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Q9JHQ5 (LZTL1_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 88. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Leucine zipper transcription factor-like protein 1
Gene names
Name:Lztfl1
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length299 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Regulates ciliary localization of the BBSome complex. Together with the BBSome complex, controls SMO ciliary trafficking and contributes to the sonic hedgehog (SHH) pathway regulation. May play a role in neurite outgrowth. May have tumor suppressor function. Ref.4 Ref.6

Subunit structure

Self-associates. Interacts with BBS9; the interaction mediates the association of LZTL1 with the BBsome complex and regulates BBSome ciliary trafficking.

Subcellular location

Cytoplasm Ref.5 Ref.6.

Tissue specificity

Highly expressed in testis. Expressed in brain, cerebellum, eye, heart, kidney, liver, lung and trachea. In small intestine, graded expression along the crypt-villus axis with high levels in the villus apex and lower levels in the crypt stem cells (at protein level). Not expressed in skeletal muscle and white adipose tissue. Ref.1 Ref.4 Ref.5 Ref.6

Induction

In hippocampus, up-regulated by exercise training. Ref.6

Sequence similarities

Belongs to the LZTFL1 family.

Sequence caution

The sequence BAC26556.1 differs from that shown. Reason: Frameshift at positions 268 and 270.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 299299Leucine zipper transcription factor-like protein 1
PRO_0000318760

Regions

Region145 – 299155Interaction with BSS9 By similarity
Coiled coil96 – 299204 Potential

Experimental info

Sequence conflict2801K → E in BAC26556. Ref.2
Sequence conflict2831D → G in BAC30817. Ref.2

Sequences

Sequence LengthMass (Da)Tools
Q9JHQ5 [UniParc].

Last modified October 1, 2000. Version 1.
Checksum: 49F19871A72D48E7

FASTA29934,773
        10         20         30         40         50         60 
MAELGLNEHH QNEVINYMRF ARSKRGLRLK TVDSCFQDLK DSRLVEETFT IDEVSEVLNG 

        70         80         90        100        110        120 
LQAVVHSEVE SELINTAYTN VLLLRQLFSQ AEKWYLKLQT DISELENREL LEQVAEFEKA 

       130        140        150        160        170        180 
EFVSSSKKPI IDITKPKLVP INEGGTTELL NKEILRLQQE NEKLKSRLKT IEIQAVNALD 

       190        200        210        220        230        240 
EKSKLERVLQ DLQLDQENQQ DLLKAQDLDD LENTVATLRS EFQKTLNDKT ENQKSLEENL 

       250        260        270        280        290 
AAAKHDLLRV QEQLSMAEKE LEKKFQQTAA YRNMKEILTK KNDQIKDLRK RLAKYESED 

« Hide

References

« Hide 'large scale' references
[1]"The LZTFL1 gene is a part of a transcriptional map covering 250 kb within the common eliminated region 1 (C3CER1) in 3p21.3."
Kiss H., Kedra D., Kiss C., Kost-Alimova M., Yang Y., Klein G., Imreh S., Dumanski J.P.
Genomics 73:10-19(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY.
[2]"The transcriptional landscape of the mammalian genome."
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. expand/collapse author list , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: C57BL/6J.
Tissue: Adrenal gland, Aorta, Embryo, Mammary gland, Oviduct and Testis.
[3]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: C57BL/6J and FVB/N.
Tissue: Salivary gland and Thymus.
[4]"Tumor-suppressive functions of leucine zipper transcription factor-like 1."
Wei Q., Zhou W., Wang W., Gao B., Wang L., Cao J., Liu Z.P.
Cancer Res. 70:2942-2950(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION AS TUMOR SUPPRESSOR, TISSUE SPECIFICITY.
[5]"A novel protein LZTFL1 regulates ciliary trafficking of the BBSome and Smoothened."
Seo S., Zhang Q., Bugge K., Breslow D.K., Searby C.C., Nachury M.V., Sheffield V.C.
PLoS Genet. 7:E1002358-E1002358(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: ASSOCIATION WITH THE BBSOME COMPLEX, TISSUE SPECIFICITY, SUBCELLULAR LOCATION.
[6]"Involvement of leucine zipper transcription factor-like protein 1 (Lztfl1) in the attenuation of cognitive impairment by exercise training."
Sakurai T., Ogasawara J., Kizaki T., Ishibashi Y., Fujiwara T., Akagawa K., Izawa T., Oh-ishi S., Haga S., Ohno H.
Biochem. Biophys. Res. Commun. 416:125-129(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION IN NEURITE OUTGROWTH, INDUCTION BY EXERCISE TRAINING, TISSUE SPECIFICITY, SUBCELLULAR LOCATION.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AJ297352 mRNA. Translation: CAB95845.1.
AK029671 mRNA. Translation: BAC26556.1. Frameshift.
AK041091 mRNA. Translation: BAC30817.1.
AK046515 mRNA. Translation: BAC32764.1.
AK054003 mRNA. Translation: BAC35616.1.
AK145263 mRNA. Translation: BAE26331.1.
AK157770 mRNA. Translation: BAE34189.1.
BC026840 mRNA. Translation: AAH26840.1.
BC098224 mRNA. Translation: AAH98224.1.
CCDSCCDS40818.1.
RefSeqNP_201579.1. NM_033322.2.
UniGeneMm.378263.
Mm.475504.

3D structure databases

ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

IntActQ9JHQ5. 2 interactions.

PTM databases

PhosphoSiteQ9JHQ5.

2D gel databases

REPRODUCTION-2DPAGEIPI00458573.
Q9JHQ5.

Proteomic databases

MaxQBQ9JHQ5.
PaxDbQ9JHQ5.
PRIDEQ9JHQ5.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000026274; ENSMUSP00000026274; ENSMUSG00000025245.
GeneID93730.
KEGGmmu:93730.
UCSCuc009sgm.1. mouse.

Organism-specific databases

CTD54585.
MGIMGI:1934860. Lztfl1.

Phylogenomic databases

eggNOGNOG68368.
GeneTreeENSGT00390000016415.
HOGENOMHOG000067838.
HOVERGENHBG054284.
InParanoidQ9JHQ5.
OMAGFNEHHQ.
PhylomeDBQ9JHQ5.
TreeFamTF329023.

Gene expression databases

BgeeQ9JHQ5.
CleanExMM_LZTFL1.
GenevestigatorQ9JHQ5.

Family and domain databases

InterProIPR026157. LZTFL1.
[Graphical view]
PANTHERPTHR21635. PTHR21635. 1 hit.
ProtoNetSearch...

Other

NextBio351571.
PROQ9JHQ5.
SOURCESearch...

Entry information

Entry nameLZTL1_MOUSE
AccessionPrimary (citable) accession number: Q9JHQ5
Secondary accession number(s): Q8BRX8, Q8CDS2
Entry history
Integrated into UniProtKB/Swiss-Prot: February 26, 2008
Last sequence update: October 1, 2000
Last modified: July 9, 2014
This is version 88 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot