KELC_DROME
ID KELC_DROME Reviewed; 1477 AA.
AC Q04652; F0JAF0; Q04653; Q86PA7; Q9VJA2;
DT 01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT 26-FEB-2008, sequence version 4.
DT 03-AUG-2022, entry version 169.
DE RecName: Full=Ring canal kelch protein;
DE Contains:
DE RecName: Full=Kelch short protein;
GN Name=kel; ORFNames=CG7210;
OS Drosophila melanogaster (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7227;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND SUBCELLULAR LOCATION.
RC TISSUE=Embryo;
RX PubMed=8453663; DOI=10.1016/0092-8674(93)90397-9;
RA Xue F., Cooley L.;
RT "Kelch encodes a component of intercellular bridges in Drosophila egg
RT chambers.";
RL Cell 72:681-693(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley;
RX PubMed=10731132; DOI=10.1126/science.287.5461.2185;
RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., Brandon R.C.,
RA Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C.,
RA Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A.,
RA An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A.,
RA Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V.,
RA Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J.,
RA Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E.,
RA Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B.,
RA Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I.,
RA Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C.,
RA Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S.,
RA Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M.,
RA Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D.,
RA Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F.,
RA Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D.,
RA Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A.,
RA Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C.,
RA McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C.,
RA Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L.,
RA Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R.,
RA Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V.,
RA Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F.,
RA Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J.,
RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R.,
RA Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y.,
RA Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T.,
RA Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S.,
RA Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W.,
RA Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M.,
RA Venter J.C.;
RT "The genome sequence of Drosophila melanogaster.";
RL Science 287:2185-2195(2000).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=Berkeley;
RX PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M.,
RA Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.;
RT "Annotation of the Drosophila melanogaster euchromatic genome: a systematic
RT review.";
RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Berkeley; TISSUE=Embryo;
RA Stapleton M., Brokstein P., Hong L., Agbayani A., Carlson J.W., Champe M.,
RA Chavez C., Dorsett V., Dresnek D., Farfan D., Frise E., George R.A.,
RA Gonzalez M., Guarin H., Kronmiller B., Li P.W., Liao G., Miranda A.,
RA Mungall C.J., Nunoo J., Pacleb J.M., Paragas V., Park S., Patel S.,
RA Phouanenavong S., Wan K.H., Yu C., Lewis S.E., Rubin G.M., Celniker S.E.;
RL Submitted (MAR-2011) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP FUNCTION, SELENOCYSTEINE AT SEC-690, SUBCELLULAR LOCATION, TISSUE
RP SPECIFICITY, AND DEVELOPMENTAL STAGE.
RC TISSUE=Embryo;
RX PubMed=9118811; DOI=10.1242/dev.124.7.1405;
RA Robinson D.N., Cooley L.;
RT "Examination of the function of two kelch proteins generated by stop codon
RT suppression.";
RL Development 124:1405-1417(1997).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-108 AND SER-111, AND
RP IDENTIFICATION BY MASS SPECTROMETRY.
RC TISSUE=Embryo;
RX PubMed=18327897; DOI=10.1021/pr700696a;
RA Zhai B., Villen J., Beausoleil S.A., Mintseris J., Gygi S.P.;
RT "Phosphoproteome analysis of Drosophila melanogaster embryos.";
RL J. Proteome Res. 7:1675-1682(2008).
CC -!- FUNCTION: Component of ring canals that regulates the flow of cytoplasm
CC between cells. May be involved in the regulation of cytoplasm flow from
CC nurse cells to the oocyte during oogenesis. Binds actin.
CC {ECO:0000269|PubMed:8453663, ECO:0000269|PubMed:9118811}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton
CC {ECO:0000269|PubMed:8453663, ECO:0000269|PubMed:9118811}. Note=Inner
CC surface of cytoplasmic bridges or ring canals present in egg chambers.
CC Subcortically in imaginal disk epithelia.
CC -!- TISSUE SPECIFICITY: Both proteins are expressed in ovaries, male
CC testis, ovariectomized females, cuticle, salivary gland and imaginal
CC disks. Kelch short protein is the predominant form and is also
CC expressed in fat bodies. On entry into metamorphosis levels of full-
CC length protein increase in testis and imaginal disks.
CC {ECO:0000269|PubMed:9118811}.
CC -!- DEVELOPMENTAL STAGE: Larvae, pupae and adults.
CC {ECO:0000269|PubMed:9118811}.
CC -!- SEQUENCE CAUTION:
CC Sequence=ADZ05867.1; Type=Erroneous termination; Note=Truncated C-terminus.; Evidence={ECO:0000305};
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DR EMBL; L08483; AAA53471.1; -; mRNA.
DR EMBL; L08483; AAA53472.2; -; mRNA.
