FLRT2_RAT
ID FLRT2_RAT Reviewed; 660 AA.
AC D3ZTV3;
DT 14-OCT-2015, integrated into UniProtKB/Swiss-Prot.
DT 20-APR-2010, sequence version 1.
DT 03-AUG-2022, entry version 91.
DE RecName: Full=Leucine-rich repeat transmembrane protein FLRT2 {ECO:0000305};
DE AltName: Full=Fibronectin-like domain-containing leucine-rich transmembrane protein 2 {ECO:0000305};
DE Flags: Precursor;
GN Name=Flrt2 {ECO:0000312|RGD:1308574};
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116 {ECO:0000312|Proteomes:UP000002494};
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Brown Norway;
RX PubMed=15057822; DOI=10.1038/nature02426;
RA Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J.,
RA Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G.,
RA Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G.,
RA Morgan M., Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G.,
RA Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S.,
RA Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T.,
RA Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T., Smith D.,
RA Lee H.-M., Gustafson E., Cahill P., Kana A., Doucette-Stamm L.,
RA Weinstock K., Fechtel K., Weiss R.B., Dunn D.M., Green E.D.,
RA Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K., Zhu B., Marra M.,
RA Schein J., Bosdet I., Fjell C., Jones S., Krzywinski M., Mathewson C.,
RA Siddiqui A., Wye N., McPherson J., Zhao S., Fraser C.M., Shetty J.,
RA Shatsman S., Geer K., Chen Y., Abramzon S., Nierman W.C., Havlak P.H.,
RA Chen R., Durbin K.J., Egan A., Ren Y., Song X.-Z., Li B., Liu Y., Qin X.,
RA Cawley S., Cooney A.J., D'Souza L.M., Martin K., Wu J.Q.,
RA Gonzalez-Garay M.L., Jackson A.R., Kalafus K.J., McLeod M.P.,
RA Milosavljevic A., Virk D., Volkov A., Wheeler D.A., Zhang Z., Bailey J.A.,
RA Eichler E.E., Tuzun E., Birney E., Mongin E., Ureta-Vidal A., Woodwark C.,
RA Zdobnov E., Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J.,
RA Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D., Schmidt J.,
RA Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M., Abril J.F.,
RA Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O., Poliakov A.,
RA Huebner N., Ganten D., Goesele C., Hummel O., Kreitler T., Lee Y.-A.,
RA Monti J., Schulz H., Zimdahl H., Himmelbauer H., Lehrach H., Jacob H.J.,
RA Bromberg S., Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E.,
RA Lazar J., Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M.,
RA Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E., Webber C.,
RA Brandt P., Nyakatura G., Adetobi M., Chiaromonte F., Elnitski L.,
RA Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K., Miller W.,
RA Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S., Zhang Y.,
RA Lindpaintner K., Andrews T.D., Caccamo M., Clamp M., Clarke L., Curwen V.,
RA Durbin R.M., Eyras E., Searle S.M., Cooper G.M., Batzoglou S., Brudno M.,
RA Sidow A., Stone E.A., Payseur B.A., Bourque G., Lopez-Otin C., Puente X.S.,
RA Chakrabarti K., Chatterji S., Dewey C., Pachter L., Bray N., Yap V.B.,
RA Caspi A., Tesler G., Pevzner P.A., Haussler D., Roskin K.M., Baertsch R.,
RA Clawson H., Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J.,
RA Rosenbloom K.R., Trumbower H., Weirauch M., Cooper D.N., Stenson P.D.,
RA Ma B., Brent M., Arumugam M., Shteynberg D., Copley R.R., Taylor M.S.,
RA Riethman H., Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S.,
RA Mockrin S., Collins F.S.;
RT "Genome sequence of the Brown Norway rat yields insights into mammalian
RT evolution.";
RL Nature 428:493-521(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Brown Norway;
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP INTERACTION WITH ADGRL3, SUBCELLULAR LOCATION, IDENTIFICATION BY MASS
RP SPECTROMETRY, AND TISSUE SPECIFICITY.
RX PubMed=22405201; DOI=10.1016/j.neuron.2012.01.018;
RA O'Sullivan M.L., de Wit J., Savas J.N., Comoletti D., Otto-Hitt S.,
RA Yates J.R. III, Ghosh A.;
RT "FLRT proteins are endogenous latrophilin ligands and regulate excitatory
RT synapse development.";
RL Neuron 73:903-910(2012).
CC -!- FUNCTION: Functions in cell-cell adhesion, cell migration and axon
CC guidance. Mediates cell-cell adhesion via its interactions with ADGRL3
CC and probably also other latrophilins that are expressed at the surface
CC of adjacent cells. May play a role in the migration of cortical neurons
CC during brain development via its interaction with UNC5D. Mediates axon
CC growth cone collapse and plays a repulsive role in neuron guidance via
CC its interaction with UNC5D, and possibly also other UNC-5 family
CC members. Plays a role in fibroblast growth factor-mediated signaling
CC cascades. Required for normal organization of the cardiac basement
CC membrane during embryogenesis, and for normal embryonic epicardium and
CC heart morphogenesis. {ECO:0000250|UniProtKB:Q8BLU0}.
