ID   KLH17_MOUSE             Reviewed;         640 AA.
AC   Q6TDP3;
DT   27-SEP-2004, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   03-AUG-2022, entry version 138.
DE   RecName: Full=Kelch-like protein 17;
DE   AltName: Full=Actinfilin;
GN   Name=Klhl17;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=C57BL/6J;
RA   Huang C.Q., Wu S.L., Shan Y.X.;
RL   Submitted (SEP-2003) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Pancreas;
RX   PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA   Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA   Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT   "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL   Cell 143:1174-1189(2010).
CC   -!- FUNCTION: Substrate-recognition component of some cullin-RING-based BCR
CC       (BTB-CUL3-RBX1) E3 ubiquitin-protein ligase complexes. The BCR(KLHL17)
CC       complex mediates the ubiquitination and subsequent degradation of
CC       GLUR6. May play a role in the actin-based neuronal function (By
CC       similarity). {ECO:0000250}.
CC   -!- PATHWAY: Protein modification; protein ubiquitination.
CC   -!- SUBUNIT: Interacts with F-actin; the interaction disrupts the F-actin
CC       structures and leads to marked changes of neuronal morphology.
CC       Component of a complex, composed of PDZK1, SYNGAP1, KLHL17 and NMDA
CC       receptors. Interacts directly with PDZK1 (via PDZ1 domain); the
CC       interaction is important for integrity of actin cytoskeleton structures
CC       in neurons. Interacts with DLG4 and SYNGAP1. Interacts (via kelch
CC       repeats) with GRIK2 (via C-terminus); the interaction targets GRIK2 for
CC       degradation via ubiquitin-proteasome pathway. Interacts with GRIK1.
CC       Interacts with (via BTB domain) CUL3; the interaction regulates surface
CC       GRIK2 expression (By similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Postsynaptic density
CC       {ECO:0000250|UniProtKB:Q8K430}. Synapse {ECO:0000250|UniProtKB:Q8K430}.
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DR   EMBL; AY423764; AAR03711.1; -; mRNA.
DR   CCDS; CCDS38999.1; -.
DR   RefSeq; NP_938047.1; NM_198305.2.
DR   AlphaFoldDB; Q6TDP3; -.
DR   SMR; Q6TDP3; -.
DR   BioGRID; 231070; 17.
DR   STRING; 10090.ENSMUSP00000101194; -.
DR   PhosphoSitePlus; Q6TDP3; -.
DR   PaxDb; Q6TDP3; -.
DR   PRIDE; Q6TDP3; -.
DR   ProteomicsDB; 264999; -.
DR   Antibodypedia; 26039; 19 antibodies from 11 providers.
DR   DNASU; 231003; -.
DR   Ensembl; ENSMUST00000105569; ENSMUSP00000101194; ENSMUSG00002076083.
DR   GeneID; 231003; -.
DR   KEGG; mmu:231003; -.
DR   UCSC; uc008wgs.2; mouse.
DR   CTD; 339451; -.
DR   MGI; MGI:2678948; Klhl17.
DR   VEuPathDB; HostDB:ENSMUSG00000078485; -.
DR   eggNOG; KOG4441; Eukaryota.
DR   GeneTree; ENSGT00940000157635; -.
DR   HOGENOM; CLU_004253_14_1_1; -.
DR   InParanoid; Q6TDP3; -.
DR   OMA; MSCVEAE; -.
DR   OrthoDB; 731760at2759; -.
DR   PhylomeDB; Q6TDP3; -.
DR   TreeFam; TF329218; -.
DR   UniPathway; UPA00143; -.
DR   BioGRID-ORCS; 231003; 2 hits in 74 CRISPR screens.
DR   ChiTaRS; Klhl17; mouse.
DR   PRO; PR:Q6TDP3; -.
DR   Proteomes; UP000000589; Chromosome 4.
DR   RNAct; Q6TDP3; protein.
DR   ExpressionAtlas; Q6TDP3; differential.
DR   Genevisible; Q6TDP3; MM.
DR   GO; GO:0015629; C:actin cytoskeleton; ISS:UniProtKB.
DR   GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR   GO; GO:0032839; C:dendrite cytoplasm; ISO:MGI.
DR   GO; GO:0043025; C:neuronal cell body; ISO:MGI.
DR   GO; GO:0014069; C:postsynaptic density; ISO:MGI.
DR   GO; GO:0051015; F:actin filament binding; ISO:MGI.
DR   GO; GO:0060090; F:molecular adaptor activity; ISS:UniProtKB.
