KLH17_RAT
ID KLH17_RAT Reviewed; 640 AA.
AC Q8K430;
DT 27-SEP-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 1.
DT 03-AUG-2022, entry version 137.
DE RecName: Full=Kelch-like protein 17;
DE AltName: Full=Actinfilin;
GN Name=Klhl17;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND
RP INTERACTION WITH ACTIN.
RC STRAIN=Sprague-Dawley;
RX PubMed=12063253; DOI=10.1074/jbc.m202076200;
RA Chen Y., Derin R., Petralia R.S., Li M.;
RT "Actinfilin, a brain-specific actin-binding protein in postsynaptic
RT density.";
RL J. Biol. Chem. 277:30495-30501(2002).
RN [2]
RP INTERACTION WITH PDZK1; DLG4; SYNGAP1 AND F-ACTIN, AND MUTAGENESIS OF
RP 638-THR--LEU-640.
RX PubMed=16054660; DOI=10.1016/j.neuropharm.2005.05.022;
RA Chen Y., Li M.;
RT "Interactions between CAP70 and actinfilin are important for integrity of
RT actin cytoskeleton structures in neurons.";
RL Neuropharmacology 49:1026-1041(2005).
RN [3]
RP FUNCTION, AND INTERACTION WITH GRIK2; GRIK1 AND CUL3.
RX PubMed=17062563; DOI=10.1074/jbc.m608194200;
RA Salinas G.D., Blair L.A., Needleman L.A., Gonzales J.D., Chen Y., Li M.,
RA Singer J.D., Marshall J.;
RT "Actinfilin is a Cul3 substrate adaptor, linking GluR6 kainate receptor
RT subunits to the ubiquitin-proteasome pathway.";
RL J. Biol. Chem. 281:40164-40173(2006).
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.
CC {ECO:0000269|PubMed:17062563}.
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. {ECO:0000269|PubMed:12063253,
CC ECO:0000269|PubMed:16054660, ECO:0000269|PubMed:17062563}.
CC -!- INTERACTION:
CC Q8K430; P31016: Dlg4; NbExp=2; IntAct=EBI-7713653, EBI-375655;
CC Q8K430; Q9JJ40: Pdzk1; NbExp=10; IntAct=EBI-7713653, EBI-7713572;
CC Q8K430; Q9QUH6: Syngap1; NbExp=2; IntAct=EBI-7713653, EBI-2310349;
CC -!- SUBCELLULAR LOCATION: Postsynaptic density
CC {ECO:0000269|PubMed:12063253}. Synapse {ECO:0000269|PubMed:12063253}.
CC -!- TISSUE SPECIFICITY: Brain specific. Broadly expressed in neurons of
CC most regions of the brain. {ECO:0000269|PubMed:12063253}.
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DR EMBL; AF505655; AAM74154.1; -; mRNA.
DR RefSeq; NP_663704.1; NM_145671.1.
DR AlphaFoldDB; Q8K430; -.
DR SMR; Q8K430; -.
DR BioGRID; 251611; 8.
DR ELM; Q8K430; -.
DR IntAct; Q8K430; 4.
DR MINT; Q8K430; -.
DR STRING; 10116.ENSRNOP00000027547; -.
DR PaxDb; Q8K430; -.
DR Ensembl; ENSRNOT00000027547; ENSRNOP00000027547; ENSRNOG00000020302.
DR GeneID; 246757; -.
DR KEGG; rno:246757; -.
DR CTD; 339451; -.
DR RGD; 708444; Klhl17.
DR eggNOG; KOG4441; Eukaryota.
DR GeneTree; ENSGT00940000157635; -.
DR HOGENOM; CLU_004253_14_1_1; -.
DR InParanoid; Q8K430; -.
DR OMA; MSCVEAE; -.
DR OrthoDB; 731760at2759; -.
DR PhylomeDB; Q8K430; -.
DR TreeFam; TF329218; -.
DR UniPathway; UPA00143; -.
DR PRO; PR:Q8K430; -.
DR Proteomes; UP000002494; Chromosome 5.
DR Bgee; ENSRNOG00000020302; Expressed in cerebellum and 19 other tissues.
DR GO; GO:0015629; C:actin cytoskeleton; IDA:UniProtKB.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0032839; C:dendrite cytoplasm; IDA:RGD.
DR GO; GO:0043025; C:neuronal cell body; IDA:RGD.
DR GO; GO:0014069; C:postsynaptic density; IDA:RGD.
DR GO; GO:0051015; F:actin filament binding; IDA:RGD.
DR GO; GO:0060090; F:molecular adaptor activity; IDA:UniProtKB.
DR GO; GO:0031208; F:POZ domain binding; IPI:RGD.
DR GO; GO:0030036; P:actin cytoskeleton organization; IDA:UniProtKB.
DR GO; GO:0007420; P:brain development; IEP:RGD.
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_0000119121"
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 REGION 638..640
FT /note="Interaction with PDZK1"
FT /evidence="ECO:0000269|PubMed:16054660"
FT COMPBIAS 20..37
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MUTAGEN 638..640
FT /note="Missing: No interaction with PDZK1."
FT /evidence="ECO:0000269|PubMed:16054660"
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
