Reviewed, UniProtKB/Swiss-Prot P48809 (RB27C_DROME)

Names and origin

Protein names

Recommended name:
    Heterogeneous nuclear ribonucleoprotein 27C
      Short name=Hrb27-C
Alternative name(s):
    hnRNP 48
    HRP48.1

Gene names

Name:	Hrb27C
Synonyms:	hrp48, Rbp7
ORF Names:	CG10377

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

General annotation (Comments)

Function	This protein is a component of ribonucleosomes. Could be needed to organize a concentration gradient of a dorsalizing morphogen (Dm) originating in the germinal vesicle.
Subcellular location	Nucleus. Cytoplasm. Note= Nuclear and/or cytoplasmic.
Sequence similarities	Contains 2 RRM (RNA recognition motif) domains.

Ontologies

Keywords
Cellular component	Cytoplasm Nucleus
Coding sequence diversity	Alternative splicing
Domain	Repeat
Ligand	RNA-binding
Molecular function	Ribonucleoprotein
PTM	Phosphoprotein
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	border follicle cell migration Inferred from mutant phenotype. Source: FlyBase negative regulation of oskar mRNA translation Traceable author statement. Source: FlyBase pole plasm oskar mRNA localization Inferred from mutant phenotype. Source: FlyBase positive regulation of translation Inferred from direct assay. Source: FlyBase regulation of nuclear mRNA splicing, via spliceosome Inferred from mutant phenotype. Source: FlyBase
Cellular component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-KW nucleoplasm Inferred from direct assay. Source: FlyBase ribonucleoprotein complex Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	mRNA 3'-UTR binding Inferred from direct assay. Source: FlyBase mRNA 5'-UTR binding Traceable author statement. Source: FlyBase nucleotide binding Inferred from electronic annotation. Source: InterPro protein binding Inferred from physical interaction. Source: IntAct single-stranded DNA binding Inferred from direct assay. Source: FlyBase
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
Fps85D	P18106-1	1	EBI-202331,EBI-197780
Rb97D	Q02926-2	1	EBI-202331,EBI-202379
tna	Q9VTB8	1	EBI-202331,EBI-162797

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]

Isoform A (identifier: P48809-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

Notes: No experimental confirmation available.

Isoform B (identifier: P48809-2)

The sequence of this isoform differs from the canonical sequence as follows:
     262-297: Missing.

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 421	421	Heterogeneous nuclear ribonucleoprotein 27C		PRO_0000081748
Regions
	Domain	7 – 88	82	RRM 1
	Domain	96 – 173	78	RRM 2
Amino acid modifications
	Modified residue	177	1	Phosphoserine
	Modified residue	366	1	Phosphoserine
	Modified residue	368	1	Phosphoserine
	Modified residue	370	1	Phosphoserine
	Modified residue	372	1	Phosphotyrosine
	Modified residue	379	1	Phosphoserine
Natural variations
	Alternative sequence	262 – 297	36	Missing in isoform B.		VSP_015738

Sequences

	Sequence		Length	Mass (Da)
	Isoform A [UniParc]. Last modified September 27, 2005. Version 2. Checksum: D59DD2A647CE23F5	FASTA	421	44,770
	10 20 30 40 50 60 MEEDERGKLF VGGLSWETTQ ENLSRYFCRF GDIIDCVVMK NNESGRSRGF GFVTFADPTN 70 80 90 100 110 120 VNHVLQNGPH TLDGRTIDPK PCNPRTLQKP KKGGGYKVFL GGLPSNVTET DLRTFFNRYG 130 140 150 160 170 180 KVTEVVIMYD QEKKKSRGFG FLSFEEESSV EHVTNERYIN LNGKQVEIKK AEPRDGSGGQ 190 200 210 220 230 240 NSNNSTVGGA YGKLGNECSH WGPHHAPINM MQGQNGQMGG PPLNMPIGAP NMMPGYQGWG 250 260 270 280 290 300 TSPQQQQYGY GNSGPGSYQG WGAPPGPQGP PPQWSNYAGP QQTQGYGGYD MYNSTSTGAP 310 320 330 340 350 360 SGPSGGGSWN SWNMPPNSAG PTGAPGAGAG TATDMYSRAQ AWATGGPSTT GPVGGMPRTG 370 380 390 400 410 420 PGNSASKSGS EYDYGGYGSG YDYDYSNYVK QEGASNYGAG PRSAYGNDSS TQPPYATSQA V
	Isoform B [UniParc]. Checksum: 7543E50FA96C9D4E		385	41,030
	10 20 30 40 50 60 MEEDERGKLF VGGLSWETTQ ENLSRYFCRF GDIIDCVVMK NNESGRSRGF GFVTFADPTN 70 80 90 100 110 120 VNHVLQNGPH TLDGRTIDPK PCNPRTLQKP KKGGGYKVFL GGLPSNVTET DLRTFFNRYG 130 140 150 160 170 180 KVTEVVIMYD QEKKKSRGFG FLSFEEESSV EHVTNERYIN LNGKQVEIKK AEPRDGSGGQ 190 200 210 220 230 240 NSNNSTVGGA YGKLGNECSH WGPHHAPINM MQGQNGQMGG PPLNMPIGAP NMMPGYQGWG 250 260 270 280 290 300 TSPQQQQYGY GNSGPGSYQG WGAPSGPSGG GSWNSWNMPP NSAGPTGAPG AGAGTATDMY 310 320 330 340 350 360 SRAQAWATGG PSTTGPVGGM PRTGPGNSAS KSGSEYDYGG YGSGYDYDYS NYVKQEGASN 370 380 YGAGPRSAYG NDSSTQPPYA TSQAV

