SRPRA_DICDI
ID SRPRA_DICDI Reviewed; 615 AA.
AC Q54ZR7; Q76P14;
DT 08-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 24-MAY-2005, sequence version 1.
DT 03-AUG-2022, entry version 112.
DE RecName: Full=Signal recognition particle receptor subunit alpha;
DE Short=SR-alpha;
DE Short=Signal recognition particle receptor;
DE AltName: Full=Docking protein alpha;
DE Short=DP-alpha;
GN Name=srpra {ECO:0000250|UniProtKB:P08240}; ORFNames=DDB_G0277377;
OS Dictyostelium discoideum (Slime mold).
OC Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales;
OC Dictyosteliaceae; Dictyostelium.
OX NCBI_TaxID=44689;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AX4;
RX PubMed=12097910; DOI=10.1038/nature00847;
RA Gloeckner G., Eichinger L., Szafranski K., Pachebat J.A., Bankier A.T.,
RA Dear P.H., Lehmann R., Baumgart C., Parra G., Abril J.F., Guigo R.,
RA Kumpf K., Tunggal B., Cox E.C., Quail M.A., Platzer M., Rosenthal A.,
RA Noegel A.A.;
RT "Sequence and analysis of chromosome 2 of Dictyostelium discoideum.";
RL Nature 418:79-85(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AX4;
RX PubMed=15875012; DOI=10.1038/nature03481;
RA Eichinger L., Pachebat J.A., Gloeckner G., Rajandream M.A., Sucgang R.,
RA Berriman M., Song J., Olsen R., Szafranski K., Xu Q., Tunggal B.,
RA Kummerfeld S., Madera M., Konfortov B.A., Rivero F., Bankier A.T.,
RA Lehmann R., Hamlin N., Davies R., Gaudet P., Fey P., Pilcher K., Chen G.,
RA Saunders D., Sodergren E.J., Davis P., Kerhornou A., Nie X., Hall N.,
RA Anjard C., Hemphill L., Bason N., Farbrother P., Desany B., Just E.,
RA Morio T., Rost R., Churcher C.M., Cooper J., Haydock S., van Driessche N.,
RA Cronin A., Goodhead I., Muzny D.M., Mourier T., Pain A., Lu M., Harper D.,
RA Lindsay R., Hauser H., James K.D., Quiles M., Madan Babu M., Saito T.,
RA Buchrieser C., Wardroper A., Felder M., Thangavelu M., Johnson D.,
RA Knights A., Loulseged H., Mungall K.L., Oliver K., Price C., Quail M.A.,
RA Urushihara H., Hernandez J., Rabbinowitsch E., Steffen D., Sanders M.,
RA Ma J., Kohara Y., Sharp S., Simmonds M.N., Spiegler S., Tivey A.,
RA Sugano S., White B., Walker D., Woodward J.R., Winckler T., Tanaka Y.,
RA Shaulsky G., Schleicher M., Weinstock G.M., Rosenthal A., Cox E.C.,
RA Chisholm R.L., Gibbs R.A., Loomis W.F., Platzer M., Kay R.R.,
RA Williams J.G., Dear P.H., Noegel A.A., Barrell B.G., Kuspa A.;
RT "The genome of the social amoeba Dictyostelium discoideum.";
RL Nature 435:43-57(2005).
CC -!- FUNCTION: Component of the SRP (signal recognition particle) receptor
CC (SR) (By similarity). Ensures, in conjunction with the signal
CC recognition particle, the correct targeting of the nascent secretory
CC proteins to the endoplasmic reticulum membrane system (By similarity).
CC Forms a guanosine 5'-triphosphate (GTP)-dependent complex with the SRP
CC subunit srp54 (By similarity). SRP receptor compaction and GTPase
CC rearrangement drive SRP-mediated cotranslational protein translocation
CC into the ER (By similarity). {ECO:0000250|UniProtKB:P08240}.
CC -!- SUBUNIT: Heterodimer of an alpha and a beta chain.
