SRP54_DANRE
ID SRP54_DANRE Reviewed; 504 AA.
AC Q7ZVN5;
DT 12-AUG-2020, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 153.
DE RecName: Full=Signal recognition particle 54 kDa protein {ECO:0000305};
DE Short=SRP54;
DE EC=3.6.5.- {ECO:0000250|UniProtKB:P61011};
GN Name=srp54 {ECO:0000312|ZFIN:ZDB-GENE-040426-818};
OS Danio rerio (Zebrafish) (Brachydanio rerio).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC Danionidae; Danioninae; Danio.
OX NCBI_TaxID=7955 {ECO:0000312|EMBL:AAH45474.1};
RN [1] {ECO:0000312|EMBL:AAH45474.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=AB {ECO:0000312|EMBL:AAH45474.1};
RG NIH - Zebrafish Gene Collection (ZGC) project;
RL Submitted (JAN-2003) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000312|Proteomes:UP000000437}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Tuebingen {ECO:0000312|Proteomes:UP000000437};
RX PubMed=23594743; DOI=10.1038/nature12111;
RA Howe K., Clark M.D., Torroja C.F., Torrance J., Berthelot C., Muffato M.,
RA Collins J.E., Humphray S., McLaren K., Matthews L., McLaren S., Sealy I.,
RA Caccamo M., Churcher C., Scott C., Barrett J.C., Koch R., Rauch G.J.,
RA White S., Chow W., Kilian B., Quintais L.T., Guerra-Assuncao J.A., Zhou Y.,
RA Gu Y., Yen J., Vogel J.H., Eyre T., Redmond S., Banerjee R., Chi J., Fu B.,
RA Langley E., Maguire S.F., Laird G.K., Lloyd D., Kenyon E., Donaldson S.,
RA Sehra H., Almeida-King J., Loveland J., Trevanion S., Jones M., Quail M.,
RA Willey D., Hunt A., Burton J., Sims S., McLay K., Plumb B., Davis J.,
RA Clee C., Oliver K., Clark R., Riddle C., Elliot D., Threadgold G.,
RA Harden G., Ware D., Begum S., Mortimore B., Kerry G., Heath P.,
RA Phillimore B., Tracey A., Corby N., Dunn M., Johnson C., Wood J., Clark S.,
RA Pelan S., Griffiths G., Smith M., Glithero R., Howden P., Barker N.,
RA Lloyd C., Stevens C., Harley J., Holt K., Panagiotidis G., Lovell J.,
RA Beasley H., Henderson C., Gordon D., Auger K., Wright D., Collins J.,
RA Raisen C., Dyer L., Leung K., Robertson L., Ambridge K., Leongamornlert D.,
RA McGuire S., Gilderthorp R., Griffiths C., Manthravadi D., Nichol S.,
RA Barker G., Whitehead S., Kay M., Brown J., Murnane C., Gray E.,
RA Humphries M., Sycamore N., Barker D., Saunders D., Wallis J., Babbage A.,
RA Hammond S., Mashreghi-Mohammadi M., Barr L., Martin S., Wray P.,
RA Ellington A., Matthews N., Ellwood M., Woodmansey R., Clark G., Cooper J.,
RA Tromans A., Grafham D., Skuce C., Pandian R., Andrews R., Harrison E.,
RA Kimberley A., Garnett J., Fosker N., Hall R., Garner P., Kelly D., Bird C.,
RA Palmer S., Gehring I., Berger A., Dooley C.M., Ersan-Urun Z., Eser C.,
RA Geiger H., Geisler M., Karotki L., Kirn A., Konantz J., Konantz M.,
RA Oberlander M., Rudolph-Geiger S., Teucke M., Lanz C., Raddatz G.,
RA Osoegawa K., Zhu B., Rapp A., Widaa S., Langford C., Yang F.,
RA Schuster S.C., Carter N.P., Harrow J., Ning Z., Herrero J., Searle S.M.,
RA Enright A., Geisler R., Plasterk R.H., Lee C., Westerfield M.,
RA de Jong P.J., Zon L.I., Postlethwait J.H., Nusslein-Volhard C.,
RA Hubbard T.J., Roest Crollius H., Rogers J., Stemple D.L.;
RT "The zebrafish reference genome sequence and its relationship to the human
RT genome.";
RL Nature 496:498-503(2013).
RN [3]
RP FUNCTION, DISRUPTION PHENOTYPE, AND DEVELOPMENTAL STAGE.
RX PubMed=28972538; DOI=10.1172/jci92876;
RA Carapito R., Konantz M., Paillard C., Miao Z., Pichot A., Leduc M.S.,
RA Yang Y., Bergstrom K.L., Mahoney D.H., Shardy D.L., Alsaleh G., Naegely L.,
RA Kolmer A., Paul N., Hanauer A., Rolli V., Mueller J.S., Alghisi E.,
RA Sauteur L., Macquin C., Morlon A., Sancho C.S., Amati-Bonneau P.,
RA Procaccio V., Mosca-Boidron A.L., Marle N., Osmani N., Lefebvre O.,
RA Goetz J.G., Unal S., Akarsu N.A., Radosavljevic M., Chenard M.P.,
RA Rialland F., Grain A., Bene M.C., Eveillard M., Vincent M., Guy J.,
RA Faivre L., Thauvin-Robinet C., Thevenon J., Myers K., Fleming M.D.,
RA Shimamura A., Bottollier-Lemallaz E., Westhof E., Lengerke C., Isidor B.,
RA Bahram S.;
RT "Mutations in signal recognition particle SRP54 cause syndromic neutropenia
RT with Shwachman-Diamond-like features.";
RL J. Clin. Invest. 127:4090-4103(2017).
