RT35_BOVIN
ID RT35_BOVIN Reviewed; 325 AA.
AC Q2YDF6; P82672;
DT 07-FEB-2006, integrated into UniProtKB/Swiss-Prot.
DT 20-DEC-2005, sequence version 1.
DT 03-AUG-2022, entry version 91.
DE RecName: Full=28S ribosomal protein S35, mitochondrial;
DE Short=MRP-S35;
DE Short=S35mt;
DE AltName: Full=28S ribosomal protein S28, mitochondrial;
DE Short=MRP-S28;
DE Short=S28mt;
DE Flags: Precursor;
GN Name=MRPS35 {ECO:0000250|UniProtKB:P82673};
GN Synonyms=MRPS28 {ECO:0000303|PubMed:11344316};
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] {ECO:0000312|EMBL:AAI10246.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Crossbred X Angus {ECO:0000312|EMBL:AAI10246.1};
RC TISSUE=Liver {ECO:0000312|EMBL:AAI10246.1};
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (NOV-2005) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000305}
RP PROTEIN SEQUENCE OF 102-123; 128-144; 179-189 AND 265-272, SUBUNIT, AND
RP SUBCELLULAR LOCATION.
RC TISSUE=Liver;
RX PubMed=11344316; DOI=10.1110/ps.35301;
RA Koc E.C., Burkhart W., Blackburn K., Koc H., Moseley A., Spremulli L.L.;
RT "Identification of four proteins from the small subunit of the mammalian
RT mitochondrial ribosome using a proteomics approach.";
RL Protein Sci. 10:471-481(2001).
RN [3] {ECO:0007744|PDB:3JD5}
RP STRUCTURE BY ELECTRON MICROSCOPY (7.00 ANGSTROMS), SUBCELLULAR LOCATION,
RP AND SUBUNIT.
RX PubMed=24799711; DOI=10.1073/pnas.1401657111;
RA Kaushal P.S., Sharma M.R., Booth T.M., Haque E.M., Tung C.S.,
RA Sanbonmatsu K.Y., Spremulli L.L., Agrawal R.K.;
RT "Cryo-EM structure of the small subunit of the mammalian mitochondrial
RT ribosome.";
RL Proc. Natl. Acad. Sci. U.S.A. 111:7284-7289(2014).
CC -!- SUBUNIT: Component of the mitochondrial ribosome small subunit (28S)
CC which comprises a 12S rRNA and about 30 distinct proteins.
CC {ECO:0000269|PubMed:11344316, ECO:0000269|PubMed:24799711}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000269|PubMed:11344316,
CC ECO:0000269|PubMed:24799711}.
CC -!- SIMILARITY: Belongs to the mitochondrion-specific ribosomal protein
CC mS35 family. {ECO:0000305}.
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DR EMBL; BC110245; AAI10246.1; -; mRNA.
DR RefSeq; NP_001069087.1; NM_001075619.2.
DR PDB; 3JD5; EM; 7.00 A; k=1-325.
DR PDB; 6NEQ; EM; 3.32 A; k=1-325.
DR PDB; 6NF8; EM; 3.48 A; k=1-325.
DR PDBsum; 3JD5; -.
DR PDBsum; 6NEQ; -.
DR PDBsum; 6NF8; -.
DR AlphaFoldDB; Q2YDF6; -.
DR SMR; Q2YDF6; -.
DR CORUM; Q2YDF6; -.
DR IntAct; Q2YDF6; 1.
DR STRING; 9913.ENSBTAP00000010567; -.
DR PaxDb; Q2YDF6; -.
DR PRIDE; Q2YDF6; -.
DR Ensembl; ENSBTAT00000010567; ENSBTAP00000010567; ENSBTAG00000006369.
DR GeneID; 513438; -.
DR KEGG; bta:513438; -.
DR CTD; 60488; -.
DR VEuPathDB; HostDB:ENSBTAG00000006369; -.
DR VGNC; VGNC:31673; MRPS35.
DR eggNOG; KOG3933; Eukaryota.
DR GeneTree; ENSGT00390000003443; -.
DR HOGENOM; CLU_060973_0_1_1; -.
DR InParanoid; Q2YDF6; -.
DR OMA; AHARDKF; -.
DR OrthoDB; 1339087at2759; -.
DR TreeFam; TF318686; -.
DR Proteomes; UP000009136; Chromosome 5.
