TSK_MOUSE
ID TSK_MOUSE Reviewed; 354 AA.
AC Q8CBR6; Q4W655;
DT 27-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT 27-JUN-2006, sequence version 2.
DT 03-AUG-2022, entry version 142.
DE RecName: Full=Tsukushi {ECO:0000303|PubMed:21856951};
DE AltName: Full=Leucine-rich repeat-containing protein 54 {ECO:0000312|MGI:MGI:2443855};
DE Flags: Precursor;
GN Name=Tsku {ECO:0000312|MGI:MGI:2443855};
GN Synonyms=Lrrc54 {ECO:0000312|MGI:MGI:2443855},
GN Tsk {ECO:0000303|PubMed:30271858};
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].
RA Kuriyama S., Ohta K., Sawai H., Takahashi M., Tanaka H.;
RT "Loss of Tsukushi causes the retinal degradation.";
RL Submitted (MAY-2005) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Urinary bladder;
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 FUNCTION, TISSUE SPECIFICITY, AND DISRUPTION PHENOTYPE.
RX PubMed=21055390; DOI=10.1016/j.bbrc.2010.10.127;
RA Ito A., Shinmyo Y., Abe T., Oshima N., Tanaka H., Ohta K.;
RT "Tsukushi is required for anterior commissure formation in mouse brain.";
RL Biochem. Biophys. Res. Commun. 402:813-818(2010).
RN [4]
RP FUNCTION, INTERACTION WITH FZD4, TISSUE SPECIFICITY, AND DISRUPTION
RP PHENOTYPE.
RX PubMed=21856951; DOI=10.1073/pnas.1100513108;
RA Ohta K., Ito A., Kuriyama S., Lupo G., Kosaka M., Ohnuma S., Nakagawa S.,
RA Tanaka H.;
RT "Tsukushi functions as a Wnt signaling inhibitor by competing with Wnt2b
RT for binding to transmembrane protein Frizzled4.";
RL Proc. Natl. Acad. Sci. U.S.A. 108:14962-14967(2011).
RN [5]
RP FUNCTION, INTERACTION WITH TGFB1, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE,
RP AND DISRUPTION PHENOTYPE.
RX PubMed=22995554; DOI=10.1016/j.ydbio.2012.08.030;
RA Niimori D., Kawano R., Felemban A., Niimori-Kita K., Tanaka H., Ihn H.,
RA Ohta K.;
RT "Tsukushi controls the hair cycle by regulating TGF-beta1 signaling.";
RL Dev. Biol. 372:81-87(2012).
RN [6]
RP FUNCTION, INTERACTION WITH NETRIN, TISSUE SPECIFICITY, AND DISRUPTION
RP PHENOTYPE.
RX PubMed=23206892; DOI=10.1016/j.ydbio.2012.11.029;
RA Hossain M., Ahmed G., Naser I.B., Shinmyo Y., Ito A., Riyadh M.A.,
RA Felemban A., Song X., Ohta K., Tanaka H.;
RT "The combinatorial guidance activities of draxin and Tsukushi are essential
RT for forebrain commissure formation.";
RL Dev. Biol. 374:58-70(2013).
RN [7]
RP FUNCTION, TISSUE SPECIFICITY, AND DISRUPTION PHENOTYPE.
RX PubMed=25159578; DOI=10.1007/s12079-014-0241-y;
RA Niimori D., Kawano R., Niimori-Kita K., Ihn H., Ohta K.;
RT "Tsukushi is involved in the wound healing by regulating the expression of
RT cytokines and growth factors.";
RL J. Cell Commun. Signal. 8:173-177(2014).
RN [8]
RP FUNCTION, TISSUE SPECIFICITY, AND DISRUPTION PHENOTYPE.
RX PubMed=30271858; DOI=10.1016/j.reth.2017.08.001;
RA Yano K., Washio K., Tsumanuma Y., Yamato M., Ohta K., Okano T., Izumi Y.;
RT "The role of Tsukushi (TSK), a small leucine-rich repeat proteoglycan, in
RT bone growth.";
RL Regen. Ther. 7:98-107(2017).
RN [9]
RP INTERACTION WITH CCN2.
