AGRL3_HUMAN
ID AGRL3_HUMAN Reviewed; 1447 AA.
AC Q9HAR2; E9PE04; O94867; Q9NWK5;
DT 10-MAY-2004, integrated into UniProtKB/Swiss-Prot.
DT 10-MAY-2004, sequence version 2.
DT 03-AUG-2022, entry version 165.
DE RecName: Full=Adhesion G protein-coupled receptor L3 {ECO:0000312|HGNC:HGNC:20974};
DE AltName: Full=Calcium-independent alpha-latrotoxin receptor 3 {ECO:0000250|UniProtKB:Q9Z173};
DE Short=CIRL-3 {ECO:0000250|UniProtKB:Q9Z173};
DE AltName: Full=Latrophilin-3 {ECO:0000312|HGNC:HGNC:20974};
DE AltName: Full=Lectomedin-3;
DE Flags: Precursor;
GN Name=ADGRL3 {ECO:0000312|HGNC:HGNC:20974};
GN Synonyms=KIAA0768 {ECO:0000312|HGNC:HGNC:20974},
GN LEC3 {ECO:0000312|HGNC:HGNC:20974}, LPHN3 {ECO:0000312|HGNC:HGNC:20974};
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
RA Douangpanya J., Puri K., Hayflick J.;
RL Submitted (SEP-2000) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15815621; DOI=10.1038/nature03466;
RA Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P.,
RA Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C.,
RA Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L.,
RA Du H., Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A.,
RA Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J.,
RA Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M.,
RA Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T.,
RA Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S.,
RA Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K.,
RA McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C.,
RA Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S.,
RA Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C.,
RA Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M.,
RA Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C.,
RA Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J.,
RA Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E.,
RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X.,
RA Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M.,
RA Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C.,
RA Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S.,
RA Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H.,
RA Wilson R.K.;
RT "Generation and annotation of the DNA sequences of human chromosomes 2 and
RT 4.";
RL Nature 434:724-731(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 279-707 (ISOFORM 3).
RC TISSUE=Colon;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 576-1447 (ISOFORM 1).
RC TISSUE=Brain;
RX PubMed=9872452; DOI=10.1093/dnares/5.5.277;
RA Nagase T., Ishikawa K., Suyama M., Kikuno R., Miyajima N., Tanaka A.,
RA Kotani H., Nomura N., Ohara O.;
RT "Prediction of the coding sequences of unidentified human genes. XI. The
RT complete sequences of 100 new cDNA clones from brain which code for large
RT proteins in vitro.";
RL DNA Res. 5:277-286(1998).
RN [5]
RP X-RAY CRYSTALLOGRAPHY (3.60 ANGSTROMS) OF 132-392 IN COMPLEX WITH FLRT3 AND
RP CALCIUM IONS, INTERACTION WITH FLRT3, IDENTIFICATION IN COMPLEXES WITH
RP FLTR3; UNC5B AND UNC5D, DISULFIDE BOND, FUNCTION, SUBCELLULAR LOCATION,
RP MUTAGENESIS OF 249-TYR--THR-252 AND ARG-308, AND REGION.
RX PubMed=26235030; DOI=10.1016/j.str.2015.06.024;
RA Lu Y.C., Nazarko O.V., Sando R. III, Salzman G.S., Suedhof T.C., Arac D.;
RT "Structural basis of latrophilin-FLRT-UNC5 interaction in cell adhesion.";
RL Structure 23:1678-1691(2015).
RN [6]
RP VARIANTS SER-247; GLN-465; MET-770 AND VAL-915.
RX PubMed=21184580; DOI=10.1002/ajmg.b.31141;
RA Domene S., Stanescu H., Wallis D., Tinloy B., Pineda D.E., Kleta R.,
RA Arcos-Burgos M., Roessler E., Muenke M.;
RT "Screening of human LPHN3 for variants with a potential impact on ADHD
RT susceptibility.";
RL Am. J. Med. Genet. B Neuropsychiatr. Genet. 156:11-18(2011).