DR EMBL; AE014134; AAF53651.1; -; Genomic_DNA.
DR EMBL; AE014134; AAN11182.3; -; Genomic_DNA.
DR EMBL; BT003250; ADZ05867.1; ALT_SEQ; mRNA.
DR PIR; A45773; A45773.
DR RefSeq; NP_476589.4; NM_057241.3.
DR RefSeq; NP_724095.1; NM_165242.2.
DR BioGRID; 61080; 62.
DR IntAct; Q04652; 2.
DR STRING; 7227.FBpp0080595; -.
DR iPTMnet; Q04652; -.
DR PaxDb; Q04652; -.
DR PRIDE; Q04652; -.
DR DNASU; 35084; -.
DR GeneID; 35084; -.
DR KEGG; dme:Dmel_CG7210; -.
DR UCSC; CG7210-RA; d. melanogaster.
DR CTD; 3792; -.
DR FlyBase; FBgn0001301; kel.
DR VEuPathDB; VectorBase:FBgn0001301; -.
DR eggNOG; KOG4441; Eukaryota.
DR HOGENOM; CLU_004193_1_0_1; -.
DR InParanoid; Q04652; -.
DR Reactome; R-DME-8951664; Neddylation.
DR Reactome; R-DME-983168; Antigen processing: Ubiquitination & Proteasome degradation.
DR BioGRID-ORCS; 35084; 0 hits in 3 CRISPR screens.
DR ChiTaRS; kel; fly.
DR GenomeRNAi; 35084; -.
DR PRO; PR:Q04652; -.
DR Proteomes; UP000000803; Chromosome 2L.
DR Genevisible; Q04652; DM.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
DR GO; GO:0035324; C:female germline ring canal; IDA:FlyBase.
DR GO; GO:0035183; C:female germline ring canal inner rim; TAS:FlyBase.
DR GO; GO:0045172; C:germline ring canal; IDA:FlyBase.
DR GO; GO:0003779; F:actin binding; IDA:FlyBase.
DR GO; GO:0030036; P:actin cytoskeleton organization; IMP:FlyBase.
DR GO; GO:0007349; P:cellularization; IMP:FlyBase.
DR GO; GO:0007301; P:female germline ring canal formation; IDA:FlyBase.
DR GO; GO:0030717; P:oocyte karyosome formation; IMP:FlyBase.
DR GO; GO:0048477; P:oogenesis; IMP:FlyBase.
DR GO; GO:0007297; P:ovarian follicle cell migration; HMP:FlyBase.
DR GO; GO:0030723; P:ovarian fusome organization; IMP:FlyBase.
DR GO; GO:0007300; P:ovarian nurse cell to oocyte transport; IMP:FlyBase.
DR Gene3D; 2.120.10.80; -; 1.
DR Gene3D; 3.30.710.10; -; 1.
DR InterPro; IPR011705; BACK.
DR InterPro; IPR000210; BTB/POZ_dom.
DR InterPro; IPR015915; Kelch-typ_b-propeller.
DR InterPro; IPR006652; Kelch_1.
DR InterPro; IPR011333; SKP1/BTB/POZ_sf.
DR Pfam; PF07707; BACK; 1.
DR Pfam; PF00651; BTB; 1.
DR Pfam; PF01344; Kelch_1; 6.
DR SMART; SM00875; BACK; 1.
DR SMART; SM00225; BTB; 1.
DR SMART; SM00612; Kelch; 6.
DR SUPFAM; SSF117281; SSF117281; 1.
DR SUPFAM; SSF54695; SSF54695; 1.
DR PROSITE; PS50097; BTB; 1.
PE 1: Evidence at protein level;
KW Actin-binding; Cytoplasm; Cytoskeleton; Developmental protein;
KW Differentiation; Kelch repeat; Oogenesis; Phosphoprotein;
KW Reference proteome; Repeat; Selenocysteine.
