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Protein

Leucine zipper transcription factor-like protein 1

Gene

Lztfl1

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

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.2 Publications

GO - Molecular functioni

  1. identical protein binding Source: MGI
  2. protein complex binding Source: UniProtKB

GO - Biological processi

  1. negative regulation of protein localization to ciliary membrane Source: MGI
  2. negative regulation of protein localization to cilium Source: MGI
Complete GO annotation...

Enzyme and pathway databases

ReactomeiREACT_325250. BBSome-mediated cargo-targeting to cilium.

Names & Taxonomyi

Protein namesi
Recommended name:
Leucine zipper transcription factor-like protein 1
Gene namesi
Name:Lztfl1
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589 Componenti: Chromosome 9

Organism-specific databases

MGIiMGI:1934860. Lztfl1.

Subcellular locationi

Cytoplasm 2 Publications

GO - Cellular componenti

  1. BBSome Source: Ensembl
  2. cytoplasm Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 299299Leucine zipper transcription factor-like protein 1PRO_0000318760Add
BLAST

Proteomic databases

MaxQBiQ9JHQ5.
PaxDbiQ9JHQ5.
PRIDEiQ9JHQ5.

2D gel databases

REPRODUCTION-2DPAGEIPI00458573.
Q9JHQ5.

PTM databases

PhosphoSiteiQ9JHQ5.

Expressioni

Tissue specificityi

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.4 Publications

Inductioni

In hippocampus, up-regulated by exercise training.1 Publication

Gene expression databases

BgeeiQ9JHQ5.
CleanExiMM_LZTFL1.
ExpressionAtlasiQ9JHQ5. baseline and differential.
GenevestigatoriQ9JHQ5.

Interactioni

Subunit structurei

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

Protein-protein interaction databases

IntActiQ9JHQ5. 2 interactions.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni145 – 299155Interaction with BSS9By similarityAdd
BLAST

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili96 – 299204Sequence AnalysisAdd
BLAST

Sequence similaritiesi

Belongs to the LZTFL1 family.Curated

Keywords - Domaini

Coiled coil

Phylogenomic databases

eggNOGiNOG68368.
GeneTreeiENSGT00390000016415.
HOGENOMiHOG000067838.
HOVERGENiHBG054284.
InParanoidiQ9JHQ5.
OMAiGFNEHHQ.
PhylomeDBiQ9JHQ5.
TreeFamiTF329023.

Family and domain databases

InterProiIPR026157. LZTFL1.
[Graphical view]
PANTHERiPTHR21635. PTHR21635. 1 hit.

Sequencei

Sequence statusi: Complete.

Q9JHQ5-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAELGLNEHH QNEVINYMRF ARSKRGLRLK TVDSCFQDLK DSRLVEETFT
60 70 80 90 100
IDEVSEVLNG LQAVVHSEVE SELINTAYTN VLLLRQLFSQ AEKWYLKLQT
110 120 130 140 150
DISELENREL LEQVAEFEKA EFVSSSKKPI IDITKPKLVP INEGGTTELL
160 170 180 190 200
NKEILRLQQE NEKLKSRLKT IEIQAVNALD EKSKLERVLQ DLQLDQENQQ
210 220 230 240 250
DLLKAQDLDD LENTVATLRS EFQKTLNDKT ENQKSLEENL AAAKHDLLRV
260 270 280 290
QEQLSMAEKE LEKKFQQTAA YRNMKEILTK KNDQIKDLRK RLAKYESED
Length:299
Mass (Da):34,773
Last modified:September 30, 2000 - v1
Checksum:i49F19871A72D48E7
GO

Sequence cautioni

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

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti280 – 2801K → E in BAC26556 (PubMed:16141072).Curated
Sequence conflicti283 – 2831D → G in BAC30817 (PubMed:16141072).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS40818.1.
RefSeqiNP_201579.1. NM_033322.2.
UniGeneiMm.378263.
Mm.475504.

Genome annotation databases

EnsembliENSMUST00000026274; ENSMUSP00000026274; ENSMUSG00000025245.
GeneIDi93730.
KEGGimmu:93730.
UCSCiuc009sgm.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS40818.1.
RefSeqiNP_201579.1. NM_033322.2.
UniGeneiMm.378263.
Mm.475504.

3D structure databases

ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiQ9JHQ5. 2 interactions.

PTM databases

PhosphoSiteiQ9JHQ5.

2D gel databases

REPRODUCTION-2DPAGEIPI00458573.
Q9JHQ5.

Proteomic databases

MaxQBiQ9JHQ5.
PaxDbiQ9JHQ5.
PRIDEiQ9JHQ5.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000026274; ENSMUSP00000026274; ENSMUSG00000025245.
GeneIDi93730.
KEGGimmu:93730.
UCSCiuc009sgm.1. mouse.

Organism-specific databases

CTDi54585.
MGIiMGI:1934860. Lztfl1.

Phylogenomic databases

eggNOGiNOG68368.
GeneTreeiENSGT00390000016415.
HOGENOMiHOG000067838.
HOVERGENiHBG054284.
InParanoidiQ9JHQ5.
OMAiGFNEHHQ.
PhylomeDBiQ9JHQ5.
TreeFamiTF329023.

Enzyme and pathway databases

ReactomeiREACT_325250. BBSome-mediated cargo-targeting to cilium.

Miscellaneous databases

NextBioi351571.
PROiQ9JHQ5.
SOURCEiSearch...

Gene expression databases

BgeeiQ9JHQ5.
CleanExiMM_LZTFL1.
ExpressionAtlasiQ9JHQ5. baseline and differential.
GenevestigatoriQ9JHQ5.

Family and domain databases

InterProiIPR026157. LZTFL1.
[Graphical view]
PANTHERiPTHR21635. PTHR21635. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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(2000) [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.
    , 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(2004) [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(2003) [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(2009) [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(2010) [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(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN NEURITE OUTGROWTH, INDUCTION BY EXERCISE TRAINING, TISSUE SPECIFICITY, SUBCELLULAR LOCATION.

Entry informationi

Entry nameiLZTL1_MOUSE
AccessioniPrimary (citable) accession number: Q9JHQ5
Secondary accession number(s): Q8BRX8, Q8CDS2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 25, 2008
Last sequence update: September 30, 2000
Last modified: March 31, 2015
This is version 94 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.