SRP19_CANLF
ID SRP19_CANLF Reviewed; 144 AA.
AC J9PAS6;
DT 25-MAY-2022, integrated into UniProtKB/Swiss-Prot.
DT 31-OCT-2012, sequence version 1.
DT 03-AUG-2022, entry version 63.
DE RecName: Full=Signal recognition particle 19 kDa protein {ECO:0000305};
DE Short=SRP19 {ECO:0000305};
GN Name=SRP19 {ECO:0000312|VGNC:VGNC:56002};
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 {ECO:0000312|Proteomes:UP000002254};
RN [1] {ECO:0000312|Proteomes:UP000002254}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Boxer {ECO:0000312|Proteomes:UP000002254};
RX PubMed=16341006; DOI=10.1038/nature04338;
RA Lindblad-Toh K., Wade C.M., Mikkelsen T.S., Karlsson E.K., Jaffe D.B.,
RA Kamal M., Clamp M., Chang J.L., Kulbokas E.J. III, Zody M.C., Mauceli E.,
RA Xie X., Breen M., Wayne R.K., Ostrander E.A., Ponting C.P., Galibert F.,
RA Smith D.R., deJong P.J., Kirkness E.F., Alvarez P., Biagi T., Brockman W.,
RA Butler J., Chin C.-W., Cook A., Cuff J., Daly M.J., DeCaprio D., Gnerre S.,
RA Grabherr M., Kellis M., Kleber M., Bardeleben C., Goodstadt L., Heger A.,
RA Hitte C., Kim L., Koepfli K.-P., Parker H.G., Pollinger J.P.,
RA Searle S.M.J., Sutter N.B., Thomas R., Webber C., Baldwin J., Abebe A.,
RA Abouelleil A., Aftuck L., Ait-Zahra M., Aldredge T., Allen N., An P.,
RA Anderson S., Antoine C., Arachchi H., Aslam A., Ayotte L., Bachantsang P.,
RA Barry A., Bayul T., Benamara M., Berlin A., Bessette D., Blitshteyn B.,
RA Bloom T., Blye J., Boguslavskiy L., Bonnet C., Boukhgalter B., Brown A.,
RA Cahill P., Calixte N., Camarata J., Cheshatsang Y., Chu J., Citroen M.,
RA Collymore A., Cooke P., Dawoe T., Daza R., Decktor K., DeGray S.,
RA Dhargay N., Dooley K., Dooley K., Dorje P., Dorjee K., Dorris L.,
RA Duffey N., Dupes A., Egbiremolen O., Elong R., Falk J., Farina A., Faro S.,
RA Ferguson D., Ferreira P., Fisher S., FitzGerald M., Foley K., Foley C.,
RA Franke A., Friedrich D., Gage D., Garber M., Gearin G., Giannoukos G.,
RA Goode T., Goyette A., Graham J., Grandbois E., Gyaltsen K., Hafez N.,
RA Hagopian D., Hagos B., Hall J., Healy C., Hegarty R., Honan T., Horn A.,
RA Houde N., Hughes L., Hunnicutt L., Husby M., Jester B., Jones C., Kamat A.,
RA Kanga B., Kells C., Khazanovich D., Kieu A.C., Kisner P., Kumar M.,
RA Lance K., Landers T., Lara M., Lee W., Leger J.-P., Lennon N., Leuper L.,
RA LeVine S., Liu J., Liu X., Lokyitsang Y., Lokyitsang T., Lui A.,
RA Macdonald J., Major J., Marabella R., Maru K., Matthews C., McDonough S.,
RA Mehta T., Meldrim J., Melnikov A., Meneus L., Mihalev A., Mihova T.,
RA Miller K., Mittelman R., Mlenga V., Mulrain L., Munson G., Navidi A.,
RA Naylor J., Nguyen T., Nguyen N., Nguyen C., Nguyen T., Nicol R., Norbu N.,
RA Norbu C., Novod N., Nyima T., Olandt P., O'Neill B., O'Neill K., Osman S.,
RA Oyono L., Patti C., Perrin D., Phunkhang P., Pierre F., Priest M.,
RA Rachupka A., Raghuraman S., Rameau R., Ray V., Raymond C., Rege F.,
RA Rise C., Rogers J., Rogov P., Sahalie J., Settipalli S., Sharpe T.,
RA Shea T., Sheehan M., Sherpa N., Shi J., Shih D., Sloan J., Smith C.,
RA Sparrow T., Stalker J., Stange-Thomann N., Stavropoulos S., Stone C.,
RA Stone S., Sykes S., Tchuinga P., Tenzing P., Tesfaye S., Thoulutsang D.,
RA Thoulutsang Y., Topham K., Topping I., Tsamla T., Vassiliev H.,
RA Venkataraman V., Vo A., Wangchuk T., Wangdi T., Weiand M., Wilkinson J.,
RA Wilson A., Yadav S., Yang S., Yang X., Young G., Yu Q., Zainoun J.,
RA Zembek L., Zimmer A., Lander E.S.;
RT "Genome sequence, comparative analysis and haplotype structure of the
RT domestic dog.";
RL Nature 438:803-819(2005).
