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Protein

Signal recognition particle subunit SRP72

Gene

SRP72

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Signal-recognition-particle (SRP) assembly has a crucial role in targeting secretory proteins to the rough endoplasmic reticulum (ER) membrane. SRP is required for the cotranslational protein translocation for ER import and preferentially recognizes strongly hydrophobic signal sequences. It is involved in targeting the nascent chain-ribosome (RNC) complex to the ER and is proposed to participate in the arrest of nascent chain elongation during membrane targeting. SRP72 binds the 7S RNA only in presence of SRP68.2 Publications

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Ribonucleoprotein

Enzyme and pathway databases

BioCyciYEAST:G3O-34101-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Signal recognition particle subunit SRP72
Alternative name(s):
Signal recognition particle 72 kDa protein homolog
Gene namesi
Name:SRP72
Ordered Locus Names:YPL210C
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
Proteomesi
  • UP000002311 Componenti: Chromosome XVI

Organism-specific databases

EuPathDBiFungiDB:YPL210C.
SGDiS000006131. SRP72.

Subcellular locationi

  • Cytoplasm By similarity
  • Endoplasmic reticulum membrane
  • Nucleus

  • Note: Transiently localizes to the nucleolus during biogenesis of the SRP. The SRP-RNC complex is bound to the endoplasmic reticulum membrane due to the interaction of the SRP with the membrane SRP-receptor (SRP101-SRP102).

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Endoplasmic reticulum, Membrane, Nucleus, Signal recognition particle

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 640640Signal recognition particle subunit SRP72PRO_0000135238Add
BLAST

Proteomic databases

MaxQBiP38688.
PeptideAtlasiP38688.

PTM databases

iPTMnetiP38688.

Interactioni

Subunit structurei

Fungal signal recognition particle (SRP) complex consists of a 7S RNA molecule (scR1) and at least six protein subunits: SRP72, SRP68, SRP54, SEC65, SRP21 and SRP14. At least SRP14, SRP21, SRP68 and SRP72 are proposed to get assembled together with scR1 RNA as a pre-SRP complex in the nucleolus which is exported to the cytoplasm.1 Publication

Binary interactionsi

WithEntry#Exp.IntActNotes
SEC65P294788EBI-18011,EBI-16641
SRP14P389856EBI-18011,EBI-17977

Protein-protein interaction databases

BioGridi35975. 27 interactions.
DIPiDIP-6763N.
IntActiP38688. 15 interactions.
MINTiMINT-620431.

Structurei

3D structure databases

ProteinModelPortaliP38688.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Repeati188 – 22134TPRAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi539 – 640102Lys-richAdd
BLAST

Sequence similaritiesi

Belongs to the SRP72 family.Curated
Contains 1 TPR repeat.Curated

Keywords - Domaini

TPR repeat

Phylogenomic databases

HOGENOMiHOG000000979.
InParanoidiP38688.
KOiK03108.
OMAiCNERVPL.
OrthoDBiEOG7B31WM.

