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   24-JAN-2024, entry version 173.
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}, LEC3
GN   {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   PDB; 7SF7; EM; 2.90 A; A=842-1138.
DR   PDB; 8DJG; X-ray; 2.65 A; E/F=24-126.
DR   PDBsum; 5CMN; -.
DR   PDBsum; 6VHH; -.
DR   PDBsum; 7SF7; -.
DR   PDBsum; 8DJG; -.
DR   AlphaFoldDB; Q9HAR2; -.
DR   EMDB; EMD-21205; -.
DR   EMDB; EMD-25076; -.
DR   SMR; Q9HAR2; -.
DR   BioGRID; 116882; 23.
DR   CORUM; Q9HAR2; -.
DR   DIP; DIP-56228N; -.
DR   IntAct; Q9HAR2; 13.
DR   STRING; 9606.ENSP00000422533; -.
DR   MEROPS; P02.011; -.
DR   TCDB; 9.A.14.6.8; the g-protein-coupled receptor (gpcr) family.
DR   UniLectin; Q9HAR2; -.
DR   GlyCosmos; Q9HAR2; 11 sites, 2 glycans.
DR   GlyGen; Q9HAR2; 14 sites, 4 O-linked glycans (6 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; 9606-ENSP00000422533; -.
DR   PeptideAtlas; Q9HAR2; -.
DR   ProteomicsDB; 19784; -.
DR   ProteomicsDB; 81420; -. [Q9HAR2-1]
DR   ProteomicsDB; 81421; -. [Q9HAR2-2]
DR   ProteomicsDB; 81422; -. [Q9HAR2-3]
DR   Pumba; Q9HAR2; -.
DR   Antibodypedia; 2755; 192 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   AGR; HGNC:20974; -.
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 1146 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 180 other cell types or tissues.
DR   ExpressionAtlas; Q9HAR2; baseline and differential.
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:0016020; C:membrane; TAS:GDB.
DR   GO; GO:0005886; C: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: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   CDD; cd16005; 7tmB2_Latrophilin-3; 1.
DR   CDD; cd22846; Gal_Rha_Lectin_LPHN3; 1.
DR   Gene3D; 1.25.40.610; -; 1.
DR   Gene3D; 2.60.120.740; -; 1.
DR   Gene3D; 2.60.220.50; -; 1.
DR   Gene3D; 4.10.1240.10; GPCR, family 2, extracellular hormone receptor domain; 1.
DR   Gene3D; 1.20.1070.10; Rhodopsin 7-helix transmembrane proteins; 1.
DR   InterPro; IPR032471; GAIN_dom_N.
DR   InterPro; IPR046338; GAIN_dom_sf.
DR   InterPro; IPR017981; GPCR_2-like_7TM.
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; IPR000922; Lectin_gal-bd_dom.
DR   InterPro; IPR043159; Lectin_gal-bd_sf.
DR   InterPro; IPR003112; Olfac-like_dom.
DR   PANTHER; PTHR12011:SF60; ADHESION G PROTEIN-COUPLED RECEPTOR L3; 1.
DR   PANTHER; PTHR12011; ADHESION G-PROTEIN COUPLED RECEPTOR; 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; PF02793; HRM; 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   SUPFAM; SSF81321; Family A G protein-coupled receptor-like; 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.
DR   Genevisible; Q9HAR2; HS.
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          31..36
FT                   /evidence="ECO:0007829|PDB:8DJG"
FT   STRAND          40..44
FT                   /evidence="ECO:0007829|PDB:8DJG"
FT   STRAND          46..48
FT                   /evidence="ECO:0007829|PDB:6VHH"
FT   STRAND          50..61
FT                   /evidence="ECO:0007829|PDB:8DJG"
FT   STRAND          63..66
FT                   /evidence="ECO:0007829|PDB:6VHH"
FT   HELIX           70..73
FT                   /evidence="ECO:0007829|PDB:8DJG"
FT   HELIX           83..91
FT                   /evidence="ECO:0007829|PDB:8DJG"
FT   STRAND          95..100
FT                   /evidence="ECO:0007829|PDB:8DJG"
FT   TURN            103..105
FT                   /evidence="ECO:0007829|PDB:8DJG"
FT   STRAND          116..124
FT                   /evidence="ECO:0007829|PDB:8DJG"
FT   TURN            845..848
FT                   /evidence="ECO:0007829|PDB:7SF7"
FT   HELIX           860..878
FT                   /evidence="ECO:0007829|PDB:7SF7"
FT   HELIX           881..888
FT                   /evidence="ECO:0007829|PDB:7SF7"
FT   STRAND          890..892
FT                   /evidence="ECO:0007829|PDB:7SF7"
FT   HELIX           897..916
FT                   /evidence="ECO:0007829|PDB:7SF7"
FT   STRAND          917..919
FT                   /evidence="ECO:0007829|PDB:7SF7"
FT   HELIX           924..956
FT                   /evidence="ECO:0007829|PDB:7SF7"
FT   HELIX           969..974
FT                   /evidence="ECO:0007829|PDB:7SF7"
FT   HELIX           977..988
FT                   /evidence="ECO:0007829|PDB:7SF7"
FT   STRAND          996..1000
FT                   /evidence="ECO:0007829|PDB:7SF7"
FT   TURN            1003..1006
FT                   /evidence="ECO:0007829|PDB:7SF7"
FT   HELIX           1009..1037
FT                   /evidence="ECO:0007829|PDB:7SF7"
FT   HELIX           1049..1053
FT                   /evidence="ECO:0007829|PDB:7SF7"
FT   HELIX           1054..1057
FT                   /evidence="ECO:0007829|PDB:7SF7"
FT   HELIX           1060..1064
FT                   /evidence="ECO:0007829|PDB:7SF7"
FT   HELIX           1066..1072
FT                   /evidence="ECO:0007829|PDB:7SF7"
FT   STRAND          1076..1078
FT                   /evidence="ECO:0007829|PDB:7SF7"
FT   HELIX           1081..1089
FT                   /evidence="ECO:0007829|PDB:7SF7"
FT   TURN            1090..1092
FT                   /evidence="ECO:0007829|PDB:7SF7"
FT   HELIX           1093..1101
FT                   /evidence="ECO:0007829|PDB:7SF7"
FT   HELIX           1106..1115
FT                   /evidence="ECO:0007829|PDB:7SF7"
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
//