Reviewed, UniProtKB/Swiss-Prot Q24434 (ORD_DROME)

Names and origin

Protein names

Recommended name:
    Protein ORD
Alternative name(s):
    Orientation disrupter protein

Gene names

Name:	ord
ORF Names:	CG3134

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

General annotation (Comments)

Function	Essential for proper maintenance of sister-chromatid cohesion in both male and female meiosis. Mutations in ord cause premature separation of the sister chromatids in meiosis I and random segregation in both meiotic divisions. Required for chiasma maintenance in female meiosis. Mutations in ord reduce recombination in female meiosis.
Subunit structure	Interacts with Sce.
Subcellular location	Nucleus. Note= In male meiosis it assembles onto chromosomes in late G2 of the meiotic cell cycle. It remains at the centromeres after chromosome condensation, through the meiosis I division until the separation of sister chromatids at anaphase II.

Ontologies

Keywords
Biological process	Meiosis
Cellular component	Nucleus
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	female meiosis sister chromatid cohesion Ref.4 Inferred from direct assay. Source: UniProtKB gamete generation Inferred from mutant phenotype. Source: FlyBase male meiosis chromosome segregation Inferred from mutant phenotype. Source: FlyBase male meiosis sister chromatid cohesion Ref.5 Inferred from direct assay. Source: UniProtKB mitosis Inferred from mutant phenotype. Source: FlyBase
Cellular component	cohesin complex Ref.6 Inferred from direct assay. Source: UniProtKB female germ cell nucleus Ref.4 Inferred from direct assay. Source: UniProtKB male germ cell nucleus Ref.5 Inferred from direct assay. Source: UniProtKB
Molecular function	protein binding Ref.6 Inferred from physical interaction. Source: UniProtKB
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
Sce	Q9VB08	2	EBI-87863,EBI-145507

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 479	479	Protein ORD		PRO_0000058080
Experimental info
	Sequence conflict	444	1	D → E in CAA63426. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	Q24434-1 [UniParc]. Last modified July 19, 2003. Version 2. Checksum: D2149D0325E2497D	FASTA	479	55,166
	10 20 30 40 50 60 MYGETTLNKN HVIKFIKLKI NNCLGCDEVE INFSKADNVH IIIYSLVTDM AKDLPAVTPV 70 80 90 100 110 120 AQAILLLCSL TYPDSDSLET IPQLKIGKGS VSMSFKVYPV NKEEETEPES ESDLDEGPST 130 140 150 160 170 180 SKQALERMVQ RAERKAKEAS TRNVHSKGIY VNVERRFDMY FALDTVSYYI NGGKRQSCPL 190 200 210 220 230 240 PEFHAKFFVR PQHSINLLRQ LHEKCSGNWL KVIQSDGDGD AFKKFKDPDS PFETFVKLFE 250 260 270 280 290 300 SNPIKPNDMM GKLAKTCLHV NEAVRLTERE FILEVFNQVR HIFEYITAQE YTVWFLVPCL 310 320 330 340 350 360 GDKDQLRSKT LEDFDLTKVR TSIRRAGDTS NIWWDHTDHN IKDILLVAFQ LDLATHVNQS 370 380 390 400 410 420 VLVISHLETL AEFSTMQYVT AFFMNDFYAK KNTEPKWICH RYLERIIDVA LFLGVIVIIE 430 440 450 460 470 YPSAFTLLQE GRHLIKCFQK ENADSSRTSQ WEIFEDVVKE NESDLEFLKE AVGKVQQNV

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Identification of ORD, a Drosophila protein essential for sister chromatid cohesion." Bickel S.E., Wyman D.W., Miyazaki W.Y., Moore D.P., Orr-Weaver T.L. EMBO J. 15:1451-1459(1996) [PubMed: 8635478] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Testis.
[2]	"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.
[3]	"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.
[4]	"The sister-chromatid cohesion protein ORD is required for chiasma maintenance in Drosophila oocytes." Bickel S.E., Orr-Weaver T.L., Balicky E.M. Curr. Biol. 12:925-929(2002) [PubMed: 12062057] [Abstract] Cited for: CHARACTERIZATION.
[5]	"Meiotic cohesion requires accumulation of ORD on chromosomes before condensation." Balicky E.M., Endres M.W., Lai C., Bickel S.E. Mol. Biol. Cell 13:3890-3900(2002) [PubMed: 12429833] [Abstract] Cited for: CHARACTERIZATION.
[6]	"A proposed role for the Polycomb group protein dRING in meiotic sister-chromatid cohesion." Balicky E.M., Young L., Orr-Weaver T.L., Bickel S.E. Chromosoma 112:231-239(2004) [PubMed: 14669021] [Abstract] Cited for: INTERACTION WITH SCE.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBLGenBankDDBJ	X92840 mRNA. Translation: CAA63426.1. AE013599 Genomic DNA. Translation: AAF46975.1.
PIR	S66578.
RefSeq	NP_726303.1.
UniGene	Dm.3857
3D structure databases
ModBase	Search...
Protein-protein interaction databases
IntAct	Q24434.
Genome annotation databases
Ensembl	CG3134. Drosophila melanogaster. [Contig view]
GeneID	37687.
KEGG	dme:Dmel_CG3134.
NMPDR	fig|7227.3.peg.7009.
Organism-specific databases
FlyBase	FBgn0003009. ord.
Phylogenomic databases
HOGENOM	Q24434.
Enzyme and pathway databases
BioCyc	DMEL-XXX-02:DMEL-XXX-02-006175-MON.
Gene expression databases
ArrayExpress	Q24434.
GermOnline	CG3134. Drosophila melanogaster.
Family and domain databases
ProtoNet	Search...
Other Resources
NextBio	804903.

Entry information

Entry name

ORD_DROME

Accession

Primary (citable) accession number: Q24434
Secondary accession number(s): Q9W1S8

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 19, 2003
Last sequence update:	July 19, 2003
Last modified:	November 4, 2008
This is version 56 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

Drosophila annotation project