DR   GO; GO:0031208; F:POZ domain binding; ISO:MGI.
DR   GO; GO:0030036; P:actin cytoskeleton organization; ISS:UniProtKB.
DR   GO; GO:0007420; P:brain development; IBA:GO_Central.
DR   GO; GO:0016567; P:protein ubiquitination; IEA:UniProtKB-UniPathway.
DR   Gene3D; 2.120.10.80; -; 2.
DR   Gene3D; 3.30.710.10; -; 1.
DR   InterPro; IPR011705; BACK.
DR   InterPro; IPR017096; BTB-kelch_protein.
DR   InterPro; IPR000210; BTB/POZ_dom.
DR   InterPro; IPR011043; Gal_Oxase/kelch_b-propeller.
DR   InterPro; IPR015915; Kelch-typ_b-propeller.
DR   InterPro; IPR006652; Kelch_1.
DR   InterPro; IPR030594; KLHL17/KLHL20.
DR   InterPro; IPR011333; SKP1/BTB/POZ_sf.
DR   PANTHER; PTHR24412:SF454; PTHR24412:SF454; 1.
DR   Pfam; PF07707; BACK; 1.
DR   Pfam; PF00651; BTB; 1.
DR   Pfam; PF01344; Kelch_1; 6.
DR   PIRSF; PIRSF037037; Kelch-like_protein_gigaxonin; 1.
DR   SMART; SM00875; BACK; 1.
DR   SMART; SM00225; BTB; 1.
DR   SMART; SM00612; Kelch; 6.
DR   SUPFAM; SSF50965; SSF50965; 1.
DR   SUPFAM; SSF54695; SSF54695; 1.
DR   PROSITE; PS50097; BTB; 1.
PE   1: Evidence at protein level;
KW   Actin-binding; Kelch repeat; Reference proteome; Repeat; Synapse;
KW   Ubl conjugation pathway.
FT   CHAIN           1..640
FT                   /note="Kelch-like protein 17"
FT                   /id="PRO_0000119120"
FT   DOMAIN          90..157
FT                   /note="BTB"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00037"
FT   DOMAIN          192..294
FT                   /note="BACK"
FT   REPEAT          341..387
FT                   /note="Kelch 1"
FT   REPEAT          388..434
FT                   /note="Kelch 2"
FT   REPEAT          436..481
FT                   /note="Kelch 3"
FT   REPEAT          482..528
FT                   /note="Kelch 4"
FT   REPEAT          530..575
FT                   /note="Kelch 5"
FT   REPEAT          576..622
FT                   /note="Kelch 6"
FT   REGION          1..50
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          287..639
FT                   /note="Interaction with F-actin"
FT                   /evidence="ECO:0000250"
FT   REGION          638..640
FT                   /note="Interaction with PDZK1"
FT                   /evidence="ECO:0000250"
FT   COMPBIAS        20..37
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   640 AA;  69732 MW;  911D9F08883DA1BC CRC64;
     MQPRGERPAG RTQSPEHSSP GPGPEAPPPP QPPAPEAERA RPRQARPAAP MEGAMQLLSR
     EGHSVAHNSK RHYHDAFVAM SRMRQRGLLC DIVLHVAAKE IRAHKVVLAS CSPYFHAMFT
     NEMSESRQTH VTLHDIDPQA LDQLVQFAYT AEIVVGEGNV QTLLPAASLL QLNGVRDACC
     KFLLSQLDPS NCLGIRGFAD THSCSDLLKA AHRYVLQHFV DVAKTEEFML LPLKQVLELV
     SSDSLNVPSE EDVYRAVLSW VKHDVDTRRQ HVPRLMKCVR LPLLSRDFLL GHVDAESLVR
     HHPDCKDLLI EALKFHLLPE QRGVLGTSRT RPRRCEGAGP VLFAVGGGSL FAIHGDCEAY
     DTRTDRWHVV ASMSTRRARV GVAAVGNRLY AVGGYDGTSD LATVESYDPV TNTWQPEVSM
     GTRRSCLGVA ALHGLLYAAG GYDGASCLNS AERYDPLTGT WTSIAAMSTR RRYVRVATLD
     GNLYAVGGYD SSSHLATVEK YEPQVNSWTP VASMLSRRSS AGVAVLEGAL YVAGGNDGTS
     CLNSVERYST KAGAWESVAP MNIRRSTHDL VAMDGWLYAV GGNDGSSSLN SIEKYNPRTN
     KWVAASCMFT RRSSVGVAVL ELLNFPPPSS PTLSVSSTSL