ID   AGRL1_RAT               Reviewed;        1515 AA.
AC   O88917; O09026; O35818; O88916;
DT   26-APR-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1998, sequence version 1.
DT   24-JAN-2024, entry version 182.
DE   RecName: Full=Adhesion G protein-coupled receptor L1 {ECO:0000312|RGD:620768};
DE   AltName: Full=Calcium-independent alpha-latrotoxin receptor 1 {ECO:0000312|RGD:620768};
DE            Short=CIRL-1 {ECO:0000303|PubMed:9830014};
DE   AltName: Full=Latrophilin-1 {ECO:0000312|RGD:620768};
DE   Flags: Precursor;
GN   Name=Adgrl1 {ECO:0000312|RGD:620768};
GN   Synonyms=Cirl {ECO:0000303|PubMed:9830014}, Cirl1
GN   {ECO:0000312|RGD:620768}, Cl1 {ECO:0000303|PubMed:9830014}, Lphn1
GN   {ECO:0000312|RGD:620768};
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;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 2; 3 AND 4), TISSUE SPECIFICITY,
RP   AND FUNCTION.
RX   PubMed=9830014; DOI=10.1074/jbc.273.49.32715;
RA   Sugita S., Ichtchenko K., Khvotchev M., Suedhof T.C.;
RT   "Alpha-latrotoxin receptor CIRL/latrophilin 1 (CL1) defines an unusual
RT   family of ubiquitous G-protein-linked receptors. G-protein coupling not
RT   required for triggering exocytosis.";
RL   J. Biol. Chem. 273:32715-32724(1998).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 4), PROTEIN SEQUENCE OF N-TERMINUS,
RP   PROTEIN SEQUENCE OF 838-850, PROTEOLYTIC PROCESSING, INTERACTION WITH
RP   SYNTAXIN, AND FUNCTION.
RX   PubMed=9208860; DOI=10.1016/s0896-6273(00)80332-3;
RA   Krasnoperov V.G., Bittner M.A., Beavis R., Kuang Y., Salnikow K.V.,
RA   Chepurny O.G., Little A.R., Plotnikov A.N., Wu D., Holz R.W.,
RA   Petrenko A.G.;
RT   "Alpha-latrotoxin stimulates exocytosis by the interaction with a neuronal
RT   G-protein-coupled receptor.";
RL   Neuron 18:925-937(1997).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), AND PARTIAL PROTEIN SEQUENCE.
RX   PubMed=9261169; DOI=10.1074/jbc.272.34.21504;
RA   Lelianova V.G., Davletov B.A., Sterling A., Rahman M.A., Grishin E.V.,
RA   Totty N.F., Ushkaryov Y.A.;
RT   "Alpha-latrotoxin receptor, latrophilin, is a novel member of the secretin
RT   family of G protein-coupled receptors.";
RL   J. Biol. Chem. 272:21504-21508(1997).
RN   [4]
RP   CHARACTERIZATION (ISOFORM 2).
RC   STRAIN=Sprague-Dawley; TISSUE=Brain;
RX   PubMed=8798521; DOI=10.1074/jbc.271.38.23239;
RA   Davletov B.A., Shamotienko O.G., Lelianova V.G., Grishin E.V.,
RA   Ushkaryov Y.A.;
RT   "Isolation and biochemical characterization of a Ca2+-independent alpha-
RT   latrotoxin-binding protein.";
RL   J. Biol. Chem. 271:23239-23245(1996).
RN   [5]
RP   CHARACTERIZATION.
RX   PubMed=9920906; DOI=10.1074/jbc.274.6.3590;
RA   Krasnoperov V., Bittner M.A., Holz R.W., Chepurny O., Petrenko A.G.;
RT   "Structural requirements for alpha-latrotoxin binding and alpha-latrotoxin-
RT   stimulated secretion. A study with calcium-independent receptor of alpha-
RT   latrotoxin (CIRL) deletion mutants.";
RL   J. Biol. Chem. 274:3590-3596(1999).
RN   [6]
RP   INTERACTION WITH PROTEINS OF THE SHANK FAMILY.
