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

 FLRT3_CHICK             Reviewed;         647 AA.
F1NUK7;
14-OCT-2015, integrated into UniProtKB/Swiss-Prot.
26-JUN-2013, sequence version 2.
28-FEB-2018, entry version 51.
RecName: Full=Leucine-rich repeat transmembrane protein FLRT3;
AltName: Full=Fibronectin-like domain-containing leucine-rich transmembrane protein 3;
Flags: Precursor;
Name=FLRT3 {ECO:0000312|Ensembl:ENSGALP00000014168};
Gallus gallus (Chicken).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes;
Phasianidae; Phasianinae; Gallus.
NCBI_TaxID=9031 {ECO:0000312|Ensembl:ENSGALP00000014168};
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=Red jungle fowl;
PubMed=15592404; DOI=10.1038/nature03154;
Hillier L.W., Miller W., Birney E., Warren W., Hardison R.C.,
Ponting C.P., Bork P., Burt D.W., Groenen M.A.M., Delany M.E.,
Dodgson J.B., Chinwalla A.T., Cliften P.F., Clifton S.W.,
Delehaunty K.D., Fronick C., Fulton R.S., Graves T.A., Kremitzki C.,
Layman D., Magrini V., McPherson J.D., Miner T.L., Minx P., Nash W.E.,
Nhan M.N., Nelson J.O., Oddy L.G., Pohl C.S., Randall-Maher J.,
Smith S.M., Wallis J.W., Yang S.-P., Romanov M.N., Rondelli C.M.,
Paton B., Smith J., Morrice D., Daniels L., Tempest H.G.,
Robertson L., Masabanda J.S., Griffin D.K., Vignal A., Fillon V.,
Jacobbson L., Kerje S., Andersson L., Crooijmans R.P., Aerts J.,
van der Poel J.J., Ellegren H., Caldwell R.B., Hubbard S.J.,
Grafham D.V., Kierzek A.M., McLaren S.R., Overton I.M., Arakawa H.,
Beattie K.J., Bezzubov Y., Boardman P.E., Bonfield J.K.,
Croning M.D.R., Davies R.M., Francis M.D., Humphray S.J., Scott C.E.,
Taylor R.G., Tickle C., Brown W.R.A., Rogers J., Buerstedde J.-M.,
Wilson S.A., Stubbs L., Ovcharenko I., Gordon L., Lucas S.,
Miller M.M., Inoko H., Shiina T., Kaufman J., Salomonsen J.,
Skjoedt K., Wong G.K.-S., Wang J., Liu B., Wang J., Yu J., Yang H.,
Nefedov M., Koriabine M., Dejong P.J., Goodstadt L., Webber C.,
Dickens N.J., Letunic I., Suyama M., Torrents D., von Mering C.,
Zdobnov E.M., Makova K., Nekrutenko A., Elnitski L., Eswara P.,
King D.C., Yang S.-P., Tyekucheva S., Radakrishnan A., Harris R.S.,
Chiaromonte F., Taylor J., He J., Rijnkels M., Griffiths-Jones S.,
Ureta-Vidal A., Hoffman M.M., Severin J., Searle S.M.J., Law A.S.,
Speed D., Waddington D., Cheng Z., Tuzun E., Eichler E., Bao Z.,
Flicek P., Shteynberg D.D., Brent M.R., Bye J.M., Huckle E.J.,
Chatterji S., Dewey C., Pachter L., Kouranov A., Mourelatos Z.,
Hatzigeorgiou A.G., Paterson A.H., Ivarie R., Brandstrom M.,
Axelsson E., Backstrom N., Berlin S., Webster M.T., Pourquie O.,
Reymond A., Ucla C., Antonarakis S.E., Long M., Emerson J.J.,
Betran E., Dupanloup I., Kaessmann H., Hinrichs A.S., Bejerano G.,
Furey T.S., Harte R.A., Raney B., Siepel A., Kent W.J., Haussler D.,
Eyras E., Castelo R., Abril J.F., Castellano S., Camara F., Parra G.,
Guigo R., Bourque G., Tesler G., Pevzner P.A., Smit A., Fulton L.A.,
Mardis E.R., Wilson R.K.;
"Sequence and comparative analysis of the chicken genome provide
unique perspectives on vertebrate evolution.";
Nature 432:695-716(2004).