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:26235030). Plays a role in the development of
CC glutamatergic synapses in the cortex. Important in determining the
CC connectivity rates between the principal neurons in the cortex.
CC {ECO:0000250|UniProtKB:Q80TS3, ECO:0000305|PubMed:26235030}.
CC -!- SUBUNIT: Interacts (via olfactomedin-like domain) with FLRT3 (via
CC extracellular domain); the interaction is direct (PubMed:26235030).
CC Identified in a complex with FLRT3 and UNC5B; does not interact with
CC UNC5B by itself (PubMed:26235030). Identified in a complex with FLRT3
CC and UNC5D; does not interact with UNC5D by itself (PubMed:26235030).
CC Interacts (via olfactomedin-like domain) with FLRT1 (via extracellular
CC domain). Interacts (via olfactomedin-like domain) with FLRT2 (via
CC extracellular domain). Interacts (via extracellular domain) with TENM1.
CC Interacts (via extracellular domain) with TENM3 (By similarity).
CC {ECO:0000250|UniProtKB:Q80TS3, ECO:0000269|PubMed:26235030}.
CC -!- INTERACTION:
CC Q9HAR2; Q9NZU0: FLRT3; NbExp=4; IntAct=EBI-2689295, EBI-1057092;
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:26235030};
CC Multi-pass membrane protein {ECO:0000305}. Cell projection, axon
CC {ECO:0000250|UniProtKB:Q80TS3}. Cell junction
CC {ECO:0000250|UniProtKB:Q80TS3}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=1;
CC IsoId=Q9HAR2-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9HAR2-2; Sequence=VSP_010235, VSP_010238, VSP_010239,
CC VSP_010240;
CC Name=3;
CC IsoId=Q9HAR2-3; Sequence=VSP_010236, VSP_010237;
CC Name=4;
CC IsoId=Q9HAR2-4; Sequence=VSP_010235, VSP_010238;
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 (By similarity). {ECO:0000250}.
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. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the G-protein coupled receptor 2 family. LN-TM7
CC subfamily. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA91375.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AF307080; AAG27462.1; -; mRNA.
DR EMBL; AK000781; BAA91375.1; ALT_INIT; mRNA.
DR EMBL; AC007511; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC020741; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC092643; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC092663; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC092668; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC096723; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC104813; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC108161; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AB018311; BAA34488.1; -; mRNA.
DR CCDS; CCDS54768.1; -. [Q9HAR2-4]
DR CCDS; CCDS82926.1; -. [Q9HAR2-2]
DR RefSeq; NP_001309175.1; NM_001322246.1. [Q9HAR2-2]
DR RefSeq; NP_001309331.1; NM_001322402.1.
DR RefSeq; NP_056051.2; NM_015236.5. [Q9HAR2-4]
DR PDB; 5CMN; X-ray; 3.60 A; E/F/G/H=132-392.
DR PDB; 6VHH; EM; 2.97 A; B=21-866.
DR PDBsum; 5CMN; -.
DR PDBsum; 6VHH; -.
DR AlphaFoldDB; Q9HAR2; -.
DR SMR; Q9HAR2; -.
DR BioGRID; 116882; 20.
DR CORUM; Q9HAR2; -.
DR DIP; DIP-56228N; -.
DR IntAct; Q9HAR2; 11.
DR STRING; 9606.ENSP00000422533; -.
DR MEROPS; P02.011; -.
DR TCDB; 9.A.14.6.8; the g-protein-coupled receptor (gpcr) family.
DR GlyGen; Q9HAR2; 11 sites, 2 O-linked glycans (3 sites).
DR iPTMnet; Q9HAR2; -.
DR PhosphoSitePlus; Q9HAR2; -.
DR SwissPalm; Q9HAR2; -.
DR BioMuta; ADGRL3; -.
DR DMDM; 47116772; -.
DR EPD; Q9HAR2; -.
DR jPOST; Q9HAR2; -.
DR MassIVE; Q9HAR2; -.
DR PaxDb; Q9HAR2; -.
DR PeptideAtlas; Q9HAR2; -.