RX   PubMed=10958799; DOI=10.1074/jbc.m006448200;
RA   Tobaben S., Suedhof T.C., Stahl B.;
RT   "The G protein-coupled receptor CL1 interacts directly with proteins of the
RT   Shank family.";
RL   J. Biol. Chem. 275:36204-36210(2000).
RN   [7]
RP   MUTAGENESIS OF TRP-815; CYS-834 AND THR-838.
RX   PubMed=12270923; DOI=10.1074/jbc.m206415200;
RA   Krasnoperov V., Lu Y., Buryanovsky L., Neubert T.A., Ichtchenko K.,
RA   Petrenko A.G.;
RT   "Post-translational proteolytic processing of the calcium-independent
RT   receptor of alpha-latrotoxin (CIRL), a natural chimera of the cell adhesion
RT   protein and the G protein-coupled receptor. Role of the G protein-coupled
RT   receptor proteolysis site (GPS) motif.";
RL   J. Biol. Chem. 277:46518-46526(2002).
RN   [8]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=16641100; DOI=10.1073/pnas.0600895103;
RA   Hoffert J.D., Pisitkun T., Wang G., Shen R.-F., Knepper M.A.;
RT   "Quantitative phosphoproteomics of vasopressin-sensitive renal cells:
RT   regulation of aquaporin-2 phosphorylation at two sites.";
RL   Proc. Natl. Acad. Sci. U.S.A. 103:7159-7164(2006).
RN   [9]
RP   TENM2 LIGAND-BINDING, INTERACTION WITH TENM2, SUBCELLULAR LOCATION, AND
RP   TISSUE SPECIFICITY.
RX   PubMed=21724987; DOI=10.1073/pnas.1019434108;
RA   Silva J.P., Lelianova V.G., Ermolyuk Y.S., Vysokov N., Hitchen P.G.,
RA   Berninghausen O., Rahman M.A., Zangrandi A., Fidalgo S., Tonevitsky A.G.,
RA   Dell A., Volynski K.E., Ushkaryov Y.A.;
RT   "Latrophilin 1 and its endogenous ligand Lasso/teneurin-2 form a high-
RT   affinity transsynaptic receptor pair with signaling capabilities.";
RL   Proc. Natl. Acad. Sci. U.S.A. 108:12113-12118(2011).
RN   [10]
RP   X-RAY CRYSTALLOGRAPHY (1.85 ANGSTROMS) OF 460-850, GLYCOSYLATION AT
RP   ASN-531; ASN-640; ASN-741; ASN-800 AND ASN-826, DISULFIDE BONDS,
RP   SUBCELLULAR LOCATION, MUTAGENESIS OF SER-802; TRP-804; CYS-834; HIS-836;
RP   LEU-837; THR-838 AND PHE-840, AND AUTOCATALYTIC PROCESSING.
RX   PubMed=22333914; DOI=10.1038/emboj.2012.26;
RA   Arac D., Boucard A.A., Bolliger M.F., Nguyen J., Soltis S.M., Sudhof T.C.,
RA   Brunger A.T.;
RT   "A novel evolutionarily conserved domain of cell-adhesion GPCRs mediates
RT   autoproteolysis.";
RL   EMBO J. 31:1364-1378(2012).
CC   -!- FUNCTION: Calcium-independent receptor of high affinity for alpha-
CC       latrotoxin, an excitatory neurotoxin present in black widow spider
CC       venom which triggers massive exocytosis from neurons and neuroendocrine
CC       cells. Receptor probably implicated in the regulation of exocytosis.
CC       {ECO:0000269|PubMed:9208860, ECO:0000269|PubMed:9830014}.
CC   -!- FUNCTION: [Isoform 2]: Receptor for TENM2 that mediates heterophilic
CC       synaptic cell-cell contact and postsynaptic specialization.