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 srprb, which contains a bona fide
CC transmembrane domain. {ECO:0000250|UniProtKB:P32916}.
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}.
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DR EMBL; AAFI02000019; EAL68875.1; -; Genomic_DNA.
DR RefSeq; XP_642799.1; XM_637707.1.
DR AlphaFoldDB; Q54ZR7; -.
DR SMR; Q54ZR7; -.
DR STRING; 44689.DDB0252680; -.
DR PaxDb; Q54ZR7; -.
DR EnsemblProtists; EAL68875; EAL68875; DDB_G0277377.
DR GeneID; 8620992; -.
DR KEGG; ddi:DDB_G0277377; -.
DR dictyBase; DDB_G0277377; srpR.
DR eggNOG; KOG0781; Eukaryota.
DR HOGENOM; CLU_009301_8_1_1; -.
DR InParanoid; Q54ZR7; -.
DR OMA; VMQARNF; -.
DR PhylomeDB; Q54ZR7; -.
DR PRO; PR:Q54ZR7; -.
DR Proteomes; UP000002195; Chromosome 2.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; ISS:UniProtKB.
DR GO; GO:0016020; C:membrane; IBA:GO_Central.
DR GO; GO:0005785; C:signal recognition particle receptor complex; 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:0005047; F:signal recognition particle binding; ISS:UniProtKB.
DR GO; GO:0006605; P:protein targeting; IBA:GO_Central.
DR GO; GO:0045047; P:protein targeting to ER; ISS:UniProtKB.
DR GO; GO:0006614; P:SRP-dependent cotranslational protein targeting to membrane; IEA:InterPro.
DR Gene3D; 1.20.120.140; -; 1.
DR Gene3D; 3.40.50.300; -; 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 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 SUPFAM; SSF47364; SSF47364; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR SUPFAM; SSF64356; SSF64356; 1.
DR PROSITE; PS00300; SRP54; 1.
PE 3: Inferred from homology;
KW Endoplasmic reticulum; GTP-binding; Membrane; Nucleotide-binding; Receptor;
KW Reference proteome.
FT CHAIN 1..615
FT /note="Signal recognition particle receptor subunit alpha"
FT /id="PRO_0000328302"
FT REGION 131..257
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 408..614
FT /note="NG domain"
FT /evidence="ECO:0000250|UniProtKB:P08240"
FT COMPBIAS 139..186
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 207..227
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 414..421
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 496..500
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 566..569
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
SQ SEQUENCE 615 AA; 69032 MW; CE7E098D820C06AE CRC64;
MLDSFTILTK GGIVLWSKEF AKIKGSPINS LIKKVLLEER SAETSFQIDS YSLKWTFSNE
FDLIFVVVYQ KIFTLLYIEE LLTTVKKRFI KMYKDLLLKL KESSDFIIVD KFQEFNFEVI
LEDVENRSKL QQTSNSAPKK YEDTDKGKLV KDQKNERAIK EGRVEKVKRK EQEKKEKAER
RKQNKANNIN DISSDDDSDD SDSSSGSDSE ENSNGATKNQ QTDVARIENS GYKKKVKDTP
DKQASSSTGK KARTWEDGKL SKKELEALNR SDNSNGTEIV REKIQKFNID MDVSSSDDDD
EEEAKPVSGF MKYFNVLTGN RVIDKQDLEP ILADFKLHLT KKNVAPDVAD KIVQSIGTGL
EGKKLATFQG VTSVVKQQME DTITRILTPK RNIDILREVQ AVKGKRPYSI VFSGVNGVGK
STNLAKVCYW LTANGYKCML AACDTFRSGA IEQLKTHADR LNVHLFERGY SKDAASVAQD
AIAFAKDTGY DVVLIDTTGR MQNNEPLMKA LSKLVNQNNV DLVLFVGEAL VGNDGVDQLT
KFDKSLSLLA NTTQTHIRTI DGIILTKFDT IDDKVGAAIS MVYSTGHPIL FLGTGQNYTD
LKRMNIKSVV KSLLH
