SRP68_CANLF
ID SRP68_CANLF Reviewed; 622 AA.
AC Q00004;
DT 01-DEC-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-1992, sequence version 1.
DT 03-AUG-2022, entry version 122.
DE RecName: Full=Signal recognition particle subunit SRP68;
DE Short=SRP68;
DE AltName: Full=Signal recognition particle 68 kDa protein;
GN Name=SRP68;
OS Canis lupus familiaris (Dog) (Canis familiaris).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Caniformia; Canidae; Canis.
OX NCBI_TaxID=9615;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND PARTIAL PROTEIN SEQUENCE.
RC STRAIN=Cocker spaniel; TISSUE=Kidney;
RX PubMed=1702390; DOI=10.1016/0014-5793(90)80518-n;
RA Herz J., Flint N., Stanley K., Frank R., Dobberstein B.;
RT "The 68 kDa protein of signal recognition particle contains a glycine-rich
RT region also found in certain RNA-binding proteins.";
RL FEBS Lett. 276:103-107(1990).
RN [2]
RP FUNCTION, AND IDENTIFICATION IN A SIGNAL RECOGNITION PARTICLE COMPLEX.
RX PubMed=6938958; DOI=10.1073/pnas.77.12.7112;
RA Walter P., Blobel G.;
RT "Purification of a membrane-associated protein complex required for protein
RT translocation across the endoplasmic reticulum.";
RL Proc. Natl. Acad. Sci. U.S.A. 77:7112-7116(1980).
RN [3]
RP FUNCTION, SUBUNIT, AND INTERACTION WITH SRP72.
RX PubMed=6413076; DOI=10.1016/0092-8674(83)90385-9;
RA Walter P., Blobel G.;
RT "Disassembly and reconstitution of signal recognition particle.";
RL Cell 34:525-533(1983).
RN [4]
RP FUNCTION, RNA BINDING, SUBUNIT, INTERACTION WITH SRP72, AND MUTAGENESIS OF
RP 564-THR--SER-622.
RC STRAIN=Cocker spaniel; TISSUE=Kidney;
RX PubMed=8388879; DOI=10.1083/jcb.121.5.977;
RA Luetcke H., Prehn S., Ashford A.J., Remus M., Frank R., Dobberstein B.;
RT "Assembly of the 68- and 72-kD proteins of signal recognition particle with
RT 7S RNA.";
RL J. Cell Biol. 121:977-985(1993).
CC -!- FUNCTION: Component of the signal recognition particle (SRP) complex, a
CC ribonucleoprotein complex that mediates the cotranslational targeting
CC of secretory and membrane proteins to the endoplasmic reticulum (ER)
CC (PubMed:6938958, PubMed:6413076). The SRP complex interacts with the
CC signal sequence in nascent secretory and membrane proteins and directs
CC them to the membrane of the ER (PubMed:6938958, PubMed:6413076). The
CC SRP complex targets the ribosome-nascent chain complex to the SRP
CC receptor (SR), which is anchored in the ER, where SR compaction and
CC GTPase rearrangement drive cotranslational protein translocation into
CC the ER (By similarity). Binds the signal recognition particle RNA (7S
CC RNA), SRP72 binds to this complex subsequently (PubMed:8388879). The
CC SRP complex possibly participates in the elongation arrest function (By
CC similarity). {ECO:0000250|UniProtKB:P38687,
CC ECO:0000250|UniProtKB:Q9UHB9, ECO:0000269|PubMed:6413076,
CC ECO:0000269|PubMed:6938958, ECO:0000269|PubMed:8388879}.
CC -!- SUBUNIT: Heterodimer with SRP72 (PubMed:6413076, PubMed:8388879).
CC SRP68/SRP72 heterodimer formation is stabilized by the presence of 7SL
CC RNA (PubMed:6413076, PubMed:8388879). Component of a signal recognition
CC particle complex that consists of a 7SL RNA molecule of 300 nucleotides
CC and six protein subunits: SRP72, SRP68, SRP54, SRP19, SRP14 and SRP9
CC (PubMed:6938958, PubMed:6413076). Within the SRP complex, interacts
CC (via C-terminus) with SRP72 (PubMed:6413076, PubMed:8388879).
CC {ECO:0000269|PubMed:6413076, ECO:0000269|PubMed:6938958,
CC ECO:0000269|PubMed:8388879}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q9UHB9}.
CC Nucleus, nucleolus {ECO:0000250|UniProtKB:Q9UHB9}. Endoplasmic
CC reticulum {ECO:0000250|UniProtKB:Q9UHB9}.
CC -!- DOMAIN: The N-terminus is required for RNA-binding.
CC {ECO:0000250|UniProtKB:Q9UHB9}.
CC -!- SIMILARITY: Belongs to the SRP68 family. {ECO:0000305}.
CC -!- CAUTION: Some authors found genomic clones that have 9 or 12
CC consecutive glycine residues instead of 15 (AA 9-27). {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAA37773.1; Type=Miscellaneous discrepancy; Note=Sequence encodes 9 consecutive glycine residues instead of 15 (AA 9-23).; Evidence={ECO:0000305};
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DR EMBL; X53744; CAA37773.1; ALT_SEQ; mRNA.
DR PIR; A58947; A58947.
DR RefSeq; NP_001003271.2; NM_001003271.1.
