ID SRPRA_HUMAN Reviewed; 638 AA.
AC P08240; A6NIB3; B2R5Z8; B4E0H3; E9PJS4; Q9BVJ4;
DT 01-AUG-1988, integrated into UniProtKB/Swiss-Prot.
DT 02-MAY-2002, sequence version 2.
DT 27-MAR-2024, entry version 219.
DE RecName: Full=Signal recognition particle receptor subunit alpha;
DE Short=SR-alpha;
DE AltName: Full=Docking protein alpha;
DE Short=DP-alpha;
GN Name=SRPRA {ECO:0000312|HGNC:HGNC:11307}; Synonyms=SRPR;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RX PubMed=3340536; DOI=10.1093/nar/16.1.361;
RA Hortsch M., Labeit S., Meyer D.I.;
RT "Complete cDNA sequence coding for human docking protein.";
RL Nucleic Acids Res. 16:361-362(1988).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Amygdala, and Thymus;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16554811; DOI=10.1038/nature04632;
RA Taylor T.D., Noguchi H., Totoki Y., Toyoda A., Kuroki Y., Dewar K.,
RA Lloyd C., Itoh T., Takeda T., Kim D.-W., She X., Barlow K.F., Bloom T.,
RA Bruford E., Chang J.L., Cuomo C.A., Eichler E., FitzGerald M.G.,
RA Jaffe D.B., LaButti K., Nicol R., Park H.-S., Seaman C., Sougnez C.,
RA Yang X., Zimmer A.R., Zody M.C., Birren B.W., Nusbaum C., Fujiyama A.,
RA Hattori M., Rogers J., Lander E.S., Sakaki Y.;
RT "Human chromosome 11 DNA sequence and analysis including novel gene
RT identification.";
RL Nature 440:497-500(2006).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Lung, Muscle, and Placenta;
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).
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=15592455; DOI=10.1038/nbt1046;
RA Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H.,
RA Zha X.-M., Polakiewicz R.D., Comb M.J.;
RT "Immunoaffinity profiling of tyrosine phosphorylation in cancer cells.";
RL Nat. Biotechnol. 23:94-101(2005).
RN [7]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.;
RT "Global, in vivo, and site-specific phosphorylation dynamics in signaling
RT networks.";
RL Cell 127:635-648(2006).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-296; SER-297 AND SER-298, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [9]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [10]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [11]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22223895; DOI=10.1074/mcp.m111.015131;
RA Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T.,
RA Giglione C.;
RT "Comparative large-scale characterisation of plant vs. mammal proteins
RT reveals similar and idiosyncratic N-alpha acetylation features.";
RL Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
RN [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-177; SER-473 AND THR-578, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-284; SER-296; SER-297 AND
RP SER-298, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [14]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25944712; DOI=10.1002/pmic.201400617;
RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D.,
RA Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
RT "N-terminome analysis of the human mitochondrial proteome.";
RL Proteomics 15:2519-2524(2015).
RN [15]
RP INTERACTION WITH ZIKA VIRUS FRENCH POLYNESIA 10087PF/2013 NS4A; ZIKA VIRUS
RP MR-766 NS4A AND DENGUE VIRUS DENV2 16681 NS4A.
RX PubMed=30550790; DOI=10.1016/j.cell.2018.11.028;
RA Shah P.S., Link N., Jang G.M., Sharp P.P., Zhu T., Swaney D.L.,
RA Johnson J.R., Von Dollen J., Ramage H.R., Satkamp L., Newton B.,
RA Huettenhain R., Petit M.J., Baum T., Everitt A., Laufman O., Tassetto M.,
RA Shales M., Stevenson E., Iglesias G.N., Shokat L., Tripathi S.,
RA Balasubramaniam V., Webb L.G., Aguirre S., Willsey A.J., Garcia-Sastre A.,
RA Pollard K.S., Cherry S., Gamarnik A.V., Marazzi I., Taunton J.,
RA Fernandez-Sesma A., Bellen H.J., Andino R., Krogan N.J.;
RT "Comparative Flavivirus-Host Protein Interaction Mapping Reveals Mechanisms
RT of Dengue and Zika Virus Pathogenesis.";
RL Cell 175:1931-1945(2018).
