RGI2_ARATH
ID RGI2_ARATH Reviewed; 1135 AA.
AC C0LGV1; Q84RP6; Q9FI77;
DT 03-NOV-2009, integrated into UniProtKB/Swiss-Prot.
DT 05-MAY-2009, sequence version 1.
DT 03-AUG-2022, entry version 92.
DE RecName: Full=LRR receptor-like serine/threonine-protein kinase RGI2 {ECO:0000303|PubMed:27229312};
DE EC=2.7.11.1 {ECO:0000255|PROSITE-ProRule:PRU00159};
DE AltName: Full=Protein RECEPTOR OF RGF1 3 {ECO:0000303|PubMed:27229311};
DE AltName: Full=Protein RGF1 INSENSITIVE 2 {ECO:0000303|PubMed:27229312};
DE AltName: Full=Protein ROOT CLAVATA-HOMOLOG1 1 {ECO:0000303|PubMed:12932329};
DE Flags: Precursor;
GN Name=RGI2 {ECO:0000303|PubMed:27229312};
GN Synonyms=RCH1 {ECO:0000303|PubMed:12932329},
GN RGFR2 {ECO:0000303|PubMed:27001831, ECO:0000303|PubMed:29339500},
GN RGFR3 {ECO:0000303|PubMed:27229311};
GN OrderedLocusNames=At5g48940 {ECO:0000312|Araport:AT5G48940};
GN ORFNames=K19E20.5 {ECO:0000312|EMBL:BAB10317.1};
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=12932329; DOI=10.1016/s0960-9822(03)00533-5;
RA Casamitjana-Martinez E., Hofhuis H.F., Xu J., Liu C.-M., Heidstra R.,
RA Scheres B.;
RT "Root-specific CLE19 overexpression and the sol1/2 suppressors implicate a
RT CLV-like pathway in the control of Arabidopsis root meristem maintenance.";
RL Curr. Biol. 13:1435-1441(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10470850; DOI=10.1093/dnares/6.3.183;
RA Kaneko T., Katoh T., Sato S., Nakamura Y., Asamizu E., Kotani H.,
RA Miyajima N., Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. IX. Sequence
RT features of the regions of 1,011,550 bp covered by seventeen P1 and TAC
RT clones.";
RL DNA Res. 6:183-195(1999).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
RX PubMed=27862469; DOI=10.1111/tpj.13415;
RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA Town C.D.;
RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT genome.";
RL Plant J. 89:789-804(2017).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=20064227; DOI=10.1186/1471-2164-11-19;
RA Gou X., He K., Yang H., Yuan T., Lin H., Clouse S.D., Li J.;
RT "Genome-wide cloning and sequence analysis of leucine-rich repeat receptor-
RT like protein kinase genes in Arabidopsis thaliana.";
RL BMC Genomics 11:19-19(2010).
RN [5]
RP TISSUE SPECIFICITY.
RX PubMed=17363254; DOI=10.1016/j.cub.2007.02.047;
RA Dello Ioio R., Linhares F.S., Scacchi E., Casamitjana-Martinez E.,
RA Heidstra R., Costantino P., Sabatini S.;
RT "Cytokinins determine Arabidopsis root-meristem size by controlling cell
RT differentiation.";
RL Curr. Biol. 17:678-682(2007).
RN [6]
RP TISSUE SPECIFICITY.
RX PubMed=18980654; DOI=10.1111/j.1365-313x.2008.03715.x;
RA Atta R., Laurens L., Boucheron-Dubuisson E., Guivarc'h A., Carnero E.,
RA Giraudat-Pautot V., Rech P., Chriqui D.;
RT "Pluripotency of Arabidopsis xylem pericycle underlies shoot regeneration
RT from root and hypocotyl explants grown in vitro.";
RL Plant J. 57:626-644(2009).
RN [7]
RP FUNCTION, DISRUPTION PHENOTYPE, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE,
RP INTERACTION WITH RGF1, GENE FAMILY, AND NOMENCLATURE.
RC STRAIN=cv. Columbia;
RX PubMed=27229311; DOI=10.1038/cr.2016.62;
RA Song W., Liu L., Wang J., Wu Z., Zhang H., Tang J., Lin G., Wang Y.,
RA Wen X., Li W., Han Z., Guo H., Chai J.;
RT "Signature motif-guided identification of receptors for peptide hormones
RT essential for root meristem growth.";
RL Cell Res. 26:674-685(2016).