RX PubMed=30232710; DOI=10.1007/s12079-018-0487-x;
RA Ohta K., Aoyama E., Ahmad S.A.I., Ito N., Anam M.B., Kubota S.,
RA Takigawa M.;
RT "CCN2/CTGF binds the small leucine rich proteoglycan protein Tsukushi.";
RL J. Cell Commun. Signal. 13:113-118(2019).
RN [10]
RP FUNCTION, SUBCELLULAR LOCATION, INDUCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=31391339; DOI=10.1172/jci.insight.129492;
RA Mouchiroud M., Camire E., Aldow M., Caron A., Jubinville E., Turcotte L.,
RA Kaci I., Beaulieu M.J., Roy C., Labbe S.M., Varin T.V., Gelinas Y.,
RA Lamothe J., Trottier J., Mitchell P.L., Guenard F., Festuccia W.T.,
RA Joubert P., Rose C.F., Karvellas C.J., Barbier O., Morissette M.C.,
RA Marette A., Laplante M.;
RT "The hepatokine Tsukushi is released in response to NAFLD and impacts
RT cholesterol homeostasis.";
RL JCI Insight 4:e129492-e129492(2019).
RN [11]
RP SUBCELLULAR LOCATION, INDUCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=30595550; DOI=10.1016/j.molmet.2018.12.004;
RA Xiong X., Wang Q., Wang S., Zhang J., Liu T., Guo L., Yu Y., Lin J.D.;
RT "Mapping the molecular signatures of diet-induced NASH and its regulation
RT by the hepatokine Tsukushi.";
RL Mol. Metab. 20:128-137(2019).
RN [12]
RP FUNCTION, SUBCELLULAR LOCATION, AND DISRUPTION PHENOTYPE.
RX PubMed=31767170; DOI=10.1016/j.molmet.2019.09.014;
RA Mouchiroud M., Camire E., Aldow M., Caron A., Jubinville E., Turcotte L.,
RA Kaci I., Beaulieu M.J., Roy C., Labbe S.M., Varin T.V., Gelinas Y.,
RA Lamothe J., Trottier J., Mitchell P.L., Guenard F., Festuccia W.T.,
RA Joubert P., Rose C.F., Karvellas C.J., Barbier O., Morissette M.C.,
RA Marette A., Laplante M.;
RT "The Hepatokine TSK does not affect brown fat thermogenic capacity, body
RT weight gain, and glucose homeostasis.";
RL Mol. Metab. 30:184-191(2019).
RN [13]
RP FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND DISRUPTION
RP PHENOTYPE.
RX PubMed=31535079; DOI=10.1038/s42255-018-0020-9;
RA Wang Q., Sharma V.P., Shen H., Xiao Y., Zhu Q., Xiong X., Guo L., Jiang L.,
RA Ohta K., Li S., Shi H., Rui L., Lin J.D.;
RT "The hepatokine Tsukushi gates energy expenditure via brown fat sympathetic
RT innervation.";
RL Nat. Metab. 1:251-260(2019).
RN [14]
RP FUNCTION, TISSUE SPECIFICITY, AND DISRUPTION PHENOTYPE.
RX PubMed=31983064; DOI=10.1111/dgd.12649;
RA Ahmad S.A.I., Anam M.B., Istiaq A., Ito N., Ohta K.;
RT "Tsukushi is essential for proper maintenance and terminal differentiation
RT of mouse hippocampal neural stem cells.";
RL Dev. Growth Differ. 62:108-117(2020).
RN [15]
RP FUNCTION, TISSUE SPECIFICITY, AND DISRUPTION PHENOTYPE.
RX PubMed=32127020; DOI=10.1186/s13041-020-00570-z;
RA Miwa T., Ohta K., Ito N., Hattori S., Miyakawa T., Takeo T., Nakagata N.,
RA Song W.J., Minoda R.;
RT "Tsukushi is essential for the development of the inner ear.";
RL Mol. Brain 13:29-29(2020).
