ID M3WSB2_FELCA Unreviewed; 504 AA.
AC M3WSB2;
DT 01-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 01-MAY-2013, sequence version 1.
DT 27-MAR-2024, entry version 61.
DE RecName: Full=Signal recognition particle 54 kDa protein {ECO:0000256|RuleBase:RU364034};
DE EC=3.6.5.- {ECO:0000256|RuleBase:RU364034};
GN Name=SRP54 {ECO:0000313|Ensembl:ENSFCAP00000017248.1,
GN ECO:0000313|VGNC:VGNC:65683};
OS Felis catus (Cat) (Felis silvestris catus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Feliformia; Felidae; Felinae; Felis.
OX NCBI_TaxID=9685 {ECO:0000313|Ensembl:ENSFCAP00000017248.1, ECO:0000313|Proteomes:UP000011712};
RN [1] {ECO:0000313|Ensembl:ENSFCAP00000017248.1, ECO:0000313|Proteomes:UP000011712}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Abyssinian {ECO:0000313|Ensembl:ENSFCAP00000017248.1,
RC ECO:0000313|Proteomes:UP000011712};
RX PubMed=17975172; DOI=10.1101/gr.6380007;
RA Pontius J.U., Mullikin J.C., Smith D.R., Lindblad-Toh K., Gnerre S.,
RA Clamp M., Chang J., Stephens R., Neelam B., Volfovsky N., Schaffer A.A.,
RA Agarwala R., Narfstrom K., Murphy W.J., Giger U., Roca A.L., Antunes A.,
RA Menotti-Raymond M., Yuhki N., Pecon-Slattery J., Johnson W.E., Bourque G.,
RA Tesler G., O'Brien S.J.;
RT "Initial sequence and comparative analysis of the cat genome.";
RL Genome Res. 17:1675-1689(2007).
RN [2] {ECO:0000313|Ensembl:ENSFCAP00000017248.1, ECO:0000313|Proteomes:UP000011712}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Abyssinian {ECO:0000313|Ensembl:ENSFCAP00000017248.1,
RC ECO:0000313|Proteomes:UP000011712};
RA Hillier L.W., Warren W., Obrien S., Wilson R.K.;
RT "Sequence assembly of the Felis catus genome version 6.2.";
RL Submitted (SEP-2011) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|Ensembl:ENSFCAP00000017248.1}
RP IDENTIFICATION.
RC STRAIN=breed Abyssinian {ECO:0000313|Ensembl:ENSFCAP00000017248.1};
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
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 As part of the SRP complex, associates with the SRP receptor (SR)
CC component SRPRA to target secretory proteins to the endoplasmic
CC reticulum membrane. Binds to the signal sequence of presecretory
CC proteins when they emerge from the ribosomes. Displays basal GTPase
CC activity, and stimulates reciprocal GTPase activation of the SR subunit
CC SRPRA. Forms a guanosine 5'-triphosphate (GTP)-dependent complex with
CC the SR subunit SRPRA. SR compaction and GTPase mediated rearrangement
CC of SR drive SRP-mediated cotranslational protein translocation into the
CC ER. Requires the presence of SRP9/SRP14 and/or SRP19 to stably interact
CC with RNA. Plays a role in proliferation and differentiation of
CC granulocytic cells, neutrophils migration capacity and exocrine
CC pancreas development. {ECO:0000256|RuleBase:RU364034}.
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; EC=3.6.5.4;
CC Evidence={ECO:0000256|ARBA:ARBA00035589};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:19670;
CC Evidence={ECO:0000256|ARBA:ARBA00035589};
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:0000256|RuleBase:RU364034};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:19670;
CC Evidence={ECO:0000256|RuleBase:RU364034};
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. Interacts with
CC RNPS1. Interacts with the SRP receptor subunit SRPRA.
CC {ECO:0000256|RuleBase:RU364034}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496,
CC ECO:0000256|RuleBase:RU364034}. Nucleus speckle
CC {ECO:0000256|RuleBase:RU364034}. Endoplasmic reticulum
CC {ECO:0000256|RuleBase:RU364034}.
CC -!- DOMAIN: The M domain binds the 7SL RNA in presence of SRP19 and binds
CC the signal sequence of presecretory proteins.
CC {ECO:0000256|RuleBase:RU364034}.
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. The two NG domains undergo cooperative
CC rearrangements upon their assembly, which culminate in the reciprocal
CC activation of the GTPase activity of one another. SRP receptor
CC compaction upon binding with cargo-loaded SRP and GTPase rearrangement
CC drive SRP-mediated cotranslational protein translocation into the ER.
