Did you know ? If you order before Friday 14h we deliver 90PCT of the the time next Tuesday, GENTAUR another in time delivery

Leucine-rich repeat transmembrane protein FLRT3 (Fibronectin-like domain-containing leucine-rich transmembrane protein 3)

 FLRT3_RAT               Reviewed;         649 AA.
B1H234;
14-OCT-2008, integrated into UniProtKB/Swiss-Prot.
29-APR-2008, sequence version 1.
23-MAY-2018, entry version 84.
RecName: Full=Leucine-rich repeat transmembrane protein FLRT3;
AltName: Full=Fibronectin-like domain-containing leucine-rich transmembrane protein 3;
Flags: Precursor;
Name=Flrt3;
Rattus norvegicus (Rat).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Rattus.
NCBI_TaxID=10116;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=Brown Norway;
Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=Brown Norway/NHsdMcwi; TISSUE=Brain;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[3]
TISSUE SPECIFICITY.
PubMed=14706654; DOI=10.1016/j.bbrc.2003.12.047;
Tsuji L., Yamashita T., Kubo T., Madura T., Tanaka H., Hosokawa K.,
Tohyama M.;
"FLRT3, a cell surface molecule containing LRR repeats and a FNIII
domain, promotes neurite outgrowth.";
Biochem. Biophys. Res. Commun. 313:1086-1091(2004).
[4]
FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, INDUCTION BY
PERIPHERAL NERVE INJURY, AND DEVELOPMENTAL STAGE.
PubMed=15485775; DOI=10.1016/j.mcn.2004.06.008;
Robinson M., Parsons Perez M.C., Tebar L., Palmer J., Patel A.,
Marks D., Sheasby A., De Felipe C., Coffin R., Livesey F.J.,
Hunt S.P.;
"FLRT3 is expressed in sensory neurons after peripheral nerve injury
and regulates neurite outgrowth.";
Mol. Cell. Neurosci. 27:202-214(2004).
[5]
INTERACTION WITH ADGRL1 AND ADGRL3, SUBCELLULAR LOCATION,
IDENTIFICATION BY MASS SPECTROMETRY, AND TISSUE SPECIFICITY.
PubMed=22405201; DOI=10.1016/j.neuron.2012.01.018;
O'Sullivan M.L., de Wit J., Savas J.N., Comoletti D., Otto-Hitt S.,
Yates J.R. III, Ghosh A.;
"FLRT proteins are endogenous latrophilin ligands and regulate
excitatory synapse development.";
Neuron 73:903-910(2012).
-!- FUNCTION: Functions in cell-cell adhesion, cell migration and axon
guidance, exerting an attractive or repulsive role depending on
its interaction partners. Plays a role in the spatial organization
of brain neurons. Plays a role in vascular development in the
retina (By similarity). Plays a role in cell-cell adhesion via its
interaction with ADGRL3 and probably also other latrophilins that
are expressed at the surface of adjacent cells (By similarity).
Interaction with the intracellular domain of ROBO1 mediates axon
attraction towards cells expressing NTN1. Mediates axon growth
cone collapse and plays a repulsive role in neuron guidance via
its interaction with UNC5B, and possibly also other UNC-5 family
members (By similarity). Promotes neurite outgrowth (in vitro) (By
similarity). Mediates cell-cell contacts that promote an increase
both in neurite number and in neurite length (PubMed:15485775).
Plays a role in the regulation of the density of glutamaergic
synapses (PubMed:22405201). Plays a role in fibroblast growth
factor-mediated signaling cascades. Required for normal
morphogenesis during embryonic development, but not for normal
embryonic patterning. Required for normal ventral closure,
headfold fusion and definitive endoderm migration during embryonic
development. Required for the formation of a normal basement
membrane and the maintenance of a normal anterior visceral
endoderm during embryonic development (By similarity).
{ECO:0000250|UniProtKB:Q8BGT1, ECO:0000250|UniProtKB:Q9NZU0,
ECO:0000269|PubMed:15485775, ECO:0000269|PubMed:22405201}.
-!- SUBUNIT: Monomer and homodimer. Self-associates (via leucine-rich
repeats), giving rise to homooligomers. Interacts with FGFR1 (By
similarity). Interacts (via extracellular domain) with
ADGRL1/LPHN1 and ADGRL3 (via olfactomedin-like domain)
(PubMed:22405201). Interacts (via extracellular domain) with LPHN2
(via olfactomedin-like domain). Interacts (via extracellular
domain) with UNC5B (via Ig domain). May also interact (via
