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Protein

Ring canal kelch protein

Gene

kel

Organism
Drosophila melanogaster (Fruit fly)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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.2 Publications

GO - Molecular functioni

  • actin binding Source: FlyBase

GO - Biological processi

  • actin cytoskeleton organization Source: FlyBase
  • cellularization Source: FlyBase
  • cytoplasmic transport, nurse cell to oocyte Source: FlyBase
  • female germline ring canal formation Source: FlyBase
  • karyosome formation Source: FlyBase
  • oogenesis Source: FlyBase
  • ovarian follicle cell migration Source: FlyBase
  • ovarian fusome organization Source: FlyBase
  • ovarian nurse cell to oocyte transport Source: FlyBase
Complete GO annotation...

Keywords - Molecular functioni

Developmental protein

Keywords - Biological processi

Differentiation, Oogenesis

Keywords - Ligandi

Actin-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Ring canal kelch protein
Cleaved into the following chain:
Gene namesi
Name:kel
ORF Names:CG7210
OrganismiDrosophila melanogaster (Fruit fly)
Taxonomic identifieri7227 [NCBI]
Taxonomic lineageiEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora
Proteomesi
  • UP000000803 Componenti: Chromosome 2L

Organism-specific databases

FlyBaseiFBgn0001301. kel.

Subcellular locationi

  • Cytoplasmcytoskeleton 2 Publications

  • Note: Inner surface of cytoplasmic bridges or ring canals present in egg chambers. Subcortically in imaginal disk epithelia.

GO - Cellular componenti

  • cell cortex Source: FlyBase
  • cytoskeleton Source: UniProtKB-SubCell
  • cytosol Source: GOC
  • female germline ring canal Source: FlyBase
  • female germline ring canal inner rim Source: FlyBase
  • germline ring canal Source: FlyBase
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Cytoskeleton

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 14771477Ring canal kelch proteinPRO_0000016651Add
BLAST
Chaini1 – 689689Kelch short proteinPRO_0000016652Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei108 – 1081Phosphoserine1 Publication
Modified residuei111 – 1111Phosphoserine1 Publication

Keywords - PTMi

Phosphoprotein

Proteomic databases

PaxDbiQ04652.
PRIDEiQ04652.

PTM databases

iPTMnetiQ04652.

Expressioni

Tissue specificityi

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.1 Publication

Developmental stagei

Larvae, pupae and adults.1 Publication

Gene expression databases

BgeeiQ04652.
GenevisibleiQ04652. DM.

Interactioni

GO - Molecular functioni

  • actin binding Source: FlyBase

Protein-protein interaction databases

BioGridi61080. 6 interactions.
IntActiQ04652. 2 interactions.
MINTiMINT-743495.
STRINGi7227.FBpp0080596.

Structurei

3D structure databases

ProteinModelPortaliQ04652.
SMRiQ04652. Positions 135-366, 402-687.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini157 – 22367BTBPROSITE-ProRule annotationAdd
BLAST
Repeati404 – 44946Kelch 1Add
BLAST
Repeati450 – 49647Kelch 2Add
BLAST
Repeati498 – 54346Kelch 3Add
BLAST
Repeati545 – 59248Kelch 4Add
BLAST
Repeati594 – 63946Kelch 5Add
BLAST
Repeati641 – 68747Kelch 6Add
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi18 – 2811Asn-richAdd
BLAST
Compositional biasi29 – 8759Gln-richAdd
BLAST
Compositional biasi29 – 368Poly-Gln
Compositional biasi78 – 836Poly-Gln

Sequence similaritiesi

Contains 1 BTB (POZ) domain.PROSITE-ProRule annotation
Contains 6 Kelch repeats.Curated

Keywords - Domaini

Kelch repeat, Repeat

Phylogenomic databases

eggNOGiKOG4441. Eukaryota.
ENOG410XNX8. LUCA.
GeneTreeiENSGT00760000118931.
InParanoidiQ04652.
KOiK10443.
OMAiFEFGRSR.
OrthoDBiEOG7ZWD17.

