0007829|PDB:2P7S"
FT   HELIX           57..59
FT                   /evidence="ECO:0007829|PDB:2P7S"
FT   STRAND          64..69
FT                   /evidence="ECO:0007829|PDB:2P7S"
FT   STRAND          74..83
FT                   /evidence="ECO:0007829|PDB:2P7S"
FT   STRAND          86..94
FT                   /evidence="ECO:0007829|PDB:2P7S"
FT   STRAND          96..101
FT                   /evidence="ECO:0007829|PDB:2P7S"
FT   STRAND          104..112
FT                   /evidence="ECO:0007829|PDB:2P7S"
SQ   SEQUENCE   114 AA;  13085 MW;  5D069CE0B3816A58 CRC64;
     KPKEDREWEK FKTKHITSQS VADFNCNRTM NDPAYTPDGQ CKPINTFIHS TTGPVKEICR
     RATGRVNKSS TQQFTLTTCK NPIRCKYSQS NTTNFICITC RDNYPVHFVK TGKC