GenomeNet

Database: UniProt
Entry: A0A0G2KA06_RAT
LinkDB: A0A0G2KA06_RAT
Original site: A0A0G2KA06_RAT 
ID   A0A0G2KA06_RAT          Unreviewed;       580 AA.
AC   A0A0G2KA06;
DT   22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT   25-MAY-2022, sequence version 2.
DT   27-MAR-2024, entry version 48.
DE   SubName: Full=Kelch-like family member 22 {ECO:0000313|Ensembl:ENSRNOP00000075207.2};
GN   Name=Klhl22 {ECO:0000313|Ensembl:ENSRNOP00000075207.2,
GN   ECO:0000313|RGD:1306288};
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 {ECO:0000313|Ensembl:ENSRNOP00000075207.2, ECO:0000313|Proteomes:UP000002494};
RN   [1] {ECO:0000313|Ensembl:ENSRNOP00000075207.2, ECO:0000313|Proteomes:UP000002494}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Brown Norway {ECO:0000313|Ensembl:ENSRNOP00000075207.2,
RC   ECO:0000313|Proteomes:UP000002494};
RX   PubMed=15057822; DOI=10.1038/nature02426;
RG   Rat Genome Sequencing Project Consortium;
RA   Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J.,
RA   Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G.,
RA   Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G.,
RA   Morgan M., Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G.,
RA   Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S.,
RA   Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T.,
RA   Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T., Smith D.,
RA   Lee H.-M., Gustafson E., Cahill P., Kana A., Doucette-Stamm L.,
RA   Weinstock K., Fechtel K., Weiss R.B., Dunn D.M., Green E.D.,
RA   Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K., Zhu B., Marra M.,
RA   Schein J., Bosdet I., Fjell C., Jones S., Krzywinski M., Mathewson C.,
RA   Siddiqui A., Wye N., McPherson J., Zhao S., Fraser C.M., Shetty J.,
RA   Shatsman S., Geer K., Chen Y., Abramzon S., Nierman W.C., Havlak P.H.,
RA   Chen R., Durbin K.J., Egan A., Ren Y., Song X.-Z., Li B., Liu Y., Qin X.,
RA   Cawley S., Cooney A.J., D'Souza L.M., Martin K., Wu J.Q.,
RA   Gonzalez-Garay M.L., Jackson A.R., Kalafus K.J., McLeod M.P.,
RA   Milosavljevic A., Virk D., Volkov A., Wheeler D.A., Zhang Z., Bailey J.A.,
RA   Eichler E.E., Tuzun E., Birney E., Mongin E., Ureta-Vidal A., Woodwark C.,
RA   Zdobnov E., Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J.,
RA   Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D., Schmidt J.,
RA   Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M., Abril J.F.,
RA   Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O., Poliakov A.,
RA   Huebner N., Ganten D., Goesele C., Hummel O., Kreitler T., Lee Y.-A.,
RA   Monti J., Schulz H., Zimdahl H., Himmelbauer H., Lehrach H., Jacob H.J.,
RA   Bromberg S., Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E.,
RA   Lazar J., Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M.,
RA   Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E., Webber C.,
RA   Brandt P., Nyakatura G., Adetobi M., Chiaromonte F., Elnitski L.,
RA   Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K., Miller W.,
RA   Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S., Zhang Y.,
RA   Lindpaintner K., Andrews T.D., Caccamo M., Clamp M., Clarke L., Curwen V.,
RA   Durbin R.M., Eyras E., Searle S.M., Cooper G.M., Batzoglou S., Brudno M.,
RA   Sidow A., Stone E.A., Payseur B.A., Bourque G., Lopez-Otin C., Puente X.S.,
RA   Chakrabarti K., Chatterji S., Dewey C., Pachter L., Bray N., Yap V.B.,
RA   Caspi A., Tesler G., Pevzner P.A., Haussler D., Roskin K.M., Baertsch R.,
RA   Clawson H., Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J.,
RA   Rosenbloom K.R., Trumbower H., Weirauch M., Cooper D.N., Stenson P.D.,
RA   Ma B., Brent M., Arumugam M., Shteynberg D., Copley R.R., Taylor M.S.,
RA   Riethman H., Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S.,
RA   Mockrin S., Collins F.S.;
RT   "Genome sequence of the Brown Norway rat yields insights into mammalian
RT   evolution.";
RL   Nature 428:493-521(2004).