Family and domain databases

Gene3Di2.130.10.80. 1 hit.
InterProiIPR011705. BACK.
IPR000210. BTB/POZ_dom.
IPR015916. Gal_Oxidase_b-propeller.
IPR006652. Kelch_1.
IPR011333. SKP1/BTB/POZ.
[Graphical view]
PfamiPF07707. BACK. 1 hit.
PF00651. BTB. 1 hit.
PF01344. Kelch_1. 6 hits.
[Graphical view]
SMARTiSM00875. BACK. 1 hit.
SM00225. BTB. 1 hit.
SM00612. Kelch. 6 hits.
[Graphical view]
SUPFAMiSSF54695. SSF54695. 1 hit.
PROSITEiPS50097. BTB. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q04652-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MIALSALLTK YTIGIMSNLS NGNSNNNNQQ QQQQQQGQNP QQPAQNEGGA
60 70 80 90 100
GAEFVAPPPG LGAAVGVAAM QQRNRLLQQQ QQQHHHHQNP AAEGSGLERG
110 120 130 140 150
SCLLRYASQN SLDESSQKHV QRPNGKERGT VGQYSNEQHT ARSFDAMNEM
160 170 180 190 200
RKQKQLCDVI LVADDVEIHA HRMVLASCSP YFYAMFTSFE ESRQARITLQ
210 220 230 240 250
SVDARALELL IDYVYTATVE VNEDNVQVLL TAANLLQLTD VRDACCDFLQ
260 270 280 290 300
TQLDASNCLG IREFADIHAC VELLNYAETY IEQHFNEVIQ FDEFLNLSHE
310 320 330 340 350
QVISLIGNDR ISVPNEERVY ECVIAWLRYD VPMREQFTSL LMEHVRLPFL
360 370 380 390 400
SKEYITQRVD KEILLEGNIV CKNLIIEALT YHLLPTETKS ARTVPRKPVG
410 420 430 440 450
MPKILLVIGG QAPKAIRSVE WYDLREEKWY QAAEMPNRRC RSGLSVLGDK
460 470 480 490 500
VYAVGGFNGS LRVRTVDVYD PATDQWANCS NMEARRSTLG VAVLNGCIYA
510 520 530 540 550
VGGFDGTTGL SSAEMYDPKT DIWRFIASMS TRRSSVGVGV VHGLLYAVGG
560 570 580 590 600
YDGFTRQCLS SVERYNPDTD TWVNVAEMSS RRSGAGVGVL NNILYAVGGH
610 620 630 640 650
DGPMVRRSVE AYDCETNSWR SVADMSYCRR NAGVVAHDGL LYVVGGDDGT
660 670 680 690 700
SNLASVEVYC PDSDSWRILP ALMTIGRSYA GVCMIDKPMU MEEQGALARQ
710 720 730 740 750
AASLAIALLD DENSQAEGTM EGAIGGAIYG NLAPAGGAAA AAAPAAPAQA
760 770 780 790 800
PQPNHPHYEN IYAPIGQPSN NNNNSGSNSN QAAAIANANA PANAEEIQQQ
810 820 830 840 850
QQPAPTEPNA NNNPQPPTAA APAPSQQQQQ QQAQPQQPQR ILPMNNYRND
860 870 880 890 900
LYDRSAAGGV CSAYDVPRAV RSGLGYRRNF RIDMQNGNRC GSGLRCTPLY
910 920 930 940 950
TNSRSNCQRQ RSFDDTESTD GYNLPYAGAG TMRYENIYEQ IRDEPLYRTS
960 970 980 990 1000
AANRVPLYTR LDVLGHGIGR IERHLSSSCG NIDHYNLGGH YAVLGHSHFG
1010 1020 1030 1040 1050
TVGHIRLNAN GSGVAAPGVA GTGTCNVPNC QGYMTAAGST VPVEYANVKV
1060 1070 1080 1090 1100
PVKNSASSFF SCLHGENSQS MTNIYKTSGT AAAMAAHNSP LTPNVSMERA
1110 1120 1130 1140 1150
SRSASAGAAG SAAAAVEEHS AADSIPSSSN INANRTTGAI PKVKTANKPA
1160 1170 1180 1190 1200
KESGGSSTAA SPILDKTTST GSGKSVTLAK KTSTAAARSS SSGDTNGNGT
1210 1220 1230 1240 1250
LNRISKSSLQ WLLVNKWLPL WIGQGPDCKV IDFNFMFSRD CVSCDTASVA
1260 1270 1280 1290 1300
SQMSNPYGTP RLSGLPQDMV RFQSSCAGAC AAAGAASTIR RDANASARPL
1310 1320 1330 1340 1350
HSTLSRLRNG EKRNPNRVAG NYQYEDPSYE NVHVQWQNGF EFGRSRDYDP
1360 1370 1380 1390 1400
NSTYHQQRPL LQRARSESPT FSNQQRRLQR QGAQAQQQSQ QPKPPGSPDP
1410 1420 1430 1440 1450
YKNYKLNADN NTFKPKPIAA DELEGAVGGA VAEIALPEVD IEVVDPVSLS
1460 1470
DNETETTSSQ NNLPSTTNSN NLNEHND
Length:1,477
Mass (Da):160,133
Last modified:February 26, 2008 - v4
Checksum:i1125703128F2BCCD
GO