RN [8]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RC STRAIN=cv. Columbia;
RX PubMed=27229312; DOI=10.1038/cr.2016.63;
RA Ou Y., Lu X., Zi Q., Xun Q., Zhang J., Wu Y., Shi H., Wei Z., Zhao B.,
RA Zhang X., He K., Gou X., Li C., Li J.;
RT "RGF1 INSENSITIVE 1 to 5, a group of LRR receptor-like kinases, are
RT essential for the perception of root meristem growth factor 1 in
RT Arabidopsis thaliana.";
RL Cell Res. 26:686-698(2016).
RN [9]
RP FUNCTION, DISRUPTION PHENOTYPE, INTERACTION WITH RGF1; GLV5/CLEL1/RGF2;
RP GLV7/CLEL3/RGF3; GLV3/RGF4; GLV10/CLEL7/RGF5 AND RGF10/CLELN, TISSUE
RP SPECIFICITY, AND DEVELOPMENTAL STAGE.
RC STRAIN=cv. Columbia;
RX PubMed=27001831; DOI=10.1073/pnas.1522639113;
RA Shinohara H., Mori A., Yasue N., Sumida K., Matsubayashi Y.;
RT "Identification of three LRR-RKs involved in perception of root meristem
RT growth factor in Arabidopsis.";
RL Proc. Natl. Acad. Sci. U.S.A. 113:3897-3902(2016).
RN [10]
RP INTERACTION WITH UBP13.
RC STRAIN=cv. Columbia;
RX PubMed=29339500; DOI=10.1073/pnas.1714177115;
RA An Z., Liu Y., Ou Y., Li J., Zhang B., Sun D., Sun Y., Tang W.;
RT "Regulation of the stability of RGF1 receptor by the ubiquitin-specific
RT proteases UBP12/UBP13 is critical for root meristem maintenance.";
RL Proc. Natl. Acad. Sci. U.S.A. 115:1123-1128(2018).
CC -!- FUNCTION: Together with RGI1, RGI3, RGI4 and RGI5, acts as receptor of
CC RGF peptides (e.g. RGF1, GLV5/CLEL1/RGF2, GLV7/CLEL3/RGF3, GLV3/RGF4,
CC GLV10/CLEL7/RGF5 and RGF10/CLELN), peptide hormones which maintain the
CC postembryonic root stem cell niche by regulating the expression levels
CC and patterns of the transcription factor PLETHORA (PLT, e.g. PLT1 and
CC PLT2) (PubMed:27229312, PubMed:27229311, PubMed:27001831). Links RGF
CC peptides signal with their downstream components (PubMed:27229311,
CC PubMed:27001831). {ECO:0000269|PubMed:27001831,
CC ECO:0000269|PubMed:27229311, ECO:0000269|PubMed:27229312}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-
CC [protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-
CC COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.1;
CC Evidence={ECO:0000255|PROSITE-ProRule:PRU00159};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-
CC threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060,
CC Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216;
CC EC=2.7.11.1; Evidence={ECO:0000255|PROSITE-ProRule:PRU00159};
CC -!- SUBUNIT: Binds to RGF peptides such as RGF1, GLV5/CLEL1/RGF2,
CC GLV7/CLEL3/RGF3, GLV3/RGF4, GLV10/CLEL7/RGF5 and RGF10/CLELN; these
CC interactions trigger the formation of heterodimers with SERK1
CC (PubMed:27001831, PubMed:27229311). Interacts with UBP13
CC (PubMed:29339500). {ECO:0000269|PubMed:27001831,
CC ECO:0000269|PubMed:27229311, ECO:0000269|PubMed:29339500}.
CC -!- INTERACTION:
CC C0LGV1; Q9LJY0: PRK4; NbExp=2; IntAct=EBI-20664449, EBI-16914444;
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Single-pass type I
CC membrane protein {ECO:0000255}.
CC -!- TISSUE SPECIFICITY: Specific to root meristems, especially in lateral
CC root meristems (LRM). {ECO:0000269|PubMed:17363254,
CC ECO:0000269|PubMed:18980654, ECO:0000269|PubMed:27001831,
CC ECO:0000269|PubMed:27229311}.
CC -!- DEVELOPMENTAL STAGE: Present in the whole roots with a predominant
CC expression in the proximal meristem, including the elongation zone, and
CC a gradual decreases toward the differentiation zone.
CC {ECO:0000269|PubMed:27001831, ECO:0000269|PubMed:27229311}.
CC -!- PTM: Phosphorylated and ubiquitinated upon interaction with RGF1, thus
CC leading to activation a subsequent degradation (By similarity).
CC Stabilized by UBP12 and UBP13-mediated deubiquitination (By
CC similarity). {ECO:0000250|UniProtKB:Q9LHP4}.
