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KLH12_MOUSE
ID   KLH12_MOUSE             Reviewed;         568 AA.
AC   Q8BZM0; Q8K225;
DT   16-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   03-AUG-2022, entry version 132.
DE   RecName: Full=Kelch-like protein 12;
DE   AltName: Full=CUL3-interacting protein 1;
GN   Name=Klhl12; Synonyms=C3ip1;
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 [LARGE SCALE MRNA] (ISOFORM 1).
RC   STRAIN=C57BL/6J; TISSUE=Diencephalon;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA   Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA   Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA   Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA   Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA   Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA   Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA   Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA   Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA   Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA   Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA   Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA   Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA   Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA   Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA   Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA   Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA   Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA   Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA   Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA   van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA   Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA   Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA   Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA   Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA   Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA   Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA   Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA   Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC   STRAIN=FVB/N; TISSUE=Mammary gland;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA project:
RT   the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3]
RP   FUNCTION.
RX   PubMed=20970343; DOI=10.1016/j.cub.2010.09.065;
RA   Funato Y., Terabayashi T., Sakamoto R., Okuzaki D., Ichise H., Nojima H.,
RA   Yoshida N., Miki H.;
RT   "Nucleoredoxin sustains Wnt/beta-catenin signaling by retaining a pool of
RT   inactive dishevelled protein.";
RL   Curr. Biol. 20:1945-1952(2010).
CC   -!- FUNCTION: Substrate-specific adapter of a BCR (BTB-CUL3-RBX1) E3
CC       ubiquitin ligase complex that acts as a negative regulator of Wnt
CC       signaling pathway and ER-Golgi transport. The BCR(KLHL12) complex is
CC       involved in ER-Golgi transport by regulating the size of COPII coats,
CC       thereby playing a key role in collagen export, which is required for
CC       embryonic stem (ES) cells division: BCR(KLHL12) acts by mediating
CC       monoubiquitination of SEC31 (SEC31A or SEC31B). The BCR(KLHL12) complex
CC       is also involved in neural crest specification: in response to
CC       cytosolic calcium increase, interacts with the heterodimer formed with
CC       PEF1 and PDCD6/ALG-2, leading to bridge together the BCR(KLHL12)
CC       complex and SEC31 (SEC31A or SEC31B), promoting monoubiquitination of
CC       SEC31 and subsequent collagen export. As part of the BCR(KLHL12)
CC       complex, also acts as a negative regulator of the Wnt signaling pathway
CC       by mediating ubiquitination and subsequent proteolysis of DVL3. The
CC       BCR(KLHL12) complex also mediates polyubiquitination of DRD4 and PEF1,
CC       without leading to degradation of these proteins.
CC       {ECO:0000250|UniProtKB:Q53G59}.
CC   -!- PATHWAY: Protein modification; protein ubiquitination.
CC   -!- SUBUNIT: Component of the BCR(KLHL12) E3 ubiquitin ligase complex, at
CC       least composed of CUL3 and KLHL12 and RBX1. This complex interacts with
CC       DVL3 upon activation of the Wnt signaling pathway by WNT3A. Interacts
CC       with DRD4, KLHL2 and SEC31A. Interacts with PEF1 and PDCD6/ALG-2;
CC       interaction takes place in response to cytosolic calcium increase and
CC       leads to bridge together the BCR(KLHL12) complex and SEC31 (SEC31A or
CC       SEC31B). {ECO:0000250|UniProtKB:Q53G59}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasmic vesicle, COPII-coated vesicle
CC       {ECO:0000250|UniProtKB:Q53G59}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q8BZM0-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q8BZM0-2; Sequence=VSP_018280;
CC   -!- DOMAIN: The BTB domain is required for interaction with CUL3.
CC       {ECO:0000250}.
CC   -!- PTM: Ubiquitinated by the SCF(FBXL17) complex, leading to its
CC       degradation by the proteasome: ubiquitination by the SCF(FBXL17)
CC       complex takes place when aberrant BTB domain dimers are formed.
CC       {ECO:0000250|UniProtKB:Q53G59}.
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DR   EMBL; AK034170; BAC28614.1; -; mRNA.
DR   EMBL; BC034514; AAH34514.1; -; mRNA.
DR   CCDS; CCDS35715.1; -. [Q8BZM0-2]
DR   CCDS; CCDS78687.1; -. [Q8BZM0-1]
DR   RefSeq; NP_001298065.1; NM_001311136.1. [Q8BZM0-1]
DR   RefSeq; NP_694768.1; NM_153128.3. [Q8BZM0-2]
DR   RefSeq; XP_006529624.1; XM_006529561.2. [Q8BZM0-1]
DR   AlphaFoldDB; Q8BZM0; -.
DR   SMR; Q8BZM0; -.
DR   STRING; 10090.ENSMUSP00000107851; -.
DR   iPTMnet; Q8BZM0; -.
DR   PhosphoSitePlus; Q8BZM0; -.
DR   EPD; Q8BZM0; -.
DR   PaxDb; Q8BZM0; -.
DR   PRIDE; Q8BZM0; -.
DR   ProteomicsDB; 263553; -. [Q8BZM0-1]
DR   ProteomicsDB; 263554; -. [Q8BZM0-2]
DR   Antibodypedia; 34533; 340 antibodies from 30 providers.
DR   DNASU; 240756; -.
DR   Ensembl; ENSMUST00000027725; ENSMUSP00000027725; ENSMUSG00000026455. [Q8BZM0-1]
DR   Ensembl; ENSMUST00000112232; ENSMUSP00000107851; ENSMUSG00000026455. [Q8BZM0-2]
DR   Ensembl; ENSMUST00000116528; ENSMUSP00000112227; ENSMUSG00000026455. [Q8BZM0-1]
DR   GeneID; 240756; -.
