AGRL3_MOUSE
ID AGRL3_MOUSE Reviewed; 1537 AA.
AC Q80TS3; Q3UHI7; Q3UM79; Q504Z9; Q5HZJ6; Q80T56;
DT 26-APR-2004, integrated into UniProtKB/Swiss-Prot.
DT 09-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 164.
DE RecName: Full=Adhesion G protein-coupled receptor L3 {ECO:0000312|MGI:MGI:2441950};
DE AltName: Full=Latrophilin-3 {ECO:0000312|MGI:MGI:2441950};
DE AltName: Full=Lectomedin-3 {ECO:0000312|MGI:MGI:2441950};
DE Flags: Precursor;
GN Name=Adgrl3 {ECO:0000312|MGI:MGI:2441950};
GN Synonyms=Kiaa0768 {ECO:0000312|MGI:MGI:2441950},
GN Lec3 {ECO:0000312|MGI:MGI:2441950}, Lphn3 {ECO:0000312|MGI:MGI:2441950};
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4), AND NUCLEOTIDE SEQUENCE
RP [LARGE SCALE MRNA] OF 672-1537 (ISOFORM 5).
RC STRAIN=C57BL/6J; TISSUE=Mammary gland;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2; 3 AND 6).
RC STRAIN=C57BL/6J; TISSUE=Brain, and Eye;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 481-1537 (ISOFORM 1).
RC TISSUE=Brain;
RX PubMed=12693553; DOI=10.1093/dnares/10.1.35;
RA Okazaki N., Kikuno R., Ohara R., Inamoto S., Aizawa H., Yuasa S.,
RA Nakajima D., Nagase T., Ohara O., Koga H.;
RT "Prediction of the coding sequences of mouse homologues of KIAA gene: II.
RT The complete nucleotide sequences of 400 mouse KIAA-homologous cDNAs
RT identified by screening of terminal sequences of cDNA clones randomly
RT sampled from size-fractionated libraries.";
RL DNA Res. 10:35-48(2003).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 803-981.
RX PubMed=12679517; DOI=10.1073/pnas.0230374100;
RA Vassilatis D.K., Hohmann J.G., Zeng H., Li F., Ranchalis J.E.,
RA Mortrud M.T., Brown A., Rodriguez S.S., Weller J.R., Wright A.C.,
RA Bergmann J.E., Gaitanaris G.A.;
RT "The G protein-coupled receptor repertoires of human and mouse.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:4903-4908(2003).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1254 AND SER-1522, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, and Lung;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [6]
RP DISRUPTION PHENOTYPE.
RX PubMed=22575564; DOI=10.1016/j.brainres.2012.04.053;
RA Wallis D., Hill D.S., Mendez I.A., Abbott L.C., Finnell R.H., Wellman P.J.,
RA Setlow B.;
RT "Initial characterization of mice null for Lphn3, a gene implicated in ADHD
RT and addiction.";
RL Brain Res. 1463:85-92(2012).
RN [7]
RP INTERACTION WITH TENM3; FLRT1; FLRT2 AND FLRT3, SUBCELLULAR LOCATION, AND
RP FUNCTION.
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).
RN [8]
RP FUNCTION, GLYCOSYLATION, INTERACTION WITH FLRT3 AND TENM1, DOMAIN, AND
RP SUBCELLULAR LOCATION.
RX PubMed=24739570; DOI=10.1186/1749-8104-9-7;
RA O'Sullivan M.L., Martini F., von Daake S., Comoletti D., Ghosh A.;
RT "LPHN3, a presynaptic adhesion-GPCR implicated in ADHD, regulates the
RT strength of neocortical layer 2/3 synaptic input to layer 5.";
RL Neural Dev. 9:7-7(2014).
