RNAS4_PANTR
ID RNAS4_PANTR Reviewed; 147 AA.
AC Q8HZQ0;
DT 21-NOV-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 115.
DE RecName: Full=Ribonuclease 4;
DE Short=RNase 4;
DE EC=3.1.27.-;
DE Flags: Precursor;
GN Name=RNASE4; Synonyms=RNS4;
OS Pan troglodytes (Chimpanzee).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Pan.
OX NCBI_TaxID=9598;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=12524352; DOI=10.1093/genetics/162.4.1825;
RA Zhang J., Webb D.M., Podlaha O.;
RT "Accelerated protein evolution and origins of human-specific features:
RT Foxp2 as an example.";
RL Genetics 162:1825-1835(2002).
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AF539548; AAN10132.1; -; Genomic_DNA.
DR RefSeq; NP_001009107.1; NM_001009107.1.
DR RefSeq; XP_009425635.1; XM_009427360.2.
DR RefSeq; XP_009425636.1; XM_009427361.2.
DR RefSeq; XP_009425637.1; XM_009427362.2.
DR AlphaFoldDB; Q8HZQ0; -.
DR SMR; Q8HZQ0; -.
DR STRING; 9598.ENSPTRP00000054975; -.
DR PaxDb; Q8HZQ0; -.
DR Ensembl; ENSPTRT00000088422; ENSPTRP00000087897; ENSPTRG00000044163.
DR GeneID; 465205; -.
DR KEGG; ptr:465205; -.
DR CTD; 6038; -.
DR VGNC; VGNC:6797; RNASE4.
DR eggNOG; ENOG502S9Q1; Eukaryota.
DR GeneTree; ENSGT00940000157645; -.
DR HOGENOM; CLU_117006_3_1_1; -.
DR InParanoid; Q8HZQ0; -.
DR OMA; VPNCRYR; -.
DR TreeFam; TF333393; -.
DR Proteomes; UP000002277; Chromosome 14.
DR Bgee; ENSPTRG00000044163; Expressed in liver and 21 other tissues.
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 3: Inferred from homology;
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_0000030884"
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; 16859 MW; F824FEA249F3EB42 CRC64;
MALQRTHSLL LLLLLTLLGL GLVQPSYGQD GMYQRFLRQH VHPEETGGSD RYCNLMMQRR
KMTLYHCKRF NTFIHEDIWN IRSICSTTNI QCKNGKMNCH EGVVKVTDCR DTGSSRAPNC
RYRAMASTRR VVIACEGNPQ VPVHFDG