DR   KEGG; mmu:240756; -.
DR   UCSC; uc007csa.1; mouse. [Q8BZM0-2]
DR   UCSC; uc007csb.1; mouse. [Q8BZM0-1]
DR   CTD; 59349; -.
DR   MGI; MGI:2385619; Klhl12.
DR   VEuPathDB; HostDB:ENSMUSG00000026455; -.
DR   eggNOG; KOG4441; Eukaryota.
DR   GeneTree; ENSGT00940000155199; -.
DR   HOGENOM; CLU_004253_14_5_1; -.
DR   InParanoid; Q8BZM0; -.
DR   OMA; SLGTQRC; -.
DR   OrthoDB; 709680at2759; -.
DR   PhylomeDB; Q8BZM0; -.
DR   TreeFam; TF329218; -.
DR   Reactome; R-MMU-4641258; Degradation of DVL.
DR   UniPathway; UPA00143; -.
DR   BioGRID-ORCS; 240756; 1 hit in 59 CRISPR screens.
DR   ChiTaRS; Klhl12; mouse.
DR   PRO; PR:Q8BZM0; -.
DR   Proteomes; UP000000589; Chromosome 1.
DR   RNAct; Q8BZM0; protein.
DR   Bgee; ENSMUSG00000026455; Expressed in otolith organ and 223 other tissues.
DR   Genevisible; Q8BZM0; MM.
DR   GO; GO:0034451; C:centriolar satellite; ISO:MGI.
DR   GO; GO:0030127; C:COPII vesicle coat; ISS:UniProtKB.
DR   GO; GO:0030134; C:COPII-coated ER to Golgi transport vesicle; ISS:UniProtKB.
DR   GO; GO:0031463; C:Cul3-RING ubiquitin ligase complex; ISS:UniProtKB.
DR   GO; GO:0043231; C:intracellular membrane-bounded organelle; ISO:MGI.
DR   GO; GO:0042802; F:identical protein binding; ISO:MGI.
DR   GO; GO:0048208; P:COPII vesicle coating; ISS:UniProtKB.
DR   GO; GO:0006888; P:endoplasmic reticulum to Golgi vesicle-mediated transport; ISS:UniProtKB.
DR   GO; GO:0014032; P:neural crest cell development; ISS:UniProtKB.
DR   GO; GO:0014029; P:neural crest formation; ISS:UniProtKB.
DR   GO; GO:0006513; P:protein monoubiquitination; ISS:UniProtKB.
DR   GO; GO:0016055; P:Wnt signaling pathway; 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; IPR011043; Gal_Oxase/kelch_b-propeller.
DR   InterPro; IPR015915; Kelch-typ_b-propeller.
DR   InterPro; IPR006652; Kelch_1.
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; SSF50965; SSF50965; 1.
DR   SUPFAM; SSF54695; SSF54695; 1.
DR   PROSITE; PS50097; BTB; 1.
PE   2: Evidence at transcript level;
KW   Alternative splicing; Cytoplasmic vesicle; ER-Golgi transport;
KW   Kelch repeat; Reference proteome; Repeat; Transport; Ubl conjugation;
KW   Ubl conjugation pathway; Wnt signaling pathway.
FT   CHAIN           1..568
FT                   /note="Kelch-like protein 12"
FT                   /id="PRO_0000234350"
FT   DOMAIN          33..100
FT                   /note="BTB"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00037"
FT   DOMAIN          135..236
FT                   /note="BACK"
FT   REPEAT          282..329
FT                   /note="Kelch 1"
FT   REPEAT          331..379
FT                   /note="Kelch 2"
FT   REPEAT          380..426
FT                   /note="Kelch 3"
FT   REPEAT          427..473
FT                   /note="Kelch 4"
FT   REPEAT          475..520
FT                   /note="Kelch 5"
FT   REPEAT          522..567
FT                   /note="Kelch 6"
FT   REGION          405..568
FT                   /note="Interaction with DVL3"
FT                   /evidence="ECO:0000250"
FT   VAR_SEQ         465..491
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:15489334"
FT                   /id="VSP_018280"
SQ   SEQUENCE   568 AA;  63246 MW;  D2A39004B5F8B79D CRC64;
     MGGIMAPKDI MTNTHAKSIL NSMNSLRKSN TLCDVTLRVE QKDFPAHRIV LAACSDYFCA
     MFTSELSEKG KPYVDIQGLT AATMEILLDF VYTETVHVTV ENVQELLPAA CLLQLKGVKQ
     ACCEFLESQL DPSNCLGIRD FAETHNCVDL MQAAEVFSQK HFPEVVQHEE FILLSQGEVE
     KLIKCDEIQV DSEEPVFEAV INWVKHAKKE REESLPDLLQ YVRMPLLTPR YITDVIDAEP
     FIRCSLQCRD LVDEAKKFHL RPELRSQMQG PRTRARLGAN EVLLVVGGFG SQQSPIDVVE
     KYDPKTQEWS FLPSITRKRR YVASVSLHDR IYVIGGYDGR SRLSSVECLD YTADEDGVWY
     SVAPMNVRRG LAGATTLGDM IYVSGGFDGS RRHTSMERYD PNIDQWSMLG DMQTAREGAG
     LVVASGIIYC LGGYDGLNIL NSVEKYDPHT GHWTNVTPMA TKRSGAGVAL LNDHIYVVGG
     FDGTAHLSSV EAYNIRTDSW TTVTSMTTPR CYVGATVLRG RLYAIAGYDG NSLLSSIECY
     DPIIDSWEVV ASMGTQRCDA GVCVLREK
 
 
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