Q04652 (KELC_DROME) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Ring canal kelch protein

Cleaved into the following chain:

1. Kelch short protein

Gene names

Name:	kel
ORF Names:	CG7210

Organism

Drosophila melanogaster (Fruit fly) [Reference proteome]

Taxonomic identifier

7227 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Protostomia › Ecdysozoa › Panarthropoda › Arthropoda › Mandibulata › Pancrustacea › Hexapoda › Insecta › Dicondylia › Pterygota › Neoptera › Endopterygota › Diptera › Brachycera › Muscomorpha › Eremoneura › Cyclorrhapha › Schizophora › Acalyptratae › Ephydroidea › Drosophilidae › Drosophilinae › Drosophilini › Drosophilina › Drosophiliti › Drosophila › Sophophora › melanogaster group › melanogaster subgroup

Protein attributes

Sequence length	1477 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Component of ring canals that regulates the flow of cytoplasm between cells. May be involved in the regulation of cytoplasm flow from nurse cells to the oocyte during oogenesis. Binds actin. Ref.1 Ref.5
Subcellular location	Cytoplasm › cytoskeleton. Note: Inner surface of cytoplasmic bridges or ring canals present in egg chambers. Subcortically in imaginal disk epithelia. Ref.1 Ref.5
Tissue specificity	Both proteins are expressed in ovaries, male testis, ovariectomized females, cuticle, salivary gland and imaginal disks. Kelch short protein is the predominant form and is also expressed in fat bodies. On entry into metamorphosis levels of full length protein increase in testis and imaginal disks. Ref.5
Developmental stage	Larvae, pupae and adults. Ref.5
Sequence similarities	Contains 1 BTB (POZ) domain. Contains 6 Kelch repeats.
Sequence caution	The sequence ADZ05867.1 differs from that shown. Reason: Erroneous termination at position 690. Translated as Sec.

