AGRL1_RAT
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 03-AUG-2022, entry version 176.
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 {ECO:0000312|RGD:620768},
GN Cl1 {ECO:0000303|PubMed:9830014}, Lphn1 {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), AND TISSUE
RP SPECIFICITY.
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, AND INTERACTION WITH
RP SYNTAXIN.
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 -!- 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.ENSRNOP00000042610; -.
DR GuidetoPHARMACOLOGY; 206; -.
DR MEROPS; P02.010; -.
DR GlyGen; O88917; 8 sites.
DR iPTMnet; O88917; -.
DR PhosphoSitePlus; O88917; -.
DR SwissPalm; O88917; -.
DR PaxDb; O88917; -.
DR PRIDE; O88917; -.
DR GeneID; 65096; -.
DR KEGG; rno:65096; -.
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; 388923at2759; -.
DR PhylomeDB; O88917; -.
DR PRO; PR:O88917; -.
DR Proteomes; UP000002494; Chromosome 19.
DR Bgee; ENSRNOG00000029134; Expressed in frontal cortex and 19 other tissues.
DR ExpressionAtlas; O88917; baseline and differential.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
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:0005887; C:integral component of plasma membrane; IBA:GO_Central.
DR GO; GO:0099056; C:integral component of presynaptic membrane; IDA:SynGO.
DR GO; GO:0043005; C:neuron projection; IDA:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR GO; GO:0014069; C:postsynaptic density; IDA:RGD.
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:0007420; P:brain development; IEP:RGD.
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 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; IPR031234; Latrophilin-1.
DR InterPro; IPR000922; Lectin_gal-bd_dom.
DR InterPro; IPR043159; Lectin_gal-bd_sf.
DR InterPro; IPR003112; Olfac-like_dom.
DR PANTHER; PTHR12011:SF62; PTHR12011:SF62; 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 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