CC -!- PTM: Autophosphorylated. {ECO:0000250|UniProtKB:O22476}.
CC -!- DISRUPTION PHENOTYPE: Smaller root meristem size and fewer root
CC meristematic cortex cells, associated with shorter roots and a slighty
CC reduced sensitivity to RGF1 (PubMed:27229311). Quintuple mutants rgi1
CC rgi2 rgi3 rgi4 rgi5 display a consistent short primary root phenotype
CC with a small size of meristem associated with a total insensitivity to
CC RGF1 and undetectable levels of PLT1 and PLT2 (PubMed:27229312). The
CC triple mutant missing RGI1, RGI2 and RGI3 is insensitive to externally
CC applied RGF peptides (e.g. RGF1 and RGF2) and has short roots
CC characterized by a strong decrease in meristematic cell number and
CC declined levels of PLT1 and PLT2 at the root tip (PubMed:27001831).
CC {ECO:0000269|PubMed:27001831, ECO:0000269|PubMed:27229311,
CC ECO:0000269|PubMed:27229312}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein
CC kinase family. {ECO:0000255|PROSITE-ProRule:PRU00159}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAB10317.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AJ550162; CAD79349.1; -; mRNA.
DR EMBL; AB017061; BAB10317.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002688; AED95745.1; -; Genomic_DNA.
DR EMBL; FJ708795; ACN59386.1; -; mRNA.
DR RefSeq; NP_199705.2; NM_124271.3.
DR AlphaFoldDB; C0LGV1; -.
DR SMR; C0LGV1; -.
DR BioGRID; 20198; 8.
DR IntAct; C0LGV1; 9.
DR STRING; 3702.AT5G48940.1; -.
DR PaxDb; C0LGV1; -.
DR PRIDE; C0LGV1; -.
DR ProteomicsDB; 225943; -.
DR EnsemblPlants; AT5G48940.1; AT5G48940.1; AT5G48940.
DR GeneID; 834952; -.
DR Gramene; AT5G48940.1; AT5G48940.1; AT5G48940.
DR KEGG; ath:AT5G48940; -.
DR Araport; AT5G48940; -.
DR TAIR; locus:2154344; AT5G48940.
DR eggNOG; ENOG502QQEU; Eukaryota.
DR HOGENOM; CLU_000288_22_1_1; -.
DR InParanoid; C0LGV1; -.
DR OMA; RANLDHG; -.
DR OrthoDB; 205337at2759; -.
DR PhylomeDB; C0LGV1; -.
DR PRO; PR:C0LGV1; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; C0LGV1; baseline and differential.
DR Genevisible; C0LGV1; AT.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0042277; F:peptide binding; IPI:UniProtKB.
DR GO; GO:0001653; F:peptide receptor activity; IMP:UniProtKB.
DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0010074; P:maintenance of meristem identity; IMP:UniProtKB.
DR GO; GO:0010078; P:maintenance of root meristem identity; IMP:UniProtKB.
DR GO; GO:0006468; P:protein phosphorylation; IEA:InterPro.
DR GO; GO:2000280; P:regulation of root development; IMP:UniProtKB.
DR GO; GO:0010082; P:regulation of root meristem growth; IGI:TAIR.
DR GO; GO:0010449; P:root meristem growth; IGI:TAIR.
DR Gene3D; 3.80.10.10; -; 4.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR001611; Leu-rich_rpt.
DR InterPro; IPR003591; Leu-rich_rpt_typical-subtyp.
DR InterPro; IPR032675; LRR_dom_sf.
DR InterPro; IPR013210; LRR_N_plant-typ.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR001245; Ser-Thr/Tyr_kinase_cat_dom.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR Pfam; PF13855; LRR_8; 4.
DR Pfam; PF08263; LRRNT_2; 1.
DR Pfam; PF07714; PK_Tyr_Ser-Thr; 1.
DR SMART; SM00369; LRR_TYP; 7.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF56112; SSF56112; 1.
DR PROSITE; PS51450; LRR; 13.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Disulfide bond; Glycoprotein; Kinase; Leucine-rich repeat;
KW Membrane; Nucleotide-binding; Phosphoprotein; Receptor; Reference proteome;
KW Repeat; Serine/threonine-protein kinase; Signal; Transferase;
KW Transmembrane; Transmembrane helix; Ubl conjugation.
