SRP72_CANLF
ID SRP72_CANLF Reviewed; 671 AA.
AC P33731;
DT 01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 147.
DE RecName: Full=Signal recognition particle subunit SRP72;
DE Short=SRP72;
DE AltName: Full=Signal recognition particle 72 kDa protein;
GN Name=SRP72;
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], PROTEIN SEQUENCE OF 113-121; 148-162; 242-254;
RP 311-322; 357-361; 363-375; 443-451; 465-475 AND 577-581, FUNCTION, SUBUNIT,
RP AND INTERACTION WITH SRP62.
RC STRAIN=Cocker spaniel; TISSUE=Kidney;
RX PubMed=8388879; DOI=10.1083/jcb.121.5.977;
RA Luetcke H., Prehn S., Ashford A.J., Remus M., Frank R., Dobberstein B.;
RT "Assembly of the 68- and 72-kD proteins of signal recognition particle with
RT 7S RNA.";
RL J. Cell Biol. 121:977-985(1993).
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, SUBUNIT, AND INTERACTION WITH SRP68.
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:6413076). The SRP complex interacts with the signal sequence in
CC nascent secretory and membrane proteins and directs them to the
CC membrane of the ER (PubMed:6413076). The SRP complex targets the
CC ribosome-nascent chain complex to the SRP receptor (SR), which is
CC anchored in the ER, where SR compaction and GTPase rearrangement drive
CC cotranslational protein translocation into the ER (By similarity).
CC Binds the signal recognition particle RNA (7SL RNA) in presence of
CC SRP68 (PubMed:8388879, PubMed:6413076). Can bind 7SL RNA with low
CC affinity (By similarity). The SRP complex possibly participates in the
CC elongation arrest function (By similarity).
CC {ECO:0000250|UniProtKB:O76094, ECO:0000250|UniProtKB:P38688,
CC ECO:0000269|PubMed:6413076, ECO:0000269|PubMed:8388879}.
CC -!- SUBUNIT: Heterodimer with SRP68 (PubMed:8388879, PubMed:6413076).
CC SRP68-SRP72 heterodimer formation is stabilized by the presence of 7SL
CC RNA (PubMed:8388879, PubMed:6413076). Component of a signal recognition
CC particle consisting of a 7SL RNA molecule of 300 nucleotides and six
CC protein subunits: SRP72, SRP68, SRP54, SRP19, SRP14 and SRP9
CC (PubMed:6938958, PubMed:6413076). Within the SRP complex, interacts
CC with SRP68 (via C-terminus) (PubMed:8388879, PubMed:6413076).
CC {ECO:0000269|PubMed:6413076, ECO:0000269|PubMed:6938958,
CC ECO:0000269|PubMed:8388879}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:O76094}.
CC Endoplasmic reticulum {ECO:0000250|UniProtKB:O76094}.
CC -!- SIMILARITY: Belongs to the SRP72 family. {ECO:0000305}.
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DR EMBL; X67813; CAA48014.1; -; mRNA.
DR PIR; A40692; A40692.
DR RefSeq; NP_001003264.1; NM_001003264.1.
DR PDB; 6FRK; EM; 3.70 A; r=1-581.
DR PDB; 7OBQ; EM; 3.90 A; z=1-671.
DR PDB; 7OBR; EM; 2.80 A; z=1-671.
DR PDBsum; 6FRK; -.
DR PDBsum; 7OBQ; -.
DR PDBsum; 7OBR; -.
DR AlphaFoldDB; P33731; -.
DR SMR; P33731; -.
DR BioGRID; 139860; 1.
DR STRING; 9612.ENSCAFP00000003266; -.
DR PaxDb; P33731; -.
DR PRIDE; P33731; -.
DR Ensembl; ENSCAFT00030039277; ENSCAFP00030034265; ENSCAFG00030021373.
DR Ensembl; ENSCAFT00040033614; ENSCAFP00040029251; ENSCAFG00040018184.
DR Ensembl; ENSCAFT00845024627; ENSCAFP00845019372; ENSCAFG00845013778.
DR GeneID; 403944; -.
DR KEGG; cfa:403944; -.
DR CTD; 6731; -.
DR VEuPathDB; HostDB:ENSCAFG00845013778; -.
DR eggNOG; KOG2376; Eukaryota.
DR GeneTree; ENSGT00390000013264; -.
DR HOGENOM; CLU_013808_1_0_1; -.
DR InParanoid; P33731; -.
DR OMA; NDMKVLA; -.
DR OrthoDB; 743414at2759; -.
DR TreeFam; TF106250; -.
DR Reactome; R-CFA-1799339; SRP-dependent cotranslational protein targeting to membrane.
DR Proteomes; UP000002254; Chromosome 13.
DR Bgee; ENSCAFG00000002244; Expressed in keratinocyte and 48 other tissues.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0005783; C:endoplasmic reticulum; ISS:UniProtKB.
