FLRT3_CHICK
ID FLRT3_CHICK Reviewed; 647 AA.
AC F1NUK7;
DT 14-OCT-2015, integrated into UniProtKB/Swiss-Prot.
DT 26-JUN-2013, sequence version 2.
DT 03-AUG-2022, entry version 71.
DE RecName: Full=Leucine-rich repeat transmembrane protein FLRT3;
DE AltName: Full=Fibronectin-like domain-containing leucine-rich transmembrane protein 3;
DE Flags: Precursor;
GN Name=FLRT3 {ECO:0000312|Ensembl:ENSGALP00000014168};
OS Gallus gallus (Chicken).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC Phasianinae; Gallus.
OX NCBI_TaxID=9031 {ECO:0000312|Ensembl:ENSGALP00000014168};
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Red jungle fowl;
RX PubMed=15592404; DOI=10.1038/nature03154;
RA Hillier L.W., Miller W., Birney E., Warren W., Hardison R.C., Ponting C.P.,
RA Bork P., Burt D.W., Groenen M.A.M., Delany M.E., Dodgson J.B.,
RA Chinwalla A.T., Cliften P.F., Clifton S.W., Delehaunty K.D., Fronick C.,
RA Fulton R.S., Graves T.A., Kremitzki C., Layman D., Magrini V.,
RA McPherson J.D., Miner T.L., Minx P., Nash W.E., Nhan M.N., Nelson J.O.,
RA Oddy L.G., Pohl C.S., Randall-Maher J., Smith S.M., Wallis J.W.,
RA Yang S.-P., Romanov M.N., Rondelli C.M., Paton B., Smith J., Morrice D.,
RA Daniels L., Tempest H.G., Robertson L., Masabanda J.S., Griffin D.K.,
RA Vignal A., Fillon V., Jacobbson L., Kerje S., Andersson L.,
RA Crooijmans R.P., Aerts J., van der Poel J.J., Ellegren H., Caldwell R.B.,
RA Hubbard S.J., Grafham D.V., Kierzek A.M., McLaren S.R., Overton I.M.,
RA Arakawa H., Beattie K.J., Bezzubov Y., Boardman P.E., Bonfield J.K.,
RA Croning M.D.R., Davies R.M., Francis M.D., Humphray S.J., Scott C.E.,
RA Taylor R.G., Tickle C., Brown W.R.A., Rogers J., Buerstedde J.-M.,
RA Wilson S.A., Stubbs L., Ovcharenko I., Gordon L., Lucas S., Miller M.M.,
RA Inoko H., Shiina T., Kaufman J., Salomonsen J., Skjoedt K., Wong G.K.-S.,
RA Wang J., Liu B., Wang J., Yu J., Yang H., Nefedov M., Koriabine M.,
RA Dejong P.J., Goodstadt L., Webber C., Dickens N.J., Letunic I., Suyama M.,
RA Torrents D., von Mering C., Zdobnov E.M., Makova K., Nekrutenko A.,
RA Elnitski L., Eswara P., King D.C., Yang S.-P., Tyekucheva S.,
RA Radakrishnan A., Harris R.S., Chiaromonte F., Taylor J., He J.,
RA Rijnkels M., Griffiths-Jones S., Ureta-Vidal A., Hoffman M.M., Severin J.,
RA Searle S.M.J., Law A.S., Speed D., Waddington D., Cheng Z., Tuzun E.,
RA Eichler E., Bao Z., Flicek P., Shteynberg D.D., Brent M.R., Bye J.M.,
RA Huckle E.J., Chatterji S., Dewey C., Pachter L., Kouranov A.,
RA Mourelatos Z., Hatzigeorgiou A.G., Paterson A.H., Ivarie R., Brandstrom M.,
RA Axelsson E., Backstrom N., Berlin S., Webster M.T., Pourquie O.,
RA Reymond A., Ucla C., Antonarakis S.E., Long M., Emerson J.J., Betran E.,
RA Dupanloup I., Kaessmann H., Hinrichs A.S., Bejerano G., Furey T.S.,
RA Harte R.A., Raney B., Siepel A., Kent W.J., Haussler D., Eyras E.,
RA Castelo R., Abril J.F., Castellano S., Camara F., Parra G., Guigo R.,
RA Bourque G., Tesler G., Pevzner P.A., Smit A., Fulton L.A., Mardis E.R.,
RA Wilson R.K.;
RT "Sequence and comparative analysis of the chicken genome provide unique
RT perspectives on vertebrate evolution.";
RL Nature 432:695-716(2004).
RN [2]
RP FUNCTION, AND DEVELOPMENTAL STAGE.
RX PubMed=21575622; DOI=10.1016/j.ydbio.2011.04.031;
RA Tomas A.R., Certal A.C., Rodriguez-Leon J.;
RT "FLRT3 as a key player on chick limb development.";
RL Dev. Biol. 355:324-333(2011).