RN [9]
RP X-RAY CRYSTALLOGRAPHY (2.16 ANGSTROMS) OF 97-459 IN COMPLEX WITH CALCIUM
RP IONS, FUNCTION, INTERACTION WITH FLRT2, DISULFIDE BONDS, GLYCOSYLATION AT
RP ASN-161, AND MUTAGENESIS OF PRO-244; ARG-246; THR-267; LYS-269; ARG-292;
RP ARG-294; ARG-324 AND GLY-326.
RX PubMed=25728924; DOI=10.1016/j.str.2015.01.013;
RA Jackson V.A., del Toro D., Carrasquero M., Roversi P., Harlos K., Klein R.,
RA Seiradake E.;
RT "Structural basis of latrophilin-FLRT interaction.";
RL Structure 23:774-781(2015).
RN [10]
RP X-RAY CRYSTALLOGRAPHY (1.60 ANGSTROMS) OF 199-495 IN COMPLEX WITH FLRT3 AND
RP CALCIUM IONS, INTERACTION WITH FLRT3, AND MUTAGENESIS OF TYR-323 AND
RP ASP-332.
RX PubMed=26235031; DOI=10.1016/j.str.2015.06.022;
RA Ranaivoson F.M., Liu Q., Martini F., Bergami F., von Daake S., Li S.,
RA Lee D., Demeler B., Hendrickson W.A., Comoletti D.;
RT "Structural and mechanistic insights into the latrophilin3-FLRT3 complex
RT that mediates glutamatergic synapse development.";
RL Structure 23:1665-1677(2015).
CC -!- FUNCTION: Plays a role in cell-cell adhesion and neuron guidance via
CC its interactions with FLRT2 and FLRT3 that are expressed at the surface
CC of adjacent cells (PubMed:22405201, PubMed:25728924, PubMed:26235031).
CC Plays a role in the development of glutamatergic synapses in the cortex
CC (PubMed:22405201, PubMed:24739570). Important in determining the
CC connectivity rates between the principal neurons in the cortex
CC (PubMed:24739570). {ECO:0000269|PubMed:22405201,
CC ECO:0000269|PubMed:24739570, ECO:0000269|PubMed:25728924,
CC ECO:0000269|PubMed:26235031}.
CC -!- SUBUNIT: Interacts (via olfactomedin-like domain) with FLRT3 (via
CC extracellular domain); the interaction is direct(PubMed:22405201,
CC PubMed:24739570, PubMed:26235031). Identified in a complex with FLRT3
CC and UNC5B; does not interact with UNC5B by itself. Identified in a
CC complex with FLRT3 and UNC5D; does not interact with UNC5D by itself
CC (By similarity). Interacts (via olfactomedin-like domain) with FLRT1
CC (via extracellular domain) (PubMed:22405201). Interacts (via
CC olfactomedin-like domain) with FLRT2 (via extracellular domain)
CC (PubMed:22405201, PubMed:25728924). Interacts (via extracellular
CC domain) with TENM1 (PubMed:24739570). Interacts (via extracellular
CC domain) with TENM3 (PubMed:22405201). {ECO:0000250|UniProtKB:Q9HAR2,
CC ECO:0000269|PubMed:22405201, ECO:0000269|PubMed:24739570,
CC ECO:0000269|PubMed:25728924, ECO:0000269|PubMed:26235031}.
CC -!- INTERACTION:
CC Q80TS3; Q8BLU0: Flrt2; NbExp=2; IntAct=EBI-770665, EBI-16146541;
CC Q80TS3; Q8BGT1: Flrt3; NbExp=6; IntAct=EBI-770665, EBI-16166902;
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:22405201,
CC ECO:0000269|PubMed:24739570}; Multi-pass membrane protein
CC {ECO:0000305}. Cell projection, axon {ECO:0000269|PubMed:22405201}.