CC -!- FUNCTION: Contributes to various developmental events and other
CC processes such as wound healing and cholesterol homeostasis through its
CC interactions with multiple signaling pathways (PubMed:21856951,
CC PubMed:22995554, PubMed:25159578, PubMed:31391339). Wnt signaling
CC inhibitor which competes with WNT2B for binding to Wnt receptor FZD4
CC and represses WNT2B-dependent development of the peripheral eye
CC (PubMed:21856951). Plays a role in regulating the hair cycle by
CC controlling TGFB1 signaling (PubMed:22995554). Required for the
CC development of the anterior commissure in the brain by inhibiting
CC neurite outgrowth (PubMed:21055390, PubMed:23206892). Essential for
CC terminal differentiation of hippocampal neural stem cells
CC (PubMed:31983064). Plays a role in regulating bone elongation and bone
CC mass by modulating growth plate chondrocyte function and overall body
CC size (PubMed:30271858). Required for development of the inner ear
CC through its involvement in stereocilia formation in inner hair cells
CC (PubMed:32127020). Facilitates wound healing by inhibiting secretion of
CC TGFB1 from macrophages which prevents myofibroblast differentiation,
CC maintaining inflammatory cell quiescence (PubMed:25159578). Plays a
CC role in cholesterol homeostasis by reducing circulating high-density
CC lipoprotein cholesterol, lowering cholesterol efflux capacity and
CC decreasing cholesterol-to-bile acid conversion in the liver
CC (PubMed:31391339). In one study, shown to negatively regulate
CC sympathetic innervation in brown fat, leading to reduced energy
CC expenditure (PubMed:31535079). In another study, shown not to affect
CC brown fat thermogenic capacity, body weight gain or glucose homeostasis
CC (PubMed:31767170). {ECO:0000269|PubMed:21055390,
CC ECO:0000269|PubMed:21856951, ECO:0000269|PubMed:22995554,
CC ECO:0000269|PubMed:23206892, ECO:0000269|PubMed:25159578,
CC ECO:0000269|PubMed:30271858, ECO:0000269|PubMed:31391339,
CC ECO:0000269|PubMed:31535079, ECO:0000269|PubMed:31767170,
CC ECO:0000269|PubMed:31983064, ECO:0000269|PubMed:32127020}.
CC -!- SUBUNIT: Interacts with FZD4 (via FZ domain); competes with WNT2B for
CC binding to FZD4, inhibiting Wnt signaling and repressing peripheral eye
CC development (PubMed:21856951). Interacts with TGFB1; the interaction
CC contributes to regulation of the hair cycle (PubMed:22995554).
CC Interacts with netrin (PubMed:23206892). Interacts with CCN2
CC (PubMed:30232710). {ECO:0000269|PubMed:21856951,
CC ECO:0000269|PubMed:22995554, ECO:0000269|PubMed:23206892,
CC ECO:0000269|PubMed:30232710}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:30595550,
CC ECO:0000269|PubMed:31391339, ECO:0000269|PubMed:31535079,
CC ECO:0000269|PubMed:31767170}.
CC -!- TISSUE SPECIFICITY: Expressed in macrophages in inflamed wounds with
CC wound expression starting 2 days post-wounding (dpw) (at protein level)
CC (PubMed:25159578). At 7 dpw, expressed from epidermis and extracellular
CC matrix in the wound edge to neoepidermis and granulation tissue and in
CC panniculus carnosus under the granulation tissue (at protein level)
CC (PubMed:25159578). After fibrosis, disappears in the dermal area at 11
CC dpw (at protein level) (PubMed:25159578). Expressed in the hair
CC follicle during morphogenesis and the hair cycle (at protein level)
CC (PubMed:22995554). In embryonic brain, strong expression in the
CC olfactory bulb, anterior olfactory nucleus, neocortex, piriform cortex,
CC glial wedge, midline zipper glia, indusium griseum and the area
CC surrounding the anterior commissure (AC) but not on AC axons (at
CC protein level) (PubMed:23206892). In the adult eye, expressed in
CC retinal layers, lens epithelium, and ciliary body where it is expressed
CC predominantly in the inner non-pigmented layer (PubMed:21856951).
CC Expressed in almost all brain regions in the embryo, in the cortex and
CC the lateral ventricle at P0 and is restricted to the subventricular
CC zone and lateral nucleus of the amygdala in adults (PubMed:21055390).
CC Prominent expression in hippocampal regions from early postnatal stages
CC until postnatal day 15 and gradually declines at later stages
CC (PubMed:31983064). Expressed in almost all bone regions in the femurs
CC of juveniles (PubMed:30271858). In the inner ear, accumulates in
CC nonprosensory regions during early embryonic stages and in both
CC nonprosensory and prosensory regions in late embryonic stages
CC (PubMed:32127020). In the adult ear, expressed in the organ of Corti,
CC spiral ganglion cells, and the stria vascularis (PubMed:32127020).
