SRP54_CANLF
ID SRP54_CANLF Reviewed; 504 AA.
AC P61010; P13624;
DT 26-APR-2004, integrated into UniProtKB/Swiss-Prot.
DT 26-APR-2004, sequence version 1.
DT 03-AUG-2022, entry version 128.
DE RecName: Full=Signal recognition particle 54 kDa protein;
DE Short=SRP54;
DE EC=3.6.5.- {ECO:0000250|UniProtKB:P61011};
GN Name=SRP54;
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=2502717; DOI=10.1038/340478a0;
RA Roemisch K., Webb J., Herz J., Prehn S., Frank R., Vingron M.,
RA Dobberstein B.;
RT "Homology of 54K protein of signal-recognition particle, docking protein
RT and two E. coli proteins with putative GTP-binding domains.";
RL Nature 340:478-482(1989).
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, AND SUBUNIT.
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 STRUCTURE BY ELECTRON MICROSCOPY (8.0 ANGSTROMS) OF THE 80S WHEAT GERM
RP RIBOSOME IN COMPLEX WITH THE NASCENT CHAIN AND THE MAMMALIAN SIGNAL
RP RECOGNITION PARTICLE.
RX PubMed=17086193; DOI=10.1038/nature05326;
RA Halic M., Blau M., Becker T., Mielke T., Pool M.R., Wild K., Sinning I.,
RA Beckmann R.;
RT "Following the signal sequence from ribosomal tunnel exit to signal
RT recognition particle.";
RL Nature 444:507-511(2006).
RN [5]
RP STRUCTURE BY ELECTRON MICROSCOPY (7.4 ANGSTROMS) OF 326-434 OF SIGNAL
RP RECOGNITION PARTICLE IN COMPLEX WITH THE 80S RIBOSOME AND THE SRP RECEPTOR.
RX PubMed=16675701; DOI=10.1126/science.1124864;
RA Halic M., Gartmann M., Schlenker O., Mielke T., Pool M.R., Sinning I.,
RA Beckmann R.;
RT "Signal recognition particle receptor exposes the ribosomal translocon
RT binding site.";
RL Science 312:745-747(2006).
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). As part of the SRP complex,
CC associates with the SRP receptor (SR) component SRPRA to target
CC secretory proteins to the endoplasmic reticulum membrane (By
CC similarity). Binds to the signal sequence of presecretory proteins when
CC they emerge from the ribosomes (By similarity). Displays basal GTPase
CC activity, and stimulates reciprocal GTPase activation of the SR subunit
CC SRPRA (By similarity). Forms a guanosine 5'-triphosphate (GTP)-
CC dependent complex with the SR subunit SRPRA (By similarity). SR
CC compaction and GTPase mediated rearrangement of SR drive SRP-mediated
CC cotranslational protein translocation into the ER (By similarity).
CC Requires the presence of SRP9/SRP14 and/or SRP19 to stably interact
CC with RNA (PubMed:6413076). Plays a role in proliferation and
CC differentiation of granulocytic cells, neutrophils migration capacity
CC and exocrine pancreas development (By similarity).
CC {ECO:0000250|UniProtKB:P61011, ECO:0000269|PubMed:6413076,
CC ECO:0000269|PubMed:6938958}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=GTP + H2O = GDP + H(+) + phosphate; Xref=Rhea:RHEA:19669,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:37565,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:58189;
CC Evidence={ECO:0000250|UniProtKB:P61011};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:19670;
CC Evidence={ECO:0000250|UniProtKB:P61011};
CC -!- SUBUNIT: Component of a signal recognition particle complex that
CC consists of a 7SL RNA molecule of 300 nucleotides and six protein
CC subunits: SRP72, SRP68, SRP54, SRP19, SRP14 and SRP9 (PubMed:6938958,
CC PubMed:6413076). Interacts with RNPS1 (By similarity). Interacts with
CC the SRP receptor subunit SRPRA (By similarity).
CC {ECO:0000250|UniProtKB:P61011, ECO:0000269|PubMed:6413076,
CC ECO:0000269|PubMed:6938958}.
CC -!- SUBCELLULAR LOCATION: Nucleus speckle {ECO:0000250|UniProtKB:P61011}.
CC Cytoplasm {ECO:0000250|UniProtKB:P61011}. Endoplasmic reticulum
CC {ECO:0000250|UniProtKB:P61011}.
