AGRL1_MOUSE
ID AGRL1_MOUSE Reviewed; 1466 AA.
AC Q80TR1; Q3UH90; Q7TNE5; Q80T49;
DT 26-APR-2004, integrated into UniProtKB/Swiss-Prot.
DT 09-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 171.
DE RecName: Full=Adhesion G protein-coupled receptor L1 {ECO:0000312|MGI:MGI:1929461};
DE AltName: Full=Calcium-independent alpha-latrotoxin receptor 1 {ECO:0000250|UniProtKB:O88917};
DE Short=CIRL-1 {ECO:0000250|UniProtKB:O88917};
DE AltName: Full=Latrophilin-1 {ECO:0000312|MGI:MGI:1929461};
DE AltName: Full=Lectomedin-2 {ECO:0000312|MGI:MGI:1929461};
DE Flags: Precursor;
GN Name=Adgrl1 {ECO:0000312|MGI:MGI:1929461};
GN Synonyms=Kiaa0821 {ECO:0000312|MGI:MGI:1929461},
GN Lec2 {ECO:0000312|MGI:MGI:1929461}, Lphn1 {ECO:0000312|MGI:MGI:1929461};
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC STRAIN=C57BL/6J; TISSUE=Brain;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 61-1466 (ISOFORM 1).
RC TISSUE=Brain;
RX PubMed=12693553; DOI=10.1093/dnares/10.1.35;
RA Okazaki N., Kikuno R., Ohara R., Inamoto S., Aizawa H., Yuasa S.,
RA Nakajima D., Nagase T., Ohara O., Koga H.;
RT "Prediction of the coding sequences of mouse homologues of KIAA gene: II.
RT The complete nucleotide sequences of 400 mouse KIAA-homologous cDNAs
RT identified by screening of terminal sequences of cDNA clones randomly
RT sampled from size-fractionated libraries.";
RL DNA Res. 10:35-48(2003).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 814-978.
RX PubMed=12679517; DOI=10.1073/pnas.0230374100;
RA Vassilatis D.K., Hohmann J.G., Zeng H., Li F., Ranchalis J.E.,
RA Mortrud M.T., Brown A., Rodriguez S.S., Weller J.R., Wright A.C.,
RA Bergmann J.E., Gaitanaris G.A.;
RT "The G protein-coupled receptor repertoires of human and mouse.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:4903-4908(2003).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1145-1466.
RC STRAIN=C57BL/6J; TISSUE=Brain;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1214; SER-1319; SER-1448 AND
RP SER-1465, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Lung, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [7]
RP INTERACTION WITH FLRT1; FLRT2 AND FLRT3.
RX PubMed=22405201; DOI=10.1016/j.neuron.2012.01.018;
RA O'Sullivan M.L., de Wit J., Savas J.N., Comoletti D., Otto-Hitt S.,
RA Yates J.R. III, Ghosh A.;
RT "FLRT proteins are endogenous latrophilin ligands and regulate excitatory
RT synapse development.";
RL Neuron 73:903-910(2012).
RN [8]
RP METHYLATION [LARGE SCALE ANALYSIS] AT ARG-1188, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain;
RX PubMed=24129315; DOI=10.1074/mcp.o113.027870;
RA Guo A., Gu H., Zhou J., Mulhern D., Wang Y., Lee K.A., Yang V., Aguiar M.,
RA Kornhauser J., Jia X., Ren J., Beausoleil S.A., Silva J.C., Vemulapalli V.,
RA Bedford M.T., Comb M.J.;
RT "Immunoaffinity enrichment and mass spectrometry analysis of protein
RT methylation.";
RL Mol. Cell. Proteomics 13:372-387(2014).
RN [9]
RP STRUCTURE BY NMR OF 29-132 IN COMPLEX WITH D-GALACTOSE AND L-RHAMNOSE,
RP GLYCOSYLATION AT ASN-98, MUTAGENESIS OF GLU-42 AND LYS-120, AND DISULFIDE
RP BONDS.
RX PubMed=18547526; DOI=10.1016/j.str.2008.02.020;
RA Vakonakis I., Langenhan T., Promel S., Russ A., Campbell I.D.;
RT "Solution structure and sugar-binding mechanism of mouse latrophilin-1 RBL:
RT a 7TM receptor-attached lectin-like domain.";
RL Structure 16:944-953(2008).
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 for TENM2 that mediates heterophilic synaptic cell-cell
CC contact and postsynaptic specialization. Receptor probably implicated
CC in the regulation of exocytosis (By similarity). {ECO:0000250}.