CC Cell junction {ECO:0000269|PubMed:22405201}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=6;
CC Name=1;
CC IsoId=Q80TS3-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q80TS3-2; Sequence=VSP_010121, VSP_010122, VSP_010123;
CC Name=3;
CC IsoId=Q80TS3-3; Sequence=VSP_022142;
CC Name=4;
CC IsoId=Q80TS3-4; Sequence=VSP_022138;
CC Name=5;
CC IsoId=Q80TS3-5; Sequence=VSP_010121;
CC Name=6;
CC IsoId=Q80TS3-6; Sequence=VSP_022139, VSP_022140, VSP_022141;
CC -!- DOMAIN: The Olfactomedin-like domain is required for the synapse-
CC promoting function and the interaction with FLRT3. The Olfactomedin-
CC like and the SUEL-type lectin domains are required for the interaction
CC with TENM1. {ECO:0000269|PubMed:24739570}.
CC -!- PTM: Proteolytically cleaved into 2 subunits, an extracellular subunit
CC and a seven-transmembrane subunit. {ECO:0000250}.
CC -!- PTM: O-glycosylated (major) and N-glycosylated.
CC {ECO:0000269|PubMed:24739570}.
CC -!- DISRUPTION PHENOTYPE: Mutant mice are viable and present no obvious
CC physical phenotype. Compared to wild-type, mutants are hyperactive, and
CC their dorsal striatum contains higher levels of the neurotransmitters
CC dopamine and serotonin. Cocaine treatment causes a higher increase in
CC locomotor activity than in wild-type. {ECO:0000269|PubMed:22575564}.
CC -!- SIMILARITY: Belongs to the G-protein coupled receptor 2 family. LN-TM7
CC subfamily. {ECO:0000305}.
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DR EMBL; AK145069; BAE26219.1; -; mRNA.
DR EMBL; AK147374; BAE27870.1; -; mRNA.
DR EMBL; BC058992; AAH58992.1; -; mRNA.
DR EMBL; BC088989; AAH88989.1; -; mRNA.
DR EMBL; BC094668; AAH94668.1; -; mRNA.
DR EMBL; AK122367; BAC65649.1; -; mRNA.
DR EMBL; AY255584; AAO85096.1; -; mRNA.
DR CCDS; CCDS39122.1; -. [Q80TS3-3]
DR CCDS; CCDS84894.1; -. [Q80TS3-5]
DR RefSeq; NP_001334298.1; NM_001347369.1. [Q80TS3-5]
DR RefSeq; NP_941991.1; NM_198702.2. [Q80TS3-3]
DR RefSeq; XP_011247767.1; XM_011249465.2. [Q80TS3-3]
DR RefSeq; XP_011247768.1; XM_011249466.2.
DR RefSeq; XP_011247773.1; XM_011249471.2. [Q80TS3-2]
DR RefSeq; XP_017176402.1; XM_017320913.1.
DR PDB; 4RMK; X-ray; 1.61 A; A=199-495.
DR PDB; 4RML; X-ray; 1.60 A; A=199-495.
DR PDB; 4YEB; X-ray; 3.19 A; A=199-495.
DR PDB; 5AFB; X-ray; 2.16 A; A=97-459.
DR PDB; 5FTT; X-ray; 3.40 A; C/D/G/H=92-463.
DR PDB; 5FTU; X-ray; 6.01 A; C/D/G/H/K/L=92-463.
DR PDB; 6JBU; X-ray; 1.85 A; A=203-461.
DR PDBsum; 4RMK; -.
DR PDBsum; 4RML; -.
DR PDBsum; 4YEB; -.
DR PDBsum; 5AFB; -.
DR PDBsum; 5FTT; -.
DR PDBsum; 5FTU; -.
DR PDBsum; 6JBU; -.
DR AlphaFoldDB; Q80TS3; -.
DR SMR; Q80TS3; -.
DR BioGRID; 235241; 5.
DR DIP; DIP-32218N; -.
DR IntAct; Q80TS3; 4.
DR MINT; Q80TS3; -.
DR STRING; 10090.ENSMUSP00000113482; -.
DR MEROPS; P02.011; -.
DR GlyConnect; 2419; 9 N-Linked glycans (5 sites). [Q80TS3-2]
DR GlyGen; Q80TS3; 10 sites, 9 N-linked glycans (5 sites).
