SRPRA_BOVIN
ID SRPRA_BOVIN Reviewed; 639 AA.
AC Q3MHE8;
DT 03-APR-2007, integrated into UniProtKB/Swiss-Prot.
DT 25-OCT-2005, sequence version 1.
DT 03-AUG-2022, entry version 104.
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 Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Hereford; TISSUE=Uterus;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
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}.
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DR EMBL; BC105264; AAI05265.1; -; mRNA.
DR RefSeq; NP_001068590.1; NM_001075122.1.
DR AlphaFoldDB; Q3MHE8; -.
DR SMR; Q3MHE8; -.
DR STRING; 9913.ENSBTAP00000018762; -.
DR PaxDb; Q3MHE8; -.
DR PRIDE; Q3MHE8; -.
DR Ensembl; ENSBTAT00000018762; ENSBTAP00000018762; ENSBTAG00000014105.
DR GeneID; 281504; -.
DR KEGG; bta:281504; -.
DR CTD; 6734; -.
DR VEuPathDB; HostDB:ENSBTAG00000014105; -.
DR VGNC; VGNC:56282; SRPRA.
DR eggNOG; KOG0781; Eukaryota.
DR GeneTree; ENSGT00550000074936; -.
DR HOGENOM; CLU_009301_8_0_1; -.
DR InParanoid; Q3MHE8; -.
DR OMA; VMQARNF; -.
DR OrthoDB; 804839at2759; -.
DR Proteomes; UP000009136; Chromosome 29.
DR Bgee; ENSBTAG00000014105; Expressed in saliva-secreting gland and 104 other tissues.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IBA:GO_Central.
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; IBA:GO_Central.
DR GO; GO:0006605; P:protein targeting; IBA:GO_Central.
DR GO; GO:0045047; P:protein targeting to ER; IBA:GO_Central.
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 SMART; SM00963; SRP54_N; 1.
DR SUPFAM; SSF47364; SSF47364; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR SUPFAM; SSF64356; SSF64356; 1.
DR PROSITE; PS00300; SRP54; 1.
PE 2: Evidence at transcript level;
KW Endoplasmic reticulum; GTP-binding; Membrane; Nucleotide-binding;
KW Phosphoprotein; Receptor; Reference proteome.
FT CHAIN 1..639
FT /note="Signal recognition particle receptor subunit alpha"
FT /id="PRO_0000282927"
FT REGION 132..317
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 420..637
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 202..246
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 291..315
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 426..433
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 521..525
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 589..592
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT MOD_RES 178
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P08240"
FT MOD_RES 285
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P08240"
FT MOD_RES 297
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P08240"
FT MOD_RES 298
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P08240"
FT MOD_RES 299
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P08240"
FT MOD_RES 474
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P08240"
FT MOD_RES 579
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P08240"
SQ SEQUENCE 639 AA; 69896 MW; 29052DEA87E08845 CRC64;
MLDFFTIFSK GGLVLWCFQG VSDSCTGPVN ALIRSVLLQE RGGNNSFTHE ALTLKYKLDN
QFELVFVVGF QKILTLTYVD KLIDDVHRLF RDKYRTEIQQ QSALSLLNGT FDFQNDFLRL
LREAEESSKI RAPTTMKKFE DSEKAKKPVR SMIETRGEKP KEKAKNNKKN KGAKKEGSDG
PLATSKAAPA EKSGLPVGPE NGEELSKEEQ IRRKREEFIQ KHGRGMEKSS KSSKSDAPKE
KGKKAPRVWA LGGSANKEVL DYSTPTTNGA PEAAPPEDIN LIRGTGPGRQ LQDLDCSSSD
DEGAAQNSTK PSATKGTLGG MFGMLKGLVG SKSLTREDME SVLDKMRDHL IAKNVAADIA
VQLCESVANK LEGKVMGTFS TVTSTVKQAL QESLVQILQP QRRVDMLRDI MDAQRHQRPY
VVTFCGVNGV GKSTNLAKIS FWLLENGFSV LIAACDTFRA GAVEQLRTHT RRLSALHPPE
KHGGRTMVQL FEKGYGKDAA GIAMEAIAFA RNQGFDVVLV DTAGRMQDNA PLMTALAKLI
TVNTPDLVLF VGEALVGNEA VDQLVKFNRA LADHSMAQTP RLIDGIVLTK FDTIDDKVGA
AISMTYITSK PIVFVGTGQT YCDLRSLNAK AVVAALMKA
