ID SRPRA_MOUSE Reviewed; 636 AA.
AC Q9DBG7; Q8VC45; Q921H1;
DT 10-MAY-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 27-MAR-2024, entry version 165.
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:0000250|UniProtKB:P08240}; Synonyms=Srpr;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Liver, and Thymus;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Colon;
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 [3]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT "Large-scale phosphorylation analysis of mouse liver.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-295; SER-296 AND SER-297, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=18630941; DOI=10.1021/pr800223m;
RA Zhou H., Ye M., Dong J., Han G., Jiang X., Wu R., Zou H.;
RT "Specific phosphopeptide enrichment with immobilized titanium ion affinity
RT chromatography adsorbent for phosphoproteome analysis.";
RL J. Proteome Res. 7:3957-3967(2008).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-295; SER-296 AND SER-297, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA Thibault P.;
RT "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL Immunity 30:143-154(2009).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-295; SER-296; SER-297 AND
RP THR-303, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
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). {ECO:0000250|UniProtKB:P08240}.
CC -!- SUBUNIT: Heterodimer with SRPRB (By similarity). Interacts with the
CC signal recognition particle (SRP) complex subunit SRP54 (By
CC similarity). {ECO:0000250|UniProtKB:P08240}.
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 -!- 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=AAH12512.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AK004967; BAB23706.1; -; mRNA.
DR EMBL; AK038017; BAC29922.1; -; mRNA.
DR EMBL; BC012512; AAH12512.1; ALT_INIT; mRNA.
DR EMBL; BC021839; AAH21839.1; -; mRNA.
DR CCDS; CCDS22959.1; -.
DR RefSeq; NP_080406.1; NM_026130.1.
DR AlphaFoldDB; Q9DBG7; -.
DR SMR; Q9DBG7; -.
DR BioGRID; 212161; 11.
DR ComplexPortal; CPX-4622; Signal recognition particle receptor complex.
DR STRING; 10090.ENSMUSP00000034541; -.
DR iPTMnet; Q9DBG7; -.
DR PhosphoSitePlus; Q9DBG7; -.
DR SwissPalm; Q9DBG7; -.
DR EPD; Q9DBG7; -.
DR jPOST; Q9DBG7; -.
DR MaxQB; Q9DBG7; -.
DR PaxDb; 10090-ENSMUSP00000034541; -.
DR PeptideAtlas; Q9DBG7; -.
DR ProteomicsDB; 254561; -.
DR Pumba; Q9DBG7; -.
DR Antibodypedia; 32980; 174 antibodies from 22 providers.
DR DNASU; 67398; -.
DR Ensembl; ENSMUST00000034541.12; ENSMUSP00000034541.6; ENSMUSG00000032042.12.
DR GeneID; 67398; -.
DR KEGG; mmu:67398; -.
DR UCSC; uc009osy.1; mouse.
DR AGR; MGI:1914648; -.
DR CTD; 6734; -.
DR MGI; MGI:1914648; Srpr.
DR VEuPathDB; HostDB:ENSMUSG00000032042; -.
DR eggNOG; KOG0781; Eukaryota.
DR GeneTree; ENSGT00550000074936; -.
DR HOGENOM; CLU_009301_8_0_1; -.
DR InParanoid; Q9DBG7; -.
DR OMA; HLGWIDK; -.
DR OrthoDB; 5475029at2759; -.
DR PhylomeDB; Q9DBG7; -.
DR TreeFam; TF106189; -.
DR BRENDA; 3.6.5.4; 3474.
DR BioGRID-ORCS; 67398; 21 hits in 78 CRISPR screens.
DR ChiTaRS; Srpr; mouse.
DR PRO; PR:Q9DBG7; -.
DR Proteomes; UP000000589; Chromosome 9.
DR RNAct; Q9DBG7; Protein.
DR Bgee; ENSMUSG00000032042; Expressed in prostate gland ventral lobe and 263 other cell types or tissues.
DR ExpressionAtlas; Q9DBG7; baseline and differential.
DR Genevisible; Q9DBG7; MM.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IBA:GO_Central.
DR GO; GO:0016020; C:membrane; ISO: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:0005047; F:signal recognition particle binding; IBA:GO_Central.
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 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..636
FT /note="Signal recognition particle receptor subunit alpha"
FT /id="PRO_0000101214"
FT REGION 132..205
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 217..246
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 280..314
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 417..634
FT /note="NG domain"
FT /evidence="ECO:0000250|UniProtKB:P08240"
FT COMPBIAS 132..176
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 217..245
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 289..312
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 423..430
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 518..522
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 586..589
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT MOD_RES 177
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P08240"
FT MOD_RES 283
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P08240"
FT MOD_RES 295
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18630941,
FT ECO:0007744|PubMed:19144319, ECO:0007744|PubMed:21183079"
FT MOD_RES 296
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18630941,
FT ECO:0007744|PubMed:19144319, ECO:0007744|PubMed:21183079"
FT MOD_RES 297
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18630941,
FT ECO:0007744|PubMed:19144319, ECO:0007744|PubMed:21183079"
FT MOD_RES 303
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 576
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P08240"
FT CONFLICT 104
FT /note="L -> S (in Ref. 2; AAH21839)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 636 AA; 69623 MW; 19C7D33196CBE410 CRC64;
MLDFFTIFSK GGLVLWCFQG VSDSCTGPVN ALIRSVLLQE RGGNNSFTHE ALTLKYKLDN
QFELVFVVGF QKILTLTYVD KLIDDVHRLF RDKYRTEIQQ QSALSLLNGT FDFQNDFLRL
LREAEESSKI RAPTTMKKFE DSEKAKKPVR SMIETRGEKT KEKAKNNKKR GAKKEGSDGT
LATSKTAPAE KSGLSAGPEN GELSKEELIR RKREEFIQKH GKGLDKSSKS TKSDTPKEKG
KKAPRVWELG GCANKEVLDY STPTTNGTPE AALSEDINLI RGTGPGGQLQ DLDCSSSDDE
GATQNTKPSA TKGTLGGMFG MLKGLVGSKS LSREDMESVL DKMRDHLIAK NVAADIAVQL
CESVANKLEG KVMGTFSTVT STVKQALQES LVQILQPQRR VDMLRDIMDA QRRQRPYVVT
FCGVNGVGKS TNLAKISFWL LENGFSVLIA ACDTFRAGAV EQLRTHTRRL TALHPPEKHG
GRTMVQLFEK GYGKDAAGIA MEAIAFARNQ GFDVVLVDTA GRMQDNAPLM TALAKLITVN
TPDLVLFVGE ALVGNEAVDQ LVKFNRALAD HSMAQTPRLI DGIVLTKFDT IDDKVGAAIS
MTYITSKPIV FVGTGQTYCD LRSLNAKAVV AALMKA
//