CC Highly expressed in the liver where it is detected primarily in
CC hepatocytes but not in non-parenchymal cells (PubMed:31535079).
CC {ECO:0000269|PubMed:21055390, ECO:0000269|PubMed:21856951,
CC ECO:0000269|PubMed:22995554, ECO:0000269|PubMed:23206892,
CC ECO:0000269|PubMed:25159578, ECO:0000269|PubMed:30271858,
CC ECO:0000269|PubMed:31535079, ECO:0000269|PubMed:31983064,
CC ECO:0000269|PubMed:32127020}.
CC -!- DEVELOPMENTAL STAGE: During the hair cycle, expression is down-
CC regulated at the first telogen stage and is up-regulated at the
CC secondary anagen stage. {ECO:0000269|PubMed:22995554}.
CC -!- INDUCTION: By endoplasmic reticulum stress and inflammation
CC (PubMed:31391339). Up-regulated in response to high-fat diet and this
CC is reversed by return to a normal diet (PubMed:30595550,
CC PubMed:31391339). {ECO:0000269|PubMed:30595550,
CC ECO:0000269|PubMed:31391339}.
CC -!- DISRUPTION PHENOTYPE: Expansion of the ciliary body and up-regulation
CC of Wnt2b and Fzd4 expression in the developing peripheral eye
CC (PubMed:21856951). Delayed hair cycle with down-regulation of Tgfb1
CC throughout the cycle and low levels of phosphorylated Smad2/3
CC (PubMed:22995554). Failure of the axons of the anterior and posterior
CC parts of the anterior commissure (AC) to cross the midline, leading to
CC an almost total absence of the AC in adults (PubMed:21055390,
CC PubMed:23206892). Reduced size of hippocampus and dentate gyrus (DG),
CC increased number of neural stem cells (NSCs) in the DG at P15, altered
CC ratio of proliferating and quiescent NSCs with an increase in the
CC number of proliferating NSCs in the DG at P15, and abnormal terminal
CC differentiation of NSCs (PubMed:31983064). Decreased weight and short
CC stature due to decreased longitudinal bone growth coupled with low bone
CC mass (PubMed:30271858). Shortened and morphologically abnormal growth
CC plates and abnormal expression of chondrogenic marker genes
CC (PubMed:30271858). Formation of abnormally short and dislocated
CC stereocilia in the inner hair cells of the ear and hearing loss
CC (PubMed:32127020). Reduced cochlear expression of Sox2 and
CC translocation of Sox2 from the nucleus to the cytoplasm in spiral
CC ganglion cells (SGCs) at P0 (PubMed:32127020). Redistribution of Bmp4
CC with diminished expression in the outer sulcus and sparse distribution
CC around the cochlear epithelium (PubMed:32127020). Reduced number of
CC SGCs at the cochlear basal turn (PubMed:32127020). Excess wound
CC inflammation with up-regulation of Tgfb1, Stat3 and Il6 during wound
CC healing (PubMed:25159578). Reduced body size, increased levels of
CC circulating high-density lipoprotein cholesterol and increased
CC cholesterol efflux (PubMed:31391339). Some studues showed increased
CC sympathetic innervation and norepinephrine release in adipose tissue,
CC leading to enhanced adrenergic signaling and thermogenesis, attenuation
CC of brown fat whitening and protection from diet-induced obesity
CC (PubMed:31535079, PubMed:30595550). Another study found no effect on
CC brown fat thermogenic capacity, protection from diet-induced obesity or
CC glucose homeostasis (PubMed:31767170). Double knockout of Tsku and
CC Draxi results in a higher frequency of AC defects than single knockout
CC of either Tsku or Draxi (PubMed:23206892).
CC {ECO:0000269|PubMed:21055390, ECO:0000269|PubMed:21856951,
CC ECO:0000269|PubMed:22995554, ECO:0000269|PubMed:23206892,
CC ECO:0000269|PubMed:25159578, ECO:0000269|PubMed:30271858,
CC ECO:0000269|PubMed:30595550, ECO:0000269|PubMed:31391339,
CC ECO:0000269|PubMed:31535079, ECO:0000269|PubMed:31767170,
CC ECO:0000269|PubMed:31983064, ECO:0000269|PubMed:32127020}.