extracellular domain) with UNC5A and UNC5C. Interacts (via
extracellular domain) with UNC5D (via extracellular domain).
Identified in complexes composed of FLRT3, ADGRL3 and UNC5B,
respectively FLRT3, ADGRL3 and UNC5D (By similarity). Interacts
(via cytoplasmic domain) with ROBO1 (By similarity).
{ECO:0000250|UniProtKB:Q8BGT1, ECO:0000250|UniProtKB:Q9NZU0,
ECO:0000269|PubMed:22405201}.
-!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:15485775,
ECO:0000269|PubMed:22405201}; Single-pass membrane protein
{ECO:0000250|UniProtKB:Q8BGT1}. Cell junction, synapse,
synaptosome {ECO:0000269|PubMed:22405201}. Cell junction, synapse,
postsynaptic cell membrane, postsynaptic density
{ECO:0000269|PubMed:22405201}. Cell projection, dendrite
{ECO:0000269|PubMed:22405201}. Cell junction, synapse
{ECO:0000269|PubMed:22405201}. Cell junction, synapse, presynaptic
cell membrane {ECO:0000269|PubMed:15485775}. Cell projection, axon
{ECO:0000269|PubMed:15485775}. Cytoplasmic vesicle
{ECO:0000269|PubMed:15485775}. Endoplasmic reticulum membrane
{ECO:0000250|UniProtKB:Q8BGT1}. Cell junction, focal adhesion
{ECO:0000250|UniProtKB:Q8BGT1}. Secreted
{ECO:0000250|UniProtKB:Q8BGT1}. Cell projection, axon
{ECO:0000250|UniProtKB:Q8BGT1}. Note=Detected on dendritic punctae
that colocalize in part with glutamaergic synapses, but not with
GABAergic synapses (PubMed:22405201). Detected on axons and at
axon termini (PubMed:15485775). Detected at neuronal growth cones.
Proteolytic cleavage in the juxtamembrane region gives rise to a
shedded ectodomain (By similarity). {ECO:0000250|UniProtKB:Q8BGT1,
ECO:0000269|PubMed:15485775, ECO:0000269|PubMed:22405201}.
-!- TISSUE SPECIFICITY: Detected in brain (at protein level)
(PubMed:22405201). Detected in brain neurons, especially in basal
ganglia, hippocampus dentate gyrus and CA3 region, cerebellum and
in olfactory bulb (PubMed:14706654, PubMed:15485775).
{ECO:0000269|PubMed:14706654, ECO:0000269|PubMed:15485775,
ECO:0000269|PubMed:22405201}.
-!- DEVELOPMENTAL STAGE: At 12 dpc, detected in the developing brain,
eye, lateral lip of the dermomyotome, somites and branchial arch.
{ECO:0000269|PubMed:15485775}.
-!- INDUCTION: Up-regulated in neurons in dorsal root ganglia in
response to peripheral nerve injury (at protein level)
(PubMed:15485775). Up-regulated in neurons in dorsal root ganglia
in response to peripheral nerve injury (PubMed:15485775).
{ECO:0000269|PubMed:15485775}.
-!- PTM: N-glycosylated. {ECO:0000250|UniProtKB:Q8BGT1}.
-!- PTM: Proteolytic cleavage in the juxtamembrane region gives rise
to a soluble ectodomain. Cleavage is probably effected by a
metalloprotease. {ECO:0000250|UniProtKB:Q8BGT1}.
-----------------------------------------------------------------------
Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
Distributed under the Creative Commons Attribution (CC BY 4.0) License
-----------------------------------------------------------------------
EMBL; CH473949; EDL80327.1; -; Genomic_DNA.
EMBL; BC160843; AAI60843.1; -; mRNA.
RefSeq; NP_001119763.1; NM_001126291.1.
UniGene; Rn.220263; -.
ProteinModelPortal; B1H234; -.
SMR; B1H234; -.
STRING; 10116.ENSRNOP00000006454; -.
iPTMnet; B1H234; -.
PhosphoSitePlus; B1H234; -.
PaxDb; B1H234; -.
PRIDE; B1H234; -.
GeneID; 366205; -.
KEGG; rno:366205; -.
UCSC; RGD:1566005; rat.
CTD; 23767; -.
RGD; 1566005; Flrt3.
eggNOG; ENOG410IIEA; Eukaryota.
eggNOG; COG4886; LUCA.
HOGENOM; HOG000290188; -.
HOVERGEN; HBG051629; -.
InParanoid; B1H234; -.
KO; K16362; -.
OrthoDB; EOG091G05YU; -.
PhylomeDB; B1H234; -.
TreeFam; TF331598; -.
PRO; PR:B1H234; -.
Proteomes; UP000002494; Unplaced.
Genevisible; B1H234; RN.
GO; GO:0043679; C:axon terminus; IDA:UniProtKB.
GO; GO:0044295; C:axonal growth cone; ISS:UniProtKB.
GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
GO; GO:0031410; C:cytoplasmic vesicle; IEA:UniProtKB-KW.
GO; GO:0030425; C:dendrite; IEA:UniProtKB-SubCell.
GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
GO; GO:0005925; C:focal adhesion; IEA:UniProtKB-SubCell.
