RNAS4_PIG
ID RNAS4_PIG Reviewed; 147 AA.
AC P15468;
DT 01-APR-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1996, sequence version 3.
DT 03-AUG-2022, entry version 122.
DE RecName: Full=Ribonuclease 4;
DE Short=RNase 4;
DE EC=3.1.27.-;
DE AltName: Full=Ribonuclease PL3;
DE Flags: Precursor;
GN Name=RNASE4; Synonyms=RNS4;
OS Sus scrofa (Pig).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX NCBI_TaxID=9823;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=8019417; DOI=10.1002/pro.5560030311;
RA Vicentini A.M., Hemmings B.A., Hofsteenge J.;
RT "Residues 36-42 of liver RNase PL3 contribute to its uridine-preferring
RT substrate specificity. Cloning of the cDNA and site-directed mutagenesis
RT studies.";
RL Protein Sci. 3:459-466(1994).
RN [2]
RP PROTEIN SEQUENCE OF 29-147.
RC TISSUE=Liver;
RX PubMed=2611266; DOI=10.1021/bi00451a040;
RA Hofsteenge J., Matthies R., Stone S.R.;
RT "Primary structure of a ribonuclease from porcine liver, a new member of
RT the ribonuclease superfamily.";
RL Biochemistry 28:9806-9813(1989).
CC -!- FUNCTION: This RNase has marked specificity towards the 3' side of
CC uridine nucleotides.
CC -!- SUBCELLULAR LOCATION: Secreted.
CC -!- SIMILARITY: Belongs to the pancreatic ribonuclease family.
CC {ECO:0000305}.
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DR EMBL; S73478; AAB31159.1; -; mRNA.
DR PIR; A53180; A53180.
DR RefSeq; NP_999101.1; NM_213936.2.
DR PDB; 5AR6; X-ray; 1.25 A; A=29-147.
DR PDB; 5ARJ; X-ray; 2.90 A; A/B/C/D=29-147.
DR PDB; 5ARK; X-ray; 2.28 A; A/B/C/D=29-147.
DR PDB; 5ARL; X-ray; 2.61 A; A/B/C/D=29-147.
DR PDBsum; 5AR6; -.
DR PDBsum; 5ARJ; -.
DR PDBsum; 5ARK; -.
DR PDBsum; 5ARL; -.
DR AlphaFoldDB; P15468; -.
DR SMR; P15468; -.
DR STRING; 9823.ENSSSCP00000022277; -.
DR PaxDb; P15468; -.
DR PeptideAtlas; P15468; -.
DR PRIDE; P15468; -.
DR Ensembl; ENSSSCT00005035802; ENSSSCP00005021808; ENSSSCG00005022658.
DR Ensembl; ENSSSCT00005035824; ENSSSCP00005021828; ENSSSCG00005022658.
DR Ensembl; ENSSSCT00005035830; ENSSSCP00005021832; ENSSSCG00005022658.
DR Ensembl; ENSSSCT00005035911; ENSSSCP00005021880; ENSSSCG00005022658.
DR Ensembl; ENSSSCT00015110783; ENSSSCP00015047406; ENSSSCG00015081231.
DR Ensembl; ENSSSCT00015110784; ENSSSCP00015047407; ENSSSCG00015081231.
DR Ensembl; ENSSSCT00015110785; ENSSSCP00015047408; ENSSSCG00015081231.
DR Ensembl; ENSSSCT00015110787; ENSSSCP00015047410; ENSSSCG00015081231.
DR Ensembl; ENSSSCT00025006398; ENSSSCP00025002649; ENSSSCG00025004731.
DR Ensembl; ENSSSCT00025006399; ENSSSCP00025002650; ENSSSCG00025004731.
DR Ensembl; ENSSSCT00025006400; ENSSSCP00025002651; ENSSSCG00025004731.
DR Ensembl; ENSSSCT00025006404; ENSSSCP00025002655; ENSSSCG00025004731.
DR Ensembl; ENSSSCT00030057885; ENSSSCP00030026351; ENSSSCG00030041623.
DR Ensembl; ENSSSCT00030057889; ENSSSCP00030026353; ENSSSCG00030041623.
DR Ensembl; ENSSSCT00030057915; ENSSSCP00030026368; ENSSSCG00030041623.
DR Ensembl; ENSSSCT00030057932; ENSSSCP00030026377; ENSSSCG00030041623.
DR Ensembl; ENSSSCT00035001107; ENSSSCP00035000302; ENSSSCG00035000933.
DR Ensembl; ENSSSCT00035001111; ENSSSCP00035000303; ENSSSCG00035000933.
DR Ensembl; ENSSSCT00035001112; ENSSSCP00035000304; ENSSSCG00035000933.
DR Ensembl; ENSSSCT00035001122; ENSSSCP00035000307; ENSSSCG00035000933.
DR Ensembl; ENSSSCT00040023502; ENSSSCP00040009924; ENSSSCG00040017428.
DR Ensembl; ENSSSCT00040023524; ENSSSCP00040009934; ENSSSCG00040017428.
DR Ensembl; ENSSSCT00040023535; ENSSSCP00040009938; ENSSSCG00040017428.
