SRPRA_CANLF
ID SRPRA_CANLF Reviewed; 638 AA.
AC P06625;
DT 01-JAN-1988, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1990, sequence version 2.
DT 03-AUG-2022, entry version 144.
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 Canis lupus familiaris (Dog) (Canis familiaris).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Caniformia; Canidae; Canis.
OX NCBI_TaxID=9615;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=2999608; DOI=10.1038/318334a0;
RA Lauffer L., Garcia P.D., Harkins R.N., Coussens L., Ullrich A., Walter P.;
RT "Topology of signal recognition particle receptor in endoplasmic reticulum
RT membrane.";
RL Nature 318:334-338(1985).
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; X03184; CAA26945.1; -; mRNA.
DR PIR; A24570; A24570.
DR AlphaFoldDB; P06625; -.
DR SMR; P06625; -.
DR STRING; 9615.ENSCAFP00000036484; -.
DR PaxDb; P06625; -.
DR eggNOG; KOG0781; Eukaryota.
DR InParanoid; P06625; -.
DR BRENDA; 3.6.5.4; 1153.
DR Proteomes; UP000002254; Unplaced.
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..638
FT /note="Signal recognition particle receptor subunit alpha"
FT /id="PRO_0000101212"
FT REGION 129..205
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 218..245
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 262..315
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 419..636
FT /note="NG domain"
FT /evidence="ECO:0000250|UniProtKB:P08240"
FT COMPBIAS 129..176
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 290..313
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:0000250|UniProtKB:P08240"
FT MOD_RES 284
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P08240"
FT MOD_RES 296
FT /note="Phosphoserine"
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 473
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P08240"
FT MOD_RES 578
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P08240"
SQ SEQUENCE 638 AA; 69672 MW; AD88CE554ACC2BC6 CRC64;
MLDFFTIFSK GGLVLWCFQG VSDSCTGPVN ALIRSVLLQE RGGNNSFTHE ALTLKYKLDN
QFELVFVVGF QKILTLTYVD KLIDDVHRLF RDKYRTEIQQ QSALSLLNGT FDFQNDFLRL
LREREESSKI RAPTTMKKFE DSEKAKKPVR SMIETRGEKP KEKAKNSKKK GAKKESSDGP
LATGKAVPAE KSGLPAGPEN GVELSKEELI RRKREEFIQK HGRGLEKSSK STKSDAPKEK
GKKAPRVWAL GGCANKEVLD YSAPTTNGAP DAAPPEDINL IRGTGPGGQL QDLDCSSSDD
EETAQNASKP SATKGTLGGM FGMLKGLVGS KSLSREDMES VLDKMRDHLI AKNVAADIAV
QLCESVANKL EGKVMGTFST VTSTVKQALQ ESLVQILQPQ RRVDMLRDIM DAQRHQRPYV
VTFCGVNGVG KSTNLAKISF WLLENGFSVL IAACDTFRAG AVEHVRTHTR RLSALHPPEK
HAGPTMVQLF EKGYGKDAAG IAMEAIAFAR NQGFDVVLVD TAGRMQDNAP LMTALAKLIT
VNTPDLVLFV GEALVGNEAV DQLVKFNRAL ADHSMAQTPR LIDGIVLTKF DTIDDKVGAA
ISMTYITSKP IVFVGTGQTY CDLRSLNAKA VVAALMKA