CC   -!- SUBUNIT: Forms a heterodimer, consisting of a large extracellular
CC       region (p120) non-covalently linked to a seven-transmembrane moiety
CC       (p85). Interacts with syntaxin and with proteins of the SHANK family
CC       via the PDZ domain (PubMed:9208860, PubMed:10958799). Isoform 2
CC       interacts with TENM2 (PubMed:21724987). Interacts (via extracellular
CC       domain) with FLRT1, FLRT2 and FLRT3 (via extracellular domain) (By
CC       similarity). {ECO:0000250|UniProtKB:Q80TR1,
CC       ECO:0000269|PubMed:10958799, ECO:0000269|PubMed:21724987,
CC       ECO:0000269|PubMed:9208860}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:21724987,
CC       ECO:0000269|PubMed:22333914}; Multi-pass membrane protein
CC       {ECO:0000269|PubMed:21724987, ECO:0000269|PubMed:22333914}.
CC   -!- SUBCELLULAR LOCATION: [Isoform 2]: Cell membrane. Cell projection,
CC       axon. Cell projection, growth cone. Synapse. Presynaptic cell membrane.
CC       Synapse, synaptosome. Note=Colocalizes with TENM2 on the cell surface,
CC       across intercellular junctions and on nerve terminals near synaptic
CC       clefts.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=4;
CC       Name=1; Synonyms=CL1BB;
CC         IsoId=O88917-1; Sequence=Displayed;
CC       Name=2; Synonyms=CL1AA;
CC         IsoId=O88917-2; Sequence=VSP_050398, VSP_050399;
CC       Name=3; Synonyms=CL1AB;
CC         IsoId=O88917-3; Sequence=VSP_050398;
CC       Name=4; Synonyms=CL1BA;
CC         IsoId=O88917-4; Sequence=VSP_050399;
CC   -!- TISSUE SPECIFICITY: Expressed in the brain (at protein level). Brain
CC       specific distribution but low levels are also detected in most tissues.
CC       {ECO:0000269|PubMed:21724987, ECO:0000269|PubMed:9830014}.
CC   -!- DOMAIN: The extracellular domain coupled to the a single transmembrane
CC       region are sufficient for full responsiveness to alpha-latrotoxin.
CC   -!- PTM: Autoproteolytically cleaved into 2 subunits, an extracellular
CC       subunit and a seven-transmembrane subunit. This proteolytic processing
CC       takes place early in the biosynthetic pathway, either in the
CC       endoplasmic reticulum or in the early compartment of the Golgi
CC       apparatus. {ECO:0000269|PubMed:9208860}.
CC   -!- SIMILARITY: Belongs to the G-protein coupled receptor 2 family.
CC       Adhesion G-protein coupled receptor (ADGR) subfamily. {ECO:0000305}.
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DR   EMBL; AF081144; AAC62650.1; -; mRNA.
DR   EMBL; AF081145; AAC62651.1; -; mRNA.
DR   EMBL; AF081146; AAC62652.1; -; mRNA.
DR   EMBL; AF081147; AAC62653.1; -; mRNA.
DR   EMBL; U72487; AAC53268.1; -; mRNA.
DR   EMBL; U78105; AAC98700.1; -; mRNA.
DR   PIR; T17138; T17138.
DR   PIR; T17145; T17145.
DR   PIR; T17149; T17149.
DR   PIR; T17156; T17156.
DR   RefSeq; NP_075251.1; NM_022962.1. [O88917-4]
DR   PDB; 4DLQ; X-ray; 1.85 A; A=460-837, B=838-850.
DR   PDB; 5OVP; X-ray; 1.50 A; B=1510-1515.
DR   PDBsum; 4DLQ; -.
DR   PDBsum; 5OVP; -.
DR   AlphaFoldDB; O88917; -.
DR   BMRB; O88917; -.
DR   SMR; O88917; -.
DR   BioGRID; 249249; 2.
DR   IntAct; O88917; 1.
DR   MINT; O88917; -.
DR   STRING; 10116.ENSRNOP00000045873; -.
DR   GuidetoPHARMACOLOGY; 206; -.
DR   MEROPS; P02.010; -.
DR   GlyCosmos; O88917; 7 sites, No reported glycans.
DR   GlyGen; O88917; 8 sites.
DR   iPTMnet; O88917; -.
DR   PhosphoSitePlus; O88917; -.