RN [16]
RP X-RAY CRYSTALLOGRAPHY (2.45 ANGSTROMS) OF 3-176 IN COMPLEX WITH SRPRB,
RP FUNCTION, AND SUBUNIT.
RX PubMed=16439358; DOI=10.1074/jbc.m512415200;
RA Schlenker O., Hendricks A., Sinning I., Wild K.;
RT "The structure of the mammalian signal recognition particle (SRP) receptor
RT as prototype for the interaction of small GTPases with Longin domains.";
RL J. Biol. Chem. 281:8898-8906(2006).
RN [17]
RP STRUCTURE BY ELECTRON MICROSCOPY (7.4 ANGSTROMS) OF 3-176 OF SIGNAL
RP RECOGNITION PARTICLE IN COMPLEX WITH THE 80S RIBOSOME AND THE SRP RECEPTOR,
RP AND FUNCTION.
RX PubMed=16675701; DOI=10.1126/science.1124864;
RA Halic M., Gartmann M., Schlenker O., Mielke T., Pool M.R., Sinning I.,
RA Beckmann R.;
RT "Signal recognition particle receptor exposes the ribosomal translocon
RT binding site.";
RL Science 312:745-747(2006).
RN [18] {ECO:0007744|PDB:7NFX}
RP STRUCTURE BY ELECTRON MICROSCOPY (3.20 ANGSTROMS) OF SIGNAL RECOGNITION
RP PARTICLE IN COMPLEX WITH RIBOSOME NASCENT CHAIN COMPLEX AND THE SRP
RP RECEPTOR, FUNCTION, INTERACTION WITH SRP54, AND MUTAGENESIS OF ARG-407.
RX PubMed=34020957; DOI=10.1126/sciadv.abg0942;
RA Lee J.H., Jomaa A., Jomaa A., Chung S., Hwang Fu Y.H., Qian R., Sun X.,
RA Hsieh H.H., Chandrasekar S., Bi X., Mattei S., Boehringer D., Weiss S.,
RA Ban N., Shan S.O.;
RT "Receptor compaction and GTPase rearrangement drive SRP-mediated
RT cotranslational protein translocation into the ER.";
RL Sci. Adv. 7:942-942(2021).
CC -!- FUNCTION: Component of the signal recognition particle (SRP) complex
CC receptor (SR) (PubMed:16439358). Ensures, in conjunction with the SRP
CC complex, the correct targeting of the nascent secretory proteins to the
CC endoplasmic reticulum membrane system (PubMed:16675701,
CC PubMed:34020957). Forms a guanosine 5'-triphosphate (GTP)-dependent
CC complex with the SRP subunit SRP54 (PubMed:34020957). SRP receptor
CC compaction and GTPase rearrangement drive SRP-mediated cotranslational
CC protein translocation into the ER (PubMed:34020957).
CC {ECO:0000269|PubMed:16439358, ECO:0000269|PubMed:16675701,
CC ECO:0000269|PubMed:34020957}.
CC -!- SUBUNIT: Heterodimer with SRPRB (PubMed:16439358). Interacts with the
CC signal recognition particle (SRP) complex subunit SRP54
CC (PubMed:34020957). {ECO:0000269|PubMed:16439358,
CC ECO:0000269|PubMed:34020957}.
CC -!- SUBUNIT: (Microbial infection) May interact with Zika virus strain Mr-
CC 766 non-structural protein 4A/NS4A (PubMed:30550790). May interact with
CC Zika virus French Polynesia 10087PF/2013 non-structural protein 4A/NS4A
CC (PubMed:30550790). {ECO:0000269|PubMed:30550790}.
CC -!- SUBUNIT: (Microbial infection) May interact with Dengue virus DENV2
CC 16681 non-structural protein 4A/NS4A. {ECO:0000269|PubMed:30550790}.
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 SR-beta, which contains a bona
CC fide transmembrane domain. {ECO:0000250|UniProtKB:P32916}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=P08240-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P08240-2; Sequence=VSP_046055;
CC -!- DOMAIN: The NG domain region, also named G domain, is a special
CC guanosine triphosphatase (GTPase) domain, which forms a guanosine 5'-
CC triphosphate (GTP)-dependent complex with a homologous NG domain in the
CC signal recognition particle (SRP) complex subunit SRP54
CC (PubMed:34020957). 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 (PubMed:34020957).
