ID   RNK_BOVIN               Reviewed;          98 AA.
AC   Q3ZC23;
DT   22-JUL-2008, integrated into UniProtKB/Swiss-Prot.
DT   27-SEP-2005, sequence version 1.
DT   03-AUG-2022, entry version 83.
DE   RecName: Full=Ribonuclease kappa;
DE            Short=RNase K;
DE            Short=RNase kappa;
DE            EC=3.1.-.- {ECO:0000250|UniProtKB:Q6P5S7};
DE   AltName: Full=V-type proton ATPase subunit f {ECO:0000303|PubMed:32764564};
DE            Short=V-ATPase subunit f {ECO:0000303|PubMed:32764564};
GN   Name=RNASEK;
OS   Bos taurus (Bovine).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC   Bovinae; Bos.
OX   NCBI_TaxID=9913;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=Crossbred X Angus; TISSUE=Ileum;
RG   NIH - Mammalian Gene Collection (MGC) project;
RL   Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0007744|PDB:6XBW}
RP   STRUCTURE BY ELECTRON MICROSCOPY (3.37 ANGSTROMS) IN COMPLEX WITH THE
RP   V-ATPASE, SUBCELLULAR LOCATION, IDENTIFICATION BY MASS SPECTROMETRY, AND
RP   TISSUE SPECIFICITY.
RX   PubMed=32764564; DOI=10.1038/s41467-020-17762-9;
RA   Wang R., Long T., Hassan A., Wang J., Sun Y., Xie X.S., Li X.;
RT   "Cryo-EM structures of intact V-ATPase from bovine brain.";
RL   Nat. Commun. 11:3921-3921(2020).
CC   -!- FUNCTION: Endoribonuclease which preferentially cleaves ApU and ApG
CC       phosphodiester bonds. Hydrolyzes UpU bonds at a lower rate (By
CC       similarity). Regulates the activity of vacuolar (H+)-ATPase (V-ATPase)
CC       which is responsible for acidifying and maintaining the pH of
CC       intracellular compartments (By similarity). Required at an early stage
CC       of receptor-mediated endocytosis (By similarity).
CC       {ECO:0000250|UniProtKB:Q6P5S7}.
CC   -!- SUBUNIT: Interacts with the proton translocation complex V0 of the V-
CC       ATPase (PubMed:32764564). Interacts with ATP6AP1 (By similarity).
CC       {ECO:0000250|UniProtKB:Q6P5S7, ECO:0000269|PubMed:32764564}.
CC   -!- SUBCELLULAR LOCATION: Endomembrane system
CC       {ECO:0000250|UniProtKB:Q6P5S7}; Multi-pass membrane protein
CC       {ECO:0000255}. Cytoplasmic vesicle, clathrin-coated vesicle membrane
CC       {ECO:0000269|PubMed:32764564}; Multi-pass membrane protein
CC       {ECO:0000255}.
CC   -!- TISSUE SPECIFICITY: Expressed in brain (at protein level).
CC       {ECO:0000269|PubMed:32764564}.
CC   -!- SIMILARITY: Belongs to the RNase K family. {ECO:0000305}.
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DR   EMBL; BC102969; AAI02970.1; -; mRNA.
DR   RefSeq; NP_001029601.1; NM_001034429.3.
DR   PDB; 6XBW; EM; 3.37 A; f=1-98.
DR   PDB; 7KHR; EM; 3.62 A; f=1-98.
DR   PDBsum; 6XBW; -.
DR   PDBsum; 7KHR; -.
DR   AlphaFoldDB; Q3ZC23; -.
DR   SMR; Q3ZC23; -.
DR   STRING; 9913.ENSBTAP00000029239; -.
DR   PaxDb; Q3ZC23; -.
DR   Ensembl; ENSBTAT00000029239; ENSBTAP00000029239; ENSBTAG00000021932.
DR   GeneID; 512886; -.
DR   KEGG; bta:512886; -.
DR   CTD; 440400; -.
DR   VEuPathDB; HostDB:ENSBTAG00000021932; -.
DR   VGNC; VGNC:34002; RNASEK.
DR   eggNOG; ENOG502S351; Eukaryota.
DR   GeneTree; ENSGT00390000009664; -.
DR   HOGENOM; CLU_140554_1_0_1; -.
DR   InParanoid; Q3ZC23; -.
DR   OMA; RQVGINC; -.
DR   OrthoDB; 1615928at2759; -.
DR   TreeFam; TF300182; -.
DR   Proteomes; UP000009136; Chromosome 19.
DR   Bgee; ENSBTAG00000021932; Expressed in neurohypophysis and 105 other tissues.
DR   GO; GO:0030665; C:clathrin-coated vesicle membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0012505; C:endomembrane system; IEA:UniProtKB-SubCell.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0000220; C:vacuolar proton-transporting V-type ATPase, V0 domain; IDA:UniProtKB.
DR   GO; GO:0004521; F:endoribonuclease activity; ISS:UniProtKB.
DR   GO; GO:0048388; P:endosomal lumen acidification; ISS:UniProtKB.
DR   GO; GO:0045851; P:pH reduction; IC:UniProtKB.
DR   GO; GO:1902600; P:proton transmembrane transport; ISS:UniProtKB.
DR   GO; GO:0006898; P:receptor-mediated endocytosis; ISS:UniProtKB.
DR   GO; GO:0019065; P:receptor-mediated endocytosis of virus by host cell; ISS:UniProtKB.
DR   InterPro; IPR026770; RNase_K.
DR   PANTHER; PTHR31733; PTHR31733; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Cytoplasmic vesicle; Endocytosis; Endonuclease;
KW   Hydrogen ion transport; Hydrolase; Ion transport; Membrane; Nuclease;
KW   Reference proteome; Transmembrane; Transmembrane helix; Transport.
FT   CHAIN           1..98
FT                   /note="Ribonuclease kappa"
FT                   /id="PRO_0000344220"
FT   TRANSMEM        13..33
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        65..85
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   HELIX           18..35
FT                   /evidence="ECO:0007829|PDB:6XBW"
FT   HELIX           65..75
FT                   /evidence="ECO:0007829|PDB:6XBW"
FT   TURN            76..80
FT                   /evidence="ECO:0007829|PDB:6XBW"
FT   HELIX           81..83
FT                   /evidence="ECO:0007829|PDB:6XBW"
SQ   SEQUENCE   98 AA;  11022 MW;  A3F2CE5CFDDB87EB CRC64;
     MASLLCCGPK LAACGIVLSA WGVIMLIMLG IFFNVHSAVL IEDVPFTEKD FENGPQNIYN
     LYEQVSYNCF IAASLYLLLG GFSFCQVRLN KRKEYMVR