FT CHAIN 1..1477
FT /note="Ring canal kelch protein"
FT /id="PRO_0000016651"
FT CHAIN 1..689
FT /note="Kelch short protein"
FT /id="PRO_0000016652"
FT DOMAIN 157..223
FT /note="BTB"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00037"
FT REPEAT 404..449
FT /note="Kelch 1"
FT REPEAT 450..496
FT /note="Kelch 2"
FT REPEAT 498..543
FT /note="Kelch 3"
FT REPEAT 545..592
FT /note="Kelch 4"
FT REPEAT 594..639
FT /note="Kelch 5"
FT REPEAT 641..687
FT /note="Kelch 6"
FT REGION 16..100
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 112..141
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 744..849
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1119..1200
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1294..1326
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1342..1417
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1443..1477
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 16..46
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 72..89
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 764..808
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 822..844
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1122..1141
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1150..1200
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1349..1392
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1449..1477
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_STD 690
FT /note="Selenocysteine"
FT /evidence="ECO:0000305"
FT MOD_RES 108
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 111
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT CONFLICT 493
FT /note="V -> A (in Ref. 1; AAA53471/AAA53472)"
FT /evidence="ECO:0000305"
FT CONFLICT 596
FT /note="A -> R (in Ref. 1; AAA53471/AAA53472)"
FT /evidence="ECO:0000305"
FT CONFLICT 824
FT /note="P -> L (in Ref. 1; AAA53472)"
FT /evidence="ECO:0000305"
FT CONFLICT 858
FT /note="G -> D (in Ref. 1; AAA53472)"
FT /evidence="ECO:0000305"
FT CONFLICT 1083
FT /note="A -> R (in Ref. 1; AAA53472)"
FT /evidence="ECO:0000305"
FT CONFLICT 1086
FT /note="A -> G (in Ref. 1; AAA53472)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1477 AA; 160133 MW; 1125703128F2BCCD CRC64;
MIALSALLTK YTIGIMSNLS NGNSNNNNQQ QQQQQQGQNP QQPAQNEGGA GAEFVAPPPG
LGAAVGVAAM QQRNRLLQQQ QQQHHHHQNP AAEGSGLERG SCLLRYASQN SLDESSQKHV
QRPNGKERGT VGQYSNEQHT ARSFDAMNEM RKQKQLCDVI LVADDVEIHA HRMVLASCSP
YFYAMFTSFE ESRQARITLQ SVDARALELL IDYVYTATVE VNEDNVQVLL TAANLLQLTD
VRDACCDFLQ TQLDASNCLG IREFADIHAC VELLNYAETY IEQHFNEVIQ FDEFLNLSHE
QVISLIGNDR ISVPNEERVY ECVIAWLRYD VPMREQFTSL LMEHVRLPFL SKEYITQRVD
KEILLEGNIV CKNLIIEALT YHLLPTETKS ARTVPRKPVG MPKILLVIGG QAPKAIRSVE
WYDLREEKWY QAAEMPNRRC RSGLSVLGDK VYAVGGFNGS LRVRTVDVYD PATDQWANCS
NMEARRSTLG VAVLNGCIYA VGGFDGTTGL SSAEMYDPKT DIWRFIASMS TRRSSVGVGV
VHGLLYAVGG YDGFTRQCLS SVERYNPDTD TWVNVAEMSS RRSGAGVGVL NNILYAVGGH
DGPMVRRSVE AYDCETNSWR SVADMSYCRR NAGVVAHDGL LYVVGGDDGT SNLASVEVYC
PDSDSWRILP ALMTIGRSYA GVCMIDKPMU MEEQGALARQ AASLAIALLD DENSQAEGTM
EGAIGGAIYG NLAPAGGAAA AAAPAAPAQA PQPNHPHYEN IYAPIGQPSN NNNNSGSNSN
QAAAIANANA PANAEEIQQQ QQPAPTEPNA NNNPQPPTAA APAPSQQQQQ QQAQPQQPQR
ILPMNNYRND LYDRSAAGGV CSAYDVPRAV RSGLGYRRNF RIDMQNGNRC GSGLRCTPLY
TNSRSNCQRQ RSFDDTESTD GYNLPYAGAG TMRYENIYEQ IRDEPLYRTS AANRVPLYTR
LDVLGHGIGR IERHLSSSCG NIDHYNLGGH YAVLGHSHFG TVGHIRLNAN GSGVAAPGVA
GTGTCNVPNC QGYMTAAGST VPVEYANVKV PVKNSASSFF SCLHGENSQS MTNIYKTSGT
AAAMAAHNSP LTPNVSMERA SRSASAGAAG SAAAAVEEHS AADSIPSSSN INANRTTGAI
PKVKTANKPA KESGGSSTAA SPILDKTTST GSGKSVTLAK KTSTAAARSS SSGDTNGNGT
LNRISKSSLQ WLLVNKWLPL WIGQGPDCKV IDFNFMFSRD CVSCDTASVA SQMSNPYGTP
RLSGLPQDMV RFQSSCAGAC AAAGAASTIR RDANASARPL HSTLSRLRNG EKRNPNRVAG
NYQYEDPSYE NVHVQWQNGF EFGRSRDYDP NSTYHQQRPL LQRARSESPT FSNQQRRLQR
QGAQAQQQSQ QPKPPGSPDP YKNYKLNADN NTFKPKPIAA DELEGAVGGA VAEIALPEVD
IEVVDPVSLS DNETETTSSQ NNLPSTTNSN NLNEHND