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:0043022; F:ribosome binding; IEA:Ensembl.
DR GO; GO:0005047; F:signal recognition particle binding; IEA:Ensembl.
DR GO; GO:0030911; F:TPR domain binding; IEA:Ensembl.
DR GO; GO:0006614; P:SRP-dependent cotranslational protein targeting to membrane; IBA:GO_Central.
DR Gene3D; 1.25.40.10; -; 4.
DR InterPro; IPR013699; Signal_recog_part_SRP72_RNA-bd.
DR InterPro; IPR026270; SRP72.
DR InterPro; IPR031545; SRP_TPR-like.
DR InterPro; IPR011990; TPR-like_helical_dom_sf.
DR InterPro; IPR019734; TPR_repeat.
DR PANTHER; PTHR14094; PTHR14094; 1.
DR Pfam; PF08492; SRP72; 1.
DR Pfam; PF17004; SRP_TPR_like; 1.
DR Pfam; PF13181; TPR_8; 2.
DR PIRSF; PIRSF038922; SRP72; 1.
DR SMART; SM00028; TPR; 5.
DR SUPFAM; SSF48452; SSF48452; 2.
DR PROSITE; PS50005; TPR; 5.
DR PROSITE; PS50293; TPR_REGION; 3.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Cytoplasm; Direct protein sequencing;
KW Endoplasmic reticulum; Isopeptide bond; Phosphoprotein; Reference proteome;
KW Repeat; Ribonucleoprotein; Signal recognition particle; TPR repeat;
KW Ubl conjugation.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:O76094"
FT CHAIN 2..671
FT /note="Signal recognition particle subunit SRP72"
FT /id="PRO_0000135233"
FT REPEAT 11..44
FT /note="TPR 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00339"
FT REPEAT 109..142
FT /note="TPR 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00339"
FT REPEAT 226..259
FT /note="TPR 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00339"
FT REPEAT 406..439
FT /note="TPR 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00339"
FT REPEAT 447..480
FT /note="TPR 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00339"
FT REGION 9..163
FT /note="Required for interaction with SRP68"
FT /evidence="ECO:0000250|UniProtKB:O76094"
FT REGION 379..509
FT /note="Required for the interaction with the SRP68/7SL RNA
FT complex"
FT /evidence="ECO:0000269|PubMed:8388879"
FT REGION 527..671
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 545..617
FT /note="RNA-binding"
FT /evidence="ECO:0000250|UniProtKB:O76094"
FT COMPBIAS 564..585
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 603..644
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 657..671
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="Blocked amino end (Ala); alternate"
FT MOD_RES 2
FT /note="N-acetylalanine; alternate"
FT /evidence="ECO:0000250|UniProtKB:O76094"
FT MOD_RES 571
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:O76094"
FT MOD_RES 618
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:O76094"
FT MOD_RES 630
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O76094"
FT MOD_RES 635
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O76094"
FT CROSSLNK 391
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO1); alternate"
FT /evidence="ECO:0000250|UniProtKB:O76094"
FT CROSSLNK 391
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0000250|UniProtKB:O76094"
SQ SEQUENCE 671 AA; 74494 MW; E490121DAA76959F CRC64;
MASGGSGGVS VPALWSEVNR YGQNGDFTRA LKTVNKILQI NKDDVTALHC KVVCLIQNGS
FKEALNVINT HTKVLANNSL SFEKAYCEYR LNRIENALKT IESANQQTDK LKELYGQVLY
RLERYDECLA VYRDLVRNSQ DDYDEERKTN LSAVVAAQSN WEKVVPENLG LQEGTHELCY
NAACALIGQG QLSQAMKILQ KAEDLCRRSL SEDSDGTEED PQAELAIIHG QMAYILQLQG
RTEEALQLYN QIIKLKPTDV GLLAVIANNI ITINKDQNVF DSKKKVKLTN AEGVEFKLSK
KQLQAIEFNK ALLAMYTNQA EQCRKISASL QSQSPEHLLP VLIQAAQLCR EKQHTKAIEL
LQEFSDQHPE NAAEIKLTMA QLKISQGNIS KACLILRSIE ELKHKPGMVS ALVTMYSHEE
DIDSAIEVFT QAIQWYQNHQ PKSSAHLSLI REAANFKLKY GRKKEAISDL EQLWKQNPKD
IHTLAQLISA YSLVDPEKAK ALSKHLPSSD SMSLKVDVEA LENSPGATYI RKKGGKVAGD
SQPKEQGQGD LKKKKKKKKG KLPKNYDPKV TPDPERWLPM RERSYYRGRK KGKKKDQIGK
GTQGATAGAS SELDASKTVS SPPTSPRPGS AATASASTSN IIPPRHQKPA GAPATKKKQQ
QKKKKGGKGG W
