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Protein

Leucine-rich repeat transmembrane protein FLRT2

Gene

Flrt2

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

Functioni

Functions in cell-cell adhesion, cell migration and axon guidance. Mediates cell-cell adhesion via its interactions with ADGRL3 and probably also other latrophilins that are expressed at the surface of adjacent cells (PubMed:21350012, PubMed:25728924 PubMed:25374360). May play a role in the migration of cortical neurons during brain development via its interaction with UNC5D (PubMed:21673655). Mediates axon growth cone collapse and plays a repulsive role in neuron guidance via its interaction with UNC5D, and possibly also other UNC-5 family members (PubMed:21673655, PubMed:25728924). Plays a role in fibroblast growth factor-mediated signaling cascades (PubMed:16872596). Required for normal organization of the cardiac basement membrane during embryogenesis, and for normal embryonic epicardium and heart morphogenesis (PubMed:21350012).5 Publications

GO - Molecular functioni

  • chemorepellent activity Source: MGI
  • fibroblast growth factor receptor binding Source: UniProtKB

GO - Biological processi

  • axon guidance Source: MGI
  • basement membrane organization Source: UniProtKB
  • cell adhesion involved in heart morphogenesis Source: UniProtKB
  • fibroblast growth factor receptor signaling pathway Source: UniProtKB
  • heart morphogenesis Source: UniProtKB
  • negative chemotaxis Source: GOC
  • positive regulation of synapse assembly Source: MGI
  • regulation of neuron migration Source: MGI
Complete GO annotation...

Keywords - Molecular functioni

Developmental protein

Keywords - Biological processi

Cell adhesion

Enzyme and pathway databases

ReactomeiR-MMU-5654687. Downstream signaling of activated FGFR1.

Names & Taxonomyi

Protein namesi
Recommended name:
Leucine-rich repeat transmembrane protein FLRT2Curated
Alternative name(s):
Fibronectin leucine rich transmembrane protein 2Imported
Gene namesi
Name:Flrt2Imported
Synonyms:Kiaa04051 Publication
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 12

Organism-specific databases

MGIiMGI:3603594. Flrt2.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini36 – 540505ExtracellularCuratedAdd
BLAST
Transmembranei541 – 56121HelicalSequence analysisAdd
BLAST
Topological domaini562 – 66099CytoplasmicCuratedAdd
BLAST

GO - Cellular componenti

  • cell-cell junction Source: UniProtKB
  • endoplasmic reticulum membrane Source: UniProtKB-SubCell
  • extracellular exosome Source: MGI
  • extracellular space Source: MGI
  • focal adhesion Source: MGI
  • integral component of plasma membrane Source: UniProtKB
  • neuron projection Source: UniProtKB-SubCell
  • proteinaceous extracellular matrix Source: UniProtKB-SubCell
  • synapse Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Cell junction, Cell membrane, Endoplasmic reticulum, Extracellular matrix, Membrane, Microsome, Secreted, Synapse, Synaptosome

Pathology & Biotechi

Disruption phenotypei

Heterozygous mice are viable and fertile, but homozygous mice display nearly complete embryonic lethality. Most embryos die at about 12.5 dpc, probably due to impaired expansion of the ventricular myocardium during development, reduced endocardial volume and heart insufficiency. Contrary to wild-type, the epicardium appears ruffled and presents numerous holes, due to defective formation of cell-cell adhesions. Still, there is a very small percentage of life-born pups that survive at least up to weaning.1 Publication

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi170 – 1701H → E or N: Abolishes interaction with UNC5D. 1 Publication
Mutagenesisi186 – 1861R → N: Abolishes homooligomerization and FLRT2-mediated cell-cell adhesion; when associated with T-188. 1 Publication
Mutagenesisi188 – 1881D → T: Abolishes homooligomerization and FLRT2-mediated cell-cell adhesion; when associated with N-186. 1 Publication
Mutagenesisi248 – 2481D → N: No effect on interaction with UNC5D; when associated with T-250. 1 Publication
Mutagenesisi250 – 2501P → T: No effect on interaction with UNC5D; when associated with N-248. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 3535Sequence analysisAdd
BLAST
Chaini36 – 660625Leucine-rich repeat transmembrane protein FLRT2PRO_0000434523Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi36 ↔ 42Combined sources
Disulfide bondi40 ↔ 49Combined sources
Glycosylationi202 – 2021N-linked (GlcNAc...)Sequence analysis
Disulfide bondi314 ↔ 339Combined sources
Disulfide bondi316 ↔ 360Combined sources

Post-translational modificationi

N-glycosylated.2 Publications
Proteolytic cleavage in the juxtamembrane region gives rise to a soluble ectodomain. Cleavage is probably effected by a metalloprotease.1 Publication

Keywords - PTMi

Disulfide bond, Glycoprotein

Proteomic databases

MaxQBiQ8BLU0.
PaxDbiQ8BLU0.