CC -!- FUNCTION: Modulates the structure and function of the apical ectodermal
CC ridge (AER) that controls embryonic limb development (PubMed:21575622).
CC Functions in cell-cell adhesion, cell migration and axon guidance,
CC exerting an attractive or repulsive role depending on its interaction
CC partners. Plays a role in the spatial organization of brain neurons.
CC Plays a role in vascular development. Plays a role in cell-cell
CC adhesion via its interaction with latrophilins that are expressed at
CC the surface of adjacent cells. Mediates axon attraction towards cells
CC expressing NTN1. Mediates axon growth cone collapse and plays a
CC repulsive role in neuron guidance via its interaction with UNC-5 family
CC members. Plays a role in the regulation of the density of glutamaergic
CC synapses. Plays a role in fibroblast growth factor-mediated signaling
CC cascades. Required for normal morphogenesis during embryonic
CC development, but not for normal embryonic patterning (By similarity).
CC {ECO:0000250|UniProtKB:Q8BGT1, ECO:0000269|PubMed:21575622}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q8BGT1};
CC Single-pass membrane protein {ECO:0000250|UniProtKB:Q8BGT1}.
CC Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:Q8BGT1}. Cell
CC junction, focal adhesion {ECO:0000250|UniProtKB:Q8BGT1}. Secreted
CC {ECO:0000250|UniProtKB:Q8BGT1}. Cell projection, axon
CC {ECO:0000250|UniProtKB:Q8BGT1}. Cell projection, growth cone membrane
CC {ECO:0000250|UniProtKB:Q8BGT1}. Note=Detected on dendritic punctae that
CC colocalize in part with glutamaergic synapses, but not with GABAergic
CC synapses. Proteolytic cleavage in the juxtamembrane region gives rise
CC to a shedded ectodomain. {ECO:0000250|UniProtKB:B1H234,
CC ECO:0000250|UniProtKB:Q8BGT1}.
CC -!- DEVELOPMENTAL STAGE: Detected in distal ectodermal cells at Hamburger
CC Hamilton stage 18 (18HH). Becomes restricted to the apical ectodermal
CC ridge (AER) (at protein level). At stage 11HH, detected in neural
CC ectoderm, developing optic placodes, the neural crest around the otic
CC placodes, and along the anterior-posterior axis in somites. Detected in
CC the ectoderm of the limb bud at 16HH to 18HH. Becomes restricted to the
CC dermomyotome closer to the neural tube at stage 18HH. At 19HH and 23HH,
CC detected in the apical ectodermal ridge, the developing eye and
CC branchial arches. {ECO:0000269|PubMed:21575622}.
CC -!- PTM: N-glycosylated. {ECO:0000250|UniProtKB:Q8BGT1}.
CC -!- PTM: Proteolytic cleavage in the juxtamembrane region gives rise to a
CC soluble ectodomain. Cleavage is probably effected by a metalloprotease.
CC {ECO:0000250|UniProtKB:Q8BGT1}.
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DR EMBL; AADN03003311; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; XP_015138909.1; XM_015283423.1.
DR AlphaFoldDB; F1NUK7; -.
DR SMR; F1NUK7; -.
DR STRING; 9031.ENSGALP00000014168; -.
DR PaxDb; F1NUK7; -.
DR Ensembl; ENSGALT00000014184; ENSGALP00000014168; ENSGALG00000008716.
DR GeneID; 428552; -.
DR KEGG; gga:428552; -.
DR CTD; 23767; -.
DR VEuPathDB; HostDB:geneid_428552; -.
DR eggNOG; ENOG502QQBZ; Eukaryota.
DR GeneTree; ENSGT00940000159704; -.
DR HOGENOM; CLU_027624_0_0_1; -.
DR InParanoid; F1NUK7; -.
DR OMA; LIWTKIG; -.
DR OrthoDB; 826997at2759; -.
DR PhylomeDB; F1NUK7; -.
DR TreeFam; TF331598; -.
DR PRO; PR:F1NUK7; -.
DR Proteomes; UP000000539; Chromosome 3.
DR Bgee; ENSGALG00000008716; Expressed in lung and 11 other tissues.
DR GO; GO:0043679; C:axon terminus; ISS:UniProtKB.
DR GO; GO:0044295; C:axonal growth cone; ISS:UniProtKB.
DR GO; GO:0005911; C:cell-cell junction; IEA:Ensembl.
DR GO; GO:0005829; C:cytosol; IEA:Ensembl.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR GO; GO:0005925; C:focal adhesion; IEA:UniProtKB-SubCell.
DR GO; GO:0098978; C:glutamatergic synapse; IEA:Ensembl.