GO; GO:0005887; C:integral component of plasma membrane; IDA:UniProtKB.
GO; GO:0099055; C:integral component of postsynaptic membrane; IDA:SynGO.
GO; GO:0014069; C:postsynaptic density; IDA:SynGO.
GO; GO:0042734; C:presynaptic membrane; IEA:UniProtKB-SubCell.
GO; GO:0097060; C:synaptic membrane; IDA:UniProtKB.
GO; GO:0004860; F:protein kinase inhibitor activity; IBA:GO_Central.
GO; GO:0007411; P:axon guidance; IGI:MGI.
GO; GO:0098742; P:cell-cell adhesion via plasma-membrane adhesion molecules; ISS:UniProtKB.
GO; GO:0019221; P:cytokine-mediated signaling pathway; IBA:GO_Central.
GO; GO:0048598; P:embryonic morphogenesis; ISS:UniProtKB.
GO; GO:0008543; P:fibroblast growth factor receptor signaling pathway; ISS:UniProtKB.
GO; GO:0060322; P:head development; ISS:UniProtKB.
GO; GO:0007507; P:heart development; ISS:UniProtKB.
GO; GO:0046426; P:negative regulation of JAK-STAT cascade; IBA:GO_Central.
GO; GO:0006469; P:negative regulation of protein kinase activity; IBA:GO_Central.
GO; GO:0031175; P:neuron projection development; IMP:UniProtKB.
GO; GO:1990138; P:neuron projection extension; IMP:UniProtKB.
GO; GO:0003345; P:proepicardium cell migration involved in pericardium morphogenesis; ISS:UniProtKB.
GO; GO:0048678; P:response to axon injury; IMP:UniProtKB.
GO; GO:0007416; P:synapse assembly; ISS:UniProtKB.
GO; GO:0050808; P:synapse organization; IMP:SynGO.
Gene3D; 3.80.10.10; -; 1.
InterPro; IPR000483; Cys-rich_flank_reg_C.
InterPro; IPR003961; FN3_dom.
InterPro; IPR001611; Leu-rich_rpt.
InterPro; IPR003591; Leu-rich_rpt_typical-subtyp.
InterPro; IPR032675; LRR_dom_sf.
InterPro; IPR000372; LRRNT.
Pfam; PF13855; LRR_8; 2.
SMART; SM00369; LRR_TYP; 7.
SMART; SM00082; LRRCT; 1.
SMART; SM00013; LRRNT; 1.
PROSITE; PS50853; FN3; 1.
PROSITE; PS51450; LRR; 8.
1: Evidence at protein level;
Cell adhesion; Cell junction; Cell membrane; Cell projection;
Complete proteome; Cytoplasmic vesicle; Developmental protein;
Disulfide bond; Endoplasmic reticulum; Glycoprotein;
Leucine-rich repeat; Membrane; Postsynaptic cell membrane;
Reference proteome; Repeat; Secreted; Signal; Synapse; Synaptosome;
Transmembrane; Transmembrane helix.
SIGNAL 1 28 {ECO:0000255}.
CHAIN 29 649 Leucine-rich repeat transmembrane protein
FLRT3.
/FTId=PRO_0000352675.
TOPO_DOM 29 528 Extracellular. {ECO:0000255}.
TRANSMEM 529 549 Helical. {ECO:0000255}.
TOPO_DOM 550 649 Cytoplasmic. {ECO:0000255}.
DOMAIN 29 58 LRRNT. {ECO:0000255}.
REPEAT 59 80 LRR 1. {ECO:0000255}.
REPEAT 84 104 LRR 2. {ECO:0000255}.
REPEAT 105 126 LRR 3. {ECO:0000255}.
REPEAT 129 150 LRR 4. {ECO:0000255}.
REPEAT 155 176 LRR 5. {ECO:0000255}.
REPEAT 177 197 LRR 6. {ECO:0000255}.
REPEAT 200 220 LRR 7. {ECO:0000255}.
REPEAT 226 247 LRR 8. {ECO:0000255}.
REPEAT 248 269 LRR 9. {ECO:0000255}.
REPEAT 272 293 LRR 10. {ECO:0000255}.
DOMAIN 305 357 LRRCT. {ECO:0000255}.
DOMAIN 405 504 Fibronectin type-III.
{ECO:0000255|PROSITE-ProRule:PRU00316}.
REGION 38 67 Interaction with ADGRL3.
{ECO:0000250|UniProtKB:Q9NZU0}.
CARBOHYD 226 226 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 282 282 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 296 296 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 31 37 {ECO:0000250|UniProtKB:Q8BGT1}.
DISULFID 35 44 {ECO:0000250|UniProtKB:Q8BGT1}.
DISULFID 309 334 {ECO:0000250|UniProtKB:Q8BGT1}.
SEQUENCE 649 AA; 72911 MW; 15DF42A55DD1F12C CRC64;
MISPAWSLFL IGTKIGLFFQ VAPLSVMAKS CPSVCRCDAG FIYCNDRSLT SIPVGIPEDA
TTLYLQNNQI NNVGIPSDLK NLLKVQRIYL YHNSLDEFPT NLPKYVKELH LQENNIRTIT
YDSLSKIPYL EELHLDDNSV SAVSIEEGAF RDSNYLRLLF LSRNHLSTIP GGLPRTIEEL
RLDDNRISTI SSPSLHGLTS LKRLVLDGNL LNNHGLGDKV FFNLVNLTEL SLVRNSLTAA
PVNLPGTSLR KLYLQDNHIN RVPPNAFSYL RQLYRLDMSN NNLSNLPQGI FDDLDNITQL
ILRNNPWYCG CKMKWVRDWL QSLPVKVNVR GLMCQAPEKV RGMAIKDLSA ELFDCKDSGI
VSTVQITTAI PNTAYPAQGQ WPAPVTKQPD IKNPKLTKDQ RTTGSPSRKT ILITVKSVTP
DTIHISWRLA LPMTALRLSW LKLGHSPAFG SITETIVTGE RSEYLVTALE PESPYRVCMV
PMETSNLYLF DETPVCIETQ TAPLRMYNPT TTLNREQEKE PYKNPNLPLA AIIGGAVALV
SIALLALVCW YVHRNGSLFS RNCAYSKGRR RKDDYAEAGT KKDNSILEIR ETSFQMLPIS
NEPISKEEFV IHTIFPPNGM NLYKNNLSES SSNRSYRDSG IPDLDHSHS


