Reviewed, UniProtKB/Swiss-Prot Q9U5L1 (SRPR_DROME)

Names and origin

Protein names

Recommended name:
    Signal recognition particle receptor subunit alpha homolog
      Short name=SR-alpha
      Short name=Docking protein alpha
      Short name=DP-alpha
Alternative name(s):
    GTP-binding protein

Gene names

Name:	Gtp-bp
ORF Names:	CG2522

Organism

Drosophila melanogaster (Fruit fly) [Complete proteome]

Taxonomic identifier

7227 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Arthropoda › Hexapoda › Insecta › Pterygota › Neoptera › Endopterygota › Diptera › Brachycera › Muscomorpha › Ephydroidea › Drosophilidae › Drosophila › Sophophora

Protein attributes

Sequence length	614 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	Ensures, in conjunction with SRP, the correct targeting of the nascent secretory proteins to the endoplasmic reticulum membrane system. May have a role in axonogenesis. Ref.4
Subunit structure	Heterodimer of an alpha and a beta chain.
Subcellular location	Endoplasmic reticulum membrane; Peripheral membrane protein By similarity. Note: Thought to be anchored in the membrane through an interaction with SR-beta, which contains a bona fide transmembrane domain By similarity.
Tissue specificity	In 8-9 hours embryos, expression is seen in a segmental pattern along embryonic ventral midline. Ref.4
Developmental stage	Expressed both maternally and zygotically. Zygotic expression peaks at 12-18 hours of embryonic development. Ref.4
Sequence similarities	Belongs to the GTP-binding SRP family.
Sequence caution	The sequence AAB27926.1 differs from that shown. Reason: Frameshift at positions 418, 424, 469 and 475. The sequence AAL28877.1 differs from that shown. Reason: Frameshift at position 347.

Ontologies

Keywords
Cellular component	Endoplasmic reticulum Membrane
Ligand	GTP-binding Nucleotide-binding
Molecular function	Receptor
PTM	Phosphoprotein
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	SRP-dependent cotranslational protein targeting to membrane Inferred from electronic annotation. Source: InterPro axonogenesis Ref.4 Inferred from expression pattern. Source: UniProtKB regulation of protein secretion Ref.4 Inferred from expression pattern. Source: UniProtKB
Cellular component	lipid particle Inferred from direct assay. Source: FlyBase signal recognition particle receptor complex Inferred from electronic annotation. Source: InterPro signal recognition particle, endoplasmic reticulum targeting Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	7S RNA binding Inferred from electronic annotation. Source: InterPro GTP binding Inferred from electronic annotation. Source: UniProtKB-KW GTPase activity Inferred from electronic annotation. Source: InterPro protein binding Inferred from physical interaction. Source: IntAct receptor activity Inferred from electronic annotation. Source: UniProtKB-KW signal recognition particle binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
obst-E	Q8T0V6	1	EBI-121637,EBI-114423

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 614	614	Signal recognition particle receptor subunit alpha homolog		PRO_0000101215
Regions
	Nucleotide binding	402 – 409	8	GTP By similarity
	Nucleotide binding	497 – 501	5	GTP By similarity
	Nucleotide binding	565 – 568	4	GTP By similarity
Amino acid modifications
	Modified residue	237	1	Phosphoserine Ref.5
	Modified residue	240	1	Phosphoserine Ref.5
	Modified residue	246	1	Phosphotyrosine Ref.5
	Modified residue	268	1	Phosphoserine Ref.5
	Modified residue	278	1	Phosphoserine Ref.5
	Modified residue	279	1	Phosphoserine Ref.5
Experimental info
	Sequence conflict	410 – 413	4	TNLA → RC Ref.4
	Sequence conflict	428	1	I → L Ref.4
	Sequence conflict	450	1	N → H Ref.4
	Sequence conflict	549	1	D → G in AAB27926. Ref.4
	Sequence conflict	556 – 558	3	PHI → RH in AAB27926. Ref.4
	Sequence conflict	567 – 573	7	FDTIDDK → LHTMQHD Ref.4