DR GO; GO:0032584; C:growth cone membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005887; C:integral component of plasma membrane; ISS:UniProtKB.
DR GO; GO:0099055; C:integral component of postsynaptic membrane; IEA:Ensembl.
DR GO; GO:0097060; C:synaptic membrane; ISS:UniProtKB.
DR GO; GO:0045499; F:chemorepellent activity; IEA:Ensembl.
DR GO; GO:0005104; F:fibroblast growth factor receptor binding; IEA:Ensembl.
DR GO; GO:0042803; F:protein homodimerization activity; IEA:Ensembl.
DR GO; GO:0007411; P:axon guidance; IEA:Ensembl.
DR GO; GO:0098742; P:cell-cell adhesion via plasma-membrane adhesion molecules; ISS:UniProtKB.
DR GO; GO:0048598; P:embryonic morphogenesis; ISS:UniProtKB.
DR GO; GO:0008543; P:fibroblast growth factor receptor signaling pathway; ISS:UniProtKB.
DR GO; GO:0060322; P:head development; ISS:UniProtKB.
DR GO; GO:0007507; P:heart development; ISS:UniProtKB.
DR GO; GO:0031175; P:neuron projection development; ISS:UniProtKB.
DR GO; GO:1990138; P:neuron projection extension; ISS:UniProtKB.
DR GO; GO:0051965; P:positive regulation of synapse assembly; IEA:Ensembl.
DR GO; GO:0003345; P:proepicardium cell migration involved in pericardium morphogenesis; ISS:UniProtKB.
DR GO; GO:0048678; P:response to axon injury; ISS:UniProtKB.
DR GO; GO:0007416; P:synapse assembly; ISS:UniProtKB.
DR GO; GO:0099560; P:synaptic membrane adhesion; IEA:Ensembl.
DR Gene3D; 3.80.10.10; -; 1.
DR InterPro; IPR000483; Cys-rich_flank_reg_C.
DR InterPro; IPR003961; FN3_dom.
DR InterPro; IPR001611; Leu-rich_rpt.
DR InterPro; IPR003591; Leu-rich_rpt_typical-subtyp.
DR InterPro; IPR032675; LRR_dom_sf.
DR InterPro; IPR000372; LRRNT.
DR Pfam; PF13855; LRR_8; 2.
DR SMART; SM00369; LRR_TYP; 7.
DR SMART; SM00082; LRRCT; 1.
DR SMART; SM00013; LRRNT; 1.
DR PROSITE; PS50853; FN3; 1.
DR PROSITE; PS51450; LRR; 8.
PE 1: Evidence at protein level;
KW Cell adhesion; Cell junction; Cell membrane; Cell projection;
KW Developmental protein; Disulfide bond; Endoplasmic reticulum; Glycoprotein;
KW Leucine-rich repeat; Membrane; Reference proteome; Repeat; Secreted;
KW Signal; Transmembrane; Transmembrane helix.
FT SIGNAL 1..28
FT /evidence="ECO:0000255"
FT CHAIN 29..647
FT /note="Leucine-rich repeat transmembrane protein FLRT3"
FT /id="PRO_0000434518"
FT TOPO_DOM 29..526
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 527..547
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 548..647
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT DOMAIN 30..62
FT /note="LRRNT"
FT /evidence="ECO:0000255"
FT REPEAT 58..82
FT /note="LRR 1"
FT /evidence="ECO:0000255"
FT REPEAT 83..105
FT /note="LRR 2"
FT /evidence="ECO:0000255"
FT REPEAT 107..126
FT /note="LRR 3"
FT /evidence="ECO:0000255"
FT REPEAT 127..152
FT /note="LRR 4"
FT /evidence="ECO:0000255"
FT REPEAT 154..179
FT /note="LRR 5"
FT /evidence="ECO:0000255"
FT REPEAT 181..197
FT /note="LRR 6"
FT /evidence="ECO:0000255"
FT REPEAT 198..223
FT /note="LRR 7"
FT /evidence="ECO:0000255"
FT REPEAT 225..246
FT /note="LRR 8"
FT /evidence="ECO:0000255"
FT REPEAT 247..269
FT /note="LRR 9"
FT /evidence="ECO:0000255"
FT REPEAT 270..293
FT /note="LRR 10"
FT /evidence="ECO:0000255"
FT DOMAIN 305..356
FT /note="LRRCT"
FT /evidence="ECO:0000255"
FT DOMAIN 404..502
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT REGION 620..647
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 620..636
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 226
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT DISULFID 31..37
FT /evidence="ECO:0000250|UniProtKB:Q9NZU0"
FT DISULFID 35..44
FT /evidence="ECO:0000250|UniProtKB:Q9NZU0"
FT DISULFID 309..334
FT /evidence="ECO:0000250|UniProtKB:Q9NZU0"
SQ 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