CC -!- FUNCTION: Binds to the signal sequence of presecretory protein when
CC they emerge from the ribosomes and transfers them to TRAM
CC (translocating chain-associating membrane protein) (By similarity).
CC Plays a role in proliferation of granulocytic cells, neutrophils
CC migration capacity and exocrine pancreas development (PubMed:28972538).
CC {ECO:0000255|RuleBase:RU364034, ECO:0000269|PubMed:28972538}.
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: Signal recognition particle consists of a 7S RNA molecule and
CC at least six protein subunits. {ECO:0000255|RuleBase:RU364034}.
CC -!- SUBCELLULAR LOCATION: Nucleus speckle {ECO:0000250|UniProtKB:P61011}.
CC Cytoplasm {ECO:0000250|UniProtKB:P61011}.
CC -!- DEVELOPMENTAL STAGE: At 26 hours post fertilization (hpf), expression
CC is ubiquitous (PubMed:28972538). Later in development, expression is
CC more pronounced in the anterior part (PubMed:28972538).
CC {ECO:0000269|PubMed:28972538}.
CC -!- DOMAIN: Has a two domain structure: the G-domain binds GTP; the M-
CC domain binds the 7S RNA in presence of SRP19 and also binds the signal
CC sequence. {ECO:0000255|RuleBase:RU364034}.
CC -!- DISRUPTION PHENOTYPE: Mutants show profound reductions in neutrophil
CC counts and chemotaxis as well as a diminished exocrine pancreas size.
CC {ECO:0000269|PubMed:28972538}.
CC -!- SIMILARITY: Belongs to the GTP-binding SRP family. SRP54 subfamily.
CC {ECO:0000255|RuleBase:RU364034}.
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DR EMBL; BX088587; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC045474; AAH45474.1; -; mRNA.
DR EMBL; BC067588; AAH67588.1; -; mRNA.
DR EMBL; BC164217; AAI64217.1; -; mRNA.
DR RefSeq; NP_957282.1; NM_200988.2.
DR AlphaFoldDB; Q7ZVN5; -.
DR SMR; Q7ZVN5; -.
DR STRING; 7955.ENSDARP00000118188; -.
DR PaxDb; Q7ZVN5; -.
DR Ensembl; ENSDART00000166649; ENSDARP00000139136; ENSDARG00000098367.
DR Ensembl; ENSDART00000169892; ENSDARP00000131757; ENSDARG00000098367.
DR GeneID; 393963; -.
DR KEGG; dre:393963; -.
DR CTD; 6729; -.
DR ZFIN; ZDB-GENE-040426-818; srp54.
DR eggNOG; KOG0780; Eukaryota.
DR GeneTree; ENSGT00550000074824; -.
DR HOGENOM; CLU_009301_6_1_1; -.
DR InParanoid; Q7ZVN5; -.
DR OMA; DTAGRHK; -.
DR OrthoDB; 463152at2759; -.
DR PhylomeDB; Q7ZVN5; -.
DR TreeFam; TF106249; -.
DR Reactome; R-DRE-1799339; SRP-dependent cotranslational protein targeting to membrane.
DR PRO; PR:Q7ZVN5; -.
DR Proteomes; UP000000437; Genome assembly.
DR Proteomes; UP000814640; Chromosome 17.
DR Bgee; ENSDARG00000098367; Expressed in cleaving embryo and 26 other tissues.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
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:0030942; F:endoplasmic reticulum signal peptide binding; IBA:GO_Central.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR GO; GO:0003924; F:GTPase activity; ISS:UniProtKB.
DR GO; GO:0031017; P:exocrine pancreas development; IMP:ZFIN.
DR GO; GO:0030851; P:granulocyte differentiation; ISS:UniProtKB.
DR GO; GO:0030593; P:neutrophil chemotaxis; IMP:ZFIN.
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; GTP-binding; Hydrolase; Nucleotide-binding; Nucleus;
KW Reference proteome; Ribonucleoprotein; RNA-binding;
KW Signal recognition particle.
FT CHAIN 1..504
FT /note="Signal recognition particle 54 kDa protein"
FT /id="PRO_0000450446"
FT REGION 1..295
FT /note="G-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; 55753 MW; BB3F977BB90797D9 CRC64;
MVLADLGRKI TSALRSLSNA TIINEEVLNA MLKEVCAALL EADVNIKLVK QLRENVKAAI
DLEEMASGLN KRRMIQHAVF KELVKLVDPG VKAWTPTKGK NNVIMFVGLQ GSGKTTTCSK
LAYYFQRKGW KTCLICADTF RAGAFDQLKQ NATKARIPFY GSYTEMDPVI IAAEGVEKFK
SENFEIIIVD TSGRHKQEDS LFEEMLQVSN AVQPDNIVYV MDASIGQACE AQAKAFKDKV
DVASVIVTKL DGHAKGGGAL SAVAATKSPI IFIGTGEHID DFEPFKTQPF ISKLLGMGDI
EGLIDKVNEL KLDDNEELID KLKHGQFTLR DMYEQFQNIM KMGPFGQIMG MIPGFGTDFM
SKGNEQESMA RLKKLMTIMD SMNDQELDNK DGAKLFSKQP NRIQRVARGS GVATRDVQEL
LTQYTKFAQM VKKMGGIKGL FKGGDMSKNV NPSQMAKLNQ QMAKMMDPRV LHHMGGMAGL
QSMMRQFQQG AAGNMKGMMG FNNM