DR iPTMnet; Q80TS3; -.
DR PhosphoSitePlus; Q80TS3; -.
DR SwissPalm; Q80TS3; -.
DR MaxQB; Q80TS3; -.
DR PaxDb; Q80TS3; -.
DR PeptideAtlas; Q80TS3; -.
DR PRIDE; Q80TS3; -.
DR ProteomicsDB; 285776; -. [Q80TS3-1]
DR ProteomicsDB; 285777; -. [Q80TS3-2]
DR ProteomicsDB; 285778; -. [Q80TS3-3]
DR ProteomicsDB; 285779; -. [Q80TS3-4]
DR ProteomicsDB; 285780; -. [Q80TS3-5]
DR ProteomicsDB; 285781; -. [Q80TS3-6]
DR Antibodypedia; 2755; 176 antibodies from 31 providers.
DR DNASU; 319387; -.
DR Ensembl; ENSMUST00000072521; ENSMUSP00000072336; ENSMUSG00000037605. [Q80TS3-3]
DR Ensembl; ENSMUST00000117407; ENSMUSP00000112388; ENSMUSG00000037605. [Q80TS3-2]
DR Ensembl; ENSMUST00000122356; ENSMUSP00000113600; ENSMUSG00000037605. [Q80TS3-5]
DR GeneID; 319387; -.
DR KEGG; mmu:319387; -.
DR UCSC; uc008xwk.1; mouse. [Q80TS3-6]
DR UCSC; uc008xwn.1; mouse. [Q80TS3-1]
DR UCSC; uc008xwp.1; mouse. [Q80TS3-3]
DR CTD; 23284; -.
DR MGI; MGI:2441950; Adgrl3.
DR VEuPathDB; HostDB:ENSMUSG00000037605; -.
DR eggNOG; KOG3545; Eukaryota.
DR eggNOG; KOG4193; Eukaryota.
DR eggNOG; KOG4729; Eukaryota.
DR GeneTree; ENSGT00940000155527; -.
DR InParanoid; Q80TS3; -.
DR OrthoDB; 388923at2759; -.
DR PhylomeDB; Q80TS3; -.
DR BioGRID-ORCS; 319387; 3 hits in 57 CRISPR screens.
DR ChiTaRS; Adgrl3; mouse.
DR PRO; PR:Q80TS3; -.
DR Proteomes; UP000000589; Chromosome 5.
DR RNAct; Q80TS3; protein.
DR Bgee; ENSMUSG00000037605; Expressed in CA1 field of hippocampus and 178 other tissues.
DR ExpressionAtlas; Q80TS3; baseline and differential.
DR Genevisible; Q80TS3; MM.
DR GO; GO:0030424; C:axon; IDA:UniProtKB.
DR GO; GO:0005911; C:cell-cell junction; IDA:UniProtKB.
DR GO; GO:0098978; C:glutamatergic synapse; IDA:SynGO.
DR GO; GO:0005887; C:integral component of plasma membrane; IDA:UniProtKB.
DR GO; GO:0005509; F:calcium ion binding; IDA:UniProtKB.
DR GO; GO:0030246; F:carbohydrate binding; IEA:UniProtKB-KW.
DR GO; GO:0004930; F:G protein-coupled receptor activity; IBA:GO_Central.
DR GO; GO:0007189; P:adenylate cyclase-activating G protein-coupled receptor signaling pathway; IBA:GO_Central.
DR GO; GO:0007420; P:brain development; IBA:GO_Central.
DR GO; GO:0007166; P:cell surface receptor signaling pathway; IEA:InterPro.
DR GO; GO:0098742; P:cell-cell adhesion via plasma-membrane adhesion molecules; IMP:UniProtKB.
DR GO; GO:0031987; P:locomotion involved in locomotory behavior; IMP:UniProtKB.
DR GO; GO:0001764; P:neuron migration; IMP:UniProtKB.