Expressioni

Tissue specificityi

Detected in adult brain (at protein level).1 Publication

Developmental stagei

Detected in embryonic brain at 13 dpc. Levels in brain decrease gradually after 15 dpc, but expression continues after birth (PubMed:21673655). Detected in embryonic myocardium, body wall and pro-epicardial organ at 9.5 dpc. Detected in the epicardial cell layer and throughout the myocardium at 10.5 dpc. Highly expressed in embryonic and neonate heart, but after that levels decrease strongly, and the protein is barely detectable 3 weeks after birth, with even lower levels after 7 and 15 weeks (at protein level) (PubMed:21350012). Detected in the anterior endoderm at 7.5 dpc. Detected on anterior somites, the allantois and mesenchymal tissue behind the developing heart at 8.5 dpc (PubMed:18448090). Detected in the cephalic mesenchyme and in tissue posterior to the developing heart at 9.5 and 10.5 dpc. Detected in the developing stomach and in a subset of the trunk sclerotome at 10.5 dpc. At 11 dpc, detected also in branchial arches, eyes and limbs (PubMed:16872596, PubMed:18448090).4 Publications

Inductioni

Up-regulated by FGF2.1 Publication

Gene expression databases

BgeeiQ6A073.
GenevisibleiQ8BLU0. MM.

Interactioni

Subunit structurei

Self-associates (via leucine-rich repeats), giving rise to homooligomers (PubMed:25374360). Interacts with FGFR1 (PubMed:16872596). Interacts with FGFR2 (PubMed:21765038). Interacts (via extracellular domain) with ADGRL1/LPHN1 (PubMed:22405201). Interacts (via extracellular domain) with ADGRL3 (via olfactomedin-like domain)(PubMed:22405201, PubMed:25728924). Interacts (via extracellular domain) with UNC5D (via the first Ig-like domain) (PubMed:21673655, PubMed:25374360). Can also interact (via extracellular domain) with UNC5B, but with much lower affinity (PubMed:21673655). Interacts (via extracellular domain) with FN1 (PubMed:24585683).7 Publications

GO - Molecular functioni

  • fibroblast growth factor receptor binding Source: UniProtKB

Protein-protein interaction databases

DIPiDIP-61401N.
STRINGi10090.ENSMUSP00000062171.

Structurei

Secondary structure

1
660
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi38 – 436Combined sources
Beta strandi46 – 483Combined sources
Beta strandi66 – 694Combined sources
Helixi82 – 843Combined sources
Beta strandi92 – 943Combined sources
Beta strandi113 – 1153Combined sources
Helixi126 – 1316Combined sources
Beta strandi137 – 1393Combined sources
Turni147 – 1493Combined sources
Turni152 – 1543Combined sources
Helixi155 – 1573Combined sources
Beta strandi163 – 1653Combined sources
Beta strandi184 – 1863Combined sources
Turni197 – 2004Combined sources
Beta strandi208 – 2103Combined sources
Turni218 – 2203Combined sources
Beta strandi234 – 2363Combined sources
Beta strandi256 – 2583Combined sources
Turni269 – 2713Combined sources
Beta strandi280 – 2823Combined sources
Beta strandi295 – 2984Combined sources
Beta strandi304 – 3063Combined sources
Helixi316 – 3183Combined sources
Helixi319 – 3279Combined sources
Beta strandi332 – 3354Combined sources
Beta strandi338 – 3425Combined sources
Turni343 – 3475Combined sources
Helixi350 – 3523Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4V2CX-ray4.00A/C35-362[»]
4V2DX-ray2.50A36-361[»]
ProteinModelPortaliQ8BLU0.
SMRiQ8BLU0. Positions 35-380.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini36 – 6328LRRNTSequence analysisAdd
BLAST
Repeati62 – 8726LRR 1Sequence analysisAdd
BLAST
Repeati88 – 10821LRR 2Sequence analysisAdd
BLAST
Repeati109 – 13123LRR 3Sequence analysisAdd
BLAST
Repeati132 – 15726LRR 4Sequence analysisAdd
BLAST
Repeati159 – 18123LRR 5Sequence analysisAdd
BLAST
Repeati183 – 20220LRR 6Sequence analysisAdd
BLAST
Repeati203 – 22826LRR 7Sequence analysisAdd
BLAST
Repeati229 – 25123LRR 8Sequence analysisAdd
BLAST
Repeati252 – 27423LRR 9Sequence analysisAdd
BLAST
Repeati275 – 29824LRR 10Sequence analysisAdd
BLAST
Domaini310 – 36253LRRCTSequence analysisAdd
BLAST
Domaini419 – 51799Fibronectin type-IIIPROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Contains 1 fibronectin type-III domain.PROSITE-ProRule annotation
Contains 10 LRR (leucine-rich) repeats.Sequence analysis1 Publication
Contains 1 LRRCT domain.Sequence analysis
Contains 1 LRRNT domain.Sequence analysis

