ID SRPRA_DROME Reviewed; 614 AA.
AC Q9U5L1; Q95RJ8; Q9VZ29;
DT 10-MAY-2004, integrated into UniProtKB/Swiss-Prot.
DT 10-MAY-2004, sequence version 2.
DT 27-MAR-2024, entry version 176.
DE RecName: Full=Signal recognition particle receptor subunit alpha homolog;
DE Short=DP-alpha;
DE Short=Docking protein alpha;
DE Short=SR-alpha;
DE AltName: Full=GTP-binding protein;
GN Name=SrpRalpha {ECO:0000312|FlyBase:FBgn0010391};
GN Synonyms=Gtp-bp {ECO:0000312|FlyBase:FBgn0010391};
GN ORFNames=CG2522 {ECO:0000312|FlyBase:FBgn0010391};
OS Drosophila melanogaster (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7227 {ECO:0000312|EMBL:AAF48002.2};
RN [1] {ECO:0000305}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley {ECO:0000269|PubMed:10731132};
RX PubMed=10731132; DOI=10.1126/science.287.5461.2185;
RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., Brandon R.C.,
RA Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C.,
RA Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A.,
RA An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A.,
RA Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V.,
RA Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J.,
RA Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E.,
RA Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B.,
RA Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I.,
RA Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C.,
RA Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S.,
RA Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M.,
RA Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D.,
RA Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F.,
RA Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D.,
RA Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A.,
RA Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C.,
RA McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C.,
RA Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L.,
RA Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R.,
RA Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V.,
RA Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F.,
RA Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J.,
RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R.,
RA Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y.,
RA Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T.,
RA Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S.,
RA Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W.,
RA Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M.,
RA Venter J.C.;
RT "The genome sequence of Drosophila melanogaster.";
RL Science 287:2185-2195(2000).
RN [2] {ECO:0000305}
RP GENOME REANNOTATION.
RC STRAIN=Berkeley;
RX PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M.,
RA Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.;
RT "Annotation of the Drosophila melanogaster euchromatic genome: a systematic
RT review.";
RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
RN [3] {ECO:0000305}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Berkeley {ECO:0000269|PubMed:12537569};
RC TISSUE=Embryo {ECO:0000269|PubMed:12537569};
RX PubMed=12537569; DOI=10.1186/gb-2002-3-12-research0080;
RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., George R.A.,
RA Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., Rubin G.M.,
RA Celniker S.E.;
RT "A Drosophila full-length cDNA resource.";
RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002).
RN [4] {ECO:0000305}
RP NUCLEOTIDE SEQUENCE OF 402-573, FUNCTION, TISSUE SPECIFICITY, AND
RP DEVELOPMENTAL STAGE.
RC TISSUE=Head {ECO:0000269|PubMed:8360279}, and
RC Ventral nerve cord {ECO:0000269|PubMed:8360279};
RX PubMed=8360279; DOI=10.1242/jcs.105.1.81;
RA Fredieu J.R., Mahowald A.P.;
RT "Characterization of a putative Drosophila GTP-binding protein.";
RL J. Cell Sci. 105:81-91(1993).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-237; SER-240; TYR-246;
RP SER-268; SER-278 AND SER-279, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC TISSUE=Embryo;
RX PubMed=18327897; DOI=10.1021/pr700696a;
RA Zhai B., Villen J., Beausoleil S.A., Mintseris J., Gygi S.P.;
RT "Phosphoproteome analysis of Drosophila melanogaster embryos.";
RL J. Proteome Res. 7:1675-1682(2008).
CC -!- FUNCTION: Component of the SRP (signal recognition particle) receptor
CC (By similarity). Ensures, in conjunction with the signal recognition
CC particle, the correct targeting of the nascent secretory proteins to
CC the endoplasmic reticulum membrane system (By similarity). Forms a
CC guanosine 5'-triphosphate (GTP)-dependent complex with the SRP subunit
CC Srp54 (By similarity). SRP receptor compaction and GTPase rearrangement
CC drive SRP-mediated cotranslational protein translocation into the ER
CC (By similarity). May have a role in axonogenesis (PubMed:8360279).
CC {ECO:0000250|UniProtKB:P08240, ECO:0000269|PubMed:8360279}.
CC -!- SUBUNIT: Heterodimer of SrpRalpha and SrpRbeta.