DR GO; GO:0051965; P:positive regulation of synapse assembly; IDA:MGI.
DR GO; GO:0042220; P:response to cocaine; IMP:UniProtKB.
DR GO; GO:0007416; P:synapse assembly; IMP:UniProtKB.
DR GO; GO:0050808; P:synapse organization; IDA:SynGO.
DR Gene3D; 2.60.120.740; -; 1.
DR Gene3D; 2.60.220.50; -; 1.
DR Gene3D; 4.10.1240.10; -; 1.
DR InterPro; IPR032471; GAIN_dom_N.
DR InterPro; IPR046338; GAIN_dom_sf.
DR InterPro; IPR017981; GPCR_2-like.
DR InterPro; IPR036445; GPCR_2_extracell_dom_sf.
DR InterPro; IPR001879; GPCR_2_extracellular_dom.
DR InterPro; IPR003924; GPCR_2_latrophilin.
DR InterPro; IPR003334; GPCR_2_latrophilin_rcpt_C.
DR InterPro; IPR000832; GPCR_2_secretin-like.
DR InterPro; IPR017983; GPCR_2_secretin-like_CS.
DR InterPro; IPR000203; GPS.
DR InterPro; IPR015630; Latrophilin-3.
DR InterPro; IPR000922; Lectin_gal-bd_dom.
DR InterPro; IPR043159; Lectin_gal-bd_sf.
DR InterPro; IPR003112; Olfac-like_dom.
DR PANTHER; PTHR12011:SF60; PTHR12011:SF60; 1.
DR Pfam; PF00002; 7tm_2; 1.
DR Pfam; PF16489; GAIN; 1.
DR Pfam; PF02140; Gal_Lectin; 1.
DR Pfam; PF01825; GPS; 1.
DR Pfam; PF02354; Latrophilin; 2.
DR Pfam; PF02191; OLF; 1.
DR PRINTS; PR00249; GPCRSECRETIN.
DR PRINTS; PR01444; LATROPHILIN.
DR SMART; SM00303; GPS; 1.
DR SMART; SM00008; HormR; 1.
DR SMART; SM00284; OLF; 1.
DR PROSITE; PS00650; G_PROTEIN_RECEP_F2_2; 1.
DR PROSITE; PS50227; G_PROTEIN_RECEP_F2_3; 1.
DR PROSITE; PS50261; G_PROTEIN_RECEP_F2_4; 1.
DR PROSITE; PS50221; GPS; 1.
DR PROSITE; PS51132; OLF; 1.
DR PROSITE; PS50228; SUEL_LECTIN; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Calcium; Cell junction; Cell membrane;
KW Cell projection; Disulfide bond; G-protein coupled receptor; Glycoprotein;
KW Lectin; Membrane; Metal-binding; Phosphoprotein; Receptor;
KW Reference proteome; Signal; Transducer; Transmembrane; Transmembrane helix.