CC -!- DOMAIN: The NG domain, also named G domain, is a special guanosine
CC triphosphatase (GTPase) domain, which binds GTP and forms a guanosine
CC 5'-triphosphate (GTP)-dependent complex with a homologous NG domain in
CC the SRP receptor subunit SRPRA (By similarity). The two NG domains
CC undergo cooperative rearrangements upon their assembly, which culminate
CC in the reciprocal activation of the GTPase activity of one another (By
CC similarity). SRP receptor compaction upon binding with cargo-loaded SRP
CC and GTPase rearrangement drive SRP-mediated cotranslational protein
CC translocation into the ER (By similarity).
CC {ECO:0000250|UniProtKB:P61011}.
CC -!- DOMAIN: The M domain binds the 7SL RNA in presence of SRP19 and binds
CC the signal sequence of presecretory proteins.
CC {ECO:0000250|UniProtKB:P61011}.
CC -!- SIMILARITY: Belongs to the GTP-binding SRP family. SRP54 subfamily.
CC {ECO:0000305}.
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DR EMBL; X16318; CAA34385.1; -; mRNA.
DR PIR; S05197; S05197.
DR RefSeq; NP_001003272.1; NM_001003272.1.
DR RefSeq; XP_005623237.1; XM_005623180.2.
DR RefSeq; XP_005623238.1; XM_005623181.2.
DR PDB; 2GO5; EM; 7.40 A; W=326-434.
DR PDB; 2J37; EM; 8.00 A; W=1-504.
DR PDB; 4UE5; EM; 9.00 A; D=1-433.
DR PDB; 6FRK; EM; 3.70 A; x=1-504.
DR PDB; 6R6G; EM; 3.70 A; AB=4-434.
DR PDB; 7OBQ; EM; 3.90 A; x=1-504.
DR PDB; 7OBR; EM; 2.80 A; x=1-504.
DR PDBsum; 2GO5; -.
DR PDBsum; 2J37; -.
DR PDBsum; 4UE5; -.
DR PDBsum; 6FRK; -.
DR PDBsum; 6R6G; -.
DR PDBsum; 7OBQ; -.
DR PDBsum; 7OBR; -.
DR AlphaFoldDB; P61010; -.
DR SMR; P61010; -.
DR STRING; 9615.ENSCAFP00000050551; -.
DR PaxDb; P61010; -.
DR PRIDE; P61010; -.
DR Ensembl; ENSCAFT00030011405; ENSCAFP00030009976; ENSCAFG00030006175.
DR Ensembl; ENSCAFT00030011482; ENSCAFP00030010046; ENSCAFG00030006175.
DR Ensembl; ENSCAFT00030011562; ENSCAFP00030010116; ENSCAFG00030006175.
DR Ensembl; ENSCAFT00030011665; ENSCAFP00030010209; ENSCAFG00030006175.
DR Ensembl; ENSCAFT00030011772; ENSCAFP00030010311; ENSCAFG00030006175.
DR Ensembl; ENSCAFT00040028476; ENSCAFP00040024744; ENSCAFG00040015385.
DR Ensembl; ENSCAFT00845003105; ENSCAFP00845002476; ENSCAFG00845001751.
DR GeneID; 403953; -.
DR KEGG; cfa:403953; -.
DR CTD; 6729; -.
DR VEuPathDB; HostDB:ENSCAFG00845001751; -.
DR eggNOG; KOG0780; Eukaryota.
DR GeneTree; ENSGT00550000074824; -.
DR HOGENOM; CLU_009301_6_1_1; -.
DR InParanoid; P61010; -.
DR OMA; DTAGRHK; -.
DR OrthoDB; 463152at2759; -.
DR TreeFam; TF106249; -.
DR BRENDA; 3.6.5.4; 1153.
DR Reactome; R-CFA-1799339; SRP-dependent cotranslational protein targeting to membrane.
DR EvolutionaryTrace; P61010; -.
DR Proteomes; UP000002254; Chromosome 8.
DR Bgee; ENSCAFG00000013331; Expressed in saliva-secreting gland and 46 other tissues.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0005783; C:endoplasmic reticulum; IEA:UniProtKB-SubCell.
DR GO; GO:0016607; C:nuclear speck; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0005786; C:signal recognition particle, endoplasmic reticulum targeting; ISS:UniProtKB.
DR GO; GO:0008312; F:7S RNA binding; ISS:UniProtKB.
DR GO; GO:0030942; F:endoplasmic reticulum signal peptide binding; IMP:UniProtKB.