Related products :

Catalog number Product name Quantity
CA47 Human Leucine-Rich Repeat Transmembrane Protein FLRT3 FLRT3 50
CSB-EL008731RA Rat Leucine-rich repeat transmembrane protein FLRT3(FLRT3) ELISA kit 96T
C486 Human Leucine-Rich Repeat Transmembrane Protein FLRT3 FLRT3 l0
C970 Leucine-Rich Repeat Transmembrane Protein FLRT3 FLRT3 lmg
C970 Leucine-Rich Repeat Transmembrane Protein FLRT3 FLRT3 500
CSB-EL008731HU Human Leucine-rich repeat transmembrane protein FLRT3(FLRT3) ELISA kit 96T
CSB-EL008731RA Rat Leucine-rich repeat transmembrane protein FLRT3(FLRT3) ELISA kit SpeciesRat 96T
C970 Recombinant Human Leucine-Rich Repeat Transmembrane Protein FLRT3 per FLRT3 (C-6His) 10ug
CSB-EL008731HU Human Leucine-rich repeat transmembrane protein FLRT3(FLRT3) ELISA kit SpeciesHuman 96T
FLT3 FLRT3 Gene fibronectin leucine rich transmembrane protein 3
FLRT3 FLRT1 Gene fibronectin leucine rich transmembrane protein 1
FLRT3_HUMAN Human ELISA Kit FOR Leucine-rich repeat transmembrane protein FLRT3 96T
CSB-EL008731RA Rat fibronectin leucine rich transmembrane protein 3 (FLRT3) ELISA kit, Species Rat, Sample Type serum, plasma 96T
CSB-EL008731HU Human fibronectin leucine rich transmembrane protein 3 (FLRT3) ELISA kit, Species Human, Sample Type serum, plasma 96T
E1501b Mouse ELISA Kit FOR Leucine-rich repeat and transmembrane domain-containing protein 1 96T
CSB-EL013194HU Human Leucine-rich repeat and transmembrane domain-containing protein 2(LRTM2) ELISA kit 96T
CSB-EL013193HU Human Leucine-rich repeat and transmembrane domain-containing protein 1(LRTM1) ELISA kit 96T
CSB-EL013193MO Mouse Leucine-rich repeat and transmembrane domain-containing protein 1(LRTM1) ELISA kit 96T
CSB-EL013194MO Mouse Leucine-rich repeat and transmembrane domain-containing protein 2(LRTM2) ELISA kit 96T
CSB-EL013087RA Rat Leucine-rich repeat, immunoglobulin-like domain and transmembrane domain-containing protein 1(LRIT1) ELISA kit 96T
E0567r Mouse ELISA Kit FOR Leucine-rich repeat, immunoglobulin-like domain and transmembrane domain-containing protein 2 96T
LURA1_RAT Mouse ELISA Kit FOR Leucine-rich repeat, immunoglobulin-like domain and transmembrane domain-containing protein 2 96T
E0517p Mouse ELISA Kit FOR Leucine-rich repeat, immunoglobulin-like domain and transmembrane domain-containing protein 1 96T
PAX8_RAT Mouse ELISA Kit FOR Leucine-rich repeat, immunoglobulin-like domain and transmembrane domain-containing protein 1 96T
CSB-EL013194MO Mouse Leucine-rich repeat and transmembrane domain-containing protein 2(LRTM2) ELISA kit SpeciesMouse 96T


