KLH22_AILME
ID KLH22_AILME Reviewed; 634 AA.
AC D2HEW7;
DT 10-AUG-2010, integrated into UniProtKB/Swiss-Prot.
DT 09-FEB-2010, sequence version 1.
DT 03-AUG-2022, entry version 73.
DE RecName: Full=Kelch-like protein 22 {ECO:0000305};
GN Name=KLHL22; ORFNames=PANDA_009375 {ECO:0000312|EMBL:EFB29357.1};
OS Ailuropoda melanoleuca (Giant panda).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Caniformia; Ursidae; Ailuropoda.
OX NCBI_TaxID=9646;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=20010809; DOI=10.1038/nature08696;
RA Li R., Fan W., Tian G., Zhu H., He L., Cai J., Huang Q., Cai Q., Li B.,
RA Bai Y., Zhang Z., Zhang Y., Wang W., Li J., Wei F., Li H., Jian M., Li J.,
RA Zhang Z., Nielsen R., Li D., Gu W., Yang Z., Xuan Z., Ryder O.A.,
RA Leung F.C., Zhou Y., Cao J., Sun X., Fu Y., Fang X., Guo X., Wang B.,
RA Hou R., Shen F., Mu B., Ni P., Lin R., Qian W., Wang G., Yu C., Nie W.,
RA Wang J., Wu Z., Liang H., Min J., Wu Q., Cheng S., Ruan J., Wang M.,
RA Shi Z., Wen M., Liu B., Ren X., Zheng H., Dong D., Cook K., Shan G.,
RA Zhang H., Kosiol C., Xie X., Lu Z., Zheng H., Li Y., Steiner C.C.,
RA Lam T.T., Lin S., Zhang Q., Li G., Tian J., Gong T., Liu H., Zhang D.,
RA Fang L., Ye C., Zhang J., Hu W., Xu A., Ren Y., Zhang G., Bruford M.W.,
RA Li Q., Ma L., Guo Y., An N., Hu Y., Zheng Y., Shi Y., Li Z., Liu Q.,
RA Chen Y., Zhao J., Qu N., Zhao S., Tian F., Wang X., Wang H., Xu L., Liu X.,
RA Vinar T., Wang Y., Lam T.W., Yiu S.M., Liu S., Zhang H., Li D., Huang Y.,
RA Wang X., Yang G., Jiang Z., Wang J., Qin N., Li L., Li J., Bolund L.,
RA Kristiansen K., Wong G.K., Olson M., Zhang X., Li S., Yang H., Wang J.,
RA Wang J.;
RT "The sequence and de novo assembly of the giant panda genome.";
RL Nature 463:311-317(2010).
CC -!- FUNCTION: Substrate-specific adapter of a BCR (BTB-CUL3-RBX1) E3
CC ubiquitin ligase complex required for chromosome alignment and
CC localization of PLK1 at kinetochores. The BCR(KLHL22) ubiquitin ligase
CC complex mediates monoubiquitination of PLK1, leading to PLK1
CC dissociation from phosphoreceptor proteins and subsequent removal from
CC kinetochores, allowing silencing of the spindle assembly checkpoint
CC (SAC) and chromosome segregation. Monoubiquitination of PLK1 does not
CC lead to PLK1 degradation. The BCR(KLHL22) ubiquitin ligase complex is
CC also responsible for the amino acid-stimulated 'Lys-48'
CC polyubiquitination and proteasomal degradation of DEPDC5. Through the
CC degradation of DEPDC5, releases the GATOR1 complex-mediated inhibition
CC of the TORC1 pathway. It is therefore an amino acid-dependent activator
CC within the amino acid-sensing branch of the TORC1 pathway, indirectly
CC regulating different cellular processes including cell growth and
CC autophagy. {ECO:0000250|UniProtKB:Q53GT1}.
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC {ECO:0000250|UniProtKB:Q53GT1}.
CC -!- SUBUNIT: Component of the BCR(KLHL22) E3 ubiquitin ligase complex, at
CC least composed of CUL3, KLHL22 and RBX1. Interacts with PLK1. Interacts
CC with DEPDC5 (via DEP domain); the interaction depends on amino acid
CC availability. Interacts with YWHAE; required for the nuclear
CC localization of KLHL22 upon amino acid starvation.
CC {ECO:0000250|UniProtKB:Q53GT1}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol
CC {ECO:0000250|UniProtKB:Q53GT1}. Cytoplasm, cytoskeleton, microtubule
CC organizing center, centrosome {ECO:0000250|UniProtKB:Q53GT1}.
CC Cytoplasm, cytoskeleton, spindle {ECO:0000250|UniProtKB:Q53GT1}.
CC Nucleus {ECO:0000250|UniProtKB:Q53GT1}. Lysosome
CC {ECO:0000250|UniProtKB:Q53GT1}. Note=Mainly cytoplasmic in prophase and
CC prometaphase. Associates with the mitotic spindle as the cells reach
CC chromosome bi-orientation. Localizes to the centrosomes shortly before
CC cells enter anaphase After anaphase onset, predominantly associates
CC with the polar microtubules connecting the 2 opposing centrosomes and
CC gradually diffuses into the cytoplasm during telophase. Localizes to
CC the nucleus upon amino acid starvation. Relocalizes to the cytosol and
CC associates with lysosomes when amino acids are available.
CC {ECO:0000250|UniProtKB:Q53GT1}.
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DR EMBL; GL192766; EFB29357.1; -; Genomic_DNA.
DR AlphaFoldDB; D2HEW7; -.
