RNAS1_CHEMY
ID RNAS1_CHEMY Reviewed; 119 AA.
AC P84844;
DT 16-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT 16-MAY-2006, sequence version 1.
DT 03-AUG-2022, entry version 62.
DE RecName: Full=Ribonuclease;
DE EC=4.6.1.18 {ECO:0000250|UniProtKB:P07998};
OS Chelonia mydas (Green sea-turtle) (Chelonia agassizi).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Testudinata; Testudines; Cryptodira; Durocryptodira;
OC Americhelydia; Chelonioidea; Cheloniidae; Chelonia.
OX NCBI_TaxID=8469;
RN [1]
RP PROTEIN SEQUENCE, SUBCELLULAR LOCATION, MASS SPECTROMETRY, AND VARIANT
RP LEU-37.
RC TISSUE=Egg white;
RX PubMed=16947078; DOI=10.1007/s10930-006-9017-4;
RA Katekaew S., Torikata T., Araki T.;
RT "The complete amino acid sequence of green turtle (Chelonia mydas) egg
RT white ribonuclease.";
RL Protein J. 25:316-327(2006).
RN [2]
RP X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS), AND DISULFIDE BONDS.
RX PubMed=20606267; DOI=10.1107/s1744309110016751;
RA Katekaew S., Kuaprasert B., Torikata T., Kakuta Y., Kimura M., Yoneda K.,
RA Araki T.;
RT "Structure of the newly found green turtle egg-white ribonuclease.";
RL Acta Crystallogr. F 66:755-759(2010).
CC -!- FUNCTION: Endonuclease that catalyzes the cleavage of RNA on the 3'
CC side of pyrimidine nucleotides. Acts on single-stranded and double-
CC stranded RNA (By similarity). {ECO:0000250}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=an [RNA] containing cytidine + H2O = an [RNA]-3'-cytidine-3'-
CC phosphate + a 5'-hydroxy-ribonucleotide-3'-[RNA].; EC=4.6.1.18;
CC Evidence={ECO:0000250|UniProtKB:P07998};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=an [RNA] containing uridine + H2O = an [RNA]-3'-uridine-3'-
CC phosphate + a 5'-hydroxy-ribonucleotide-3'-[RNA].; EC=4.6.1.18;
CC Evidence={ECO:0000250|UniProtKB:P07998};
CC -!- SUBUNIT: Monomer. Interacts with and forms tight 1:1 complexes with
CC RNH1. Dimerization of two such complexes may occur. Interaction with
CC RNH1 inhibits this protein (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:16947078}.
CC -!- MASS SPECTROMETRY: Mass=12942.1; Method=MALDI;
CC Evidence={ECO:0000269|PubMed:16947078};
CC -!- MASS SPECTROMETRY: Mass=12967.8; Method=MALDI; Note=Variant Leu-37.;
CC Evidence={ECO:0000269|PubMed:16947078};
CC -!- SIMILARITY: Belongs to the pancreatic ribonuclease family.
CC {ECO:0000255}.
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DR PDB; 2ZPO; X-ray; 1.60 A; A=1-119.
DR PDBsum; 2ZPO; -.
DR AlphaFoldDB; P84844; -.
DR SMR; P84844; -.
DR STRING; 8469.XP_007067544.1; -.
DR eggNOG; ENOG502S9Q1; Eukaryota.
DR EvolutionaryTrace; P84844; -.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0016829; F:lyase activity; IEA:UniProtKB-KW.
DR GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR GO; GO:0004522; F:ribonuclease A activity; IEA:UniProtKB-EC.
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 PRINTS; PR00794; RIBONUCLEASE.
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 Hydrolase; Lyase; Nuclease; Secreted.
FT CHAIN 1..119
FT /note="Ribonuclease"
FT /id="PRO_0000234484"
FT ACT_SITE 11
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:P07998"
FT ACT_SITE 114
FT /note="Proton donor"
FT /evidence="ECO:0000250|UniProtKB:P07998"
FT BINDING 6
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 9
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 41..45
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P07998"
FT BINDING 82
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT DISULFID 26..81
FT /evidence="ECO:0000269|PubMed:20606267"
FT DISULFID 40..92
FT /evidence="ECO:0000269|PubMed:20606267"
FT DISULFID 58..107
FT /evidence="ECO:0000269|PubMed:20606267"
FT VARIANT 37
FT /note="S -> L"
FT /evidence="ECO:0000269|PubMed:16947078"
FT HELIX 3..11
FT /evidence="ECO:0007829|PDB:2ZPO"
FT HELIX 22..32
FT /evidence="ECO:0007829|PDB:2ZPO"
FT STRAND 36..39
FT /evidence="ECO:0007829|PDB:2ZPO"
FT STRAND 42..47
FT /evidence="ECO:0007829|PDB:2ZPO"
FT HELIX 51..55
FT /evidence="ECO:0007829|PDB:2ZPO"
FT HELIX 56..58
FT /evidence="ECO:0007829|PDB:2ZPO"
FT TURN 59..61
FT /evidence="ECO:0007829|PDB:2ZPO"
FT STRAND 62..64
FT /evidence="ECO:0007829|PDB:2ZPO"
FT STRAND 69..74
FT /evidence="ECO:0007829|PDB:2ZPO"
FT STRAND 76..86
FT /evidence="ECO:0007829|PDB:2ZPO"
FT STRAND 94..101
FT /evidence="ECO:0007829|PDB:2ZPO"
FT STRAND 103..108
FT /evidence="ECO:0007829|PDB:2ZPO"
FT STRAND 111..118
FT /evidence="ECO:0007829|PDB:2ZPO"
SQ SEQUENCE 119 AA; 12947 MW; 702C2F204A28056E CRC64;
ETRYEKFLRQ HVDYPRTAAP DTRTYCNQMM QRRGMTSPVC KFTNTFVHAS AASITTICGP
GGAPAGGNLR DSTASFALTT CRLQGGSQRP PCNYNGGTST QRIRIACDGG LPVHYDRAI