Sequence cautioni

The sequence ADZ05867.1 differs from that shown. Reason: Erroneous termination at position 690. Translated as Sec.Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti493 – 4931V → A in AAA53471 (PubMed:8453663).Curated
Sequence conflicti493 – 4931V → A in AAA53472 (PubMed:8453663).Curated
Sequence conflicti596 – 5961A → R in AAA53471 (PubMed:8453663).Curated
Sequence conflicti596 – 5961A → R in AAA53472 (PubMed:8453663).Curated
Sequence conflicti824 – 8241P → L in AAA53472 (PubMed:8453663).Curated
Sequence conflicti858 – 8581G → D in AAA53472 (PubMed:8453663).Curated
Sequence conflicti1083 – 10831A → R in AAA53472 (PubMed:8453663).Curated
Sequence conflicti1086 – 10861A → G in AAA53472 (PubMed:8453663).Curated

Non-standard residue

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Non-standard residuei690 – 6901SelenocysteineCurated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
PIRiA45773.
RefSeqiNP_476589.4. NM_057241.3.
NP_724095.1. NM_165242.2.
UniGeneiDm.17986.

Genome annotation databases

EnsemblMetazoaiFBtr0081043; FBpp0080596; FBgn0001301.
GeneIDi35084.
KEGGidme:Dmel_CG7210.
UCSCiCG7210-RA. d. melanogaster.

Keywords - Coding sequence diversityi

Selenocysteine

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
PIRiA45773.
RefSeqiNP_476589.4. NM_057241.3.
NP_724095.1. NM_165242.2.
UniGeneiDm.17986.

3D structure databases

ProteinModelPortaliQ04652.
SMRiQ04652. Positions 135-366, 402-687.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi61080. 6 interactions.
IntActiQ04652. 2 interactions.
MINTiMINT-743495.
STRINGi7227.FBpp0080596.

PTM databases

iPTMnetiQ04652.

Proteomic databases

PaxDbiQ04652.
PRIDEiQ04652.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblMetazoaiFBtr0081043; FBpp0080596; FBgn0001301.
GeneIDi35084.
KEGGidme:Dmel_CG7210.
UCSCiCG7210-RA. d. melanogaster.

Organism-specific databases

CTDi3792.
FlyBaseiFBgn0001301. kel.

Phylogenomic databases

eggNOGiKOG4441. Eukaryota.
ENOG410XNX8. LUCA.
GeneTreeiENSGT00760000118931.
InParanoidiQ04652.
KOiK10443.
OMAiFEFGRSR.
OrthoDBiEOG7ZWD17.

Miscellaneous databases

ChiTaRSikel. fly.
GenomeRNAii35084.
PROiQ04652.

Gene expression databases

BgeeiQ04652.
GenevisibleiQ04652. DM.

Family and domain databases

Gene3Di2.130.10.80. 1 hit.
InterProiIPR011705. BACK.
IPR000210. BTB/POZ_dom.
IPR015916. Gal_Oxidase_b-propeller.
IPR006652. Kelch_1.
IPR011333. SKP1/BTB/POZ.
[Graphical view]
PfamiPF07707. BACK. 1 hit.
PF00651. BTB. 1 hit.
PF01344. Kelch_1. 6 hits.
[Graphical view]
SMARTiSM00875. BACK. 1 hit.
SM00225. BTB. 1 hit.
SM00612. Kelch. 6 hits.
[Graphical view]
SUPFAMiSSF54695. SSF54695. 1 hit.
PROSITEiPS50097. BTB. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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. Cited for: GENOME REANNOTATION.
    Strain: Berkeley.
  4. 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, 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, IDENTIFICATION BY MASS SPECTROMETRY.
    Tissue: Embryo.

Entry informationi

Entry nameiKELC_DROME
AccessioniPrimary (citable) accession number: Q04652
Secondary accession number(s): F0JAF0
, Q04653, Q86PA7, Q9VJA2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1994
Last sequence update: February 26, 2008
Last modified: June 8, 2016
This is version 137 of the entry and version 4 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programDrosophila annotation project

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Drosophila
    Drosophila: entries, gene names and cross-references to FlyBase
  2. SIMILARITY comments
    Index of protein domains and families

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.