DR   SwissPalm; O88917; -.
DR   PaxDb; 10116-ENSRNOP00000042610; -.
DR   GeneID; 65096; -.
DR   KEGG; rno:65096; -.
DR   AGR; RGD:620768; -.
DR   CTD; 22859; -.
DR   RGD; 620768; Adgrl1.
DR   VEuPathDB; HostDB:ENSRNOG00000029134; -.
DR   eggNOG; KOG3545; Eukaryota.
DR   eggNOG; KOG4193; Eukaryota.
DR   eggNOG; KOG4729; Eukaryota.
DR   InParanoid; O88917; -.
DR   OrthoDB; 1114672at2759; -.
DR   PhylomeDB; O88917; -.
DR   PRO; PR:O88917; -.
DR   Proteomes; UP000002494; Chromosome 19.
DR   Bgee; ENSRNOG00000029134; Expressed in frontal cortex and 19 other cell types or tissues.
DR   ExpressionAtlas; O88917; baseline and differential.
DR   GO; GO:0030424; C:axon; IDA:UniProtKB.
DR   GO; GO:0098978; C:glutamatergic synapse; IDA:SynGO.
DR   GO; GO:0030426; C:growth cone; IDA:UniProtKB.
DR   GO; GO:0043005; C:neuron projection; IDA:UniProtKB.
DR   GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR   GO; GO:0042734; C:presynaptic membrane; IDA:UniProtKB.
DR   GO; GO:0045202; C:synapse; IDA:UniProtKB.
DR   GO; GO:0030246; F:carbohydrate binding; IEA:UniProtKB-KW.
DR   GO; GO:0050839; F:cell adhesion molecule binding; IDA:UniProtKB.
DR   GO; GO:0004930; F:G protein-coupled receptor activity; IDA:RGD.
DR   GO; GO:0016524; F:latrotoxin receptor activity; IDA:UniProtKB.
DR   GO; GO:0015643; F:toxic substance binding; IPI:RGD.
DR   GO; GO:0007189; P:adenylate cyclase-activating G protein-coupled receptor signaling pathway; IBA:GO_Central.
DR   GO; GO:0035584; P:calcium-mediated signaling using intracellular calcium source; IDA:UniProtKB.
DR   GO; GO:0007166; P:cell surface receptor signaling pathway; IEA:InterPro.
DR   GO; GO:0007157; P:heterophilic cell-cell adhesion via plasma membrane cell adhesion molecules; IDA:UniProtKB.
DR   GO; GO:0051965; P:positive regulation of synapse assembly; ISO:RGD.
DR   GO; GO:0090129; P:positive regulation of synapse maturation; IDA:UniProtKB.
DR   CDD; cd16007; 7tmB2_Latrophilin-1; 1.
DR   CDD; cd22844; Gal_Rha_Lectin_LPHN1; 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; IPR031234; Latrophilin-1_TM.
DR   InterPro; IPR000922; Lectin_gal-bd_dom.
DR   InterPro; IPR043159; Lectin_gal-bd_sf.
DR   InterPro; IPR003112; Olfac-like_dom.
DR   PANTHER; PTHR12011:SF62; ADHESION G PROTEIN-COUPLED RECEPTOR L1; 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; 1.
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.
PE   1: Evidence at protein level;
KW   3D-structure; Alternative splicing; Cell membrane; Cell projection;
KW   Direct protein sequencing; Disulfide bond; G-protein coupled receptor;
KW   Glycoprotein; Lectin; Membrane; Methylation; Phosphoprotein; Receptor;
KW   Reference proteome; Signal; Synapse; Synaptosome; Transducer;
KW   Transmembrane; Transmembrane helix.