CC {ECO:0000250|UniProtKB:P32916}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000250|UniProtKB:P32916}; Peripheral membrane protein
CC {ECO:0000250|UniProtKB:P32916}; Cytoplasmic side
CC {ECO:0000250|UniProtKB:P32916}. Note=Thought to be anchored in the
CC membrane through an interaction with SrpRbeta, which contains a bona
CC fide transmembrane domain. {ECO:0000250|UniProtKB:P32916}.
CC -!- TISSUE SPECIFICITY: In 8-9 hours embryos, expression is seen in a
CC segmental pattern along embryonic ventral midline.
CC {ECO:0000269|PubMed:8360279}.
CC -!- DEVELOPMENTAL STAGE: Expressed both maternally and zygotically. Zygotic
CC expression peaks at 12-18 hours of embryonic development.
CC {ECO:0000269|PubMed:8360279}.
CC -!- DOMAIN: The NG domain, also named G domain, is a special guanosine
CC triphosphatase (GTPase) domain, which forms a guanosine 5'-triphosphate
CC (GTP)-dependent complex with a homologous NG domain in the signal
CC recognition particle (SRP) complex subunit SRP54 (By similarity). The
CC two NG domains undergo cooperative rearrangements upon their assembly,
CC which culminate in the reciprocal activation of the GTPase activity of
CC one another (By similarity). GTPase induced rearrangement of SR drives
CC SRP-mediated cotranslational protein translocation into the ER (By
CC similarity). {ECO:0000250|UniProtKB:P08240}.
CC -!- SIMILARITY: Belongs to the GTP-binding SRP family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAB27926.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=AAL28877.1; Type=Frameshift; Evidence={ECO:0000305};
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AE014298; AAF48002.2; -; Genomic_DNA.
DR EMBL; AY061329; AAL28877.1; ALT_FRAME; mRNA.
DR EMBL; S65640; AAB27926.1; ALT_FRAME; mRNA.
DR RefSeq; NP_524887.2; NM_080148.3.
DR AlphaFoldDB; Q9U5L1; -.
DR SMR; Q9U5L1; -.
DR BioGRID; 70718; 11.
DR ComplexPortal; CPX-2235; Signal recognition particle receptor complex.
DR IntAct; Q9U5L1; 5.
DR STRING; 7227.FBpp0073336; -.
DR iPTMnet; Q9U5L1; -.
DR PaxDb; 7227-FBpp0073336; -.
DR DNASU; 47251; -.
DR EnsemblMetazoa; FBtr0073480; FBpp0073336; FBgn0010391.
DR GeneID; 47251; -.
DR KEGG; dme:Dmel_CG2522; -.
DR AGR; FB:FBgn0010391; -.
DR CTD; 47251; -.
DR FlyBase; FBgn0010391; SrpRalpha.
DR VEuPathDB; VectorBase:FBgn0010391; -.
DR eggNOG; KOG0781; Eukaryota.
DR GeneTree; ENSGT00550000074936; -.
DR HOGENOM; CLU_009301_8_1_1; -.
DR InParanoid; Q9U5L1; -.
DR OMA; HLGWIDK; -.
DR OrthoDB; 5475029at2759; -.
DR PhylomeDB; Q9U5L1; -.
DR BioGRID-ORCS; 47251; 0 hits in 1 CRISPR screen.
DR GenomeRNAi; 47251; -.
DR PRO; PR:Q9U5L1; -.
DR Proteomes; UP000000803; Chromosome X.
DR Bgee; FBgn0010391; Expressed in spermathecum and 44 other cell types or tissues.
DR ExpressionAtlas; Q9U5L1; baseline and differential.
DR Genevisible; Q9U5L1; DM.
DR GO; GO:0012505; C:endomembrane system; HDA:FlyBase.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IDA:UniProtKB.
DR GO; GO:0005785; C:signal recognition particle receptor complex; IEA:InterPro.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR GO; GO:0003924; F:GTPase activity; IBA:GO_Central.
DR GO; GO:0003723; F:RNA binding; NAS:UniProtKB.
DR GO; GO:0005047; F:signal recognition particle binding; IBA:GO_Central.
DR GO; GO:0007409; P:axonogenesis; IEP:UniProtKB.
DR GO; GO:0006886; P:intracellular protein transport; IEA:InterPro.
DR GO; GO:0045047; P:protein targeting to ER; IBA:GO_Central.
DR GO; GO:0050708; P:regulation of protein secretion; IEP:UniProtKB.