DR Ensembl; ENSSSCT00040023599; ENSSSCP00040009971; ENSSSCG00040017428.
DR Ensembl; ENSSSCT00050004490; ENSSSCP00050001779; ENSSSCG00050003361.
DR Ensembl; ENSSSCT00050004495; ENSSSCP00050001782; ENSSSCG00050003361.
DR Ensembl; ENSSSCT00050004519; ENSSSCP00050001795; ENSSSCG00050003361.
DR Ensembl; ENSSSCT00050004539; ENSSSCP00050001806; ENSSSCG00050003361.
DR Ensembl; ENSSSCT00055031343; ENSSSCP00055024955; ENSSSCG00055015921.
DR Ensembl; ENSSSCT00055031368; ENSSSCP00055024972; ENSSSCG00055015921.
DR Ensembl; ENSSSCT00055031376; ENSSSCP00055024979; ENSSSCG00055015921.
DR Ensembl; ENSSSCT00055031463; ENSSSCP00055025052; ENSSSCG00055015921.
DR Ensembl; ENSSSCT00060036938; ENSSSCP00060015718; ENSSSCG00060027285.
DR Ensembl; ENSSSCT00060036949; ENSSSCP00060015725; ENSSSCG00060027285.
DR Ensembl; ENSSSCT00060036953; ENSSSCP00060015727; ENSSSCG00060027285.
DR Ensembl; ENSSSCT00060036973; ENSSSCP00060015737; ENSSSCG00060027285.
DR Ensembl; ENSSSCT00065081779; ENSSSCP00065035614; ENSSSCG00065059715.
DR Ensembl; ENSSSCT00065081787; ENSSSCP00065035620; ENSSSCG00065059715.
DR Ensembl; ENSSSCT00065081792; ENSSSCP00065035624; ENSSSCG00065059715.
DR Ensembl; ENSSSCT00065081809; ENSSSCP00065035632; ENSSSCG00065059715.
DR GeneID; 396976; -.
DR KEGG; ssc:396976; -.
DR CTD; 6038; -.
DR eggNOG; ENOG502S9Q1; Eukaryota.
DR InParanoid; P15468; -.
DR OrthoDB; 1549558at2759; -.
DR Proteomes; UP000008227; Unplaced.
DR Proteomes; UP000314985; Unplaced.
DR GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR GO; GO:0004519; F:endonuclease activity; IEA:UniProtKB-KW.
DR GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR GO; GO:0004540; F:ribonuclease activity; IBA:GO_Central.
DR GO; GO:0050830; P:defense response to Gram-positive bacterium; IBA:GO_Central.
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; Nuclease; Pyrrolidone carboxylic acid; Reference proteome;
KW Secreted; Signal.
FT SIGNAL 1..28
FT /evidence="ECO:0000269|PubMed:2611266"
FT CHAIN 29..147
FT /note="Ribonuclease 4"
FT /id="PRO_0000030886"
FT ACT_SITE 40
FT /note="Proton acceptor"
FT /evidence="ECO:0000250"
FT ACT_SITE 144
FT /note="Proton donor"
FT /evidence="ECO:0000250"
FT BINDING 38
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 68..72
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 93
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 110
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT MOD_RES 29
FT /note="Pyrrolidone carboxylic acid"
FT /evidence="ECO:0000250|UniProtKB:P15467"
FT DISULFID 53..109
FT /evidence="ECO:0000250|UniProtKB:P34096"
FT DISULFID 67..120
FT /evidence="ECO:0000250|UniProtKB:P34096"
FT DISULFID 85..135
FT /evidence="ECO:0000250|UniProtKB:P34096"
FT DISULFID 92..99
FT /evidence="ECO:0000250|UniProtKB:P34096"
FT HELIX 29..40
FT /evidence="ECO:0007829|PDB:5AR6"
FT HELIX 50..59
FT /evidence="ECO:0007829|PDB:5AR6"
FT STRAND 62..66
FT /evidence="ECO:0007829|PDB:5AR6"
FT STRAND 69..74
FT /evidence="ECO:0007829|PDB:5AR6"
FT HELIX 78..84
FT /evidence="ECO:0007829|PDB:5AR6"
FT STRAND 95..97
FT /evidence="ECO:0007829|PDB:5ARJ"
FT STRAND 99..111
FT /evidence="ECO:0007829|PDB:5AR6"
FT STRAND 117..119
FT /evidence="ECO:0007829|PDB:5ARL"
FT STRAND 122..136
FT /evidence="ECO:0007829|PDB:5AR6"
FT TURN 137..140
FT /evidence="ECO:0007829|PDB:5AR6"
FT STRAND 141..145
FT /evidence="ECO:0007829|PDB:5AR6"
SQ SEQUENCE 147 AA; 16863 MW; B2626C2984237BC5 CRC64;
MALQRTHVLL LLLLLTLLGL GLVQPSYGQD RMYQRFLRQH VDPDATGGND AYCNLMMQRR
KMTSHYCKRF NTFIHEDIWN IRSICSTSNI QCKNGQMNCH EGVVKVTDCR ETGSSRAPNC
RYRAMASTRR VVIACEGNPE VPVHFDK