CC GTPase induced rearrangement of SR drives SRP-mediated cotranslational
CC protein translocation into the ER (PubMed:34020957).
CC {ECO:0000269|PubMed:34020957}.
CC -!- SIMILARITY: Belongs to the GTP-binding SRP family. {ECO:0000305}.
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DR EMBL; X06272; CAA29608.1; -; mRNA.
DR EMBL; AK303379; BAG64435.1; -; mRNA.
DR EMBL; AK312377; BAG35295.1; -; mRNA.
DR EMBL; AP001318; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471065; EAW67686.1; -; Genomic_DNA.
DR EMBL; BC001162; AAH01162.1; -; mRNA.
DR EMBL; BC009110; AAH09110.1; -; mRNA.
DR EMBL; BC013583; AAH13583.1; -; mRNA.
DR CCDS; CCDS31717.1; -. [P08240-1]
DR CCDS; CCDS53722.1; -. [P08240-2]
DR PIR; A29440; A29440.
DR RefSeq; NP_001171313.1; NM_001177842.1. [P08240-2]
DR RefSeq; NP_003130.2; NM_003139.3. [P08240-1]
DR PDB; 2FH5; X-ray; 2.45 A; A=3-176.
DR PDB; 2GO5; EM; 7.40 A; 1=3-176.
DR PDB; 5L3Q; X-ray; 3.20 A; B/D=1-638.
DR PDB; 6Y32; X-ray; 2.60 A; B/D/F/H=332-638.
DR PDB; 7NFX; EM; 3.20 A; y=1-638.
DR PDBsum; 2FH5; -.
DR PDBsum; 2GO5; -.
DR PDBsum; 5L3Q; -.
DR PDBsum; 6Y32; -.
DR PDBsum; 7NFX; -.
DR AlphaFoldDB; P08240; -.
DR EMDB; EMD-12303; -.
DR SMR; P08240; -.
DR BioGRID; 112612; 302.
DR ComplexPortal; CPX-630; Signal recognition particle receptor complex.
DR IntAct; P08240; 100.
DR MINT; P08240; -.
DR STRING; 9606.ENSP00000328023; -.
DR ChEMBL; CHEMBL4105934; -.
DR GlyGen; P08240; 5 sites, 1 O-linked glycan (4 sites).
DR iPTMnet; P08240; -.
DR MetOSite; P08240; -.
DR PhosphoSitePlus; P08240; -.
DR SwissPalm; P08240; -.
DR BioMuta; SRPRA; -.
DR DMDM; 20455516; -.
DR EPD; P08240; -.
DR jPOST; P08240; -.
DR MassIVE; P08240; -.
DR MaxQB; P08240; -.
DR PaxDb; 9606-ENSP00000328023; -.
DR PeptideAtlas; P08240; -.
DR ProteomicsDB; 21234; -.
DR ProteomicsDB; 52097; -. [P08240-1]
DR Pumba; P08240; -.
DR Antibodypedia; 32980; 174 antibodies from 22 providers.
DR DNASU; 6734; -.
DR Ensembl; ENST00000332118.11; ENSP00000328023.5; ENSG00000182934.12. [P08240-1]
DR Ensembl; ENST00000532259.1; ENSP00000435508.1; ENSG00000182934.12. [P08240-2]
DR GeneID; 6734; -.
DR KEGG; hsa:6734; -.
DR MANE-Select; ENST00000332118.11; ENSP00000328023.5; NM_003139.4; NP_003130.2.
DR UCSC; uc001qdh.4; human. [P08240-1]
DR AGR; HGNC:11307; -.
DR CTD; 6734; -.
DR DisGeNET; 6734; -.
DR GeneCards; SRPRA; -.
DR HGNC; HGNC:11307; SRPRA.
DR HPA; ENSG00000182934; Low tissue specificity.
DR MalaCards; SRPRA; -.
DR MIM; 182180; gene.
DR neXtProt; NX_P08240; -.
DR OpenTargets; ENSG00000182934; -.
DR PharmGKB; PA36131; -.
DR VEuPathDB; HostDB:ENSG00000182934; -.
DR eggNOG; KOG0781; Eukaryota.
DR GeneTree; ENSGT00550000074936; -.
DR HOGENOM; CLU_009301_8_0_1; -.
DR InParanoid; P08240; -.