Family and domain databases

Gene3Di1.25.40.10. 3 hits.
InterProiIPR013699. Signal_recog_part_SRP72_RNA-bd.
IPR026270. SRP72.
IPR013026. TPR-contain_dom.
IPR011990. TPR-like_helical_dom.
[Graphical view]
PANTHERiPTHR14094. PTHR14094. 1 hit.
PfamiPF08492. SRP72. 1 hit.
[Graphical view]
PIRSFiPIRSF038922. SRP72. 1 hit.
SUPFAMiSSF48452. SSF48452. 2 hits.
PROSITEiPS50293. TPR_REGION. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P38688-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAKDNLTNLL SQLNIQLSQD EHSQVEQTCV KLLDSGCENP ADVFRRCLVA
60 70 80 90 100
VIQQDKYQKA LHYLKKFKHI DDKYGRKFAL EKLYIFYKLN MPDEFNTLYT
110 120 130 140 150
AIITDDLDTV LKKDIESLRG ILHVRAQYCY KNGLYQEAFK IYQHLASHNE
160 170 180 190 200
KDQDSQIELS CNERVPLSVA TELMNRSPLV TPMDESSYDL LFNESFIMAS
210 220 230 240 250
VGKYDKAIEL LEKALQGATN EGYQNDINTI KLQLSFVLQM VGKTAQSKEI
260 270 280 290 300
LKGLLQELKA DSPFSLICQN NLNAFVDFSK YNTNFNLLLR ELNVEKLNTF
310 320 330 340 350
NLQTFTHEQW SNIQRNVLFL RLFNNVKIHS QESLLSRTFD KYSKLVDNVT
360 370 380 390 400
LESYKTQAKK LYHHTTKTIL SGTDGSTIGI LLLTIQLLII EKEWENAIRI
410 420 430 440 450
GELFLNESWK SSFEKFNDSQ AIVCYILFEL YKIKGRNNSK SVLLKKLGSV
460 470 480 490 500
RVQLSGKIQE NIPFWKHVGF ELLSMGNAKE SKALLREISN FSKGDADVLV
510 520 530 540 550
DRVVSSDSLD IAQGIDLVRD IDIDKLIQLG VKPLESSAKR SKNTAVSKVQ
560 570 580 590 600
KRKVLELKKK RKIKRLEKFL QGRDTSKLPD PERWLPLRDR STYRPKKKQQ
610 620 630 640
GAKQTQGGAM NKKSEQALDI SKKGKPTVNK KPKNKKKGRK
Length:640
Mass (Da):73,541
Last modified:November 8, 2005 - v2
Checksum:iDB2F536212F0871B
GO

Sequence cautioni

The sequence AAA53400.1 differs from that shown. Reason: Erroneous initiation. Curated
The sequence CAA97925.1 differs from that shown. Reason: Erroneous initiation. Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L35178 Genomic DNA. Translation: AAA53400.1. Different initiation.
Z73566 Genomic DNA. Translation: CAA97925.1. Different initiation.
BK006949 Genomic DNA. Translation: DAA11226.1.
PIRiS47929.
RefSeqiNP_015114.2. NM_001184024.1.

Genome annotation databases

EnsemblFungiiYPL210C; YPL210C; YPL210C.
GeneIDi855891.
KEGGisce:YPL210C.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L35178 Genomic DNA. Translation: AAA53400.1. Different initiation.
Z73566 Genomic DNA. Translation: CAA97925.1. Different initiation.
BK006949 Genomic DNA. Translation: DAA11226.1.
PIRiS47929.
RefSeqiNP_015114.2. NM_001184024.1.

3D structure databases

ProteinModelPortaliP38688.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi35975. 27 interactions.
DIPiDIP-6763N.
IntActiP38688. 15 interactions.
MINTiMINT-620431.

PTM databases

iPTMnetiP38688.

Proteomic databases

MaxQBiP38688.
PeptideAtlasiP38688.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYPL210C; YPL210C; YPL210C.
GeneIDi855891.
KEGGisce:YPL210C.

Organism-specific databases

EuPathDBiFungiDB:YPL210C.
SGDiS000006131. SRP72.

Phylogenomic databases

HOGENOMiHOG000000979.
InParanoidiP38688.
KOiK03108.
OMAiCNERVPL.
OrthoDBiEOG7B31WM.

Enzyme and pathway databases

BioCyciYEAST:G3O-34101-MONOMER.

Miscellaneous databases

PROiP38688.