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Characterization of the major hnRNP proteins from Drosophila melanogaster." Matunis E.L., Matunis M.J., Dreyfuss G. J. Cell Biol. 116:257-269(1992) [PubMed: 1730754] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM B). Strain: Canton-S. Tissue: Embryo.
[2]	"Rapidly evolving genes of Drosophila: differing levels of selective pressure in testis, ovary, and head tissues between sibling species." Jagadeeshan S., Singh R.S. Mol. Biol. Evol. 22:1793-1801(2005) [PubMed: 15917496] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM A). Tissue: Ovary.
[3]	"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.
[4]	"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.
[5]	"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] (ISOFORM A). Strain: Berkeley. Tissue: Embryo and Ovary.
[6]	"Isolation of RRM-type RNA-binding protein genes and the analysis of their relatedness by using a numerical approach." Kim Y.J., Baker B.S. Mol. Cell. Biol. 13:174-183(1993) [PubMed: 8417324] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 10-53.
[7]	"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-177; SER-366; SER-368; SER-370; TYR-372 AND SER-379, MASS SPECTROMETRY. Tissue: Embryo.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBLGenBankDDBJ	X62639 mRNA. Translation: CAA44505.1. DQ062784 mRNA. Translation: AAY56657.1. AE014134 Genomic DNA. Translation: AAF52456.1. AY069699 mRNA. Translation: AAL39844.1. AY128430 mRNA. Translation: AAM75023.1. S51720 mRNA. Translation: AAB24628.1.
PIR	D41732.
RefSeq	NP_476869.1. NP_723228.1. NP_723229.1.
UniGene	Dm.1997
3D structure databases
HSSP	HSSP built from PDB template 1L3K based on UniProtKB P09651.
ModBase	Search...
Protein-protein interaction databases
IntAct	P48809.
Genome annotation databases
Ensembl	CG10377. Drosophila melanogaster. [Contig view]
GeneID	33968.
KEGG	dme:Dmel_CG10377.
Organism-specific databases
FlyBase	FBgn0004838. Hrb27C.
Phylogenomic databases
HOGENOM	P48809.
Gene expression databases
ArrayExpress	P48809.
GermOnline	CG10377. Drosophila melanogaster.
Family and domain databases
InterPro	IPR012677. a_b_plait_nuc_bd. IPR000504. RRM_RNP1. [Graphical view]
Gene3D	G3DSA:3.30.70.330. a_b_plait_nuc_bd. 2 hits.
Pfam	PF00076. RRM_1. 2 hits. [Graphical view]
SMART	SM00360. RRM. 2 hits. [Graphical view]
PROSITE	PS50102. RRM. 2 hits. [Graphical view]
ProtoNet	Search...
Other Resources
NextBio	786189.

Entry information

Entry name

RB27C_DROME

Accession

Primary (citable) accession number: P48809
Secondary accession number(s): Q7JPT5, Q9TY67, Q9VM68

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 1, 1996
Last sequence update:	September 27, 2005
Last modified:	November 25, 2008
This is version 69 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

Drosophila annotation project