Sequences

	Sequence		Length	Mass (Da)
	Q9U5L1-1 [UniParc]. Last modified May 10, 2004. Version 2. Checksum: 2679CDE81E257490	FASTA	614	67,795
	10 20 30 40 50 60 MLDFVVIFTK GGVVLWHSNA SGNSFASCIN SLIRGVILEE RNTEAKYYEE DHLAVQFKLD 70 80 90 100 110 120 NELDLVYAAI FQKVIKLNYL DGFLADMQAA FKEKYGDIRL GDDYDFDREY RRVLSAAEEA 130 140 150 160 170 180 SAKQVKAPKT MRSYNESQKS KKTVASMIQD DKKPVEKRVN IQEAPPPSKS QPSSPPTGSP 190 200 210 220 230 240 MDKIIMEKRR KLREKLTPTK KTSPSDSKSS KPEKAGKKPR VWDLGGNSKD AALLDRSRDS 250 260 270 280 290 300 PDDVQYQNIN SELVGTMQGV IRDLDVESED EADNEDASSE GEAEEQVQSK KGKRGGLLSY 310 320 330 340 350 360 FKGIVGAKTM SLADLQPALE KMRDHLISKN VASEIAAKLC DSVAASLDGK QMGTFDSIAS 370 380 390 400 410 420 QVKEALTESL VRILSPKRRI DIIRDALESK RNGRPYTIIF CGVNGVGKST NLAKICFWLI 430 440 450 460 470 480 ENDFNVLIAA CDTFRAGAVE QLRTHTRHLN ALHPAAKHDG RNMVQLYEKG YGKDAAGIAM 490 500 510 520 530 540 EAIKFAHDTR VDVVLVDTAG RMQDNEPLMR SLSKLIKVNN PDLVLFVGEA LVGNEAVDQL 550 560 570 580 590 600 VKFNQSLADY SSNENPHIID GIVLTKFDTI DDKVGAAISM TYITGQPIVF VGTGQTYADL 610 KAINVNAVVN SLMK

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"The genome sequence of Drosophila melanogaster." Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., Sutton G.G., Wortman J.R., Yandell M.D. , Zhang Q., Chen L.X., Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D., Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J., Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C. Science 287:2185-2195(2000) [PubMed: 10731132] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: Berkeley.
[2]	"Annotation of the Drosophila melanogaster euchromatic genome: a systematic review." Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S., Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E., Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P., Bettencourt B.R., Celniker S.E., de Grey A.D.N.J. , Drysdale R.A., Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E. Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002) [PubMed: 12537572] [Abstract] Cited for: GENOME REANNOTATION.
[3]	"A Drosophila full-length cDNA resource." Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., George R.A., Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., Rubin G.M., Celniker S.E. Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002) [PubMed: 12537569] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: Berkeley. Tissue: Embryo.
[4]	"Characterization of a putative Drosophila GTP-binding protein." Fredieu J.R., Mahowald A.P. J. Cell Sci. 105:81-91(1993) [PubMed: 8360279] [Abstract] Cited for: NUCLEOTIDE SEQUENCE OF 402-573, FUNCTION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE. Tissue: Head and Ventral nerve cord.
[5]	"Phosphoproteome analysis of Drosophila melanogaster embryos." Zhai B., Villen J., Beausoleil S.A., Mintseris J., Gygi S.P. J. Proteome Res. 7:1675-1682(2008) [PubMed: 18327897] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-237; SER-240; TYR-246; SER-268; SER-278 AND SER-279, MASS SPECTROMETRY. Tissue: Embryo.

Cross-references

Sequence databases
EMBLGenBankDDBJ	AE014298 Genomic DNA. Translation: AAF48002.2. AY061329 mRNA. Translation: AAL28877.1. Frameshift. S65640 mRNA. Translation: AAB27926.1. Frameshift.
RefSeq	NP_524887.2.
UniGene	Dm.129
3D structure databases
HSSP	HSSP built from PDB template 1LS1 based on UniProtKB O07347.
ModBase	Search...
Protein-protein interaction databases
IntAct	Q9U5L1. 6 interactions.
Genome annotation databases
Ensembl	FBgn0010391. Drosophila melanogaster. [Contig view]
GeneID	47251.
KEGG	dme:Dmel_CG2522.
NMPDR	fig|7227.3.peg.17362.
Organism-specific databases
FlyBase	FBgn0010391. Gtp-bp.
Phylogenomic databases
HOGENOM	Q9U5L1.
OMA	Q9U5L1. FVVGFQK.
Enzyme and pathway databases
BioCyc	DMEL-XXX-02:DMEL-XXX-02-001433-MON.
Gene expression databases
ArrayExpress	Q9U5L1.
GermOnline	CG2522. Drosophila melanogaster.
Family and domain databases
InterPro	IPR003593. ATPase_AAA+_core. IPR007222. Sig_recog_particle_rcpt_asu_N. IPR000897. Signal_recog_part_SRP54_GTPase. IPR013822. Signal_recog_particl_SRP54_hlx. [Graphical view]
Pfam	PF04086. SRP-alpha_N. 1 hit. PF00448. SRP54. 1 hit. PF02881. SRP54_N. 1 hit. [Graphical view]
ProDom	PD000819. SRP54. 1 hit. [Graphical view] [Entries sharing at least one domain]
SMART	SM00382. AAA. 1 hit. [Graphical view]
PROSITE	PS00300. SRP54. 1 hit. [Graphical view]
ProtoNet	Search...
Other Resources
NextBio	838983.

Entry information

Entry name

SRPR_DROME

Accession

Primary (citable) accession number: Q9U5L1
Secondary accession number(s): Q95RJ8, Q9VZ29

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 10, 2004
Last sequence update:	May 10, 2004
Last modified:	June 16, 2009
This is version 68 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

Drosophila annotation project