[2]
FUNCTION, AND DEVELOPMENTAL STAGE.
PubMed=21575622; DOI=10.1016/j.ydbio.2011.04.031;
Tomas A.R., Certal A.C., Rodriguez-Leon J.;
"FLRT3 as a key player on chick limb development.";
Dev. Biol. 355:324-333(2011).
-!- FUNCTION: Modulates the structure and function of the apical
ectodermal ridge (AER) that controls embryonic limb development
(PubMed:21575622). 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. Plays a role in cell-cell adhesion via its
interaction with latrophilins that are expressed at the surface of
adjacent cells. Mediates axon attraction towards cells expressing
NTN1. Mediates axon growth cone collapse and plays a repulsive
role in neuron guidance via its interaction with UNC-5 family
members. Plays a role in the regulation of the density of
glutamaergic synapses. Plays a role in fibroblast growth factor-
mediated signaling cascades. Required for normal morphogenesis
during embryonic development, but not for normal embryonic
patterning (By similarity). {ECO:0000250|UniProtKB:Q8BGT1,
ECO:0000269|PubMed:21575622}.
-!- SUBCELLULAR LOCATION: Cell membrane
{ECO:0000250|UniProtKB:Q8BGT1}; Single-pass membrane protein
{ECO:0000250|UniProtKB:Q8BGT1}. 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 at neuronal growth
cones. Proteolytic cleavage in the juxtamembrane region gives rise
to a shedded ectodomain. {ECO:0000250|UniProtKB:Q8BGT1}.
-!- DEVELOPMENTAL STAGE: Detected in distal ectodermal cells at
Hamburger Hamilton stage 18 (18HH). Becomes restricted to the
apical ectodermal ridge (AER) (at protein level). At stage 11HH,
detected in neural ectoderm, developing optic placodes, the neural
crest around the otic placodes, and along the anterior-posterior
axis in somites. Detected in the ectoderm of the limb bud at 16HH
to 18HH. Becomes restricted to the dermomyotome closer to the
neural tube at stage 18HH. At 19HH and 23HH, detected in the
apical ectodermal ridge, the developing eye and branchial arches.
{ECO:0000269|PubMed:21575622}.
-!- 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}.
-----------------------------------------------------------------------
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EMBL; AADN03003311; -; NOT_ANNOTATED_CDS; Genomic_DNA.
RefSeq; XP_015138909.1; XM_015283423.1.
UniGene; Gga.50441; -.
SMR; F1NUK7; -.
STRING; 9031.ENSGALP00000014168; -.
PaxDb; F1NUK7; -.
Ensembl; ENSGALT00000014184; ENSGALP00000014168; ENSGALG00000008716.
GeneID; 428552; -.
KEGG; gga:428552; -.
CTD; 23767; -.
eggNOG; ENOG410IIEA; Eukaryota.
eggNOG; COG4886; LUCA.
GeneTree; ENSGT00760000118969; -.
InParanoid; F1NUK7; -.
KO; K16362; -.
OMA; SPYRVCM; -.
OrthoDB; EOG091G05YU; -.
PhylomeDB; F1NUK7; -.
TreeFam; TF331598; -.
Reactome; R-GGA-5654687; Downstream signaling of activated FGFR1.
PRO; PR:F1NUK7; -.
Proteomes; UP000000539; Chromosome 3.
Bgee; ENSGALG00000008716; -.
GO; GO:0043679; C:axon terminus; ISS:UniProtKB.
GO; GO:0044295; C:axonal growth cone; ISS:UniProtKB.
GO; GO:0005911; C:cell-cell junction; IEA:Ensembl.
GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
GO; GO:0005829; C:cytosol; IEA:Ensembl.
GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
GO; GO:0005615; C:extracellular space; IEA:Ensembl.
GO; GO:0005925; C:focal adhesion; IEA:UniProtKB-SubCell.
GO; GO:0005887; C:integral component of plasma membrane; ISS:UniProtKB.
GO; GO:0097060; C:synaptic membrane; ISS:UniProtKB.
GO; GO:0045499; F:chemorepellent activity; IEA:Ensembl.
GO; GO:0005104; F:fibroblast growth factor receptor binding; IEA:Ensembl.
GO; GO:0042803; F:protein homodimerization activity; IEA:Ensembl.