RN   [2] {ECO:0007829|PubMed:16641100}
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=16641100; DOI=10.1073/pnas.0600895103;
RA   Hoffert J.D., Pisitkun T., Wang G., Shen R.F., Knepper M.A.;
RT   "Quantitative phosphoproteomics of vasopressin-sensitive renal cells:
RT   regulation of aquaporin-2 phosphorylation at two sites.";
RL   Proc. Natl. Acad. Sci. U.S.A. 103:7159-7164(2006).
RN   [3] {ECO:0000313|Ensembl:ENSRNOP00000075207.2}
RP   IDENTIFICATION.
RC   STRAIN=Brown Norway {ECO:0000313|Ensembl:ENSRNOP00000075207.2};
RG   Ensembl;
RL   Submitted (NOV-2023) to UniProtKB.
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DR   AlphaFoldDB; A0A0G2KA06; -.
DR   jPOST; A0A0G2KA06; -.
DR   Ensembl; ENSRNOT00000091675.2; ENSRNOP00000075207.2; ENSRNOG00000001878.8.
DR   RGD; 1306288; Klhl22.
DR   VEuPathDB; HostDB:ENSRNOG00000001878; -.
DR   GeneTree; ENSGT00940000159598; -.
DR   OrthoDB; 5472491at2759; -.
DR   UniPathway; UPA00143; -.
DR   Proteomes; UP000002494; Chromosome 11.
DR   Bgee; ENSRNOG00000001878; Expressed in skeletal muscle tissue and 19 other cell types or tissues.
DR   ExpressionAtlas; A0A0G2KA06; baseline and differential.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR   GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-KW.
DR   GO; GO:0016567; P:protein ubiquitination; IEA:UniProtKB-UniPathway.
DR   Gene3D; 1.25.40.420; -; 1.
DR   Gene3D; 2.120.10.80; Kelch-type beta propeller; 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; IPR011333; SKP1/BTB/POZ_sf.
DR   PANTHER; PTHR45632:SF5; KELCH-LIKE PROTEIN 22; 1.
DR   PANTHER; PTHR45632; LD33804P; 1.
DR   Pfam; PF07707; BACK; 1.
DR   Pfam; PF00651; BTB; 1.
DR   Pfam; PF01344; Kelch_1; 2.
DR   Pfam; PF13415; Kelch_3; 1.
DR   Pfam; PF13964; Kelch_6; 1.
DR   PIRSF; PIRSF037037; Kelch-like_protein_gigaxonin; 2.
DR   SMART; SM00875; BACK; 1.
DR   SMART; SM00225; BTB; 1.
DR   SMART; SM00612; Kelch; 6.
DR   SUPFAM; SSF117281; Kelch motif; 1.
DR   SUPFAM; SSF54695; POZ domain; 1.
DR   PROSITE; PS50097; BTB; 1.
PE   1: Evidence at protein level;
KW   Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW   Kelch repeat {ECO:0000256|ARBA:ARBA00022441};
KW   Proteomics identification {ECO:0007829|PeptideAtlas:A0A0G2KA06};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002494};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737};
KW   Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786}.
FT   DOMAIN          50..117
FT                   /note="BTB"
FT                   /evidence="ECO:0000259|PROSITE:PS50097"
FT   REGION          546..580
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        548..562
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   580 AA;  65477 MW;  9A72F0CA29534501 CRC64;
     MAEEQDFAQL CKLSTQPSHS HCVNNTYRST QHSQALLRGL LALRDSGILF DVVLVVEGRH
     IEAHRILLAA SCDYFRGMFA GGLKEMEQEE VLIHGVSYNA MCQILHFIYT SELELSLSNV
     QETLVAACQL QIPEIIHFCC DFLMSWVDEE NILDVYRLAE LFDLNRLTQQ LDTYILKNFV
     AFSRTDKYRQ LPLEKVYSLL SSNRLELGPS PLRDTVASAL MYHRNESLQP SLQGPHTELR
     SDFQCVVGFG GIHSTPSTIL SDQAKYLNPL LGEWKHFTAS LAPRMSNQGI AVLNNFVYLI
     GGDNNVQGFR AESRCWRYDP RHNRWFQIQS LQQEHADLCV CVVGKYIYAV AGRDYHNNLS
     AVERYDPATN SWEYVAPLKK EVYAHAGTTL QGKMYITCGR RGEDYLKETH CYDPGSNTWH
     TLADGPVRRA WHGMAALLDK LFVIGGSNND AGYRRDVHQV ACYSCTSRQW SSVCPLPAGH
     GEPGIAVLDN RIYVLGGRSH NRGSRTGYVH IYDMEKDCWE EGPQLNNSIS GLAACVLTLP
     RSLLHEQPRG TPNRSQADAD FASEVMSVSD WEEFDNSSED
//
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