DR GO; GO:0019003; F:GDP binding; ISS:UniProtKB.
DR GO; GO:0005525; F:GTP binding; ISS:UniProtKB.
DR GO; GO:0003924; F:GTPase activity; ISS:UniProtKB.
DR GO; GO:0043021; F:ribonucleoprotein complex binding; IEA:Ensembl.
DR GO; GO:0031017; P:exocrine pancreas development; ISS:UniProtKB.
DR GO; GO:0030851; P:granulocyte differentiation; ISS:UniProtKB.
DR GO; GO:0030593; P:neutrophil chemotaxis; ISS:UniProtKB.
DR GO; GO:0045047; P:protein targeting to ER; IMP:UniProtKB.
DR GO; GO:0006617; P:SRP-dependent cotranslational protein targeting to membrane, signal sequence recognition; IMP:UniProtKB.
DR GO; GO:0006616; P:SRP-dependent cotranslational protein targeting to membrane, translocation; IDA:UniProtKB.
DR Gene3D; 1.10.260.30; -; 1.
DR Gene3D; 1.20.120.140; -; 1.
DR Gene3D; 3.40.50.300; -; 1.
DR HAMAP; MF_00306; SRP54; 1.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR036891; Signal_recog_part_SRP54_M_sf.
DR InterPro; IPR013822; Signal_recog_particl_SRP54_hlx.
DR InterPro; IPR004125; Signal_recog_particle_SRP54_M.
DR InterPro; IPR036225; SRP/SRP_N.
DR InterPro; IPR022941; SRP54.
DR InterPro; IPR006325; SRP54_euk.
DR InterPro; IPR000897; SRP54_GTPase_dom.
DR InterPro; IPR042101; SRP54_N_sf.
DR PANTHER; PTHR11564; PTHR11564; 1.
DR Pfam; PF00448; SRP54; 1.
DR Pfam; PF02881; SRP54_N; 1.
DR Pfam; PF02978; SRP_SPB; 1.
DR SMART; SM00382; AAA; 1.
DR SMART; SM00962; SRP54; 1.
DR SMART; SM00963; SRP54_N; 1.
DR SUPFAM; SSF47364; SSF47364; 1.
DR SUPFAM; SSF47446; SSF47446; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR TIGRFAMs; TIGR01425; SRP54_euk; 1.
DR PROSITE; PS00300; SRP54; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; Direct protein sequencing; Endoplasmic reticulum;
KW GTP-binding; Hydrolase; Nucleotide-binding; Nucleus; Reference proteome;
KW Ribonucleoprotein; RNA-binding; Signal recognition particle.
FT CHAIN 1..504
FT /note="Signal recognition particle 54 kDa protein"
FT /id="PRO_0000101191"
FT REGION 1..295
FT /note="NG-domain"
FT /evidence="ECO:0000250|UniProtKB:P61011"
FT REGION 296..504
FT /note="M-domain"
FT /evidence="ECO:0000250|UniProtKB:P61011"
FT BINDING 108..115
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 190..194
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 248..251
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
SQ SEQUENCE 504 AA; 55705 MW; 7D7630A43BC5EC2C CRC64;
MVLADLGRKI TSALRSLSNA TIINEEVLNA MLKEVCTALL EADVNIKLVK QLRENVKSAI
DLEEMASGLN KRKMIQHAVF KELVKLVDPG VKAWTPTKGK QNVIMFVGLQ GSGKTTTCSK
LAYYYQRKGW KTCLICADTF RAGAFDQLKQ NATKARIPFY GSYTEMDPVI IASEGVEKFK
NENFEIIIVD TSGRHKQEDS LFEEMLQVAN AIQPDNIVYV MDASIGQACE AQAKAFKDKV
DVASVIVTKL DGHAKGGGAL SAVAATKSPI IFIGTGEHID DFEPFKTQPF ISKLLGMGDI
EGLIDKVNEL KLDDNEALIE KLKHGQFTLR DMYEQFQNIM KMGPFSQILG MIPGFGTDFM
SKGNEQESMA RLKKLMTIMD SMNDQELDST DGAKVFSKQP GRIQRVARGS GVSTRDVQEL
LTQYTKFAQM VKKMGGIKGL FKGGDMSKNV SQSQMAKLNQ QMAKMMDPRV LHHMGGMAGL
QSMMRQFQQG AAGNMKGMMG FNNM
