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SRP14_CANLF
ID   SRP14_CANLF             Reviewed;         110 AA.
AC   P16255; Q28277;
DT   01-AUG-1990, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1997, sequence version 2.
DT   25-MAY-2022, entry version 124.
DE   RecName: Full=Signal recognition particle 14 kDa protein;
DE            Short=SRP14;
GN   Name=SRP14;
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].
RA   Baugh C., Wilson C.;
RT   "Canine SRP14 coding region.";
RL   Submitted (JUN-1996) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 14-95, AND PROTEIN SEQUENCE OF 2-19 AND
RP   77-95.
RC   TISSUE=Kidney;
RX   PubMed=2557625; DOI=10.1073/pnas.86.24.9747;
RA   Strub K., Walter P.;
RT   "Isolation of a cDNA clone of the 14-kDa subunit of the signal recognition
RT   particle by cross-hybridization of differently primed polymerase chain
RT   reactions.";
RL   Proc. Natl. Acad. Sci. U.S.A. 86:9747-9751(1989).
RN   [3]
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   [4]
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).
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). SRP9 together with SRP14 and the Alu portion of the
CC       SRP RNA, constitutes the elongation arrest domain of SRP
CC       (PubMed:6938958, PubMed:6413076). The complex of SRP9 and SRP14 is
CC       required for SRP RNA binding (PubMed:6938958, PubMed:6413076).
CC       {ECO:0000269|PubMed:6413076, ECO:0000269|PubMed:6938958}.
CC   -!- SUBUNIT: Heterodimer with SRP9; binds RNA as heterodimer
CC       (PubMed:6413076). Component of a signal recognition particle complex
CC       that consists of a 7SL RNA molecule of 300 nucleotides and six protein
CC       subunits: SRP72, SRP68, SRP54, SRP19, SRP14 and SRP9 (PubMed:6938958,
CC       PubMed:6413076). {ECO:0000269|PubMed:6413076,
CC       ECO:0000269|PubMed:6938958}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm.
CC   -!- SIMILARITY: Belongs to the SRP14 family. {ECO:0000305}.
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DR   EMBL; U57440; AAB02232.1; -; mRNA.
DR   EMBL; M29265; AAA30898.1; -; mRNA.
DR   PIR; A34501; A34501.
DR   RefSeq; NP_001003251.1; NM_001003251.1.
DR   PDB; 4UE5; EM; 9.00 A; B=2-95.
DR   PDB; 6FRK; EM; 3.70 A; z=1-110.
DR   PDB; 6R6G; EM; 3.70 A; AE=2-95.
DR   PDB; 7OBR; EM; 2.80 A; t=1-110.
DR   PDBsum; 4UE5; -.
DR   PDBsum; 6FRK; -.
DR   PDBsum; 6R6G; -.
DR   PDBsum; 7OBR; -.
DR   AlphaFoldDB; P16255; -.
DR   SMR; P16255; -.
DR   STRING; 9612.ENSCAFP00000041095; -.
DR   PaxDb; P16255; -.
DR   GeneID; 403930; -.
DR   KEGG; cfa:403930; -.
DR   CTD; 6727; -.
DR   eggNOG; KOG1761; Eukaryota.
DR   InParanoid; P16255; -.
DR   OrthoDB; 1634105at2759; -.
DR   Proteomes; UP000002254; Unplaced.
DR   GO; GO:0005829; C:cytosol; TAS:Reactome.
DR   GO; GO:0005786; C:signal recognition particle, endoplasmic reticulum targeting; IEA:UniProtKB-KW.
DR   GO; GO:0008312; F:7S RNA binding; IEA:InterPro.
DR   GO; GO:0030942; F:endoplasmic reticulum signal peptide binding; IEA:InterPro.
DR   GO; GO:0006614; P:SRP-dependent cotranslational protein targeting to membrane; IEA:InterPro.
DR   Gene3D; 3.30.720.10; -; 1.
DR   InterPro; IPR003210; Signal_recog_particle_SRP14.
DR   InterPro; IPR009018; Signal_recog_particle_SRP9/14.
DR   PANTHER; PTHR12013; PTHR12013; 1.
DR   Pfam; PF02290; SRP14; 1.
DR   SUPFAM; SSF54762; SSF54762; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Cytoplasm; Direct protein sequencing; Phosphoprotein;
KW   Reference proteome; Ribonucleoprotein; RNA-binding;
KW   Signal recognition particle.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000250|UniProtKB:P37108"
FT   CHAIN           2..110
FT                   /note="Signal recognition particle 14 kDa protein"
FT                   /id="PRO_0000135188"
FT   REGION          90..110
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         45
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P16254"
FT   CONFLICT        92
FT                   /note="D -> C (in Ref. 2; AA sequence)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   110 AA;  12487 MW;  0D01DF1392082FD9 CRC64;
     MVLLESEQFL TELTRLFQKC RLSGSVFITL KKYDGRTKPI PRKGSVEGFE PSDNKCLLRA
     TDGKKKISTV VSSKEVNKFQ MAYSNLLRAN MDGLKKRDKK SKSKKSKPAQ
 
 
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