 

GENTAUR Belgium BVBA BE0473327336
Voortstraat 49, 1910 Kampenhout BELGIUM
Tel 0032 16 58 90 45

Fax 0032 16 50 90 45
info@gentaur.com | Gentaur





GENTAUR Ltd.
Howard Frank Turnberry House
1404-1410 High Road
Whetstone London N20 9BH
Tel 020 3393 8531 Fax 020 8445 9411
uk@gentaur.com | Gentaur

 

 




GENTAUR France SARL
9, rue Lagrange, 75005 Paris
Tel 01 43 25 01 50

Fax 01 43 25 01 60
RCS Paris B 484 237 888

SIRET 48423788800017

BNP PARIBAS PARIS PL MAUBERT BIC BNPAFRPPPRG

france@gentaur.com | Gentaur

GENTAUR GmbH
Marienbongard 20
52062 Aachen Deutschland
Support Karolina Elandt
Tel: 0035929830070
Fax: (+49) 241 56 00 47 88

Logistic :0241 40 08 90 86
Bankleitzahl 39050000
IBAN lautet DE8839050000107569353
Handelsregister Aachen HR B 16058
Umsatzsteuer-Identifikationsnummer *** DE 815175831
Steuernummer 201/5961/3925
de@gentaur.com | Gentaur

GENTAUR U.S.A
Genprice Inc, Logistics
547, Yurok Circle
San Jose, CA 95123
CA 95123
Tel (408) 780-0908,
Fax (408) 780-0908,
sales@genprice.com

Genprice Inc, Invoices and accounting
6017 Snell Ave, Ste 357
San Jose, CA 95123




GENTAUR Nederland BV
NL850396268B01 KVK nummer 52327027
Kuiper 1
5521 DG Eersel Nederland
Tel:  0208-080893  Fax: 0497-517897
nl@gentaur.com | Gentaur
IBAN: NL04 RABO 0156 9854 62   SWIFT RABONL2U






GENTAUR Spain
tel:0911876558
spain@gentaur.com | Gentaur






ГЕНТАУЪР БЪЛГАРИЯ
ID # 201 358 931 /BULSTAT
София 1000, ул. "Граф Игнатиев" 53 вх. В, ет. 2
Tel 0035924682280 Fax 0035924808322
e-mail: Sofia@gentaur.com | Gentaur
IBAN: BG11FINV91501014771636
BIC: FINVBGSF

GENTAUR Poland Sp. z o.o.


ul. Grunwaldzka 88/A m.2
81-771 Sopot, Poland
TEL Gdansk 058 710 33 44 FAX  058 710 33 48              

poland@gentaur.com | Gentaur

Other countries

Österreich +43720880899

Canada Montreal +15149077481

Ceská republika Praha +420246019719

Danmark +4569918806

Finland Helsset +358942419041

Magyarország Budapest +3619980547

Ireland Dublin+35316526556

Luxembourg+35220880274

Norge Oslo+4721031366

Sverige Stockholm+46852503438

Schweiz Züri+41435006251

US New York+17185132983

GENTAUR Italy
SRL IVA IT03841300167
Piazza Giacomo Matteotti, 6
24122 Bergamo Tel 02 36 00 65 93
Fax 02 36 00 65 94
italia@gentaur.com | Gentaur