SRPR_SCHPO
ID SRPR_SCHPO Reviewed; 547 AA.
AC O43032;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1998, sequence version 1.
DT 03-AUG-2022, entry version 139.
DE RecName: Full=Signal recognition particle receptor subunit alpha homolog;
DE Short=SR-alpha;
DE AltName: Full=Docking protein alpha;
DE Short=DP-alpha;
GN Name=srp101; ORFNames=SPBC3B9.03;
OS Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC Schizosaccharomyces.
OX NCBI_TaxID=284812;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=972 / ATCC 24843;
RX PubMed=11859360; DOI=10.1038/nature724;
RA Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.,
RA Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S.,
RA Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S.,
RA Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D.,
RA Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P.,
RA Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K.,
RA O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M.,
RA Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N.,
RA Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A.,
RA Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R.,
RA Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M.,
RA Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A.,
RA Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A.,
RA Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H.,
RA Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S.,
RA Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C.,
RA Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A.,
RA Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M.,
RA del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S.,
RA Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R.,
RA Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G.,
RA Nurse P.;
RT "The genome sequence of Schizosaccharomyces pombe.";
RL Nature 415:871-880(2002).
CC -!- FUNCTION: Component of the SRP (signal recognition particle) receptor
CC (SR). Ensures, in conjunction with the signal recognition particle, the
CC correct targeting of the nascent secretory proteins to the endoplasmic
CC reticulum membrane system. GTP hydrolysis may enhance the fidelity of
CC and provide unidirectionality to the targeting reaction (By
CC similarity). {ECO:0000250|UniProtKB:P32916}.
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 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; CU329671; CAA17783.1; -; Genomic_DNA.
DR PIR; T40342; T40342.
DR RefSeq; NP_596660.1; NM_001022582.2.
DR AlphaFoldDB; O43032; -.
DR SMR; O43032; -.
DR STRING; 4896.SPBC3B9.03.1; -.
DR iPTMnet; O43032; -.
DR MaxQB; O43032; -.
DR PaxDb; O43032; -.
DR PRIDE; O43032; -.
DR EnsemblFungi; SPBC3B9.03.1; SPBC3B9.03.1:pep; SPBC3B9.03.
DR GeneID; 2540909; -.
DR KEGG; spo:SPBC3B9.03; -.
DR PomBase; SPBC3B9.03; srp101.
DR VEuPathDB; FungiDB:SPBC3B9.03; -.
DR eggNOG; KOG0781; Eukaryota.
DR HOGENOM; CLU_009301_8_1_1; -.
DR InParanoid; O43032; -.
DR OMA; NDQRLMG; -.
DR PhylomeDB; O43032; -.
DR PRO; PR:O43032; -.
DR Proteomes; UP000002485; Chromosome II.
DR GO; GO:0005829; C:cytosol; HDA:PomBase.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IBA:GO_Central.
DR GO; GO:0016020; C:membrane; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; HDA:PomBase.
DR GO; GO:0005785; C:signal recognition particle receptor complex; ISO:PomBase.
DR GO; GO:0005525; F:GTP binding; ISM:PomBase.
DR GO; GO:0003924; F:GTPase activity; ISM:PomBase.
DR GO; GO:0005047; F:signal recognition particle binding; ISO:PomBase.
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; ISO:PomBase.
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 3: Inferred from homology;
KW Endoplasmic reticulum; GTP-binding; Membrane; Nucleotide-binding; Receptor;
KW Reference proteome.
FT CHAIN 1..547
FT /note="Signal recognition particle receptor subunit alpha
FT homolog"
FT /id="PRO_0000316024"
FT REGION 124..174
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 343..546
FT /note="NG domain"
FT /evidence="ECO:0000250|UniProtKB:P08240"
FT COMPBIAS 124..140
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 141..155
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 349..356
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 437..441
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 498..501
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
SQ SEQUENCE 547 AA; 61078 MW; 42E920E528E22361 CRC64;
MIDLFAIVNK GGIVLWKKTN SLVNLKCLQV LFHEAFLSEQ RTVNNTVTFD RYTMQYQEAT
QYSIVFVVVF QDLKCMAYSQ SLLNSAHNIF LNLFKEKLED RQVPNEAEVE KLFAPIFNRK
SAQLENETDT KSLPVEANND NSARKKNEYE MKKKGAQSKQ TNAPKKGKKQ LRKWDDQITE
EEQAALNYSS QASSASQTVD NSQLSSIVGN NNKFQKTGSG DVIISDLEMD PNQTISNKSA
SSAFSLFSNL IGGKYLKEED LSPILKQMQE HLTKKNVANS IALELCESVK ASLINKKVGS
FDTVKNTVNK AFRDRLTQIL TPSTSLDLLH SIRSVRKNEN RPYTISLIGV NGVGKSTTLA
KIAYWLLSNN FRILVAACDT FRSGAIEQLG VHVKNLQSLK GSSIELFAQG YGKDSSFVVK
NAVEYAKQNS FDVILIDTAG RRHNDQRLMG SLEKFTKATK LDKIFQVAEA LVGTDSLAQA
KHFQASLYHR PLDGFIISKV DTVGQLVGVM VGMVYAVRVP IIFVGIGQTY SDLRTLSVDW
VVDQLMK