CC -!- SUBUNIT: Self-associates (via leucine-rich repeats), giving rise to
CC homooligomers. Interacts with FGFR1. Interacts with FGFR2. Interacts
CC (via extracellular domain) with ADGRL1/LPHN1 (By similarity). Interacts
CC (via extracellular domain) with ADGRL3 (via olfactomedin-like domain)
CC (PubMed:22405201). Interacts (via extracellular domain) with UNC5D (via
CC the first Ig-like domain). Can also interact (via extracellular domain)
CC with UNC5B, but with much lower affinity. Interacts (via extracellular
CC domain) with FN1 (By similarity). {ECO:0000250|UniProtKB:Q8BLU0,
CC ECO:0000269|PubMed:22405201}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q8BLU0};
CC Single-pass membrane protein {ECO:0000250|UniProtKB:Q8BLU0}.
CC Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:Q8BLU0}. Synapse,
CC synaptosome {ECO:0000269|PubMed:22405201}. Cell junction, focal
CC adhesion {ECO:0000250|UniProtKB:Q8BLU0}. Secreted, extracellular space,
CC extracellular matrix {ECO:0000250|UniProtKB:Q8BLU0}. Microsome membrane
CC {ECO:0000250|UniProtKB:Q8BLU0}. Secreted
CC {ECO:0000250|UniProtKB:Q8BLU0}. Note=Proteolytic cleavage gives rise to
CC a shedded ectodomain. {ECO:0000250|UniProtKB:Q8BLU0}.
CC -!- TISSUE SPECIFICITY: Detected in brain (at protein level).
CC {ECO:0000269|PubMed:22405201}.
CC -!- PTM: N-glycosylated. {ECO:0000250|UniProtKB:Q8BLU0}.
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:Q8BLU0}.
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DR EMBL; AABR07065291; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH473982; EDL81682.1; -; Genomic_DNA.
DR RefSeq; NP_001100220.1; NM_001106750.1.
DR RefSeq; XP_006240478.1; XM_006240416.3.
DR RefSeq; XP_008762982.1; XM_008764760.2.
DR AlphaFoldDB; D3ZTV3; -.
DR SMR; D3ZTV3; -.
DR STRING; 10116.ENSRNOP00000004955; -.
DR GlyGen; D3ZTV3; 1 site.
DR PhosphoSitePlus; D3ZTV3; -.
DR PaxDb; D3ZTV3; -.
DR Ensembl; ENSRNOT00000004955; ENSRNOP00000004955; ENSRNOG00000003732.
DR Ensembl; ENSRNOT00000108960; ENSRNOP00000076725; ENSRNOG00000003732.
DR Ensembl; ENSRNOT00000113363; ENSRNOP00000083901; ENSRNOG00000003732.
DR Ensembl; ENSRNOT00000120043; ENSRNOP00000079728; ENSRNOG00000003732.
DR GeneID; 299236; -.
DR KEGG; rno:299236; -.
DR UCSC; RGD:1308574; rat.
DR CTD; 23768; -.
DR RGD; 1308574; Flrt2.
DR eggNOG; ENOG502QSJU; Eukaryota.
DR GeneTree; ENSGT00940000158937; -.
DR HOGENOM; CLU_027624_0_0_1; -.
DR InParanoid; D3ZTV3; -.
DR OMA; PTVPDWD; -.
DR OrthoDB; 826997at2759; -.
DR PhylomeDB; D3ZTV3; -.
DR TreeFam; TF315838; -.
DR Reactome; R-RNO-5654687; Downstream signaling of activated FGFR1.
DR PRO; PR:D3ZTV3; -.
DR Proteomes; UP000002494; Chromosome 6.
DR Proteomes; UP000234681; Chromosome 6.
DR Bgee; ENSRNOG00000003732; Expressed in frontal cortex and 15 other tissues.
DR GO; GO:0005911; C:cell-cell junction; ISS:UniProtKB.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005615; C:extracellular space; ISO:RGD.
DR GO; GO:0005925; C:focal adhesion; IEA:UniProtKB-SubCell.
DR GO; GO:0005887; C:integral component of plasma membrane; ISS:UniProtKB.
DR GO; GO:0043005; C:neuron projection; IEA:UniProtKB-KW.
DR GO; GO:0045202; C:synapse; IEA:UniProtKB-SubCell.
DR GO; GO:0045499; F:chemorepellent activity; ISO:RGD.
DR GO; GO:0005104; F:fibroblast growth factor receptor binding; ISO:RGD.
DR GO; GO:0007411; P:axon guidance; ISO:RGD.
DR GO; GO:0071711; P:basement membrane organization; ISS:UniProtKB.
DR GO; GO:0061343; P:cell adhesion involved in heart morphogenesis; ISS:UniProtKB.
DR GO; GO:0008543; P:fibroblast growth factor receptor signaling pathway; ISS:UniProtKB.
DR GO; GO:0003007; P:heart morphogenesis; ISS:UniProtKB.