FT   SIGNAL          1..24
FT                   /evidence="ECO:0000269|PubMed:9208860"
FT   CHAIN           25..1515
FT                   /note="Adhesion G protein-coupled receptor L1"
FT                   /id="PRO_0000012908"
FT   TOPO_DOM        25..857
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        858..878
FT                   /note="Helical; Name=1"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        879..892
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        893..913
FT                   /note="Helical; Name=2"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        914..919
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        920..940
FT                   /note="Helical; Name=3"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        941..964
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        965..985
FT                   /note="Helical; Name=4"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        986..1001
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        1002..1022
FT                   /note="Helical; Name=5"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        1023..1049
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        1050..1070
FT                   /note="Helical; Name=6"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        1071..1074
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        1075..1095
FT                   /note="Helical; Name=7"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        1096..1515
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          40..129
FT                   /note="SUEL-type lectin"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00260"
FT   DOMAIN          139..398
FT                   /note="Olfactomedin-like"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00446"
FT   DOMAIN          798..849
FT                   /note="GPS"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00098"
FT   REGION          400..468
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1144..1184
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1291..1316
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1337..1369
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1401..1470
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1492..1515
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        407..431
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1401..1419
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1445..1465
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         42
FT                   /ligand="alpha-L-rhamnose"
FT                   /ligand_id="ChEBI:CHEBI:27907"
FT                   /evidence="ECO:0000250|UniProtKB:Q80TR1"
FT   BINDING         117..120
FT                   /ligand="alpha-L-rhamnose"
FT                   /ligand_id="ChEBI:CHEBI:27907"
FT                   /evidence="ECO:0000250|UniProtKB:Q80TR1"
FT   SITE            837..838
FT                   /note="Cleavage; by autolysis"
FT                   /evidence="ECO:0000269|PubMed:12270923,
FT                   ECO:0000269|PubMed:22333914, ECO:0000269|PubMed:9208860"
FT   MOD_RES         1237
FT                   /note="Omega-N-methylarginine"
FT                   /evidence="ECO:0000250|UniProtKB:Q80TR1"
FT   MOD_RES         1263
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q80TR1"
FT   MOD_RES         1497
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q80TR1"
FT   MOD_RES         1514
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q80TR1"
FT   CARBOHYD        98
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        531
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000269|PubMed:22333914"
FT   CARBOHYD        640
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000269|PubMed:22333914"
FT   CARBOHYD        741
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000269|PubMed:22333914"
FT   CARBOHYD        800
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000269|PubMed:22333914"
FT   CARBOHYD        805
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        826
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000269|PubMed:22333914"
FT   DISULFID        41..71
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00446"
FT   DISULFID        50..128
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00446"
FT   DISULFID        83..115
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00446"
FT   DISULFID        96..102
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00446"
FT   DISULFID        140..322
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00446"
FT   DISULFID        480..515
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00446,
FT                   ECO:0000269|PubMed:22333914"
FT   DISULFID        503..532
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00446,
FT                   ECO:0000269|PubMed:22333914"
FT   DISULFID        801..832
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00446,
FT                   ECO:0000269|PubMed:22333914"
FT   DISULFID        820..834
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00446,
FT                   ECO:0000269|PubMed:22333914"
FT   VAR_SEQ         132..137
FT                   /note="KVEQKV -> I (in isoform 2 and isoform 3)"
FT                   /evidence="ECO:0000303|PubMed:9261169,
FT                   ECO:0000303|PubMed:9830014"
FT                   /id="VSP_050398"
FT   VAR_SEQ         1146..1189
FT                   /note="Missing (in isoform 2 and isoform 4)"
FT                   /evidence="ECO:0000303|PubMed:9208860,
FT                   ECO:0000303|PubMed:9261169, ECO:0000303|PubMed:9830014"
FT                   /id="VSP_050399"
FT   MUTAGEN         802
FT                   /note="S->R: Strongly reduced cleavage."
FT                   /evidence="ECO:0000269|PubMed:22333914"
FT   MUTAGEN         804
FT                   /note="W->I: Abolishes cleavage."
FT                   /evidence="ECO:0000269|PubMed:22333914"
FT   MUTAGEN         815
FT                   /note="W->S: Abolishes cleavage. Abolishes cell surface
FT                   localization."
FT                   /evidence="ECO:0000269|PubMed:12270923"
FT   MUTAGEN         834
FT                   /note="C->S: Strongly reduced cleavage."