DR OMA; HLGWIDK; -.
DR OrthoDB; 5475029at2759; -.
DR PhylomeDB; P08240; -.
DR TreeFam; TF106189; -.
DR BRENDA; 3.6.5.4; 2681.
DR PathwayCommons; P08240; -.
DR Reactome; R-HSA-1799339; SRP-dependent cotranslational protein targeting to membrane.
DR Reactome; R-HSA-381038; XBP1(S) activates chaperone genes.
DR SignaLink; P08240; -.
DR SIGNOR; P08240; -.
DR BioGRID-ORCS; 6734; 598 hits in 1145 CRISPR screens.
DR ChiTaRS; SRPRA; human.
DR EvolutionaryTrace; P08240; -.
DR GenomeRNAi; 6734; -.
DR Pharos; P08240; Tchem.
DR PRO; PR:P08240; -.
DR Proteomes; UP000005640; Chromosome 11.
DR RNAct; P08240; Protein.
DR Bgee; ENSG00000182934; Expressed in parotid gland and 205 other cell types or tissues.
DR Genevisible; P08240; HS.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IBA:GO_Central.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0016020; C:membrane; IDA:MGI.
DR GO; GO:0005785; C:signal recognition particle receptor complex; EXP:ComplexPortal.
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; HDA:UniProtKB.
DR GO; GO:0005047; F:signal recognition particle binding; IBA:GO_Central.
DR GO; GO:0006613; P:cotranslational protein targeting to membrane; TAS:ProtInc.
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:0006617; P:SRP-dependent cotranslational protein targeting to membrane, signal sequence recognition; NAS:ComplexPortal.
DR CDD; cd14826; SR_alpha_SRX; 1.
DR CDD; cd17876; SRalpha_C; 1.
DR DisProt; DP00893; -.
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 3D-structure; Alternative splicing; Endoplasmic reticulum; GTP-binding;
KW Membrane; Nucleotide-binding; Phosphoprotein; Receptor; Reference proteome.
FT CHAIN 1..638
FT /note="Signal recognition particle receptor subunit alpha"
FT /id="PRO_0000101213"
FT REGION 132..244
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 283..316
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 419..636
FT /note="NG domain"
FT /evidence="ECO:0000303|PubMed:34020957"
FT COMPBIAS 132..176
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 204..244
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 283..314
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 425..432
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 520..524
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 588..591
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT MOD_RES 177
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 284
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 296
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:24275569"
FT MOD_RES 297
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:24275569"
FT MOD_RES 298
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:24275569"
FT MOD_RES 473
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 578
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT VAR_SEQ 40..67
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_046055"
FT MUTAGEN 407
FT /note="R->A: Reduced SR compaction. Impaired interaction
FT with SRP. Impaired detachement from ribosome. Does not
FT impair GTP hydrolysis by the SRP-SR complex."
FT /evidence="ECO:0000269|PubMed:34020957"