FT SIGNAL 1..19
FT /evidence="ECO:0000255"
FT CHAIN 20..1537
FT /note="Adhesion G protein-coupled receptor L3"
FT /id="PRO_0000070344"
FT TOPO_DOM 20..949
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 950..970
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 971..978
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 979..999
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1000..1007
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 1008..1028
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1029..1050
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 1051..1071
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1072..1088
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 1089..1109
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1110..1142
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 1143..1163
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1164..1169
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 1170..1190
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1191..1537
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 103..192
FT /note="SUEL-type lectin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00260"
FT DOMAIN 202..461
FT /note="Olfactomedin-like"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00446"
FT DOMAIN 883..934
FT /note="GPS"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00098"
FT REGION 53..80
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 317..347
FT /note="Interaction with FLRT3"
FT REGION 521..540
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1213..1237
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1512..1537
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 332
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000269|PubMed:25728924"
FT BINDING 380
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000269|PubMed:25728924"
FT BINDING 381
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000269|PubMed:25728924"
FT BINDING 435
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000269|PubMed:25728924"
FT MOD_RES 1254
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1522
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT CARBOHYD 161
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255, ECO:0000269|PubMed:25728924,
FT ECO:0007744|PDB:5AFB"
FT CARBOHYD 532
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 617
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 827
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 840
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 885
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 911
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1000
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1166
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 104..134
FT /evidence="ECO:0007744|PDB:5AFB"
FT DISULFID 113..191
FT /evidence="ECO:0007744|PDB:5AFB"
FT DISULFID 146..178
FT /evidence="ECO:0007744|PDB:5AFB"
FT DISULFID 159..165
FT /evidence="ECO:0007744|PDB:5AFB"
FT DISULFID 203..385
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00446,
FT ECO:0007744|PDB:5AFB"
FT VAR_SEQ 1..239
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_022138"
FT VAR_SEQ 195..200
FT /note="KVEQKV -> I (in isoform 6)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_022139"
FT VAR_SEQ 650
FT /note="H -> Q (in isoform 6)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_022140"
FT VAR_SEQ 651..1537
FT /note="Missing (in isoform 6)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_022141"
FT VAR_SEQ 1132..1140
FT /note="Missing (in isoform 2 and isoform 5)"
FT /evidence="ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:16141072"
FT /id="VSP_010121"
FT VAR_SEQ 1272..1351
FT /note="EGLLNNARDTSVMDTLPLNGNHGNSYSIAGGEYLSNCVQIIDRGYNHNETAL
FT EKKILKELTSNYIPSYLNNHERSSEQNR -> GAMANHLISNALLRPHGTNNPYNTLLG
FT EPAVCNNPSISMYNTQEPYRETSMGVKLNIAYQIGASEQCQGYKCHGYSTTEW (in
FT isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_010122"
FT VAR_SEQ 1272
FT /note="E -> EPYRETK (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_022142"
FT VAR_SEQ 1352..1537
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_010123"
FT MUTAGEN 244
FT /note="P->N: Strongly reduces FLRT2 binding; when
FT associated with T-246."
FT /evidence="ECO:0000269|PubMed:25728924"
FT MUTAGEN 246
FT /note="R->T: Strongly reduces FLRT2 binding; when
FT associated with N-244."
FT /evidence="ECO:0000269|PubMed:25728924"
FT MUTAGEN 267
FT /note="T->N: Strongly reduces FLRT2 binding; when
FT associated with T-269."
FT /evidence="ECO:0000269|PubMed:25728924"
FT MUTAGEN 269
FT /note="K->T: Strongly reduces FLRT2 binding; when
FT associated with N-267."
FT /evidence="ECO:0000269|PubMed:25728924"
FT MUTAGEN 292
FT /note="R->N: Abolishes interaction with FLRT2; when
FT associated with T-294."
FT /evidence="ECO:0000269|PubMed:25728924"
FT MUTAGEN 294
FT /note="R->T: Abolishes interaction with FLRT2; when
FT associated with N-292."
FT /evidence="ECO:0000269|PubMed:25728924"
FT MUTAGEN 323
FT /note="Y->A: Abolishes FLRT3 binding."
FT /evidence="ECO:0000269|PubMed:26235031"
FT MUTAGEN 324
FT /note="R->N: Abolishes interaction with FLRT2; when
FT associated with T-326."
FT /evidence="ECO:0000269|PubMed:25728924"
FT MUTAGEN 326
FT /note="G->T: Abolishes interaction with FLRT2; when
FT associated with N-324."
FT /evidence="ECO:0000269|PubMed:25728924"
FT MUTAGEN 332
FT /note="D->A: Strongly reduces FLRT3 binding."
