KLHL2_RAT
ID KLHL2_RAT Reviewed; 593 AA.
AC F1LZF0;
DT 01-MAY-2013, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2013, sequence version 3.
DT 03-AUG-2022, entry version 49.
DE RecName: Full=Kelch-like protein 2;
DE AltName: Full=Mayven;
GN Name=Klhl2;
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 [LARGE SCALE GENOMIC DNA].
RC STRAIN=Brown Norway;
RX PubMed=15057822; DOI=10.1038/nature02426;
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]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-175.
RC STRAIN=Sprague-Dawley; TISSUE=Brain;
RA Katinka M., Da Silva C., Cruaud C., Pravenec M., Poulain J., Wincker P.,
RA Weissenbach J.;
RL Submitted (JUN-2010) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP SUBCELLULAR LOCATION, ACTIN BINDING, SUBUNIT, AND TISSUE SPECIFICITY.
RX PubMed=10397770; DOI=10.1091/mbc.10.7.2361;
RA Soltysik-Espanola M.B., Rogers R.A., Jiang S., Kim T.A., Gaedigk R.,
RA White R.A., Avraham H., Avraham S.;
RT "Characterization of Mayven, a novel actin-binding protein predominantly
RT expressed in brain.";
RL Mol. Biol. Cell 10:2361-2375(1999).
RN [4]
RP FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH FYN, AND TISSUE
RP SPECIFICITY.
RX PubMed=15715669; DOI=10.1111/j.1471-4159.2004.02946.x;
RA Jiang S., Avraham H.K., Park S.Y., Kim T.A., Bu X., Seng S., Avraham S.;
RT "Process elongation of oligodendrocytes is promoted by the Kelch-related
RT actin-binding protein Mayven.";
RL J. Neurochem. 92:1191-1203(2005).
RN [5]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=20504342; DOI=10.1186/1471-2202-11-63;
RA Montague P., Kennedy P.G., Barnett S.C.;
RT "Subcellular localization of Mayven following expression of wild type and
RT mutant EGFP tagged cDNAs.";
RL BMC Neurosci. 11:63-63(2010).
CC -!- FUNCTION: Component of a cullin-RING-based BCR (BTB-CUL3-RBX1) E3
CC ubiquitin-protein ligase complex that mediates the ubiquitination of
CC target proteins, such as NPTXR, leading most often to their proteasomal
CC degradation. Responsible for degradative ubiquitination of the WNK
CC kinases WNK1, WNK3 and WNK4 (By similarity). Promotes growth of cell
CC projections in oligodendrocyte precursors. Plays a role in the
CC reorganization of the actin cytoskeleton. {ECO:0000250,
CC ECO:0000269|PubMed:15715669, ECO:0000269|PubMed:20504342}.
CC -!- SUBUNIT: Component of a cullin-RING-based BCR (BTB-CUL3-RBX1) E3
CC ubiquitin-protein ligase complex. Interacts with NPTXR and CUL3.
CC Interacts with KLHL12 (By similarity). Binds actin. Interacts (via N-
CC terminus) with FYN (via SH3 domain). {ECO:0000250,
CC ECO:0000269|PubMed:10397770, ECO:0000269|PubMed:15715669}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton. Cell projection, ruffle
CC {ECO:0000250}. Cell projection. Cell projection, lamellipodium.
CC Cytoplasm, cytosol. Note=When over-expressed, colocalizes with NPTXR in
CC perinuclear aggresomes (By similarity). A proportion colocalizes with
CC the actin cytoskeleton. {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Detected in brain neurons, oligodendrocytes and
CC astrocytes (at protein level). {ECO:0000269|PubMed:10397770,
CC ECO:0000269|PubMed:15715669}.
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DR EMBL; FQ080481; -; NOT_ANNOTATED_CDS; mRNA.
DR AlphaFoldDB; F1LZF0; -.
DR SMR; F1LZF0; -.
DR STRING; 10116.ENSRNOP00000049839; -.