FT                   /evidence="ECO:0000269|PubMed:12270923,
FT                   ECO:0000269|PubMed:22333914"
FT   MUTAGEN         834
FT                   /note="C->W: Abolishes cleavage. Abolishes cell surface
FT                   localization."
FT                   /evidence="ECO:0000269|PubMed:12270923,
FT                   ECO:0000269|PubMed:22333914"
FT   MUTAGEN         836
FT                   /note="H->S: Abolishes cleavage. No effect on cell surface
FT                   localization."
FT                   /evidence="ECO:0000269|PubMed:22333914"
FT   MUTAGEN         837
FT                   /note="L->A: Abolishes cleavage. No effect on cell surface
FT                   localization."
FT                   /evidence="ECO:0000269|PubMed:22333914"
FT   MUTAGEN         838
FT                   /note="T->G: Abolishes cleavage. No effect on cell surface
FT                   localization."
FT                   /evidence="ECO:0000269|PubMed:12270923,
FT                   ECO:0000269|PubMed:22333914"
FT   MUTAGEN         838
FT                   /note="T->P: Abolishes cleavage. Abolishes cell surface
FT                   localization."
FT                   /evidence="ECO:0000269|PubMed:12270923,
FT                   ECO:0000269|PubMed:22333914"
FT   MUTAGEN         840
FT                   /note="F->A: Strongly reduced cleavage."
FT                   /evidence="ECO:0000269|PubMed:22333914"
FT   STRAND          483..485
FT                   /evidence="ECO:0007829|PDB:4DLQ"
FT   STRAND          488..490
FT                   /evidence="ECO:0007829|PDB:4DLQ"
FT   STRAND          498..502
FT                   /evidence="ECO:0007829|PDB:4DLQ"
FT   STRAND          508..515
FT                   /evidence="ECO:0007829|PDB:4DLQ"
FT   TURN            517..519
FT                   /evidence="ECO:0007829|PDB:4DLQ"
FT   HELIX           536..545
FT                   /evidence="ECO:0007829|PDB:4DLQ"
FT   HELIX           550..560
FT                   /evidence="ECO:0007829|PDB:4DLQ"
FT   HELIX           567..590
FT                   /evidence="ECO:0007829|PDB:4DLQ"
FT   HELIX           605..627
FT                   /evidence="ECO:0007829|PDB:4DLQ"
FT   HELIX           630..632
FT                   /evidence="ECO:0007829|PDB:4DLQ"
FT   HELIX           633..636
FT                   /evidence="ECO:0007829|PDB:4DLQ"
FT   HELIX           641..663
FT                   /evidence="ECO:0007829|PDB:4DLQ"
FT   STRAND          668..675
FT                   /evidence="ECO:0007829|PDB:4DLQ"
FT   STRAND          677..687
FT                   /evidence="ECO:0007829|PDB:4DLQ"
FT   STRAND          695..697
FT                   /evidence="ECO:0007829|PDB:4DLQ"
FT   STRAND          704..709
FT                   /evidence="ECO:0007829|PDB:4DLQ"
FT   HELIX           711..716
FT                   /evidence="ECO:0007829|PDB:4DLQ"