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 (By similarity). Interacts (via extracellular
CC domain) with FLRT1, FLRT2 and FLRT3 (via extracellular domain)
CC (PubMed:22405201). {ECO:0000250|UniProtKB:O88917,
CC ECO:0000269|PubMed:22405201}.
CC -!- SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. Cell
CC projection, axon {ECO:0000250|UniProtKB:O88917}. Cell projection,
CC growth cone {ECO:0000250|UniProtKB:O88917}. Synapse
CC {ECO:0000250|UniProtKB:O88917}. Presynaptic cell membrane
CC {ECO:0000250|UniProtKB:O88917}. Synapse, synaptosome
CC {ECO:0000250|UniProtKB:O88917}. Note=Colocalizes with TENM2 on the cell
CC surface, across intercellular junctions and on nerve terminals near
CC synaptic clefts. {ECO:0000250|UniProtKB:O88917}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q80TR1-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q80TR1-2; Sequence=VSP_022137;
CC -!- DOMAIN: The extracellular domain coupled to the a single transmembrane
CC region are sufficient for full responsiveness to alpha-latrotoxin.
CC {ECO:0000250}.
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:0000250|UniProtKB:O88917}.
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; AK147519; BAE27967.1; -; mRNA.
DR EMBL; AK122380; BAC65662.1; -; mRNA.
DR EMBL; AC156028; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AY255594; AAO85106.1; -; mRNA.
DR EMBL; BC055793; AAH55793.1; -; mRNA.
DR CCDS; CCDS52613.1; -. [Q80TR1-1]
DR RefSeq; NP_851382.2; NM_181039.2. [Q80TR1-1]
DR RefSeq; XP_006531189.1; XM_006531126.2. [Q80TR1-2]
DR RefSeq; XP_006531190.1; XM_006531127.2. [Q80TR1-2]
DR RefSeq; XP_006531191.1; XM_006531128.2. [Q80TR1-2]
DR PDB; 2JX9; NMR; -; A=29-131.
DR PDB; 2JXA; NMR; -; A=29-131.
DR PDB; 6SKA; X-ray; 3.86 A; D=35-391.
DR PDBsum; 2JX9; -.
DR PDBsum; 2JXA; -.
DR PDBsum; 6SKA; -.
DR AlphaFoldDB; Q80TR1; -.
DR BMRB; Q80TR1; -.
DR SMR; Q80TR1; -.
DR BioGRID; 237029; 8.
DR IntAct; Q80TR1; 1.
DR MINT; Q80TR1; -.
DR STRING; 10090.ENSMUSP00000118452; -.
DR MEROPS; P02.010; -.
DR UniLectin; Q80TR1; -.
DR GlyConnect; 2111; 4 N-Linked glycans (2 sites).
DR GlyGen; Q80TR1; 7 sites, 4 N-linked glycans (2 sites).
DR iPTMnet; Q80TR1; -.
DR PhosphoSitePlus; Q80TR1; -.
DR MaxQB; Q80TR1; -.
DR PaxDb; Q80TR1; -.
DR PeptideAtlas; Q80TR1; -.
DR PRIDE; Q80TR1; -.
DR ProteomicsDB; 282041; -. [Q80TR1-1]
DR ProteomicsDB; 282042; -. [Q80TR1-2]
DR Antibodypedia; 13625; 151 antibodies from 28 providers.
DR Ensembl; ENSMUST00000131717; ENSMUSP00000118579; ENSMUSG00000013033. [Q80TR1-2]
DR Ensembl; ENSMUST00000141158; ENSMUSP00000118452; ENSMUSG00000013033. [Q80TR1-1]
DR GeneID; 330814; -.
DR KEGG; mmu:330814; -.
DR UCSC; uc009mlh.2; mouse. [Q80TR1-1]
DR CTD; 22859; -.
DR MGI; MGI:1929461; Adgrl1.
DR VEuPathDB; HostDB:ENSMUSG00000013033; -.
DR eggNOG; KOG3545; Eukaryota.
DR eggNOG; KOG4193; Eukaryota.
DR eggNOG; KOG4729; Eukaryota.
DR GeneTree; ENSGT00940000159684; -.
DR InParanoid; Q80TR1; -.
DR OMA; EQSPPWA; -.
DR OrthoDB; 388923at2759; -.
DR PhylomeDB; Q80TR1; -.
DR TreeFam; TF351999; -.
DR BioGRID-ORCS; 330814; 5 hits in 72 CRISPR screens.