RN [2]
RP FUNCTION, AND IDENTIFICATION IN A SIGNAL RECOGNITION PARTICLE COMPLEX.
RX PubMed=6938958; DOI=10.1073/pnas.77.12.7112;
RA Walter P., Blobel G.;
RT "Purification of a membrane-associated protein complex required for protein
RT translocation across the endoplasmic reticulum.";
RL Proc. Natl. Acad. Sci. U.S.A. 77:7112-7116(1980).
RN [3]
RP FUNCTION, RNA BINDING, AND SUBUNIT.
RX PubMed=6413076; DOI=10.1016/0092-8674(83)90385-9;
RA Walter P., Blobel G.;
RT "Disassembly and reconstitution of signal recognition particle.";
RL Cell 34:525-533(1983).
RN [4] {ECO:0007744|PDB:4UE5}
RP STRUCTURE BY ELECTRON MICROSCOPY (9.00 ANGSTROMS) OF 14-120.
RX PubMed=26344568; DOI=10.1038/nsmb.3086;
RA Beckert B., Kedrov A., Sohmen D., Kempf G., Wild K., Sinning I.,
RA Stahlberg H., Wilson D.N., Beckmann R.;
RT "Translational arrest by a prokaryotic signal recognition particle is
RT mediated by RNA interactions.";
RL Nat. Struct. Mol. Biol. 22:767-773(2015).
RN [5] {ECO:0007744|PDB:6FRK}
RP STRUCTURE BY ELECTRON MICROSCOPY (3.70 ANGSTROMS) OF 13-117.
RX PubMed=29567807; DOI=10.1126/science.aar7924;
RA Kobayashi K., Jomaa A., Lee J.H., Chandrasekar S., Boehringer D.,
RA Shan S.O., Ban N.;
RT "Structure of a prehandover mammalian ribosomal SRPSRP receptor targeting
RT complex.";
RL Science 360:323-327(2018).
RN [6] {ECO:0007744|PDB:6R6G}
RP STRUCTURE BY ELECTRON MICROSCOPY (3.70 ANGSTROMS) OF 13-117.
RX PubMed=31246176; DOI=10.7554/elife.46267;
RA Shanmuganathan V., Schiller N., Magoulopoulou A., Cheng J., Braunger K.,
RA Cymer F., Berninghausen O., Beatrix B., Kohno K., von Heijne G.,
RA Beckmann R.;
RT "Structural and mutational analysis of the ribosome-arresting human
RT XBP1u.";
RL Elife 8:0-0(2019).
RN [7] {ECO:0007744|PDB:7OBQ, ECO:0007744|PDB:7OBR}
RP STRUCTURE BY ELECTRON MICROSCOPY (2.80 ANGSTROMS) IN COMPLEX WITH RIBOSOME
RP NASCENT CHAIN COMPLEX AND THE SRP RECEPTOR.
RX PubMed=34260909; DOI=10.1016/j.celrep.2021.109350;
RA Jomaa A., Eitzinger S., Zhu Z., Chandrasekar S., Kobayashi K., Shan S.O.,
RA Ban N.;
RT "Molecular mechanism of cargo recognition and handover by the mammalian
RT signal recognition particle.";
RL Cell Rep. 36:109350-109350(2021).
CC -!- FUNCTION: Component of the signal recognition particle (SRP) complex, a
CC ribonucleoprotein complex that mediates the cotranslational targeting
CC of secretory and membrane proteins to the endoplasmic reticulum (ER)
CC (PubMed:6938958, PubMed:6413076). Binds directly to 7SL RNA
CC (PubMed:6413076). Mediates binding of SRP54 to the SRP complex
CC (PubMed:6413076). {ECO:0000269|PubMed:6413076,
CC ECO:0000269|PubMed:6938958}.
CC -!- SUBUNIT: Component of a signal recognition particle complex that
CC consists of a 7SL RNA molecule of 300 nucleotides and six protein
CC subunits: SRP72, SRP68, SRP54, SRP19, SRP14 and SRP9. Interacts with
CC IPO5, IPO7, IPO8, KPNB1 and TNPO1. Interactions with IPO8 and TNPO1 may
CC be involved in SRP19 import into the nucleus (By similarity).