DR GO; GO:0006614; P:SRP-dependent cotranslational protein targeting to membrane; IEA:InterPro.
DR CDD; cd14826; SR_alpha_SRX; 1.
DR CDD; cd17876; SRalpha_C; 1.
DR Gene3D; 3.30.450.60; -; 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 InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR011012; Longin-like_dom_sf.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR007222; Sig_recog_particle_rcpt_asu_N.
DR InterPro; IPR013822; Signal_recog_particl_SRP54_hlx.
DR InterPro; IPR036225; SRP/SRP_N.
DR InterPro; IPR000897; SRP54_GTPase_dom.
DR InterPro; IPR042101; SRP54_N_sf.
DR PANTHER; PTHR43134; SIGNAL RECOGNITION PARTICLE RECEPTOR SUBUNIT ALPHA; 1.
DR PANTHER; PTHR43134:SF1; SIGNAL RECOGNITION PARTICLE RECEPTOR SUBUNIT ALPHA; 1.
DR Pfam; PF04086; SRP-alpha_N; 1.
DR Pfam; PF00448; SRP54; 1.
DR Pfam; PF02881; SRP54_N; 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; SSF64356; SNARE-like; 1.
DR PROSITE; PS00300; SRP54; 1.
PE 1: Evidence at protein level;
KW Endoplasmic reticulum; GTP-binding; Membrane; Nucleotide-binding;
KW Phosphoprotein; Receptor; Reference proteome.
FT CHAIN 1..614
FT /note="Signal recognition particle receptor subunit alpha
FT homolog"
FT /id="PRO_0000101215"
FT REGION 119..244
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 268..290
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 396..613
FT /note="NG domain"
FT /evidence="ECO:0000250|UniProtKB:P08240"
FT COMPBIAS 128..144
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 145..159
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 183..224
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 268..282
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 402..409
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250, ECO:0000305"
FT BINDING 497..501
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250, ECO:0000305"
FT BINDING 565..568
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250, ECO:0000305"
FT MOD_RES 237
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 240
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 246
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 268
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 278
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 279
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT CONFLICT 410..413
FT /note="TNLA -> RC (in Ref. 4)"
FT /evidence="ECO:0000305"
FT CONFLICT 428
FT /note="I -> L (in Ref. 4)"
FT /evidence="ECO:0000305"
FT CONFLICT 450
FT /note="N -> H (in Ref. 4)"
FT /evidence="ECO:0000305"
FT CONFLICT 549
FT /note="D -> G (in Ref. 4; AAB27926)"
FT /evidence="ECO:0000305"
FT CONFLICT 556..558
FT /note="PHI -> RH (in Ref. 4; AAB27926)"
FT /evidence="ECO:0000305"
FT CONFLICT 567..573
FT /note="FDTIDDK -> LHTMQHD (in Ref. 4)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 614 AA; 67795 MW; 2679CDE81E257490 CRC64;
MLDFVVIFTK GGVVLWHSNA SGNSFASCIN SLIRGVILEE RNTEAKYYEE DHLAVQFKLD
NELDLVYAAI FQKVIKLNYL DGFLADMQAA FKEKYGDIRL GDDYDFDREY RRVLSAAEEA
SAKQVKAPKT MRSYNESQKS KKTVASMIQD DKKPVEKRVN IQEAPPPSKS QPSSPPTGSP
MDKIIMEKRR KLREKLTPTK KTSPSDSKSS KPEKAGKKPR VWDLGGNSKD AALLDRSRDS
PDDVQYQNIN SELVGTMQGV IRDLDVESED EADNEDASSE GEAEEQVQSK KGKRGGLLSY
FKGIVGAKTM SLADLQPALE KMRDHLISKN VASEIAAKLC DSVAASLDGK QMGTFDSIAS
QVKEALTESL VRILSPKRRI DIIRDALESK RNGRPYTIIF CGVNGVGKST NLAKICFWLI
ENDFNVLIAA CDTFRAGAVE QLRTHTRHLN ALHPAAKHDG RNMVQLYEKG YGKDAAGIAM
EAIKFAHDTR VDVVLVDTAG RMQDNEPLMR SLSKLIKVNN PDLVLFVGEA LVGNEAVDQL
VKFNQSLADY SSNENPHIID GIVLTKFDTI DDKVGAAISM TYITGQPIVF VGTGQTYADL
KAINVNAVVN SLMK
//