CC -!- MISCELLANEOUS: This factor is named 'Tsukushi' because its expression
CC pattern in chick embryos is similar to the shape of the Japanese
CC horsetail plant, tsukushi. {ECO:0000250|UniProtKB:Q65Z91}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAC29069.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=BAE23270.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AB214184; BAD98727.1; -; mRNA.
DR EMBL; AK035461; BAC29069.1; ALT_INIT; mRNA.
DR EMBL; AK137208; BAE23270.1; ALT_INIT; mRNA.
DR CCDS; CCDS21469.1; -.
DR RefSeq; NP_001019790.1; NM_001024619.3.
DR RefSeq; NP_001162011.1; NM_001168539.1.
DR RefSeq; NP_001162012.1; NM_001168540.1.
DR RefSeq; NP_001162013.1; NM_001168541.1.
DR RefSeq; XP_006507895.1; XM_006507832.2.
DR RefSeq; XP_006507896.1; XM_006507833.1.
DR RefSeq; XP_006507897.1; XM_006507834.2.
DR RefSeq; XP_006507898.1; XM_006507835.2.
DR RefSeq; XP_006507899.1; XM_006507836.3.
DR RefSeq; XP_006507900.1; XM_006507837.1.
DR AlphaFoldDB; Q8CBR6; -.
DR SMR; Q8CBR6; -.
DR STRING; 10090.ENSMUSP00000091713; -.
DR GlyGen; Q8CBR6; 3 sites.
DR iPTMnet; Q8CBR6; -.
DR PhosphoSitePlus; Q8CBR6; -.
DR MaxQB; Q8CBR6; -.
DR PaxDb; Q8CBR6; -.
DR PRIDE; Q8CBR6; -.
DR ProteomicsDB; 297981; -.
DR Antibodypedia; 2163; 84 antibodies from 18 providers.
DR DNASU; 244152; -.
DR Ensembl; ENSMUST00000094161; ENSMUSP00000091713; ENSMUSG00000049580.
DR Ensembl; ENSMUST00000164726; ENSMUSP00000130917; ENSMUSG00000049580.
DR Ensembl; ENSMUST00000165257; ENSMUSP00000128431; ENSMUSG00000049580.
DR Ensembl; ENSMUST00000165901; ENSMUSP00000127242; ENSMUSG00000049580.
DR Ensembl; ENSMUST00000167405; ENSMUSP00000131789; ENSMUSG00000049580.
DR Ensembl; ENSMUST00000179780; ENSMUSP00000137437; ENSMUSG00000049580.
DR Ensembl; ENSMUST00000206414; ENSMUSP00000146025; ENSMUSG00000049580.
DR GeneID; 244152; -.
DR KEGG; mmu:244152; -.
DR UCSC; uc009ikh.2; mouse.
DR CTD; 25987; -.
DR MGI; MGI:2443855; Tsku.
DR VEuPathDB; HostDB:ENSMUSG00000049580; -.
DR eggNOG; KOG0619; Eukaryota.
DR GeneTree; ENSGT00940000160984; -.
DR HOGENOM; CLU_785168_0_0_1; -.
DR InParanoid; Q8CBR6; -.
DR OMA; SQDVRCR; -.
DR OrthoDB; 1168051at2759; -.
DR PhylomeDB; Q8CBR6; -.
DR TreeFam; TF343079; -.
DR BioGRID-ORCS; 244152; 3 hits in 74 CRISPR screens.
DR PRO; PR:Q8CBR6; -.
DR Proteomes; UP000000589; Chromosome 7.
DR RNAct; Q8CBR6; protein.
DR Bgee; ENSMUSG00000049580; Expressed in gall bladder and 130 other tissues.
DR ExpressionAtlas; Q8CBR6; baseline and differential.
DR Genevisible; Q8CBR6; MM.
DR GO; GO:0031012; C:extracellular matrix; IBA:GO_Central.
DR GO; GO:0005615; C:extracellular space; IDA:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0050431; F:transforming growth factor beta binding; IPI:UniProtKB.