DR PDB; 4UE5; EM; 9.00 A; C=55-249.
DR PDB; 6FRK; EM; 3.70 A; u=55-622.
DR PDB; 6R6G; EM; 3.70 A; AI=55-249.
DR PDB; 7OBQ; EM; 3.90 A; u=1-622.
DR PDB; 7OBR; EM; 2.80 A; u=1-622.
DR PDBsum; 4UE5; -.
DR PDBsum; 6FRK; -.
DR PDBsum; 6R6G; -.
DR PDBsum; 7OBQ; -.
DR PDBsum; 7OBR; -.
DR AlphaFoldDB; Q00004; -.
DR SMR; Q00004; -.
DR STRING; 9615.ENSCAFP00000007483; -.
DR PaxDb; Q00004; -.
DR PRIDE; Q00004; -.
DR Ensembl; ENSCAFT00040002094; ENSCAFP00040001787; ENSCAFG00040001082.
DR GeneID; 403952; -.
DR KEGG; cfa:403952; -.
DR CTD; 6730; -.
DR eggNOG; KOG2460; Eukaryota.
DR InParanoid; Q00004; -.
DR OrthoDB; 1019762at2759; -.
DR Proteomes; UP000002254; Unplaced.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0005783; C:endoplasmic reticulum; IEA:UniProtKB-SubCell.
DR GO; GO:0005925; C:focal adhesion; IEA:Ensembl.
DR GO; GO:0005730; C:nucleolus; IEA:UniProtKB-SubCell.
DR GO; GO:0005786; C:signal recognition particle, endoplasmic reticulum targeting; IBA:GO_Central.
DR GO; GO:0008312; F:7S RNA binding; IEA:Ensembl.
DR GO; GO:0030942; F:endoplasmic reticulum signal peptide binding; IEA:InterPro.
DR GO; GO:0019904; F:protein domain specific binding; IEA:Ensembl.
DR GO; GO:0043022; F:ribosome binding; IEA:Ensembl.
DR GO; GO:0005047; F:signal recognition particle binding; IBA:GO_Central.
DR GO; GO:0009410; P:response to xenobiotic stimulus; IEA:Ensembl.
DR GO; GO:0006614; P:SRP-dependent cotranslational protein targeting to membrane; IEA:InterPro.
DR CDD; cd15481; SRP68-RBD; 1.
DR Gene3D; 1.10.3450.40; -; 1.
DR InterPro; IPR026258; SRP68.
DR InterPro; IPR034652; SRP68-RBD.
DR InterPro; IPR038253; SRP68_N_sf.
DR PANTHER; PTHR12860; PTHR12860; 1.
DR Pfam; PF16969; SRP68; 1.
DR PIRSF; PIRSF038995; SRP68; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Cytoplasm; Direct protein sequencing;
KW Endoplasmic reticulum; Nucleus; Phosphoprotein; Reference proteome;
KW Ribonucleoprotein; RNA-binding; Signal recognition particle.
FT CHAIN 1..622
FT /note="Signal recognition particle subunit SRP68"
FT /id="PRO_0000135226"
FT REGION 1..231
FT /note="RNA-binding"
FT /evidence="ECO:0000269|PubMed:8388879"
FT REGION 1..50
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 564..592
FT /note="Required for interaction with SRP72"
FT /evidence="ECO:0000269|PubMed:8388879"
FT COMPBIAS 32..46
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 45
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9UHB9"
FT MOD_RES 238
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9UHB9"
FT MOD_RES 448
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q9UHB9"
FT MUTAGEN 564..622
FT /note="Missing: Abolishes the interaction with SRP72."
FT /evidence="ECO:0000269|PubMed:8388879"
SQ SEQUENCE 622 AA; 70275 MW; DB03DFB0DAE8B942 CRC64;
MAAEKQVPGG GGGGGGGGGG GGGSGGGRGA GGEENKENER PSAGSKANRE FGDSLSLEIL
QIIKESQQQH GLRHGDFQRY RGYCSRRQRR LRKTLNFKMG NRHKFTGKKV TEDLLTDNRY
LLLVLMDAER AWSYAMQLKQ EANTEPRKRF HLLSRLRKAV KHAEELERLC ESNRVDAKTK
LEAQAYTAYL SGMLRFEHQE WKAAIEAFNK CKTIYEKLAS AFTEEQAVLY NQRVEEISPN
IRYCAYNIGD QSAINELMQM RLRSGGTEGL LAEKLEALIT QTRAKQAATM SEVEWRGRTV
PVKIDKVRIF LLGLADNEAA IAQAESEETK ERLFESMLSE CRDAIQAVRE ELKPDQKQRD
YTLDGESGKV SNLQYLHSYL TYIKLSTAIR RNENMAKGLQ KALQQQPEDE SKRSPRPQDL
IRLYDIILQN LVELLQLPGL EEDRAFQKEI GLKTLVFKAY RCFFIAQSYV LVKKWSEALV
LYDRVLKYAN EVNSDAGAFR NSLKDLPDVQ ELITQVRSEK CSLQAAAILD ASDSHQPETS
SQVKDNKPLV ERFETFCLDP SLVTKQANLV HFPPGFQPIP CKPLFFDLAL NHVAFPPLED
KLEQKTKSGL TGYIKGIFGF RS