DR PRIDE; Q9HAR2; -.
DR ProteomicsDB; 19784; -.
DR ProteomicsDB; 81420; -. [Q9HAR2-1]
DR ProteomicsDB; 81421; -. [Q9HAR2-2]
DR ProteomicsDB; 81422; -. [Q9HAR2-3]
DR Antibodypedia; 2755; 176 antibodies from 31 providers.
DR DNASU; 23284; -.
DR Ensembl; ENST00000512091.6; ENSP00000423388.1; ENSG00000150471.17. [Q9HAR2-2]
DR Ensembl; ENST00000514591.5; ENSP00000422533.1; ENSG00000150471.17. [Q9HAR2-4]
DR GeneID; 23284; -.
DR KEGG; hsa:23284; -.
DR UCSC; uc003hcq.5; human. [Q9HAR2-1]
DR CTD; 23284; -.
DR DisGeNET; 23284; -.
DR GeneCards; ADGRL3; -.
DR HGNC; HGNC:20974; ADGRL3.
DR HPA; ENSG00000150471; Tissue enhanced (brain).
DR MIM; 616417; gene.
DR neXtProt; NX_Q9HAR2; -.
DR OpenTargets; ENSG00000150471; -.
DR PharmGKB; PA134968284; -.
DR VEuPathDB; HostDB:ENSG00000150471; -.
DR eggNOG; KOG3545; Eukaryota.
DR eggNOG; KOG4193; Eukaryota.
DR eggNOG; KOG4729; Eukaryota.
DR GeneTree; ENSGT00940000155527; -.
DR HOGENOM; CLU_002753_0_1_1; -.
DR InParanoid; Q9HAR2; -.
DR PhylomeDB; Q9HAR2; -.
DR TreeFam; TF351999; -.
DR PathwayCommons; Q9HAR2; -.
DR SignaLink; Q9HAR2; -.
DR BioGRID-ORCS; 23284; 2 hits in 1070 CRISPR screens.
DR ChiTaRS; ADGRL3; human.
DR GenomeRNAi; 23284; -.
DR Pharos; Q9HAR2; Tbio.
DR PRO; PR:Q9HAR2; -.
DR Proteomes; UP000005640; Chromosome 4.
DR RNAct; Q9HAR2; protein.
DR Bgee; ENSG00000150471; Expressed in adrenal tissue and 179 other tissues.
DR ExpressionAtlas; Q9HAR2; baseline and differential.
DR Genevisible; Q9HAR2; HS.
DR GO; GO:0030424; C:axon; ISS:UniProtKB.
DR GO; GO:0005911; C:cell-cell junction; ISS:UniProtKB.
DR GO; GO:0098978; C:glutamatergic synapse; IBA:GO_Central.
DR GO; GO:0016021; C:integral component of membrane; TAS:GDB.
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; IDA:UniProtKB.
DR GO; GO:0007186; P:G protein-coupled receptor signaling pathway; TAS:GDB.
DR GO; GO:0001764; P:neuron migration; ISS:UniProtKB.
DR GO; GO:0007416; P:synapse assembly; ISS:UniProtKB.
