ID   KELC_ANOST              Reviewed;        1499 AA.
AC   Q70JS2; Q70JS3;
DT   27-SEP-2004, integrated into UniProtKB/Swiss-Prot.
DT   26-FEB-2008, sequence version 2.
DT   23-FEB-2022, entry version 62.
DE   RecName: Full=Ring canal kelch homolog;
DE   AltName: Full=Kelch-like protein 1;
DE   Contains:
DE     RecName: Full=Kelch short protein;
GN   Name=kel {ECO:0000312|EMBL:CAE12056.1};
OS   Anopheles stephensi (Indo-Pakistan malaria mosquito).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Diptera; Nematocera; Culicoidea; Culicidae;
OC   Anophelinae; Anopheles.
OX   NCBI_TaxID=30069;
RN   [1] {ECO:0000312|EMBL:CAE12056.1}
RP   NUCLEOTIDE SEQUENCE [MRNA].
RA   Venanzi S., Battaglia P.A.;
RT   "Identification and molecular characterization of a kelch-like protein in
RT   Anopheles stephensi.";
RL   Submitted (JUL-2003) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: May play a role in organizing the actin cytoskeleton.
CC       {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000250}.
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DR   EMBL; AJ577207; CAE12055.1; -; mRNA.
DR   EMBL; AJ577207; CAE12056.1; -; mRNA.
DR   STRING; 30069.Q70JS2; -.
DR   PRIDE; Q70JS2; -.
DR   VEuPathDB; VectorBase:ASTE008691; -.
DR   VEuPathDB; VectorBase:ASTEI03909; -.
DR   VEuPathDB; VectorBase:ASTEI06646; -.
DR   VEuPathDB; VectorBase:LOC118514686; -.
DR   Proteomes; UP000076408; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR   GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
DR   GO; GO:0003779; F:actin binding; IEA:UniProtKB-KW.
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   2: Evidence at transcript level;
KW   Actin-binding; Cytoplasm; Cytoskeleton; Kelch repeat; Reference proteome;
KW   Repeat; Selenocysteine.
FT   CHAIN           1..1499
FT                   /note="Ring canal kelch homolog"
FT                   /id="PRO_0000016649"
FT   CHAIN           1..636
FT                   /note="Kelch short protein"
FT                   /id="PRO_0000016650"
FT   DOMAIN          100..166
FT                   /note="BTB"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00037"
FT   REPEAT          351..396
FT                   /note="Kelch 1"
FT                   /evidence="ECO:0000255"
FT   REPEAT          397..443
FT                   /note="Kelch 2"
FT                   /evidence="ECO:0000255"
FT   REPEAT          444..490
FT                   /note="Kelch 3"
FT                   /evidence="ECO:0000255"
FT   REPEAT          492..539
FT                   /note="Kelch 4"
FT                   /evidence="ECO:0000255"
FT   REPEAT          541..586
FT                   /note="Kelch 5"
FT                   /evidence="ECO:0000255"
FT   REPEAT          588..634
FT                   /note="Kelch 6"
FT                   /evidence="ECO:0000255"
FT   REGION          679..806
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          825..890
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          980..1018
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1033..1091
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1103..1173
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1276..1321
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1342..1499
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        686..719
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1033..1064
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1103..1150
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1402..1418
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1435..1452
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1455..1477
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   NON_STD         637
FT                   /note="Selenocysteine"
FT                   /evidence="ECO:0000269|Ref.1"
SQ   SEQUENCE   1499 AA;  160267 MW;  2F68F6067ECF08D4 CRC64;
     MLSFIQYTLG IMSSLGNGNN QHNINSNTGS SQNSAAEGTM ERGSCILVRY ASQNSLDESS
     QKQLPRSNGK EKTTGAYRNN IHTQRSFEAM NMMREQNLLC DVVLVAEGIE IPAHKMVLAS
     CSPYFYAMFT GFEESRQDRI TLQGVDPRAL QLLIEYVYRA VVEVTEDNVQ ILLTAANLLQ
     LTDVRDACCD YLQTQLDPSN CLGIRDFADI HGCIDLLNYA ETYIEQHFSE VVQFDEFLNL
     TSDQVAHLIK SDRLSVPTEE KVYECVITWI QYDVNGRQHH LAELMEHVRL PLLSQDYLVQ
     YVEKEQLMKG DLQCKDYIIE ALKYHLLKGE QKTCFKTPRT IPRQPVGLPK VLLVIGGQAP
     KAIRSVECYD LREEKWYQVA EMPTRRCRAG LAVLGDKVYA VGGFNGSLRV KTVDVYDPVL
     DQWTTSHNME ARRSTLGVAV LNNCIYAVGG FDGSTGLSSA EMFDPKRQEW RLIASMSTRR
     SSVGVGVVNG LLYAVGGYDG ASRQCLASVE RYNPSTDTWT QIAEMSARRS GAGVGVLDNI
     LYAVGGHDGP LVRKSVEAYD PATNTWRAVG DMAFCRRNAG VVAHNGMLYV VGGDDGLSNL
     ASVEVYSPES DSWRILPSSM SIGRSYAGVA MIDKPLUSEQ QGARVATKQS YASHHPTGTI
     YSRYANCAAL QQAQNEAAAG QAAGFGNDDE NSQAEGLNPE PANSNNSAPN GNNVHYENIY
     ESIEQFAPLN GGNGGNGGAH AGIPAGSNPL QYAVLNQPQP GPSGLGPGQA HRSLGGERGA
     VGGGGGGGGA VGGGCIPPPP PSMLHSMQQL YHPMAYRNEL YDRTAGYDVP RGRPAPSYYQ
     NQPPTGPSAN GRCPNLHLDL NRVRYPSGAS AQQQQRTPRQ RSFDDTESYH YYRCQNQSNG
     TAKYDNLYER VREEPAYQNT GSFAPAANRA AGLFGRFDVI GHGVGRIERH LSSSCGNIDH
     YSLGGHYAVL GHSHLGTMGH IRLNQSNSSS ASSASPYGAN GPATTSQPNP TKDSSSVNVK
     SFLSCLGGEN SQSMNNLNKS SAAHGTASGS APAANGNEAT LPGSISGGAS GGGAGGAGSS
     GGNGGQGSSI MGGLASAAAV GVNGTGASTS TTLGGKSTGA IPKISRKSKQ SQQQGPSDPT
     AGTSAPQSLA GGNGLPPVDV SLGAPADPMY ANGCGGRVTK PSLQWLLVNK WLPLWVGQTP
     PDYKFIDFNF MFSRNCDGCS SAGGSHGQQQ QQPQELVRYG TIDQADYIPP AREYPTMTGS
     YPRVLRNTPQ LARLREHEYE NVPLNDPPPG RGLRGIASPL QVGRARSESP SRPPGSDPLR
     TWAFDFENNT FRPARSPALA TSSGLAINRE KPREVRRITD GTFGARDLAQ PDTEKPGPSG
     LASKLALLKQ PEPDKEDGRL SSASSSSDSD NFAIESLAAE SSGGQPDEEE EEEGGSTRSG
     VGRRDDGGRV VGNSTEKENV GSSSNETSDS LNYDGPASAD RSLSEDEVEA ARPDNTASE