FT   STRAND          722..732
FT                   /evidence="ECO:0007829|PDB:4DLQ"
FT   HELIX           733..736
FT                   /evidence="ECO:0007829|PDB:4DLQ"
FT   STRAND          759..762
FT                   /evidence="ECO:0007829|PDB:4DLQ"
FT   STRAND          766..773
FT                   /evidence="ECO:0007829|PDB:4DLQ"
FT   STRAND          779..789
FT                   /evidence="ECO:0007829|PDB:4DLQ"
FT   STRAND          796..806
FT                   /evidence="ECO:0007829|PDB:4DLQ"
FT   TURN            808..810
FT                   /evidence="ECO:0007829|PDB:4DLQ"
FT   STRAND          813..816
FT                   /evidence="ECO:0007829|PDB:4DLQ"
FT   STRAND          820..825
FT                   /evidence="ECO:0007829|PDB:4DLQ"
FT   STRAND          827..836
FT                   /evidence="ECO:0007829|PDB:4DLQ"
FT   STRAND          839..847
FT                   /evidence="ECO:0007829|PDB:4DLQ"
FT   STRAND          1511..1514
FT                   /evidence="ECO:0007829|PDB:5OVP"
SQ   SEQUENCE   1515 AA;  166615 MW;  0BF3B900C54F17B7 CRC64;
     MARLAAALWS LCVTTVLVTS ATQGLSRAGL PFGLMRRELA CEGYPIELRC PGSDVIMVEN
     ANYGRTDDKI CDADPFQMEN VQCYLPDAFK IMSQRCNNRT QCVVVAGSDA FPDPCPGTYK
     YLEVQYDCVP YKVEQKVFVC PGTLQKVLEP TSTHESEHQS GAWCKDPLQA GDRIYVMPWI
     PYRTDTLTEY ASWEDYVAAR HTTTYRLPNR VDGTGFVVYD GAVFYNKERT RNIVKYDLRT
     RIKSGETVIN TANYHDTSPY RWGGKTDIDL AVDENGLWVI YATEGNNGRL VVSQLNPYTL
     RFEGTWETGY DKRSASNAFM VCGVLYVLRS VYVDDDSEAA GNRVDYAFNT NANREEPVSL
     AFPNPYQFVS SVDYNPRDNQ LYVWNNYFVV RYSLEFGPPD PSAGPATSPP LSTTTTARPT
     PLTSTASPAA TTPLRRAPLT THPVGAINQL GPDLPPATAP APSTRRPPAP NLHVSPELFC
     EPREVRRVQW PATQQGMLVE RPCPKGTRGI ASFQCLPALG LWNPRGPDLS NCTSPWVNQV
     AQKIKSGENA ANIASELARH TRGSIYAGDV SSSVKLMEQL LDILDAQLQA LRPIERESAG
     KNYNKMHKRE RTCKDYIKAV VETVDNLLRP EALESWKDMN ATEQVHTATM LLDVLEEGAF
     LLADNVREPA RFLAAKQNVV LEVTVLSTEG QVQELVFPQE YASESSIQLS ANTIKQNSRN
     GVVKVVFILY NNLGLFLSTE NATVKLAGEA GTGGPGGASL VVNSQVIAAS INKESSRVFL
     MDPVIFTVAH LEAKNHFNAN CSFWNYSERS MLGYWSTQGC RLVESNKTHT TCACSHLTNF
     AVLMAHREIY QGRINELLLS VITWVGIVIS LVCLAICIST FCFLRGLQTD RNTIHKNLCI
     NLFLAELLFL VGIDKTQYEV ACPIFAGLLH YFFLAAFSWL CLEGVHLYLL LVEVFESEYS
     RTKYYYLGGY CFPALVVGIA AAIDYRSYGT EKACWLRVDN YFIWSFIGPV SFVIVVNLVF
     LMVTLHKMIR SSSVLKPDSS RLDNIKSWAL GAIALLFLLG LTWAFGLLFI NKESVVMAYL
     FTTFNAFQGV FIFVFHCALQ KKVHKEYSKC LRHSYCCIRS PPGGAHGSLK TSAMRSNTRY
     YTGTQVPGQG RHIHQVSLGP RGRSALPESQ KDPGGQSGPG DPLTFGLCPS RIRRMWNDTV
     RKQTESSFMA GDINSTPTLN RGTMGNHLLT NPVLQPRGGT SPYNTLIAES VGFNPSSPPV
     FNSPGSYREP KHPLGGREAC GMDTLPLNGN FNNSYSLRSG DFPPGDGGPE PPRGRNLADA
     AAFEKMIISE LVHNNLRGAS GGAKGPPPEP PVPPVPGVSE DEAGGPGGAD RAEIELLYKA
     LEEPLLLPRA QSVLYQSDLD ESESCTAEDG ATSRPLSSPP GRDSLYASGA NLRDSPSYPD
     SSPEGPNEAL PPPPPAPPGP PEIYYTSRPP ALVARNPLQG YYQVRRPSHE GYLAAPSLEG
     PGPDGDGQMQ LVTSL
//