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..1447
FT /note="Adhesion G protein-coupled receptor L3"
FT /id="PRO_0000012913"
FT TOPO_DOM 20..866
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 867..889
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 890..901
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 902..919
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 920..933
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 934..956
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 957..968
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 969..988
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 989..1007
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 1008..1030
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1031..1049
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 1050..1072
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1073..1081
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 1082..1104
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1105..1447
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 35..124
FT /note="SUEL-type lectin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00260"
FT DOMAIN 134..393
FT /note="Olfactomedin-like"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00446"
FT DOMAIN 802..853
FT /note="GPS"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00098"
FT REGION 249..279
FT /note="Interaction with FLRT3"
FT /evidence="ECO:0000269|PubMed:26235030"
FT REGION 426..473
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1123..1147
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1423..1447
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 430..473
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 264
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000269|PubMed:26235030,
FT ECO:0007744|PDB:5CMN"
FT BINDING 312
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000269|PubMed:26235030,
FT ECO:0007744|PDB:5CMN"
FT BINDING 313
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000269|PubMed:26235030,
FT ECO:0007744|PDB:5CMN"
FT BINDING 367
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000269|PubMed:26235030,
FT ECO:0007744|PDB:5CMN"
FT SITE 841..842
FT /note="Cleavage"
FT /evidence="ECO:0000250"
FT MOD_RES 1164
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q80TS3"
FT CARBOHYD 93
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 464
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 549
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 746
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 759
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 804
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 830
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1076
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 36..66
FT /evidence="ECO:0000269|PubMed:26235030,
FT ECO:0007744|PDB:5CMN"
FT DISULFID 45..123
FT /evidence="ECO:0000269|PubMed:26235030,
FT ECO:0007744|PDB:5CMN"
FT DISULFID 78..110
FT /evidence="ECO:0000269|PubMed:26235030,
FT ECO:0007744|PDB:5CMN"
FT DISULFID 91..97
FT /evidence="ECO:0000269|PubMed:26235030,
FT ECO:0007744|PDB:5CMN"
FT DISULFID 135..317
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00446,
FT ECO:0000269|PubMed:26235030, ECO:0007744|PDB:5CMN"
FT VAR_SEQ 623
FT /note="K -> KLQKRERSCRAYVQ (in isoform 2 and isoform 4)"
FT /evidence="ECO:0000303|Ref.1"
FT /id="VSP_010235"
FT VAR_SEQ 668..707
FT /note="ADNLLKTDIVRENTDNIKLEVARLSTEGNLEDLKFPENMG -> VLQVCLPV
FT REQSFLPFFSFFIFFFSFLPFIPLKFRLAKNK (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_010236"
FT VAR_SEQ 708..1447
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_010237"
FT VAR_SEQ 1050
FT /note="I -> INYEDNRPFI (in isoform 2 and isoform 4)"
FT /evidence="ECO:0000303|Ref.1"
FT /id="VSP_010238"
FT VAR_SEQ 1183..1218
FT /note="GLLNNARDTSVMDTLPLNGNHGNSYSIASGEYLSNC -> PYRETSMGVKLN
FT IAYQIGASEQCQGYKCHGYSTTEW (in isoform 2)"
FT /evidence="ECO:0000303|Ref.1"
FT /id="VSP_010239"
FT VAR_SEQ 1219..1447
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|Ref.1"
FT /id="VSP_010240"
FT VARIANT 247
FT /note="A -> S"
FT /evidence="ECO:0000269|PubMed:21184580"
FT /id="VAR_064477"
FT VARIANT 465
FT /note="R -> Q (in dbSNP:rs35106420)"
FT /evidence="ECO:0000269|PubMed:21184580"
FT /id="VAR_055934"
FT VARIANT 770
FT /note="T -> M"
FT /evidence="ECO:0000269|PubMed:21184580"
FT /id="VAR_064478"
FT VARIANT 915
FT /note="L -> V"
FT /evidence="ECO:0000269|PubMed:21184580"
FT /id="VAR_064479"
FT MUTAGEN 249..252
FT /note="YHDT->AHAA: Strongly reduces FLRT3 binding.
FT Abolishes FLRT3 binding; when associated with A-308."
FT /evidence="ECO:0000269|PubMed:26235030"
FT MUTAGEN 308
FT /note="R->A: Abolishes FLRT3 binding; when associated with
FT 249-A--A-252."