FT /evidence="ECO:0000269|PubMed:26235031"
FT CONFLICT 381
FT /note="A -> S (in Ref. 2; AAH94668)"
FT /evidence="ECO:0000305"
FT CONFLICT 1252
FT /note="K -> R (in Ref. 1; BAE27870)"
FT /evidence="ECO:0000305"
FT CONFLICT 1375
FT /note="A -> T (in Ref. 1; BAE26219)"
FT /evidence="ECO:0000305"
FT CONFLICT 1495
FT /note="V -> M (in Ref. 1; BAE26219)"
FT /evidence="ECO:0000305"
FT STRAND 101..104
FT /evidence="ECO:0007829|PDB:5FTT"
FT STRAND 108..112
FT /evidence="ECO:0007829|PDB:5FTT"
FT STRAND 118..129
FT /evidence="ECO:0007829|PDB:5FTT"
FT STRAND 131..134
FT /evidence="ECO:0007829|PDB:5FTT"
FT TURN 138..141
FT /evidence="ECO:0007829|PDB:5FTT"
FT HELIX 151..158
FT /evidence="ECO:0007829|PDB:5FTT"
FT TURN 159..161
FT /evidence="ECO:0007829|PDB:5FTT"
FT STRAND 163..168
FT /evidence="ECO:0007829|PDB:5FTT"
FT TURN 171..173
FT /evidence="ECO:0007829|PDB:5FTT"
FT STRAND 184..192
FT /evidence="ECO:0007829|PDB:5FTT"
FT STRAND 199..202
FT /evidence="ECO:0007829|PDB:5FTT"
FT STRAND 206..218
FT /evidence="ECO:0007829|PDB:4RML"
FT STRAND 220..227
FT /evidence="ECO:0007829|PDB:4RML"
FT STRAND 230..232
FT /evidence="ECO:0007829|PDB:5FTT"
FT STRAND 237..241
FT /evidence="ECO:0007829|PDB:4RML"
FT TURN 244..246
FT /evidence="ECO:0007829|PDB:6JBU"
FT STRAND 249..255
FT /evidence="ECO:0007829|PDB:4RML"
FT HELIX 256..261
FT /evidence="ECO:0007829|PDB:4RML"
FT STRAND 265..269
FT /evidence="ECO:0007829|PDB:4RML"
FT STRAND 274..277
FT /evidence="ECO:0007829|PDB:4RML"
FT STRAND 280..282
FT /evidence="ECO:0007829|PDB:4RML"
FT STRAND 285..290
FT /evidence="ECO:0007829|PDB:4RML"
FT STRAND 293..300
FT /evidence="ECO:0007829|PDB:4RML"
FT TURN 301..304
FT /evidence="ECO:0007829|PDB:4RML"
FT STRAND 305..311
FT /evidence="ECO:0007829|PDB:4RML"
FT STRAND 318..321
FT /evidence="ECO:0007829|PDB:4RMK"
FT STRAND 330..336
FT /evidence="ECO:0007829|PDB:4RML"
FT STRAND 339..346
FT /evidence="ECO:0007829|PDB:4RML"
FT TURN 347..351
FT /evidence="ECO:0007829|PDB:4RML"
FT STRAND 352..358
FT /evidence="ECO:0007829|PDB:4RML"
FT TURN 360..362
FT /evidence="ECO:0007829|PDB:4RML"
FT STRAND 365..374
FT /evidence="ECO:0007829|PDB:4RML"
FT HELIX 375..377
FT /evidence="ECO:0007829|PDB:4RML"
FT STRAND 378..384
FT /evidence="ECO:0007829|PDB:4RML"
