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LZTL1_MOUSE
ID   LZTL1_MOUSE             Reviewed;         299 AA.
AC   Q9JHQ5; Q8BRX8; Q8CDS2;
DT   26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   03-AUG-2022, entry version 132.
DE   RecName: Full=Leucine zipper transcription factor-like protein 1;
GN   Name=Lztfl1;
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 [MRNA], AND TISSUE SPECIFICITY.
RX   PubMed=11352561; DOI=10.1006/geno.2000.6498;
RA   Kiss H., Kedra D., Kiss C., Kost-Alimova M., Yang Y., Klein G., Imreh S.,
RA   Dumanski J.P.;
RT   "The LZTFL1 gene is a part of a transcriptional map covering 250 kb within
RT   the common eliminated region 1 (C3CER1) in 3p21.3.";
RL   Genomics 73:10-19(2001).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J;
RC   TISSUE=Adrenal gland, Aorta, Embryo, Mammary gland, Oviduct, and Testis;
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   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J, and FVB/N; TISSUE=Salivary gland, and Thymus;
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   [4]
RP   FUNCTION AS TUMOR SUPPRESSOR, AND TISSUE SPECIFICITY.
RX   PubMed=20233871; DOI=10.1158/0008-5472.can-09-3826;
RA   Wei Q., Zhou W., Wang W., Gao B., Wang L., Cao J., Liu Z.P.;
RT   "Tumor-suppressive functions of leucine zipper transcription factor-like
RT   1.";
RL   Cancer Res. 70:2942-2950(2010).
RN   [5]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC   Spleen, and Testis;
RX   PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA   Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA   Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT   "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL   Cell 143:1174-1189(2010).
RN   [6]
RP   ASSOCIATION WITH THE BBSOME COMPLEX, TISSUE SPECIFICITY, AND SUBCELLULAR
RP   LOCATION.
RX   PubMed=22072986; DOI=10.1371/journal.pgen.1002358;
RA   Seo S., Zhang Q., Bugge K., Breslow D.K., Searby C.C., Nachury M.V.,
RA   Sheffield V.C.;
RT   "A novel protein LZTFL1 regulates ciliary trafficking of the BBSome and
RT   Smoothened.";
RL   PLoS Genet. 7:E1002358-E1002358(2011).
RN   [7]
RP   FUNCTION IN NEURITE OUTGROWTH, INDUCTION BY EXERCISE TRAINING, TISSUE
RP   SPECIFICITY, AND SUBCELLULAR LOCATION.
RX   PubMed=22093827; DOI=10.1016/j.bbrc.2011.11.008;
RA   Sakurai T., Ogasawara J., Kizaki T., Ishibashi Y., Fujiwara T., Akagawa K.,
RA   Izawa T., Oh-ishi S., Haga S., Ohno H.;
RT   "Involvement of leucine zipper transcription factor-like protein 1 (Lztfl1)
RT   in the attenuation of cognitive impairment by exercise training.";
RL   Biochem. Biophys. Res. Commun. 416:125-129(2011).
CC   -!- FUNCTION: Regulates ciliary localization of the BBSome complex.
CC       Together with the BBSome complex, controls SMO ciliary trafficking and
CC       contributes to the sonic hedgehog (SHH) pathway regulation. May play a
CC       role in neurite outgrowth. May have tumor suppressor function.
CC       {ECO:0000269|PubMed:20233871, ECO:0000269|PubMed:22093827}.
CC   -!- SUBUNIT: Self-associates. Interacts with BBS9; the interaction mediates
CC       the association of LZTL1 with the BBsome complex and regulates BBSome
CC       ciliary trafficking.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:22072986,
CC       ECO:0000269|PubMed:22093827}.
CC   -!- TISSUE SPECIFICITY: Highly expressed in testis. Expressed in brain,
CC       cerebellum, eye, heart, kidney, liver, lung and trachea. In small
CC       intestine, graded expression along the crypt-villus axis with high
CC       levels in the villus apex and lower levels in the crypt stem cells (at
CC       protein level). Not expressed in skeletal muscle and white adipose
CC       tissue. {ECO:0000269|PubMed:11352561, ECO:0000269|PubMed:20233871,
CC       ECO:0000269|PubMed:22072986, ECO:0000269|PubMed:22093827}.
CC   -!- INDUCTION: In hippocampus, up-regulated by exercise training.
CC       {ECO:0000269|PubMed:22093827}.
CC   -!- SIMILARITY: Belongs to the LZTFL1 family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAC26556.1; Type=Frameshift; Evidence={ECO:0000305};
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DR   EMBL; AJ297352; CAB95845.1; -; mRNA.
DR   EMBL; AK029671; BAC26556.1; ALT_FRAME; mRNA.
DR   EMBL; AK041091; BAC30817.1; -; mRNA.
DR   EMBL; AK046515; BAC32764.1; -; mRNA.
DR   EMBL; AK054003; BAC35616.1; -; mRNA.
DR   EMBL; AK145263; BAE26331.1; -; mRNA.
DR   EMBL; AK157770; BAE34189.1; -; mRNA.
DR   EMBL; BC026840; AAH26840.1; -; mRNA.