DR SMR; D2HEW7; -.
DR STRING; 9646.ENSAMEP00000011753; -.
DR PRIDE; D2HEW7; -.
DR eggNOG; KOG4441; Eukaryota.
DR HOGENOM; CLU_004253_14_3_1; -.
DR InParanoid; D2HEW7; -.
DR OMA; ERDCWEE; -.
DR TreeFam; TF328485; -.
DR UniPathway; UPA00143; -.
DR Proteomes; UP000008912; Unassembled WGS sequence.
DR GO; GO:0005813; C:centrosome; ISS:UniProtKB.
DR GO; GO:0031463; C:Cul3-RING ubiquitin ligase complex; ISS:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0005829; C:cytosol; ISS:UniProtKB.
DR GO; GO:0045171; C:intercellular bridge; IEA:Ensembl.
DR GO; GO:0005764; C:lysosome; IEA:UniProtKB-SubCell.
DR GO; GO:0072686; C:mitotic spindle; ISS:UniProtKB.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0005827; C:polar microtubule; ISS:UniProtKB.
DR GO; GO:0071889; F:14-3-3 protein binding; IEA:Ensembl.
DR GO; GO:0051301; P:cell division; ISS:UniProtKB.
DR GO; GO:0071233; P:cellular response to leucine; ISS:UniProtKB.
DR GO; GO:0000070; P:mitotic sister chromatid segregation; ISS:UniProtKB.
DR GO; GO:0007094; P:mitotic spindle assembly checkpoint signaling; ISS:UniProtKB.
DR GO; GO:0010507; P:negative regulation of autophagy; ISS:UniProtKB.
DR GO; GO:0030307; P:positive regulation of cell growth; ISS:UniProtKB.
DR GO; GO:1904263; P:positive regulation of TORC1 signaling; ISS:UniProtKB.
DR GO; GO:0043161; P:proteasome-mediated ubiquitin-dependent protein catabolic process; ISS:UniProtKB.
DR GO; GO:0006513; P:protein monoubiquitination; ISS:UniProtKB.
DR Gene3D; 2.120.10.80; -; 1.
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; IPR015915; Kelch-typ_b-propeller.
DR InterPro; IPR006652; Kelch_1.
DR InterPro; IPR030575; KLHL22.
DR InterPro; IPR011333; SKP1/BTB/POZ_sf.
DR PANTHER; PTHR45632:SF5; PTHR45632:SF5; 1.
DR Pfam; PF07707; BACK; 1.
DR Pfam; PF00651; BTB; 1.
DR Pfam; PF01344; Kelch_1; 2.
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; SSF117281; SSF117281; 1.
DR SUPFAM; SSF54695; SSF54695; 1.
DR PROSITE; PS50097; BTB; 1.
PE 3: Inferred from homology;
KW Acetylation; Cell cycle; Cell division; Cytoplasm; Cytoskeleton;
KW Kelch repeat; Lysosome; Mitosis; Nucleus; Phosphoprotein;
KW Reference proteome; Repeat; Ubl conjugation pathway.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:Q53GT1"
FT CHAIN 2..634
FT /note="Kelch-like protein 22"
FT /id="PRO_0000396634"
FT DOMAIN 50..117
FT /note="BTB"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00037"
FT REPEAT 299..349
FT /note="Kelch 1"
FT REPEAT 350..399
FT /note="Kelch 2"
FT REPEAT 400..446
FT /note="Kelch 3"
FT REPEAT 448..493
FT /note="Kelch 4"
FT REPEAT 494..544
FT /note="Kelch 5"
FT REPEAT 545..593
FT /note="Kelch 6"
FT REGION 600..634
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000250|UniProtKB:Q53GT1"
FT MOD_RES 463
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:D3ZZC3"
FT MOD_RES 466
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:D3ZZC3"
FT MOD_RES 605
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q53GT1"
SQ SEQUENCE 634 AA; 71793 MW; CECEEC2C859875F5 CRC64;
MAEEQEFTQL CKLPVQPSHP HCVNNTYRSA QHSQALLRGL LALRDSGILF DVVLVVEGRH
IEAHRILLAA SCDYFRGMFA GGLKEMEQEE VLIHGVSYNA MCQILHFIYT SELELSLSNV
QETLVAACQL QIPEIIHFCC DFLMSWVDEE NILDVYRLAE LFDLSRLTEQ LDTYILKNFV
AFSRTDKYRQ LPLEKVYSLL SSNRLEVSCE TEVYEGALLY HYTLEQVQAD QISLHEPPKL
LETVRFPLME AEVLQRLHDK LDPSPLRDTV ANALMYHRNE SLQPSLQGPH TELRSDFQCV
VGFGGIHSTP STVLSDQAKY LNPLLGEWKH FTASLAPRMS NQGIAVLNNF VYLIGGDNNV
QGFRAESRCW RYDPRHNRWF QIQSLQQEHA DLCVCVVGRY IYAVAGRDYH NDLNAVERYD
PTTNSWAYVA PLKREVYAHA GATLEGKMYV TCGRRGEDYL KETHCYDPDS NTWHSLADGP
VRRAWHGMAT LLDKLYVIGG SNNDAGYRRD VHQVACYSCT SGQWSSVCPL PAGHGEPGIA
VLDTRIYVLG GRSHNRGSRT GYVHIYDVEK DCWEEGPQLD NSISGLAACV LTLPRTLLLE
PPRGTPDRSQ ADPDFASEVM SVSDWEEFDN SSED