DR GO; GO:0051965; P:positive regulation of synapse assembly; ISO:RGD.
DR GO; GO:2001222; P:regulation of neuron migration; ISO:RGD.
DR Gene3D; 2.60.40.10; -; 1.
DR Gene3D; 3.80.10.10; -; 1.
DR InterPro; IPR000483; Cys-rich_flank_reg_C.
DR InterPro; IPR003961; FN3_dom.
DR InterPro; IPR036116; FN3_sf.
DR InterPro; IPR013783; Ig-like_fold.
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; 3.
DR Pfam; PF01463; LRRCT; 1.
DR SMART; SM00369; LRR_TYP; 7.
DR SMART; SM00082; LRRCT; 1.
DR SMART; SM00013; LRRNT; 1.
DR SUPFAM; SSF49265; SSF49265; 1.
DR PROSITE; PS50853; FN3; 1.
PE 1: Evidence at protein level;
KW Cell adhesion; Cell junction; Cell membrane; Developmental protein;
KW Disulfide bond; Endoplasmic reticulum; Extracellular matrix; Glycoprotein;
KW Leucine-rich repeat; Membrane; Microsome; Reference proteome; Repeat;
KW Secreted; Signal; Synapse; Synaptosome; Transmembrane; Transmembrane helix.
FT SIGNAL 1..35
FT /evidence="ECO:0000255"
FT CHAIN 36..660
FT /note="Leucine-rich repeat transmembrane protein FLRT2"
FT /id="PRO_0000434524"
FT TOPO_DOM 36..540
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 541..561
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 562..660
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT DOMAIN 36..67
FT /note="LRRNT"
FT /evidence="ECO:0000255"
FT REPEAT 62..87
FT /note="LRR 1"
FT /evidence="ECO:0000255"
FT REPEAT 88..108
FT /note="LRR 2"
FT /evidence="ECO:0000255"
FT REPEAT 109..131
FT /note="LRR 3"
FT /evidence="ECO:0000255"
FT REPEAT 132..157
FT /note="LRR 4"
FT /evidence="ECO:0000255"
FT REPEAT 159..181
FT /note="LRR 5"
FT /evidence="ECO:0000255"
FT REPEAT 183..202
FT /note="LRR 6"
FT /evidence="ECO:0000255"
FT REPEAT 203..228
FT /note="LRR 7"
FT /evidence="ECO:0000255"
FT REPEAT 229..251
FT /note="LRR 8"
FT /evidence="ECO:0000255"
FT REPEAT 252..274
FT /note="LRR 9"
FT /evidence="ECO:0000255"
FT REPEAT 275..298
FT /note="LRR 10"
FT /evidence="ECO:0000255"
FT DOMAIN 338..361
FT /note="LRRCT"
FT /evidence="ECO:0000255"
FT DOMAIN 419..517
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT REGION 372..413
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 372..390
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 391..405
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 202
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 36..42
FT /evidence="ECO:0000250|UniProtKB:Q8BGT1"
FT DISULFID 40..49
FT /evidence="ECO:0000250|UniProtKB:Q8BGT1"
FT DISULFID 314..339
FT /evidence="ECO:0000250|UniProtKB:Q8BGT1"
FT DISULFID 316..360
FT /evidence="ECO:0000250|UniProtKB:Q8BLU0"
SQ SEQUENCE 660 AA; 73874 MW; D0D7C4E8136D1FAB CRC64;
MGLQTAKWPS HGTFVLKFWL IMSLGLYSHV SKLLACPSVC RCDRNFVYCN ERSLTSVPLG
IPEGVTVLYL HNNQINNAGF PAELHNVQSV HTVYLYGNQL DEFPMNLPKN VRVLHLQENN
IQTISRAALA QLLKLEELHL DDNSISTVGV EDGAFREAIS LKLLFLSKNH LSSVPVGLPV
DLQELRVDEN RIAVISDMAF QNLTSLERLI VDGNLLTNKG IADGTFSHLT KLKEFSIVRN
SLSHPPPDLP GTHLIRLYLQ DNQINHIPLT AFANLRKLER LDISNNQLRM LTQGVFDHLS
NLKQLTARNN PWFCDCSIKW VTEWLKYIPS SLNVRGFMCQ GPEQVRGMAV RELNMNLLSC
PTTTPGLPVF TPAPSTVSPT TQSPTVSVPS PSRGSVPPAP APSKLPTIPD WDGRERATPP
ISERIQLSIH FVNDTSIQVS WLSLFTVMAY KLTWVKMGHS LVGGIVQERI VSGEKQHLSL
VNLEPRSTYR ICLVPLDAFN YRTVEDTICS EATTHASYLN NGSNTASSHE QTTSHTMGSP
FLLAGLIGGA VIFVLVVLLS VFCWHMHKKG RYTSQKWKYN RGRRKDDYCE AGTKKDNSIL
EMTETSFQIV SLNNDQLLKG DFRLQPIYTP NGGINYTDCH IPNNMRYCNS SVPDLEHCHT