CC {ECO:0000256|RuleBase:RU364034}.
CC -!- SIMILARITY: Belongs to the GTP-binding SRP family. SRP54 subfamily.
CC {ECO:0000256|ARBA:ARBA00005450, ECO:0000256|RuleBase:RU364034}.
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DR EMBL; AANG04004459; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; XP_003987586.1; XM_003987537.4.
DR RefSeq; XP_006932864.1; XM_006932802.3.
DR AlphaFoldDB; M3WSB2; -.
DR STRING; 9685.ENSFCAP00000017248; -.
DR PaxDb; 9685-ENSFCAP00000017248; -.
DR Ensembl; ENSFCAT00000023128.4; ENSFCAP00000017248.1; ENSFCAG00000032033.4.
DR GeneID; 101089523; -.
DR KEGG; fca:101089523; -.
DR CTD; 6729; -.
DR VGNC; VGNC:65683; SRP54.
DR eggNOG; KOG0780; Eukaryota.
DR GeneTree; ENSGT00550000074824; -.
DR HOGENOM; CLU_009301_6_1_1; -.
DR InParanoid; M3WSB2; -.
DR OMA; GMTGQDA; -.
DR OrthoDB; 1110531at2759; -.
DR Proteomes; UP000011712; Chromosome B3.
DR Bgee; ENSFCAG00000032033; Expressed in embryonic head and 10 other cell types or 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:0005786; C:signal recognition particle, endoplasmic reticulum targeting; IBA:GO_Central.
DR GO; GO:0008312; F:7S RNA binding; IBA:GO_Central.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR GO; GO:0030942; F:endoplasmic reticulum signal peptide binding; IBA:GO_Central.
DR GO; GO:0019003; F:GDP binding; IEA:Ensembl.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0043021; F:ribonucleoprotein complex binding; IEA:Ensembl.
DR GO; GO:0030851; P:granulocyte differentiation; IEA:Ensembl.
DR GO; GO:0006616; P:SRP-dependent cotranslational protein targeting to membrane, translocation; IBA:GO_Central.
DR CDD; cd17875; SRP54_G; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR Gene3D; 1.20.120.140; Signal recognition particle SRP54, nucleotide-binding domain; 1.
DR Gene3D; 1.10.260.30; Signal recognition particle, SRP54 subunit, M-domain; 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 NCBIfam; TIGR01425; SRP54_euk; 1.
DR PANTHER; PTHR11564:SF5; SIGNAL RECOGNITION PARTICLE 54 KDA PROTEIN; 1.
DR PANTHER; PTHR11564; SIGNAL RECOGNITION PARTICLE 54K PROTEIN SRP54; 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; Domain of the SRP/SRP receptor G-proteins; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR SUPFAM; SSF47446; Signal peptide-binding domain; 1.
DR PROSITE; PS00300; SRP54; 1.
PE 3: Inferred from homology;
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490, ECO:0000256|RuleBase:RU364034};
KW Endoplasmic reticulum {ECO:0000256|ARBA:ARBA00022824,
KW ECO:0000256|RuleBase:RU364034};
KW GTP-binding {ECO:0000256|ARBA:ARBA00023134, ECO:0000256|RuleBase:RU364034};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU364034};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU364034}; Nucleus {ECO:0000256|RuleBase:RU364034};
KW Reference proteome {ECO:0000313|Proteomes:UP000011712};
KW Ribonucleoprotein {ECO:0000256|ARBA:ARBA00023274,
KW ECO:0000256|RuleBase:RU364034};
KW RNA-binding {ECO:0000256|ARBA:ARBA00022884, ECO:0000256|RuleBase:RU364034};
KW Signal recognition particle {ECO:0000256|ARBA:ARBA00023135,
KW ECO:0000256|RuleBase:RU364034}.
FT DOMAIN 269..282
FT /note="SRP54-type proteins GTP-binding"
FT /evidence="ECO:0000259|PROSITE:PS00300"
SQ SEQUENCE 504 AA; 55691 MW; A25321F1E13A9CB2 CRC64;
MVLADLGRKI TSALRSLSNA TIINEEVLNA MLKEVCTALL EADVNIKLVK QLRENVKSAI
DLEEMASGLN KRKMIQHAVF KELVKLVDPG VKAWTPTKGK QNVIMFVGLQ GSGKTTTCSK
LAYYYQRKGW KTCLICADTF RAGAFDQLKQ NATKARIPFY GSYTEMDPVI IASEGVDKFK
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
//