Family and domain databases

Gene3Di1.25.40.10. 3 hits.
InterProiIPR013699. Signal_recog_part_SRP72_RNA-bd.
IPR026270. SRP72.
IPR013026. TPR-contain_dom.
IPR011990. TPR-like_helical_dom.
[Graphical view]
PANTHERiPTHR14094. PTHR14094. 1 hit.
PfamiPF08492. SRP72. 1 hit.
[Graphical view]
PIRSFiPIRSF038922. SRP72. 1 hit.
SUPFAMiSSF48452. SSF48452. 2 hits.
PROSITEiPS50293. TPR_REGION. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Subunits of the Saccharomyces cerevisiae signal recognition particle required for its functional expression."
    Brown J.D., Hann B.C., Medzihradszky K.F., Niwa M., Burlingame A.L., Walter P.
    EMBO J. 13:4390-4400(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PARTIAL PROTEIN SEQUENCE, FUNCTION, IDENTIFICATION IN THE SRP COMPLEX.
    Strain: ATCC 204508 / S288c.
  2. "The nucleotide sequence of Saccharomyces cerevisiae chromosome XVI."
    Bussey H., Storms R.K., Ahmed A., Albermann K., Allen E., Ansorge W., Araujo R., Aparicio A., Barrell B.G., Badcock K., Benes V., Botstein D., Bowman S., Brueckner M., Carpenter J., Cherry J.M., Chung E., Churcher C.M.
    , Coster F., Davis K., Davis R.W., Dietrich F.S., Delius H., DiPaolo T., Dubois E., Duesterhoeft A., Duncan M., Floeth M., Fortin N., Friesen J.D., Fritz C., Goffeau A., Hall J., Hebling U., Heumann K., Hilbert H., Hillier L.W., Hunicke-Smith S., Hyman R.W., Johnston M., Kalman S., Kleine K., Komp C., Kurdi O., Lashkari D., Lew H., Lin A., Lin D., Louis E.J., Marathe R., Messenguy F., Mewes H.-W., Mirtipati S., Moestl D., Mueller-Auer S., Namath A., Nentwich U., Oefner P., Pearson D., Petel F.X., Pohl T.M., Purnelle B., Rajandream M.A., Rechmann S., Rieger M., Riles L., Roberts D., Schaefer M., Scharfe M., Scherens B., Schramm S., Schroeder M., Sdicu A.-M., Tettelin H., Urrestarazu L.A., Ushinsky S., Vierendeels F., Vissers S., Voss H., Walsh S.V., Wambutt R., Wang Y., Wedler E., Wedler H., Winnett E., Zhong W.-W., Zollner A., Vo D.H., Hani J.
    Nature 387:103-105(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  3. Cited for: GENOME REANNOTATION.
    Strain: ATCC 204508 / S288c.
  4. "Elongation arrest is a physiologically important function of signal recognition particle."
    Mason N., Ciufo L.F., Brown J.D.
    EMBO J. 19:4164-4174(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  5. "Biogenesis of the signal recognition particle (SRP) involves import of SRP proteins into the nucleolus, assembly with the SRP-RNA, and Xpo1p-mediated export."
    Grosshans H., Deinert K., Hurt E.C., Simos G.
    J. Cell Biol. 153:745-762(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: ASSEMBLY OF THE SRP COMPLEX, SUBCELLULAR LOCATION.
  6. "Sequencing and comparison of yeast species to identify genes and regulatory elements."
    Kellis M., Patterson N., Endrizzi M., Birren B.W., Lander E.S.
    Nature 423:241-254(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION OF PROBABLE INITIATION SITE.
  7. Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
  8. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
  9. "A multidimensional chromatography technology for in-depth phosphoproteome analysis."
    Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.
    Mol. Cell. Proteomics 7:1389-1396(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiSRP72_YEAST
AccessioniPrimary (citable) accession number: P38688
Secondary accession number(s): D6W3G0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1995
Last sequence update: November 8, 2005
Last modified: June 8, 2016
This is version 138 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Miscellaneous

Present with 11800 molecules/cell in log phase SD medium.1 Publication

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families
  2. Yeast
    Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
  3. Yeast chromosome XVI
    Yeast (Saccharomyces cerevisiae) chromosome XVI: entries and gene names

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.