FT /evidence="ECO:0000269|PubMed:26235030"
FT STRAND 41..44
FT /evidence="ECO:0007829|PDB:6VHH"
FT STRAND 46..48
FT /evidence="ECO:0007829|PDB:6VHH"
FT STRAND 55..61
FT /evidence="ECO:0007829|PDB:6VHH"
FT STRAND 63..66
FT /evidence="ECO:0007829|PDB:6VHH"
FT HELIX 70..73
FT /evidence="ECO:0007829|PDB:6VHH"
FT HELIX 83..90
FT /evidence="ECO:0007829|PDB:6VHH"
FT STRAND 94..99
FT /evidence="ECO:0007829|PDB:6VHH"
FT TURN 103..105
FT /evidence="ECO:0007829|PDB:6VHH"
FT STRAND 116..121
FT /evidence="ECO:0007829|PDB:6VHH"
SQ SEQUENCE 1447 AA; 161812 MW; 54B7E7DBE516447A CRC64;
MWPSQLLIFM MLLAPIIHAF SRAPIPMAVV RRELSCESYP IELRCPGTDV IMIESANYGR
TDDKICDSDP AQMENIRCYL PDAYKIMSQR CNNRTQCAVV AGPDVFPDPC PGTYKYLEVQ
YECVPYKVEQ KVFLCPGLLK GVYQSEHLFE SDHQSGAWCK DPLQASDKIY YMPWTPYRTD
TLTEYSSKDD FIAGRPTTTY KLPHRVDGTG FVVYDGALFF NKERTRNIVK FDLRTRIKSG
EAIIANANYH DTSPYRWGGK SDIDLAVDEN GLWVIYATEQ NNGKIVISQL NPYTLRIEGT
WDTAYDKRSA SNAFMICGIL YVVKSVYEDD DNEATGNKID YIYNTDQSKD SLVDVPFPNS
YQYIAAVDYN PRDNLLYVWN NYHVVKYSLD FGPLDSRSGQ AHHGQVSYIS PPIHLDSELE
RPSVKDISTT GPLGMGSTTT STTLRTTTLS PGRSTTPSVS GRRNRSTSTP SPAVEVLDDM
TTHLPSASSQ IPALEESCEA VEAREIMWFK TRQGQIAKQP CPAGTIGVST YLCLAPDGIW
DPQGPDLSNC SSPWVNHITQ KLKSGETAAN IARELAEQTR NHLNAGDITY SVRAMDQLVG
LLDVQLRNLT PGGKDSAARS LNKAMVETVN NLLQPQALNA WRDLTTSDQL RAATMLLHTV
EESAFVLADN LLKTDIVREN TDNIKLEVAR LSTEGNLEDL KFPENMGHGS TIQLSANTLK
QNGRNGEIRV AFVLYNNLGP YLSTENASMK LGTEALSTNH SVIVNSPVIT AAINKEFSNK
VYLADPVVFT VKHIKQSEEN FNPNCSFWSY SKRTMTGYWS TQGCRLLTTN KTHTTCSCNH
LTNFAVLMAH VEVKHSDAVH DLLLDVITWV GILLSLVCLL ICIFTFCFFR GLQSDRNTIH
KNLCISLFVA ELLFLIGINR TDQPIACAVF AALLHFFFLA AFTWMFLEGV QLYIMLVEVF
ESEHSRRKYF YLVGYGMPAL IVAVSAAVDY RSYGTDKVCW LRLDTYFIWS FIGPATLIIM
LNVIFLGIAL YKMFHHTAIL KPESGCLDNI KSWVIGAIAL LCLLGLTWAF GLMYINESTV
IMAYLFTIFN SLQGMFIFIF HCVLQKKVRK EYGKCLRTHC CSGKSTESSI GSGKTSGSRT
PGRYSTGSQS RIRRMWNDTV RKQSESSFIT GDINSSASLN REGLLNNARD TSVMDTLPLN
GNHGNSYSIA SGEYLSNCVQ IIDRGYNHNE TALEKKILKE LTSNYIPSYL NNHERSSEQN
RNLMNKLVNN LGSGREDDAI VLDDATSFNH EESLGLELIH EESDAPLLPP RVYSTENHQP
HHYTRRRIPQ DHSESFFPLL TNEHTEDLQS PHRDSLYTSM PTLAGVAATE SVTTSTQTEP
PPAKCGDAED VYYKSMPNLG SRNHVHQLHT YYQLGRGSSD GFIVPPNKDG TPPEGSSKGP
AHLVTSL