Ontologies

Keywords
Biological process	Differentiation Oogenesis
Cellular component	Cytoplasm Cytoskeleton
Coding sequence diversity	Selenocysteine
Domain	Kelch repeat Repeat
Ligand	Actin-binding
Molecular function	Developmental protein
PTM	Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	actin cytoskeleton organization Inferred from mutant phenotype PubMed 15979065. Source: FlyBase cellularization Inferred from mutant phenotype PubMed 16421189. Source: FlyBase female germline ring canal formation Inferred from direct assay PubMed 7925006. Source: FlyBase karyosome formation Inferred from mutant phenotype PubMed 15979065. Source: FlyBase ovarian follicle cell migration Inferred from mutant phenotype PubMed 1783295. Source: FlyBase ovarian fusome organization Inferred from mutant phenotype PubMed 15979065. Source: FlyBase
Cellular_component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-KW cytoskeleton Inferred from electronic annotation. Source: UniProtKB-SubCell female germline ring canal inner rim Traceable author statement PubMed 10556087PubMed 9093858. Source: FlyBase
Molecular_function	actin binding Inferred from direct assay PubMed 11854310. Source: FlyBase
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 1477	1477	Ring canal kelch protein		PRO_0000016651
	Chain	1 – 689	689	Kelch short protein		PRO_0000016652
Regions
	Domain	157 – 223	67	BTB
	Repeat	404 – 449	46	Kelch 1
	Repeat	450 – 496	47	Kelch 2
	Repeat	498 – 543	46	Kelch 3
	Repeat	545 – 592	48	Kelch 4
	Repeat	594 – 639	46	Kelch 5
	Repeat	641 – 687	47	Kelch 6
	Compositional bias	18 – 28	11	Asn-rich
	Compositional bias	29 – 87	59	Gln-rich
	Compositional bias	29 – 36	8	Poly-Gln
	Compositional bias	78 – 83	6	Poly-Gln
Amino acid modifications
	Non-standard residue	690	1	Selenocysteine Probable
	Modified residue	108	1	Phosphoserine Ref.6
	Modified residue	111	1	Phosphoserine Ref.6
Experimental info
	Sequence conflict	493	1	V → A in AAA53471. Ref.1
	Sequence conflict	493	1	V → A in AAA53472. Ref.1
	Sequence conflict	596	1	A → R in AAA53471. Ref.1
	Sequence conflict	596	1	A → R in AAA53472. Ref.1
	Sequence conflict	824	1	P → L in AAA53472. Ref.1
	Sequence conflict	858	1	G → D in AAA53472. Ref.1
	Sequence conflict	1083	1	A → R in AAA53472. Ref.1
	Sequence conflict	1086	1	A → G in AAA53472. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	Q04652 [UniParc]. Last modified February 26, 2008. Version 4. Checksum: 1125703128F2BCCD	FASTA	1,477	160,133
	10 20 30 40 50 60 MIALSALLTK YTIGIMSNLS NGNSNNNNQQ QQQQQQGQNP QQPAQNEGGA GAEFVAPPPG 70 80 90 100 110 120 LGAAVGVAAM QQRNRLLQQQ QQQHHHHQNP AAEGSGLERG SCLLRYASQN SLDESSQKHV 130 140 150 160 170 180 QRPNGKERGT VGQYSNEQHT ARSFDAMNEM RKQKQLCDVI LVADDVEIHA HRMVLASCSP 190 200 210 220 230 240 YFYAMFTSFE ESRQARITLQ SVDARALELL IDYVYTATVE VNEDNVQVLL TAANLLQLTD 250 260 270 280 290 300 VRDACCDFLQ TQLDASNCLG IREFADIHAC VELLNYAETY IEQHFNEVIQ FDEFLNLSHE 310 320 330 340 350 360 QVISLIGNDR ISVPNEERVY ECVIAWLRYD VPMREQFTSL LMEHVRLPFL SKEYITQRVD 370 380 390 400 410 420 KEILLEGNIV CKNLIIEALT YHLLPTETKS ARTVPRKPVG MPKILLVIGG QAPKAIRSVE 430 440 450 460 470 480 WYDLREEKWY QAAEMPNRRC RSGLSVLGDK VYAVGGFNGS LRVRTVDVYD PATDQWANCS 490 500 510 520 530 540 NMEARRSTLG VAVLNGCIYA VGGFDGTTGL SSAEMYDPKT DIWRFIASMS TRRSSVGVGV 550 560 570 580 590 600 VHGLLYAVGG YDGFTRQCLS SVERYNPDTD TWVNVAEMSS RRSGAGVGVL NNILYAVGGH 610 620 630 640 650 660 DGPMVRRSVE AYDCETNSWR SVADMSYCRR NAGVVAHDGL LYVVGGDDGT SNLASVEVYC 670 680 690 700 710 720 PDSDSWRILP ALMTIGRSYA GVCMIDKPMU MEEQGALARQ AASLAIALLD DENSQAEGTM 730 740 750 760 770 780 EGAIGGAIYG NLAPAGGAAA AAAPAAPAQA PQPNHPHYEN IYAPIGQPSN NNNNSGSNSN 790 800 810 820 830 840 QAAAIANANA PANAEEIQQQ QQPAPTEPNA NNNPQPPTAA APAPSQQQQQ QQAQPQQPQR 850 860 870 880 890 900 ILPMNNYRND LYDRSAAGGV CSAYDVPRAV RSGLGYRRNF RIDMQNGNRC GSGLRCTPLY 910 920 930 940 950 960 TNSRSNCQRQ RSFDDTESTD GYNLPYAGAG TMRYENIYEQ IRDEPLYRTS AANRVPLYTR 970 980 990 1000 1010 1020 LDVLGHGIGR IERHLSSSCG NIDHYNLGGH YAVLGHSHFG TVGHIRLNAN GSGVAAPGVA 1030 1040 1050 1060 1070 1080 GTGTCNVPNC QGYMTAAGST VPVEYANVKV PVKNSASSFF SCLHGENSQS MTNIYKTSGT 1090 1100 1110 1120 1130 1140 AAAMAAHNSP LTPNVSMERA SRSASAGAAG SAAAAVEEHS AADSIPSSSN INANRTTGAI 1150 1160 1170 1180 1190 1200 PKVKTANKPA KESGGSSTAA SPILDKTTST GSGKSVTLAK KTSTAAARSS SSGDTNGNGT 1210 1220 1230 1240 1250 1260 LNRISKSSLQ WLLVNKWLPL WIGQGPDCKV IDFNFMFSRD CVSCDTASVA SQMSNPYGTP 1270 1280 1290 1300 1310 1320 RLSGLPQDMV RFQSSCAGAC AAAGAASTIR RDANASARPL HSTLSRLRNG EKRNPNRVAG 1330 1340 1350 1360 1370 1380 NYQYEDPSYE NVHVQWQNGF EFGRSRDYDP NSTYHQQRPL LQRARSESPT FSNQQRRLQR 1390 1400 1410 1420 1430 1440 QGAQAQQQSQ QPKPPGSPDP YKNYKLNADN NTFKPKPIAA DELEGAVGGA VAEIALPEVD 1450 1460 1470 IEVVDPVSLS DNETETTSSQ NNLPSTTNSN NLNEHND