DR ChiTaRS; Adgrl1; mouse.
DR EvolutionaryTrace; Q80TR1; -.
DR PRO; PR:Q80TR1; -.
DR Proteomes; UP000000589; Chromosome 8.
DR RNAct; Q80TR1; protein.
DR Bgee; ENSMUSG00000013033; Expressed in CA3 field of hippocampus and 240 other tissues.
DR ExpressionAtlas; Q80TR1; baseline and differential.
DR Genevisible; Q80TR1; MM.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0030424; C:axon; ISS:UniProtKB.
DR GO; GO:0098978; C:glutamatergic synapse; ISO:MGI.
DR GO; GO:0030426; C:growth cone; ISS:UniProtKB.
DR GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
DR GO; GO:0099056; C:integral component of presynaptic membrane; ISO:MGI.
DR GO; GO:0043005; C:neuron projection; ISS:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
DR GO; GO:0014069; C:postsynaptic density; ISO:MGI.
DR GO; GO:0042734; C:presynaptic membrane; ISS:UniProtKB.
DR GO; GO:0045202; C:synapse; ISS:UniProtKB.
DR GO; GO:0030246; F:carbohydrate binding; IEA:UniProtKB-KW.
DR GO; GO:0050839; F:cell adhesion molecule binding; ISS:UniProtKB.
DR GO; GO:0004930; F:G protein-coupled receptor activity; ISO:MGI.
DR GO; GO:0016524; F:latrotoxin receptor activity; ISS:UniProtKB.
DR GO; GO:0015643; F:toxic substance binding; ISO:MGI.
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; ISS: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; ISS:UniProtKB.
DR GO; GO:0051965; P:positive regulation of synapse assembly; IDA:MGI.
DR GO; GO:0090129; P:positive regulation of synapse maturation; 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; 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 Disulfide bond; G-protein coupled receptor; Glycoprotein; Lectin; Membrane;
KW Methylation; Phosphoprotein; Receptor; Reference proteome; Signal; Synapse;
KW Synaptosome; Transducer; Transmembrane; Transmembrane helix.
FT SIGNAL 1..28
FT /evidence="ECO:0000255"
FT CHAIN 29..1466
FT /note="Adhesion G protein-coupled receptor L1"
FT /id="PRO_0000070342"
FT TOPO_DOM 29..852
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 853..873
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 874..887
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 888..908
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 909..914
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 915..935
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 936..958
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 959..979
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 980..996
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 997..1017
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1018..1044
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 1045..1065
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1066..1069
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 1070..1090
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1091..1466
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 134..393
FT /note="Olfactomedin-like"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00446"
FT DOMAIN 793..844
FT /note="GPS"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00098"
FT REGION 395..463
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1242..1267
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1288..1319
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1352..1421
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1443..1466
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 402..426
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1352..1370
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1396..1416
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:0007744|PDB:2JXA"
FT BINDING 117..120
FT /ligand="alpha-L-rhamnose"
FT /ligand_id="ChEBI:CHEBI:27907"
FT /evidence="ECO:0007744|PDB:2JXA"
FT SITE 832..833
FT /note="Cleavage; by autolysis"
FT /evidence="ECO:0000250|UniProtKB:O88917"
FT MOD_RES 1188
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES 1214
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1319
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1448
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1465
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT CARBOHYD 98
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:18547526"
FT CARBOHYD 526
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 635
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 736
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 795
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 800
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 821
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 41..71
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00446,
FT ECO:0000269|PubMed:18547526"
FT DISULFID 50..128
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00446,
FT ECO:0000269|PubMed:18547526"
FT DISULFID 83..115
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00446,
FT ECO:0000269|PubMed:18547526"
FT DISULFID 96..102
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00446,
FT ECO:0000269|PubMed:18547526"
FT DISULFID 135..317
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00446"
FT DISULFID 475..510
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00446"
FT DISULFID 498..527
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00446"
FT DISULFID 796..827
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00446"
FT DISULFID 815..829
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00446"
FT VAR_SEQ 1..171
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_022137"
FT MUTAGEN 42
FT /note="E->A,R: Abrogates L-rhamnose binding."
FT /evidence="ECO:0000269|PubMed:18547526"
FT MUTAGEN 42
FT /note="E->D,Q: 100-fold decreased affinity for L-rhamnose."
FT /evidence="ECO:0000269|PubMed:18547526"
FT MUTAGEN 120
FT /note="K->A,R: Abrogates L-rhamnose binding."