Keywords - Domaini

Leucine-rich repeat, Repeat, Signal, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiENOG410IHC8. Eukaryota.
ENOG4111ID7. LUCA.
GeneTreeiENSGT00760000118969.
HOGENOMiHOG000290188.
HOVERGENiHBG051629.
KOiK16362.
OMAiFPAELHN.
OrthoDBiEOG7RZ5PF.
PhylomeDBiQ8BLU0.
TreeFamiTF315838.

Family and domain databases

Gene3Di2.60.40.10. 1 hit.
3.80.10.10. 3 hits.
InterProiIPR000483. Cys-rich_flank_reg_C.
IPR003961. FN3_dom.
IPR013783. Ig-like_fold.
IPR032675. L_dom-like.
IPR001611. Leu-rich_rpt.
IPR003591. Leu-rich_rpt_typical-subtyp.
IPR000372. LRRNT.
[Graphical view]
PfamiPF00041. fn3. 1 hit.
PF13855. LRR_8. 3 hits.
PF01463. LRRCT. 1 hit.
[Graphical view]
SMARTiSM00369. LRR_TYP. 7 hits.
SM00082. LRRCT. 1 hit.
SM00013. LRRNT. 1 hit.
[Graphical view]
SUPFAMiSSF49265. SSF49265. 1 hit.
SSF52058. SSF52058. 1 hit.
PROSITEiPS50853. FN3. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q8BLU0-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MGLQTTKWPG RGAFILKFWL IISLGLYLQV SKLLACPSVC RCDRNFVYCN
60 70 80 90 100
ERSLTSVPLG IPEGVTVLYL HNNQINNAGF PAELHNVQSV HTVYLYGNQL
110 120 130 140 150
DEFPMNLPKN VRVLHLQENN IQTISRAALA QLLKLEELHL DDNSISTVGV
160 170 180 190 200
EDGAFREAIS LKLLFLSKNH LSSVPVGLPV DLQELRVDEN RIAVISDMAF
210 220 230 240 250
QNLTSLERLI VDGNLLTNKG IAEGTFSHLT KLKEFSIVRN SLSHPPPDLP
260 270 280 290 300
GTHLIRLYLQ DNQINHIPLT AFANLRKLER LDISNNQLRM LTQGVFDHLS
310 320 330 340 350
NLKQLTARNN PWFCDCSIKW VTEWLKYIPS SLNVRGFMCQ GPEQVRGMAV
360 370 380 390 400
RELNMNLLSC PTTTPGLPVF TPAPSTVSPT TQSPTLSVPS PSRGSVPPAP
410 420 430 440 450
TPSKLPTIPD WDGRERVTPP ISERIQLSIH FVNDTSIQVS WLSLFTVMAY
460 470 480 490 500
KLTWVKMGHS LVGGIVQERI VSGEKQHLSL VNLEPRSTYR ICLVPLDAFN
510 520 530 540 550
YRTVEDTICS EATTHASYLN NGSNTASSHE QTTSHSMGSP FLLAGLIGGA
560 570 580 590 600
VIFVLVVLLS VFCWHMHKKG RYTSQKWKYN RGRRKDDYCE AGTKKDNSIL
610 620 630 640 650
EMTETSFQIV SLNNDQLLKG DFRLQPIYTP NGGINYTDCH IPNNMRYCNS
660
SVPDLEHCHT
Length:660
Mass (Da):73,948
Last modified:March 1, 2003 - v1
Checksum:i5C1A9BBA3142C020
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY495669 mRNA. Translation: AAR92202.1.
AK041311 mRNA. Translation: BAC30900.1.
AK135149 mRNA. Translation: BAE22441.1.
AC122430 Genomic DNA. No translation available.
AC125487 Genomic DNA. No translation available.
CH466549 Genomic DNA. Translation: EDL18942.1.
BC096471 mRNA. Translation: AAH96471.1.
BC138297 mRNA. Translation: AAI38298.1.
BC138298 mRNA. Translation: AAI38299.1.
AK172945 mRNA. Translation: BAD32223.1.
CCDSiCCDS26094.1.
RefSeqiNP_958926.1. NM_201518.4.
XP_006516118.1. XM_006516055.2.
XP_011242434.1. XM_011244132.1.
UniGeneiMm.341948.