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Kelch encodes a component of intercellular bridges in Drosophila egg chambers." Xue F., Cooley L. Cell 72:681-693(1993) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBCELLULAR LOCATION. Tissue: Embryo.
[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] [Europe PMC] [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] [Europe PMC] [Abstract] Cited for: GENOME REANNOTATION. Strain: Berkeley.
[4]	Stapleton M., Brokstein P., Hong L., Agbayani A., Carlson J.W., Champe M., Chavez C., Dorsett V., Dresnek D., Farfan D., Frise E., George R.A., Gonzalez M., Guarin H., Kronmiller B., Li P.W., Liao G., Miranda A. , Mungall C.J., Nunoo J., Pacleb J.M., Paragas V., Park S., Patel S., Phouanenavong S., Wan K.H., Yu C., Lewis S.E., Rubin G.M., Celniker S.E. Submitted (MAR-2011) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: Berkeley. Tissue: Embryo.
[5]	"Examination of the function of two kelch proteins generated by stop codon suppression." Robinson D.N., Cooley L. Development 124:1405-1417(1997) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, PROBABLE SELENOCYSTEINE AT SEC-690, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE. Tissue: Embryo.
[6]	"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] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-108 AND SER-111, MASS SPECTROMETRY. Tissue: Embryo.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	L08483 mRNA. Translation: AAA53471.1. L08483 mRNA. Translation: AAA53472.2. AE014134 Genomic DNA. Translation: AAF53651.1. AE014134 Genomic DNA. Translation: AAN11182.3. BT003250 mRNA. Translation: ADZ05867.1. Sequence problems.
PIR	A45773.
RefSeq	NP_476589.4. NM_057241.2. NP_724095.1. NM_165242.1.
UniGene	Dm.17986.
3D structure databases
ProteinModelPortal	Q04652.
SMR	Q04652. Positions 135-366, 402-687.
ModBase	Search...
Protein-protein interaction databases
IntAct	Q04652. 1 interaction.
MINT	MINT-743495.
Proteomic databases
PaxDb	Q04652.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	35084.
KEGG	dme:Dmel_CG7210.
UCSC	CG7210-RA. d. melanogaster.
Organism-specific databases
CTD	3792.
FlyBase	FBgn0001301. kel.
Phylogenomic databases
eggNOG	NOG149197.
InParanoid	Q04652.
KO	K10443.
OMA	LREEKWY.
OrthoDB	EOG42NGF7.
Gene expression databases
Bgee	Q04652.
GermOnline	CG7210. Drosophila melanogaster.
Family and domain databases
Gene3D	2.130.10.80. 1 hit. 3.30.710.10. 1 hit.
InterPro	IPR011705. BACK. IPR000210. BTB/POZ-like. IPR011333. BTB/POZ_fold. IPR013069. BTB_POZ. IPR015916. Gal_Oxidase_b-propeller. IPR006652. Kelch_1. [Graphical view]
Pfam	PF07707. BACK. 1 hit. PF00651. BTB. 1 hit. PF01344. Kelch_1. 6 hits. [Graphical view]
SMART	SM00875. BACK. 1 hit. SM00225. BTB. 1 hit. SM00612. Kelch. 6 hits. [Graphical view]
SUPFAM	SSF54695. BTB/POZ_fold. 1 hit.
PROSITE	PS50097. BTB. 1 hit. [Graphical view]
ProtoNet	Search...
Other
ChiTaRS	KEL. drosophila.
GenomeRNAi	35084.
NextBio	791777.

Entry information

Entry name

KELC_DROME

Accession

Primary (citable) accession number: Q04652
Secondary accession number(s): F0JAF0 , Q04653, Q86PA7, Q9VJA2

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 1, 1994
Last sequence update:	February 26, 2008
Last modified:	May 1, 2013
This is version 115 of the entry and version 4 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Drosophila annotation project