FT STRAND 387..393
FT /evidence="ECO:0007829|PDB:4RML"
FT STRAND 405..412
FT /evidence="ECO:0007829|PDB:4RML"
FT TURN 413..416
FT /evidence="ECO:0007829|PDB:4RML"
FT STRAND 417..424
FT /evidence="ECO:0007829|PDB:4RML"
FT STRAND 428..430
FT /evidence="ECO:0007829|PDB:6JBU"
FT STRAND 434..438
FT /evidence="ECO:0007829|PDB:4RML"
FT TURN 439..442
FT /evidence="ECO:0007829|PDB:4RML"
FT STRAND 443..448
FT /evidence="ECO:0007829|PDB:4RML"
FT STRAND 451..460
FT /evidence="ECO:0007829|PDB:4RML"
SQ SEQUENCE 1537 AA; 171080 MW; F55EAB142C987A69 CRC64;
MWPPQLLILT MLLAPVVHGG KHNERHPALA APLRHAERSP GGALPPRHLL QQPAAERSTA
HRGQGPRGAA RGVRGPGAPG AQIAAQAFSR APIPMAVVRR ELSCESYPIE LRCPGTDVIM
IESANYGRTD DKICDSDPAQ MENIRCYLPD AYKIMSQRCN NRTQCAVVAG PDVFPDPCPG
TYKYLEVQYE CVPYKVEQKV FLCPGLLKGV YQSEHLFESD HQSGAWCKDP LQASDKIYYM
PWTPYRTDTL TEYSSKDDFI AGRPTTTYKL PHRVDGTGFV VYDGALFFNK ERTRNIVKFD
LRTRIKSGEA IIANANYHDT SPYRWGGKSD IDLAVDENGL WVIYATEQNN GKIVISQLNP
YTLRIEGTWD TAYDKRSASN AFMICGILYV VKSVYEDDDN EATGNKIDYI YNTDQSKDSL
VDVPFPNSYQ YIAAVDYNPR DNLLYVWNNY HVVKYSLDFG PLDSRSGPVH HGQVSYISPP
IHLDSELERP PVRGISTTGS LGMGSTTTST TLRTTTWNIG RSTTASLPGR RNRSTSTPSP
AVEVLDDVTT HLPSAASQIP AMEESCEAVE AREIMWFKTR QGQVAKQPCP AGTIGVSTYL
CLAPDGIWDP QGPDLSNCSS PWVNHITQKL KSGETAANIA RELAEQTRNH LNAGDITYSV
RAMDQLVGLL DVQLRNLTPG GKDSAARSLN KLQKRERSCR AYVQAMVETV NNLLQPQALN
AWRDLTTSDQ LRAATMLLDT VEESAFVLAD NLLKTDIVRE NTDNIQLEVA RLSTEGNLED
LKFPENMGHG STIQLSANTL KQNGRNGEIR VAFVLYNNLG PYLSTENASM KLGTEAMSTN
HSVIVNSPVI TAAINKEFSN KVYLADPVVF TVKHIKQSEE NFNPNCSFWS YSKRTMTGYW
STQGCRLLTT NKTHTTCSCN HLTNFAVLMA HVEVKHSDAV HDLLLDVITW VGILLSLVCL
LICIFTFCFF RGLQSDRNTI HKNLCISLFV AELLFLIGIN RTDQPIACAV FAALLHFFFL
AAFTWMFLEG VQLYIMLVEV FESEHSRRKY FYLVGYGMPA LIVAVSAAVD YRSYGTDKVC
WLRLDTYFIW SFIGPATLII MLNVIFLGIA LYKMFHHTAI LKPESGCLDN INYEDNRPFI
KSWVIGAIAL LCLLGLTWAF GLMYINESTV IMAYLFTIFN SLQGMFIFIF HCVLQKKVRK
EYGKCLRTHC CSGKSTESSI GSGKTSGSRT PGRYSTGSQS RIRRMWNDTV RKQSESSFIT
GDINSSASLN REGLLNNARD TSVMDTLPLN GNHGNSYSIA GGEYLSNCVQ IIDRGYNHNE
TALEKKILKE LTSNYIPSYL NNHERSSEQN RNMMNKLVNN LGSGSEDDAI VLDDAASFNH
EESLGLELIH EESDAPLLPP RVYSTDNHQP HHYSRRRFPQ DHSESFFPLL TDEHTEDLQS
PHRDSLYTSM PALAGVPAAD SVTTSTQTEA AAAKGGDAED VYYKSMPNLG SRNHVHPLHA
YYQLGRGSSD GFIVPPNKDG ASPEGTSKGP AHLVTSL
