SRP54_RAT
ID SRP54_RAT Reviewed; 504 AA.
AC Q6AYB5;
DT 16-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT 13-SEP-2004, sequence version 1.
DT 03-AUG-2022, entry version 129.
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 Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Kidney;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
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 (By similarity). As part of the SRP complex, associates with the SRP
CC receptor (SR) component SRPRA to target secretory proteins to the
CC endoplasmic reticulum membrane (By similarity). Binds to the signal
CC sequence of presecretory proteins when they emerge from the ribosomes
CC (By similarity). Displays basal GTPase activity, and stimulates
CC reciprocal GTPase activation of the SR subunit SRPRA (By similarity).
CC Forms a guanosine 5'-triphosphate (GTP)-dependent complex with the SR
CC subunit SRPRA (By similarity). SR compaction and GTPase mediated
CC rearrangement of SR drive SRP-mediated cotranslational protein
CC translocation into the ER (By similarity). Requires the presence of
CC SRP9/SRP14 and/or SRP19 to stably interact with RNA (By similarity).
CC Plays a role in proliferation and differentiation of granulocytic
CC cells, neutrophils migration capacity and exocrine pancreas development
CC (By similarity). {ECO:0000250|UniProtKB:P61010,
CC ECO:0000250|UniProtKB:P61011}.
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 (SRP) complex that
CC consists of a 7SL RNA molecule of 300 nucleotides and six protein
CC subunits: SRP72, SRP68, SRP54, SRP19, SRP14 and SRP9 (By similarity).
CC Interacts with RNPS1 (By similarity). Interacts with the SRP receptor
CC subunit SRPRA (By similarity). {ECO:0000250|UniProtKB:P61011}.
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; BC079117; AAH79117.1; -; mRNA.
DR RefSeq; NP_446323.1; NM_053871.1.
DR AlphaFoldDB; Q6AYB5; -.
DR SMR; Q6AYB5; -.
DR BioGRID; 250535; 1.
DR STRING; 10116.ENSRNOP00000048945; -.
DR iPTMnet; Q6AYB5; -.
DR PhosphoSitePlus; Q6AYB5; -.
DR jPOST; Q6AYB5; -.
DR PaxDb; Q6AYB5; -.
DR PRIDE; Q6AYB5; -.
DR Ensembl; ENSRNOT00000052076; ENSRNOP00000048945; ENSRNOG00000032776.
DR GeneID; 116650; -.
DR KEGG; rno:116650; -.
DR UCSC; RGD:621390; rat.
DR CTD; 24067; -.
DR RGD; 621390; Srp54.
DR eggNOG; KOG0780; Eukaryota.
DR GeneTree; ENSGT00550000074824; -.
DR HOGENOM; CLU_009301_6_1_1; -.
DR InParanoid; Q6AYB5; -.
DR OMA; DTAGRHK; -.
DR OrthoDB; 463152at2759; -.
DR PhylomeDB; Q6AYB5; -.
DR TreeFam; TF106249; -.
DR Reactome; R-RNO-1799339; SRP-dependent cotranslational protein targeting to membrane.
DR PRO; PR:Q6AYB5; -.
DR Proteomes; UP000002494; Chromosome 6.
DR Bgee; ENSRNOG00000032776; Expressed in pancreas and 19 other tissues.
DR Genevisible; Q6AYB5; RN.
DR GO; GO:0005737; C:cytoplasm; ISO:RGD.
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; ISO:RGD.
DR GO; GO:0005786; C:signal recognition particle, endoplasmic reticulum targeting; ISO:RGD.
DR GO; GO:0008312; F:7S RNA binding; ISO:RGD.
DR GO; GO:0030942; F:endoplasmic reticulum signal peptide binding; ISO:RGD.
DR GO; GO:0019003; F:GDP binding; ISO:RGD.
DR GO; GO:0005525; F:GTP binding; ISO:RGD.
DR GO; GO:0003924; F:GTPase activity; ISS:UniProtKB.
DR GO; GO:0043021; F:ribonucleoprotein complex binding; ISO:RGD.
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; ISO:RGD.
DR GO; GO:0006616; P:SRP-dependent cotranslational protein targeting to membrane, translocation; IBA:GO_Central.
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; 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; SSF47446; SSF47446; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR TIGRFAMs; TIGR01425; SRP54_euk; 1.
DR PROSITE; PS00300; SRP54; 1.
PE 2: Evidence at transcript level;
KW Cytoplasm; Endoplasmic reticulum; GTP-binding; Hydrolase;
KW Nucleotide-binding; Nucleus; Reference proteome; Ribonucleoprotein;
KW RNA-binding; Signal recognition particle.
FT CHAIN 1..504
FT /note="Signal recognition particle 54 kDa protein"
FT /id="PRO_0000101196"
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; 7D518671BE41545A CRC64;
MVLADLGRKI TSALRSLSNA TIINEEVLNA MLKEVCTALL EADVNIKLVK QLRENVKSAI
DLEEMASGLN KRKMIQHAVF KELVKLVDPG VKAWTPTKGK QNVIMFVGLQ GSGKTTTCSK
LAYFYQRKGW KTCLICADTF RAGAFDQLKQ NATKARIPFY GSYTEMDPVI IASEGVEKFK
NENFEIIIVD TSGRHKQEDS LFEEMLQVSN 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