GO; GO:0004860; F:protein kinase inhibitor activity; IBA:GO_Central.
GO; GO:0007411; P:axon guidance; IEA:Ensembl.
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; ISS:UniProtKB.
GO; GO:1990138; P:neuron projection extension; ISS:UniProtKB.
GO; GO:0051965; P:positive regulation of synapse assembly; IEA:Ensembl.
GO; GO:0003345; P:proepicardium cell migration involved in pericardium morphogenesis; ISS:UniProtKB.
GO; GO:0048678; P:response to axon injury; ISS:UniProtKB.
GO; GO:0007416; P:synapse assembly; ISS:UniProtKB.
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; Developmental protein; Disulfide bond;
Endoplasmic reticulum; Glycoprotein; Leucine-rich repeat; Membrane;
Reference proteome; Repeat; Secreted; Signal; Transmembrane;
Transmembrane helix.
SIGNAL 1 28 {ECO:0000255}.
CHAIN 29 647 Leucine-rich repeat transmembrane protein
FLRT3.
/FTId=PRO_0000434518.
TOPO_DOM 29 526 Extracellular. {ECO:0000305}.
TRANSMEM 527 547 Helical. {ECO:0000255}.
TOPO_DOM 548 647 Cytoplasmic. {ECO:0000305}.
DOMAIN 30 62 LRRNT. {ECO:0000255}.
REPEAT 58 82 LRR 1. {ECO:0000255}.
REPEAT 83 105 LRR 2. {ECO:0000255}.
REPEAT 107 126 LRR 3. {ECO:0000255}.
REPEAT 127 152 LRR 4. {ECO:0000255}.
REPEAT 154 179 LRR 5. {ECO:0000255}.
REPEAT 181 197 LRR 6. {ECO:0000255}.
REPEAT 198 223 LRR 7. {ECO:0000255}.
REPEAT 225 246 LRR 8. {ECO:0000255}.
REPEAT 247 269 LRR 9. {ECO:0000255}.
REPEAT 270 293 LRR 10. {ECO:0000255}.
DOMAIN 305 356 LRRCT. {ECO:0000255}.
DOMAIN 404 502 Fibronectin type-III.
{ECO:0000255|PROSITE-ProRule:PRU00316}.
CARBOHYD 226 226 N-linked (GlcNAc...) asparagine.
{ECO:0000255|PROSITE-ProRule:PRU00498}.
DISULFID 31 37 {ECO:0000250|UniProtKB:Q9NZU0}.
DISULFID 35 44 {ECO:0000250|UniProtKB:Q9NZU0}.
DISULFID 309 334 {ECO:0000250|UniProtKB:Q9NZU0}.
SEQUENCE 647 AA; 73292 MW; DB00547703A78321 CRC64;
MITVPWSVFL IWTKIGLLLD MAPYSVAAKP CPSVCRCDVG FIYCNDRDLT SIPTGIPEDA
TNLFLQNNQI NNAGIPSELK NLRRVERIFL YHNSLDEFPT NLPKYVKELH LQENNIRTIT
YDSLSQIPYL EELHLDDNSV SAVSIEDGAF RDNIYLRLLF LSRNHLSTIP WGLPKTIEEL
RLDDNRISTI SELSLQDLTN LKRLVLDGNL LNNHGLGDKV FMNLVNLTEL SLVRNSLTAA
PVNLPGTNLR KLYLQENHIN HVPPNAFSYL RQLYRLDMSN NNLSNLPQGV FDDLDNITQL
FLRNNPWHCG CKMKWVRDWL QSLPLKVNVR GLMCQAPEKV RGMAIKDLNA ELFDCKDDMS
TIQITTAVPN TLYPAQGHWP VSVTKQPDIK TPNLNKNYRT TASPVRKIIT IFVKSVSTET
IHISWKVALP MTALRLSWLK MGHSPAFGSI TETIVTGDRS DYLLTALEPE SPYRVCMVPM
ETSNIYLSDE TPECIETETA PLKMYNPTTT LNREQEKEPY KNSSVPLAAI IGGAVALVAL
ALLALVCWYV HRNGALFSRH CAYSKGRRRK DDYAEAGTKK DNSILEIRET SFQMIPITND
QVSKEEFVIH TIFPPNGMNL YKNSHSESSS NRSYRDSGIP DSDHSHS


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