DR Bgee; ENSBTAG00000006369; Expressed in oocyte and 106 other tissues.
DR GO; GO:0005743; C:mitochondrial inner membrane; TAS:Reactome.
DR GO; GO:0005763; C:mitochondrial small ribosomal subunit; IDA:UniProtKB.
DR GO; GO:0003735; F:structural constituent of ribosome; HDA:UniProtKB.
DR GO; GO:0032543; P:mitochondrial translation; HDA:UniProtKB.
DR InterPro; IPR039848; Ribosomal_S24/S35.
DR InterPro; IPR019349; Ribosomal_S24/S35_mit.
DR PANTHER; PTHR13490; PTHR13490; 1.
DR Pfam; PF10213; MRP-S28; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Direct protein sequencing; Mitochondrion; Reference proteome;
KW Ribonucleoprotein; Ribosomal protein; Transit peptide.
FT TRANSIT 1..?
FT /note="Mitochondrion"
FT /evidence="ECO:0000305"
FT CHAIN ?..325
FT /note="28S ribosomal protein S35, mitochondrial"
FT /id="PRO_0000046054"
FT REGION 27..62
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 40..60
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CONFLICT 130..131
FT /note="DF -> NY (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT HELIX 58..61
FT /evidence="ECO:0007829|PDB:6NEQ"
FT HELIX 68..71
FT /evidence="ECO:0007829|PDB:6NEQ"
FT TURN 80..82
FT /evidence="ECO:0007829|PDB:6NEQ"
FT STRAND 94..96
FT /evidence="ECO:0007829|PDB:6NEQ"
FT HELIX 106..109
FT /evidence="ECO:0007829|PDB:6NEQ"
FT HELIX 114..116
FT /evidence="ECO:0007829|PDB:6NEQ"
FT HELIX 118..124
FT /evidence="ECO:0007829|PDB:6NEQ"
FT HELIX 125..129
FT /evidence="ECO:0007829|PDB:6NEQ"
FT HELIX 142..148
FT /evidence="ECO:0007829|PDB:6NEQ"
FT STRAND 151..159
FT /evidence="ECO:0007829|PDB:6NEQ"
FT STRAND 161..163
FT /evidence="ECO:0007829|PDB:6NEQ"
FT TURN 168..171
FT /evidence="ECO:0007829|PDB:6NEQ"
FT STRAND 173..182
FT /evidence="ECO:0007829|PDB:6NEQ"
FT HELIX 186..196
FT /evidence="ECO:0007829|PDB:6NEQ"
FT TURN 202..204
FT /evidence="ECO:0007829|PDB:6NEQ"
FT STRAND 206..209
FT /evidence="ECO:0007829|PDB:6NEQ"
FT STRAND 214..216
FT /evidence="ECO:0007829|PDB:6NEQ"
FT HELIX 217..232
FT /evidence="ECO:0007829|PDB:6NEQ"
FT HELIX 240..242
FT /evidence="ECO:0007829|PDB:6NF8"
FT TURN 247..249
FT /evidence="ECO:0007829|PDB:6NEQ"
FT STRAND 250..252
FT /evidence="ECO:0007829|PDB:6NEQ"
FT HELIX 259..274
FT /evidence="ECO:0007829|PDB:6NEQ"
FT HELIX 283..287
FT /evidence="ECO:0007829|PDB:6NEQ"
FT HELIX 290..302
FT /evidence="ECO:0007829|PDB:6NEQ"
FT HELIX 308..321
FT /evidence="ECO:0007829|PDB:6NEQ"
SQ SEQUENCE 325 AA; 37070 MW; 0C202F0C4F553E46 CRC64;
MAAPSLPAWL ALQTRARTLR AFSTAVSPVT GAQRLSPPTT ERTSKHERAP RRKALPPRTE
KMSVDQDWPS VYPVAAPFKP SAVPLPVRMG YPVKRGVPMA KEGNLELLKI PNFLHLTPVA
IKKHCEALKD FCTEWPAALD SDEKCEKHFP IEIDTADYIS SGPSIRNPKA RVVTLRVKLS
SLNLDDHAKK KLIKLVGDRY CKSTDVLTIK TDRCPLKRQN YDYAMYLLTV LYHESWKTEE
WEKKKTEADM EEYVWKDSAS EKNILETLFQ IKAAEKNTEL SKEELLSTKE VEDYKNSVVS
LKNEGDNENT ISQYKESVKR LLHLM