DR GO; GO:0021960; P:anterior commissure morphogenesis; IMP:UniProtKB.
DR GO; GO:0043010; P:camera-type eye development; IMP:MGI.
DR GO; GO:0033344; P:cholesterol efflux; IMP:UniProtKB.
DR GO; GO:0042632; P:cholesterol homeostasis; IMP:UniProtKB.
DR GO; GO:0008203; P:cholesterol metabolic process; IMP:UniProtKB.
DR GO; GO:0061073; P:ciliary body morphogenesis; IMP:MGI.
DR GO; GO:0021540; P:corpus callosum morphogenesis; IMP:MGI.
DR GO; GO:0097009; P:energy homeostasis; IMP:UniProtKB.
DR GO; GO:0021766; P:hippocampus development; IMP:UniProtKB.
DR GO; GO:0060122; P:inner ear receptor cell stereocilium organization; IMP:UniProtKB.
DR GO; GO:0021670; P:lateral ventricle development; IMP:MGI.
DR GO; GO:1904761; P:negative regulation of myofibroblast differentiation; IMP:UniProtKB.
DR GO; GO:0010977; P:negative regulation of neuron projection development; IMP:UniProtKB.
DR GO; GO:0030512; P:negative regulation of transforming growth factor beta receptor signaling pathway; IBA:GO_Central.
DR GO; GO:0032911; P:negative regulation of transforming growth factor beta1 production; IMP:UniProtKB.
DR GO; GO:0030178; P:negative regulation of Wnt signaling pathway; IDA:MGI.
DR GO; GO:0042635; P:positive regulation of hair cycle; IMP:UniProtKB.
DR GO; GO:0010468; P:regulation of gene expression; IMP:MGI.
DR GO; GO:0042060; P:wound healing; IMP:UniProtKB.
DR Gene3D; 3.80.10.10; -; 2.
DR InterPro; IPR001611; Leu-rich_rpt.
DR InterPro; IPR003591; Leu-rich_rpt_typical-subtyp.
DR InterPro; IPR032675; LRR_dom_sf.
DR Pfam; PF13855; LRR_8; 2.
DR SMART; SM00369; LRR_TYP; 7.
DR PROSITE; PS51450; LRR; 8.
PE 1: Evidence at protein level;
KW Developmental protein; Glycoprotein; Leucine-rich repeat; Neurogenesis;
KW Reference proteome; Repeat; Secreted; Signal.
FT SIGNAL 1..17
FT /evidence="ECO:0000255"
FT CHAIN 18..354
FT /note="Tsukushi"
FT /id="PRO_0000240408"
FT DOMAIN 18..59
FT /note="LRRNT"
FT REPEAT 60..81
FT /note="LRR 1"
FT REPEAT 86..107
FT /note="LRR 2"
FT REPEAT 110..131
FT /note="LRR 3"
FT REPEAT 133..154
FT /note="LRR 4"
FT REPEAT 160..180
FT /note="LRR 5"
FT REPEAT 186..207
FT /note="LRR 6"
FT REPEAT 208..228
FT /note="LRR 7"
FT REPEAT 231..253
FT /note="LRR 8"
FT REPEAT 256..277
FT /note="LRR 9"
FT REPEAT 281..302
FT /note="LRR 10"
FT CARBOHYD 75
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 138
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 191
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 354 AA; 38362 MW; 11CF35A6A82C68EF CRC64;
MLCSLFLLLL AVGRVQTTRP CFPGCQCEEE TFGLFDSFSL IRVDCSSLGP HIVPVPIPLD
TAHLDLSSNR LETVNESVLA GPGYTTLAGL DLSYNLLTSI MPSAFSRLRY LESLDLSHNG
LAALPAEIFT SSPLSDINLS HNRLREVSIS AFTTHSQGRA LHVDLSHNLI HRLLPHPARA
SLPAPTIQSL NLSWNRFRAV PDLRDLPLRY LSLDGNPLAT INPDAFMGLA GLTHLSLASL
QGILHLPPHG FRELPGLQVL DLSGNPKLKW AGAEVFSGLG LLQELDLSGS SLVPLPEMLL
HHLPALQSVS VGQDVQCRRL VREGAYHRQP GSSPKVVLHC GDTQESAARG PDIL