FT /evidence="ECO:0000269|PubMed:18547526"
FT STRAND 36..41
FT /evidence="ECO:0007829|PDB:2JX9"
FT STRAND 44..49
FT /evidence="ECO:0007829|PDB:2JX9"
FT STRAND 54..66
FT /evidence="ECO:0007829|PDB:2JX9"
FT STRAND 68..71
FT /evidence="ECO:0007829|PDB:2JX9"
FT HELIX 75..78
FT /evidence="ECO:0007829|PDB:2JX9"
FT HELIX 87..96
FT /evidence="ECO:0007829|PDB:2JX9"
FT STRAND 99..107
FT /evidence="ECO:0007829|PDB:2JX9"
FT HELIX 108..110
FT /evidence="ECO:0007829|PDB:2JX9"
FT STRAND 121..131
FT /evidence="ECO:0007829|PDB:2JX9"
SQ SEQUENCE 1466 AA; 161686 MW; 937199B072336C9E CRC64;
MARLAAALWS LCVTTVLVTS ATQGLSRAGL PFGLMRRELA CEGYPIELRC PGSDVIMVEN
ANYGRTDDKI CDADPFQMEN VQCYLPDAFK IMSQRCNNRT QCVVVAGSDA FPDPCPGTYK
YLEVQYDCVP YIFVCPGTLQ KVLEPTSTHE SEHQSGAWCK DPLQAGDRIY VMPWIPYRTD
TLTEYASWED YVAARHTTTY RLPNRVDGTG FVVYDGAVFY NKERTRNIVK YDLRTRIKSG
ETVINTANYH DTSPYRWGGK TDIDLAVDEN GLWVIYATEG NNGRLVVSQL NPYTLRFEGT
WETGYDKRSA SNAFMVCGVL YVLRSVYVDD DSEAAGNRVD YAFNTNANRE EPVSLAFPNP
YQFVSSVDYN PRDNQLYVWN NYFVVRYSLE FGPPDPSAGP ATSPPLSTTT TARPTPLTST
ASPAATTPLR RAPLTTHPVG AINQLGPDLP PATAPAPSTR RPPAPNLHVS PELFCEPREV
RRVQWPATQQ GMLVERPCPK GTRGIASFQC LPALGLWNPR GPDLSNCTSP WVNQVAQKIK
SGENAANIAS ELARHTRGSI YAGDVSSSVK LMEQLLDILD AQLQALRPIE RESAGKNYNK
MHKRERTCKD YIKAVVETVD NLLRPEALES WKDMNATEQV HTATMLLDVL EEGAFLLADN
VREPARFLAA KQNVVLEVTV LNTEGQVQEL VFPQEYPSEN SIQLSANTIK QNSRNGVVKV
VFILYNNLGL FLSTENATVK LAGEAGTGGP GGASLVVNSQ VIAASINKES SRVFLMDPVI
FTVAHLEAKN HFNANCSFWN YSERSMLGYW STQGCRLVES NKTHTTCACS HLTNFAVLMA
HREIYQGRIN ELLLSVITWV GIVISLVCLA ICISTFCFLR GLQTDRNTIH KNLCINLFLA
ELLFLVGIDK TQYEVACPIF AGLLHYFFLA AFSWLCLEGV HLYLLLVEVF ESEYSRTKYY
YLGGYCFPAL VVGIAAAIDY RSYGTEKACW LRVDNYFIWS FIGPVSFVIV VNLVFLMVTL
HKMIRSSSVL KPDSSRLDNI KSWALGAIAL LFLLGLTWAF GLLFINKESV VMAYLFTTFN
AFQGVFIFVF HCALQKKVHK EYSKCLRHSY CCIRSPPGGT HGSLKTSAMR SNTRYYTGTQ
SRIRRMWNDT VRKQTESSFM AGDINSTPTL NRGTMGNHLL TNPVLQPRGG TSPYNTLIAE
SVGFNPSSPP VFNSPGSYRE PKHPLGGREA CGMDTLPLNG NFNNSYSLRS GDFPPGDGGP
EPPRGRNLAD AAAFEKMIIS ELVHNNLRGA SGGAKGPPPE PPVPPVPGVS EDEAGGPGSA
DRAEIELLYK ALEEPLLLPR AQSVLYQSDL DESESCTAED GATSRPLSSP PGRDSLYASG
ANLRDSPSYP DSSPEGPNEA LPPPPPAPPG PPEIYYTSRP PALVARNPLQ GYYQVRRPSH
EGYLAAPSLE GPGPDGDGQM QLVTSL