DR PaxDb; F1LZF0; -.
DR PRIDE; F1LZF0; -.
DR Ensembl; ENSRNOT00000047223; ENSRNOP00000049839; ENSRNOG00000029441.
DR RGD; 1306388; Klhl2.
DR eggNOG; KOG4441; Eukaryota.
DR GeneTree; ENSGT00940000156434; -.
DR InParanoid; F1LZF0; -.
DR TreeFam; TF329218; -.
DR Reactome; R-RNO-8951664; Neddylation.
DR Reactome; R-RNO-983168; Antigen processing: Ubiquitination & Proteasome degradation.
DR PRO; PR:F1LZF0; -.
DR Proteomes; UP000002494; Chromosome 16.
DR GO; GO:0015629; C:actin cytoskeleton; 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; IEA:UniProtKB-SubCell.
DR GO; GO:0030027; C:lamellipodium; IEA:UniProtKB-SubCell.
DR GO; GO:0001726; C:ruffle; IEA:UniProtKB-SubCell.
DR GO; GO:0003779; F:actin binding; ISS:UniProtKB.
DR GO; GO:0042802; F:identical protein binding; ISO:RGD.
DR GO; GO:0016567; P:protein ubiquitination; ISS:UniProtKB.
DR CDD; cd18338; BTB_POZ_KLHL2_Mayven; 1.
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; IPR044072; KLHL2_BTB/POZ.
DR InterPro; IPR011333; SKP1/BTB/POZ_sf.
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; SSF117281; SSF117281; 1.
DR SUPFAM; SSF54695; SSF54695; 1.
DR PROSITE; PS50097; BTB; 1.
PE 1: Evidence at protein level;
KW Actin-binding; Cell projection; Cytoplasm; Cytoskeleton; Kelch repeat;
KW Reference proteome; Repeat; Ubl conjugation pathway.
FT CHAIN 1..593
FT /note="Kelch-like protein 2"
FT /id="PRO_0000422073"
FT DOMAIN 56..123
FT /note="BTB"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00037"
FT REPEAT 308..353
FT /note="Kelch 1"
FT REPEAT 354..400
FT /note="Kelch 2"
FT REPEAT 402..447
FT /note="Kelch 3"
FT REPEAT 449..496
FT /note="Kelch 4"
FT REPEAT 497..543
FT /note="Kelch 5"
FT REPEAT 545..591
FT /note="Kelch 6"
FT REGION 1..29
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 593 AA; 65983 MW; 10CAFD7426176590 CRC64;
MESPPLPPAC TKQGHQKPLD SKDENPEKHC PLTVNPWHMK KAFKVMNELR SQNLLCDVTI
VAEDMEIPAH RVVLAACSPY FHAMFTGEMS ESRAKRVRIK EVDGWTLRML IDYVYTAEIQ
VTEENVQVLL PAAGLLQLQD VKKTCCEFLE SQLHPVNCLG IRAFADMHAC TDLLNKANTY
AEQHFADVVL SEEFLNLGIE QVCSLISSDK LTISSEEKVF EAVIAWVNHD KDVRQEFMAR
LMEHVRLPLL PREYLVQRVE EEALVKNSSA CKDYLIEAMK YHLLPTEQRM LMKSVRTRLR
TPMNLPKLMV VVGGQAPKAI RSVECYDFKE ERWHQVAELP SRRCRAGMVY MAGLVFAVGG
FNGSLRVRTV DSYDPVKDQW TSVANMRDRR STLGAAVLNG LLYAVGGFDG STGLSSVEAY
NIKSNEWFHV APMNTRRSSV GVGVVGGLLY AVGGYDGASR QCLSTVECYN ATANEWTYIA
EMSTRRSGAG VGVLNNLLYA VGGHDGPLVR KSVEVYDPTT NAWRQVADMN MCRRNAGVCA
VNGLLYVVGG DDGSCNLASV EYYNPTTDKW TVVSSCMSTG RSYAGVTVID KPL
