RNAS4_PONAB
ID RNAS4_PONAB Reviewed; 147 AA.
AC Q5NVS4;
DT 24-JAN-2006, integrated into UniProtKB/Swiss-Prot.
DT 04-JAN-2005, sequence version 1.
DT 03-AUG-2022, entry version 84.
DE RecName: Full=Ribonuclease 4;
DE Short=RNase 4;
DE EC=3.1.27.-;
DE Flags: Precursor;
GN Name=RNASE4;
OS Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Pongo.
OX NCBI_TaxID=9601;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Liver;
RG The German cDNA consortium;
RL Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: This RNase has marked specificity towards the 3' side of
CC uridine nucleotides. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the pancreatic ribonuclease family.
CC {ECO:0000305}.
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DR EMBL; CR925928; CAI29589.1; -; mRNA.
DR RefSeq; NP_001127675.1; NM_001134203.2.
DR RefSeq; XP_009247114.1; XM_009248839.1.
DR AlphaFoldDB; Q5NVS4; -.
DR SMR; Q5NVS4; -.
DR STRING; 9601.ENSPPYP00000006341; -.
DR Ensembl; ENSPPYT00000006595; ENSPPYP00000006341; ENSPPYG00000005573.
DR GeneID; 100174757; -.
DR KEGG; pon:100174757; -.
DR CTD; 6038; -.
DR eggNOG; ENOG502S9Q1; Eukaryota.
DR GeneTree; ENSGT00940000157645; -.
DR HOGENOM; CLU_117006_3_1_1; -.
DR InParanoid; Q5NVS4; -.
DR OMA; VPNCRYR; -.
DR TreeFam; TF333393; -.
DR Proteomes; UP000001595; Chromosome 14.
DR GO; GO:0005615; C:extracellular space; IEA:Ensembl.
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; IEA:Ensembl.
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 2: Evidence at transcript level;
KW Disulfide bond; Endonuclease; Hydrolase; Nuclease;
KW Pyrrolidone carboxylic acid; Reference proteome; Secreted; Signal.
FT SIGNAL 1..28
FT /evidence="ECO:0000250"
FT CHAIN 29..147
FT /note="Ribonuclease 4"
FT /id="PRO_0000045837"
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"
SQ SEQUENCE 147 AA; 16855 MW; 699DFDC11FD515A2 CRC64;
MALQRTHSLL LLLLLTLLGL GLVQPSYGQD GMYQRFLRQH VHPEETGGND RYCNLMMQRR
KMTLYHCKRF NTFIHEDIWN IRSICSTTNI QCKNGKTNCH EGVVKVTDCR DTGSSRAPNC
RYRAMASTRR VVIACEGNPQ VPVHFDG