DR   EMBL; BC098224; AAH98224.1; -; mRNA.
DR   CCDS; CCDS40818.1; -.
DR   RefSeq; NP_201579.1; NM_033322.2.
DR   AlphaFoldDB; Q9JHQ5; -.
DR   SMR; Q9JHQ5; -.
DR   BioGRID; 220275; 6.
DR   IntAct; Q9JHQ5; 3.
DR   STRING; 10090.ENSMUSP00000026274; -.
DR   iPTMnet; Q9JHQ5; -.
DR   PhosphoSitePlus; Q9JHQ5; -.
DR   REPRODUCTION-2DPAGE; IPI00458573; -.
DR   REPRODUCTION-2DPAGE; Q9JHQ5; -.
DR   EPD; Q9JHQ5; -.
DR   jPOST; Q9JHQ5; -.
DR   MaxQB; Q9JHQ5; -.
DR   PaxDb; Q9JHQ5; -.
DR   PRIDE; Q9JHQ5; -.
DR   ProteomicsDB; 291982; -.
DR   Antibodypedia; 29604; 272 antibodies from 28 providers.
DR   DNASU; 93730; -.
DR   Ensembl; ENSMUST00000026274; ENSMUSP00000026274; ENSMUSG00000025245.
DR   GeneID; 93730; -.
DR   KEGG; mmu:93730; -.
DR   UCSC; uc009sgm.1; mouse.
DR   CTD; 54585; -.
DR   MGI; MGI:1934860; Lztfl1.
DR   VEuPathDB; HostDB:ENSMUSG00000025245; -.
DR   eggNOG; ENOG502QRGB; Eukaryota.
DR   GeneTree; ENSGT00390000016415; -.
DR   HOGENOM; CLU_083519_0_0_1; -.
DR   InParanoid; Q9JHQ5; -.
DR   OMA; LAKYETE; -.
DR   OrthoDB; 1107668at2759; -.
DR   PhylomeDB; Q9JHQ5; -.
DR   TreeFam; TF329023; -.
DR   Reactome; R-MMU-5620922; BBSome-mediated cargo-targeting to cilium.
DR   BioGRID-ORCS; 93730; 3 hits in 70 CRISPR screens.
DR   ChiTaRS; Lztfl1; mouse.
DR   PRO; PR:Q9JHQ5; -.
DR   Proteomes; UP000000589; Chromosome 9.
DR   RNAct; Q9JHQ5; protein.
DR   Bgee; ENSMUSG00000025245; Expressed in spermatid and 252 other tissues.
DR   ExpressionAtlas; Q9JHQ5; baseline and differential.
DR   Genevisible; Q9JHQ5; MM.
DR   GO; GO:0005929; C:cilium; IDA:MGI.
DR   GO; GO:0005737; C:cytoplasm; IDA:MGI.
DR   GO; GO:0005829; C:cytosol; ISO:MGI.
DR   GO; GO:0002177; C:manchette; IDA:MGI.
DR   GO; GO:0062063; F:BBSome binding; IDA:MGI.
DR   GO; GO:0042802; F:identical protein binding; ISO:MGI.
DR   GO; GO:0044877; F:protein-containing complex binding; IDA:UniProtKB.
DR   GO; GO:0030317; P:flagellated sperm motility; IMP:MGI.
DR   GO; GO:1903568; P:negative regulation of protein localization to ciliary membrane; ISO:MGI.
DR   GO; GO:1903565; P:negative regulation of protein localization to cilium; ISO:MGI.
DR   GO; GO:0007283; P:spermatogenesis; IMP:MGI.
DR   InterPro; IPR026157; LZTFL1.
DR   PANTHER; PTHR21635; PTHR21635; 1.
DR   Pfam; PF15294; Leu_zip; 1.
PE   1: Evidence at protein level;
KW   Coiled coil; Cytoplasm; Reference proteome.
FT   CHAIN           1..299
FT                   /note="Leucine zipper transcription factor-like protein 1"
FT                   /id="PRO_0000318760"
FT   REGION          145..299
FT                   /note="Interaction with BSS9"
FT                   /evidence="ECO:0000250"
FT   COILED          96..299
FT                   /evidence="ECO:0000255"
FT   CONFLICT        280
FT                   /note="K -> E (in Ref. 2; BAC26556)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        283
FT                   /note="D -> G (in Ref. 2; BAC30817)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   299 AA;  34773 MW;  49F19871A72D48E7 CRC64;
     MAELGLNEHH QNEVINYMRF ARSKRGLRLK TVDSCFQDLK DSRLVEETFT IDEVSEVLNG
     LQAVVHSEVE SELINTAYTN VLLLRQLFSQ AEKWYLKLQT DISELENREL LEQVAEFEKA
     EFVSSSKKPI IDITKPKLVP INEGGTTELL NKEILRLQQE NEKLKSRLKT IEIQAVNALD
     EKSKLERVLQ DLQLDQENQQ DLLKAQDLDD LENTVATLRS EFQKTLNDKT ENQKSLEENL
     AAAKHDLLRV QEQLSMAEKE LEKKFQQTAA YRNMKEILTK KNDQIKDLRK RLAKYESED
 
 
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