Genome annotation databases

EnsembliENSMUST00000057324; ENSMUSP00000062171; ENSMUSG00000047414.
ENSMUST00000110117; ENSMUSP00000105744; ENSMUSG00000047414.
GeneIDi399558.
KEGGimmu:399558.
UCSCiuc007olc.2. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY495669 mRNA. Translation: AAR92202.1.
AK041311 mRNA. Translation: BAC30900.1.
AK135149 mRNA. Translation: BAE22441.1.
AC122430 Genomic DNA. No translation available.
AC125487 Genomic DNA. No translation available.
CH466549 Genomic DNA. Translation: EDL18942.1.
BC096471 mRNA. Translation: AAH96471.1.
BC138297 mRNA. Translation: AAI38298.1.
BC138298 mRNA. Translation: AAI38299.1.
AK172945 mRNA. Translation: BAD32223.1.
CCDSiCCDS26094.1.
RefSeqiNP_958926.1. NM_201518.4.
XP_006516118.1. XM_006516055.2.
XP_011242434.1. XM_011244132.1.
UniGeneiMm.341948.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4V2CX-ray4.00A/C35-362[»]
4V2DX-ray2.50A36-361[»]
ProteinModelPortaliQ8BLU0.
SMRiQ8BLU0. Positions 35-380.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

DIPiDIP-61401N.
STRINGi10090.ENSMUSP00000062171.

Proteomic databases

MaxQBiQ8BLU0.
PaxDbiQ8BLU0.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000057324; ENSMUSP00000062171; ENSMUSG00000047414.
ENSMUST00000110117; ENSMUSP00000105744; ENSMUSG00000047414.
GeneIDi399558.
KEGGimmu:399558.
UCSCiuc007olc.2. mouse.

Organism-specific databases

CTDi23768.
MGIiMGI:3603594. Flrt2.
RougeiSearch...

Phylogenomic databases

eggNOGiENOG410IHC8. Eukaryota.
ENOG4111ID7. LUCA.
GeneTreeiENSGT00760000118969.
HOGENOMiHOG000290188.
HOVERGENiHBG051629.
KOiK16362.
OMAiFPAELHN.
OrthoDBiEOG7RZ5PF.
PhylomeDBiQ8BLU0.
TreeFamiTF315838.

Enzyme and pathway databases

ReactomeiR-MMU-5654687. Downstream signaling of activated FGFR1.

Miscellaneous databases

ChiTaRSiFlrt2. mouse.
PROiQ8BLU0.
SOURCEiSearch...

Gene expression databases

BgeeiQ6A073.
GenevisibleiQ8BLU0. MM.