FT CONFLICT 81
FT /note="K -> R (in Ref. 1; CAA29608)"
FT /evidence="ECO:0000305"
FT CONFLICT 201
FT /note="G -> E (in Ref. 1; CAA29608)"
FT /evidence="ECO:0000305"
FT CONFLICT 306..307
FT /note="NS -> TL (in Ref. 1; CAA29608)"
FT /evidence="ECO:0000305"
FT CONFLICT 632
FT /note="V -> L (in Ref. 2; BAG64435)"
FT /evidence="ECO:0000305"
FT STRAND 3..9
FT /evidence="ECO:0007829|PDB:2FH5"
FT STRAND 12..19
FT /evidence="ECO:0007829|PDB:2FH5"
FT TURN 20..22
FT /evidence="ECO:0007829|PDB:2FH5"
FT HELIX 28..35
FT /evidence="ECO:0007829|PDB:2FH5"
FT HELIX 37..39
FT /evidence="ECO:0007829|PDB:2FH5"
FT STRAND 53..59
FT /evidence="ECO:0007829|PDB:2FH5"
FT TURN 60..63
FT /evidence="ECO:0007829|PDB:2FH5"
FT STRAND 64..71
FT /evidence="ECO:0007829|PDB:2FH5"
FT HELIX 73..75
FT /evidence="ECO:0007829|PDB:2FH5"
FT HELIX 76..93
FT /evidence="ECO:0007829|PDB:2FH5"
FT HELIX 95..99
FT /evidence="ECO:0007829|PDB:2FH5"
FT STRAND 100..102
FT /evidence="ECO:0007829|PDB:2FH5"
FT HELIX 104..107
FT /evidence="ECO:0007829|PDB:2FH5"
FT HELIX 114..127
FT /evidence="ECO:0007829|PDB:2FH5"
FT HELIX 332..351
FT /evidence="ECO:0007829|PDB:6Y32"
FT HELIX 356..370
FT /evidence="ECO:0007829|PDB:6Y32"
FT HELIX 378..397
FT /evidence="ECO:0007829|PDB:6Y32"
FT HELIX 405..415
FT /evidence="ECO:0007829|PDB:6Y32"
FT STRAND 419..424
FT /evidence="ECO:0007829|PDB:6Y32"
FT HELIX 431..444
FT /evidence="ECO:0007829|PDB:6Y32"
FT STRAND 449..454
FT /evidence="ECO:0007829|PDB:6Y32"
FT HELIX 461..472
FT /evidence="ECO:0007829|PDB:6Y32"
FT HELIX 473..475
FT /evidence="ECO:0007829|PDB:6Y32"
FT HELIX 478..481
FT /evidence="ECO:0007829|PDB:6Y32"
FT STRAND 486..490
FT /evidence="ECO:0007829|PDB:6Y32"
FT STRAND 494..496
FT /evidence="ECO:0007829|PDB:6Y32"
FT HELIX 498..512
FT /evidence="ECO:0007829|PDB:6Y32"
FT STRAND 515..521
FT /evidence="ECO:0007829|PDB:6Y32"
FT HELIX 529..542
FT /evidence="ECO:0007829|PDB:6Y32"
FT STRAND 545..552
FT /evidence="ECO:0007829|PDB:6Y32"
FT HELIX 558..572
FT /evidence="ECO:0007829|PDB:6Y32"
FT STRAND 576..578
FT /evidence="ECO:0007829|PDB:6Y32"
FT STRAND 584..588
FT /evidence="ECO:0007829|PDB:6Y32"
FT HELIX 590..592
FT /evidence="ECO:0007829|PDB:5L3Q"
FT HELIX 599..606
FT /evidence="ECO:0007829|PDB:6Y32"
FT STRAND 611..615
FT /evidence="ECO:0007829|PDB:6Y32"
FT STRAND 617..619
FT /evidence="ECO:0007829|PDB:6Y32"
FT HELIX 628..637
FT /evidence="ECO:0007829|PDB:6Y32"
SQ SEQUENCE 638 AA; 69811 MW; 967F943CEE3FA79E CRC64;
MLDFFTIFSK GGLVLWCFQG VSDSCTGPVN ALIRSVLLQE RGGNNSFTHE ALTLKYKLDN
QFELVFVVGF QKILTLTYVD KLIDDVHRLF RDKYRTEIQQ QSALSLLNGT FDFQNDFLRL
LREAEESSKI RAPTTMKKFE DSEKAKKPVR SMIETRGEKP KEKAKNSKKK GAKKEGSDGP
LATSKPVPAE KSGLPVGPEN GVELSKEELI RRKREEFIQK HGRGMEKSNK STKSDAPKEK
GKKAPRVWEL GGCANKEVLD YSTPTTNGTP EAALSEDINL IRGTGSGGQL QDLDCSSSDD
EGAAQNSTKP SATKGTLGGM FGMLKGLVGS KSLSREDMES VLDKMRDHLI AKNVAADIAV
QLCESVANKL EGKVMGTFST VTSTVKQALQ ESLVQILQPQ RRVDMLRDIM DAQRRQRPYV
VTFCGVNGVG KSTNLAKISF WLLENGFSVL IAACDTFRAG AVEQLRTHTR RLSALHPPEK
HGGRTMVQLF EKGYGKDAAG IAMEAIAFAR NQGFDVVLVD TAGRMQDNAP LMTALAKLIT
VNTPDLVLFV GEALVGNEAV DQLVKFNRAL ADHSMAQTPR LIDGIVLTKF DTIDDKVGAA
ISMTYITSKP IVFVGTGQTY CDLRSLNAKA VVAALMKA
//