CC {ECO:0000250|UniProtKB:P09132, ECO:0000269|PubMed:6413076,
CC ECO:0000269|PubMed:6938958}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P09132}.
CC Nucleus, nucleolus {ECO:0000250|UniProtKB:P09132}. Nucleus, nucleoplasm
CC {ECO:0000250|UniProtKB:P09132}. Note=Although the signal recognition
CC particle complex acts in the cytoplasm, it assembles at least in part
CC in the nucleus and/or the nucleolus. SRP19 nuclear import may be
CC mediated by IPO8/Imp8 and TPNO1/Trn. {ECO:0000250|UniProtKB:P09132}.
CC -!- SIMILARITY: Belongs to the SRP19 family. {ECO:0000305}.
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DR EMBL; AAEX03001951; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AAEX03003224; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; NP_001239220.1; NM_001252291.1.
DR PDB; 4UE5; EM; 9.00 A; F=14-120.
DR PDB; 6FRK; EM; 3.70 A; q=13-117.
DR PDB; 6R6G; EM; 3.70 A; AC=13-117.
DR PDB; 7OBQ; EM; 3.90 A; q=1-144.
DR PDB; 7OBR; EM; 2.80 A; q=1-144.
DR PDBsum; 4UE5; -.
DR PDBsum; 6FRK; -.
DR PDBsum; 6R6G; -.
DR PDBsum; 7OBQ; -.
DR PDBsum; 7OBR; -.
DR SMR; J9PAS6; -.
DR STRING; 9612.ENSCAFP00000042903; -.
DR PaxDb; J9PAS6; -.
DR Ensembl; ENSCAFT00000094065; ENSCAFP00000072799; ENSCAFG00000031549.
DR Ensembl; ENSCAFT00030027714; ENSCAFP00030024186; ENSCAFG00030014933.
DR Ensembl; ENSCAFT00030031031; ENSCAFP00030027072; ENSCAFG00030016821.
DR Ensembl; ENSCAFT00040015862; ENSCAFP00040013754; ENSCAFG00040008463.
DR Ensembl; ENSCAFT00845006124; ENSCAFP00845004869; ENSCAFG00845003444.
DR GeneID; 606764; -.
DR KEGG; cfa:606764; -.
DR CTD; 6728; -.
DR VEuPathDB; HostDB:ENSCAFG00845003444; -.
DR VGNC; VGNC:56002; SRP19.
DR eggNOG; KOG3198; Eukaryota.
DR GeneTree; ENSGT00390000004950; -.
DR HOGENOM; CLU_064201_2_1_1; -.
DR InParanoid; J9PAS6; -.
DR OMA; CVENPTH; -.
DR OrthoDB; 1552706at2759; -.
DR TreeFam; TF106248; -.
DR Reactome; R-CFA-1799339; SRP-dependent cotranslational protein targeting to membrane.
DR Proteomes; UP000002254; Chromosome 3.
DR Bgee; ENSCAFG00000031549; Expressed in testis and 48 other tissues.
DR GO; GO:0005730; C:nucleolus; IEA:UniProtKB-SubCell.
DR GO; GO:0005786; C:signal recognition particle, endoplasmic reticulum targeting; IBA:GO_Central.
DR GO; GO:0008312; F:7S RNA binding; IBA:GO_Central.
DR GO; GO:0006617; P:SRP-dependent cotranslational protein targeting to membrane, signal sequence recognition; IBA:GO_Central.
DR Gene3D; 3.30.56.30; -; 1.
DR InterPro; IPR002778; Signal_recog_particle_SRP19.
DR InterPro; IPR036521; SRP19-like_sf.
DR PANTHER; PTHR17453; PTHR17453; 1.
DR Pfam; PF01922; SRP19; 1.
DR SUPFAM; SSF69695; SSF69695; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; Nucleus; Reference proteome; Ribonucleoprotein;
KW RNA-binding; Signal recognition particle.
FT CHAIN 1..144
FT /note="Signal recognition particle 19 kDa protein"
FT /id="PRO_0000455158"
FT REGION 117..144
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 120..134
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 144 AA; 16156 MW; 175F661CEC1379AF CRC64;
MACAAARSPA EQDRFICIYP AYLNNKKTIA EGRRIPISKA VENPTATEIQ DVCSAVGLNV
FLEKNKMYSR EWNRDVQYRG RVRVQLKQED GSLCLVQFPS RKSVMLYAAE MIPKLKTRTQ
KTGGGDQSLQ QGEGSKKGKG KKKK