Family and domain databases

Gene3Di2.60.40.10. 1 hit.
3.80.10.10. 3 hits.
InterProiIPR000483. Cys-rich_flank_reg_C.
IPR003961. FN3_dom.
IPR013783. Ig-like_fold.
IPR032675. L_dom-like.
IPR001611. Leu-rich_rpt.
IPR003591. Leu-rich_rpt_typical-subtyp.
IPR000372. LRRNT.
[Graphical view]
PfamiPF00041. fn3. 1 hit.
PF13855. LRR_8. 3 hits.
PF01463. LRRCT. 1 hit.
[Graphical view]
SMARTiSM00369. LRR_TYP. 7 hits.
SM00082. LRRCT. 1 hit.
SM00013. LRRNT. 1 hit.
[Graphical view]
SUPFAMiSSF49265. SSF49265. 1 hit.
SSF52058. SSF52058. 1 hit.
PROSITEiPS50853. FN3. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Regulated expression of FLRT genes implies a functional role in the regulation of FGF signalling during mouse development."
    Haines B.P., Wheldon L.M., Summerbell D., Heath J.K., Rigby P.W.J.
    Dev. Biol. 297:14-25(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, INTERACTION WITH FGFR1, SUBCELLULAR LOCATION, GLYCOSYLATION, DEVELOPMENTAL STAGE, INDUCTION BY FGF2.
    Strain: C57BL/6 X CBAImported.
  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(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: C57BL/6J.
    Tissue: Cerebellum.
  3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: C57BL/6JImported.
  4. Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.
    Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  5. "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: FVB/N.
    Tissue: Brain and Mammary cancer.
  6. "Prediction of the coding sequences of mouse homologues of KIAA gene: IV. The complete nucleotide sequences of 500 mouse KIAA-homologous cDNAs identified by screening of terminal sequences of cDNA clones randomly sampled from size-fractionated libraries."
    Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S., Saga Y., Seino S., Nishimura M., Kaisho T., Hoshino K., Kitamura H., Nagase T., Ohara O., Koga H.
    DNA Res. 11:205-218(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 24-660.
    Tissue: BrainImported.
  7. "Ventral closure, headfold fusion and definitive endoderm migration defects in mouse embryos lacking the fibronectin leucine-rich transmembrane protein FLRT3."
    Maretto S., Mueller P.S., Aricescu A.R., Cho K.W., Bikoff E.K., Robertson E.J.
    Dev. Biol. 318:184-193(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: DEVELOPMENTAL STAGE.
  8. "The fibronectin leucine-rich repeat transmembrane protein Flrt2 is required in the epicardium to promote heart morphogenesis."
    Mueller P.S., Schulz R., Maretto S., Costello I., Srinivas S., Bikoff E., Robertson E.
    Development 138:1297-1308(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: DISRUPTION PHENOTYPE, FUNCTION, DEVELOPMENTAL STAGE, TISSUE SPECIFICITY.
  9. Cited for: SUBCELLULAR LOCATION, PROTEOLYTIC CLEAVAGE, DEVELOPMENTAL STAGE, GLYCOSYLATION, INTERACTION WITH UNC5D AND UNC5B.
  10. "Mouse FLRT2 interacts with the extracellular and intracellular regions of FGFR2."
    Wei K., Xu Y., Tse H., Manolson M.F., Gong S.G.
    J. Dent. Res. 90:1234-1239(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH FGFR2.
  11. "FLRT proteins are endogenous latrophilin ligands and regulate excitatory synapse development."
    O'Sullivan M.L., de Wit J., Savas J.N., Comoletti D., Otto-Hitt S., Yates J.R. III, Ghosh A.
    Neuron 73:903-910(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH ADGRL1 AND ADGRL3, SUBCELLULAR LOCATION.
  12. "FLRT2 interacts with fibronectin in the ATDC5 chondroprogenitor cells."
    Flintoff K.A., Arudchelvan Y., Gong S.G.
    J. Cell. Physiol. 229:1538-1547(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION, INTERACTION WITH FN1.
  13. Cited for: INTERACTION WITH ADGRL3, FUNCTION.
  14. "FLRT structure: balancing repulsion and cell adhesion in cortical and vascular development."
    Seiradake E., del Toro D., Nagel D., Cop F., Haertl R., Ruff T., Seyit-Bremer G., Harlos K., Border E.C., Acker-Palmer A., Jones E.Y., Klein R.
    Neuron 84:370-385(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.50 ANGSTROMS) OF 36-361 IN COMPLEX WITH UNC5D, FUNCTION, SUBCELLULAR LOCATION, SUBUNIT, INTERACTION WITH UNC5D, DISULFIDE BONDS, DOMAIN, MUTAGENESIS OF HIS-170; ARG-186; ASP-188; ASP-248 AND PRO-250.

Entry informationi

Entry nameiFLRT2_MOUSE
AccessioniPrimary (citable) accession number: Q8BLU0
Secondary accession number(s): Q6A073
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 14, 2015
Last sequence update: March 1, 2003
Last modified: June 8, 2016
This is version 133 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

3D-structure, Complete proteome, Reference proteome

Documents

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

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 one 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.