FT SIGNAL 1..35
FT /evidence="ECO:0000255"
FT CHAIN 36..1135
FT /note="LRR receptor-like serine/threonine-protein kinase
FT RGI2"
FT /id="PRO_0000387518"
FT TOPO_DOM 36..723
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 724..744
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 745..1135
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REPEAT 105..129
FT /note="LRR 1"
FT /evidence="ECO:0000255"
FT REPEAT 130..153
FT /note="LRR 2"
FT /evidence="ECO:0000255"
FT REPEAT 154..177
FT /note="LRR 3"
FT /evidence="ECO:0000255"
FT REPEAT 179..203
FT /note="LRR 4"
FT /evidence="ECO:0000255"
FT REPEAT 226..250
FT /note="LRR 5"
FT /evidence="ECO:0000255"
FT REPEAT 251..274
FT /note="LRR 6"
FT /evidence="ECO:0000255"
FT REPEAT 276..298
FT /note="LRR 7"
FT /evidence="ECO:0000255"
FT REPEAT 299..323
FT /note="LRR 8"
FT /evidence="ECO:0000255"
FT REPEAT 325..345
FT /note="LRR 9"
FT /evidence="ECO:0000255"
FT REPEAT 346..370
FT /note="LRR 10"
FT /evidence="ECO:0000255"
FT REPEAT 372..395
FT /note="LRR 11"
FT /evidence="ECO:0000255"
FT REPEAT 397..418
FT /note="LRR 12"
FT /evidence="ECO:0000255"
FT REPEAT 419..442
FT /note="LRR 13"
FT /evidence="ECO:0000255"
FT REPEAT 444..466
FT /note="LRR 14"
FT /evidence="ECO:0000255"
FT REPEAT 467..490
FT /note="LRR 15"
FT /evidence="ECO:0000255"
FT REPEAT 491..514
FT /note="LRR 16"
FT /evidence="ECO:0000255"
FT REPEAT 516..538
FT /note="LRR 17"
FT /evidence="ECO:0000255"
FT REPEAT 539..562
FT /note="LRR 18"
FT /evidence="ECO:0000255"
FT REPEAT 564..586
FT /note="LRR 19"
FT /evidence="ECO:0000255"
FT REPEAT 587..610
FT /note="LRR 20"
FT /evidence="ECO:0000255"
FT REPEAT 612..634
FT /note="LRR 21"
FT /evidence="ECO:0000255"
FT REPEAT 635..658
FT /note="LRR 22"
FT /evidence="ECO:0000255"
FT REPEAT 659..683
FT /note="LRR 23"
FT /evidence="ECO:0000255"
FT DOMAIN 785..1066
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 1077..1135
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 186..187
FT /note="Small peptide recognition"
FT /evidence="ECO:0000250|UniProtKB:C0LGR3"
FT MOTIF 208..211
FT /note="Small peptide recognition"
FT /evidence="ECO:0000250|UniProtKB:C0LGR3"
FT MOTIF 231..236
FT /note="Small peptide recognition"
FT /evidence="ECO:0000250|UniProtKB:C0LGR3"
FT MOTIF 259
FT /note="Small peptide recognition"
FT /evidence="ECO:0000250|UniProtKB:C0LGR3"
FT MOTIF 281..283
FT /note="Small peptide recognition"
FT /evidence="ECO:0000250|UniProtKB:C0LGR3"
FT MOTIF 329..332
FT /note="Small peptide recognition"
FT /evidence="ECO:0000250|UniProtKB:C0LGR3"
FT MOTIF 351..353
FT /note="Small peptide recognition"
FT /evidence="ECO:0000250|UniProtKB:C0LGR3"
FT MOTIF 399..403
FT /note="Small peptide recognition"
FT /evidence="ECO:0000250|UniProtKB:C0LGR3"
FT MOTIF 425..428
FT /note="Small peptide recognition"
FT /evidence="ECO:0000250|UniProtKB:C0LGR3"
FT MOTIF 447..451
FT /note="Small peptide recognition"
FT /evidence="ECO:0000250|UniProtKB:C0LGR3"
FT MOTIF 471..473
FT /note="Small peptide recognition"
FT /evidence="ECO:0000250|UniProtKB:C0LGR3"
FT COMPBIAS 1095..1135
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 920
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 791..799
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 813
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT SITE 813
FT /note="Essential for autophosphorylation activity"
FT /evidence="ECO:0000250|UniProtKB:Q9LHP4"
FT MOD_RES 777
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:O22476"
FT MOD_RES 868
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:O22476"
FT MOD_RES 907
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:C0LGT6"
FT MOD_RES 963
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:C0LGT6"
FT MOD_RES 970
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:Q9M0G7"
FT CARBOHYD 101
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 117
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 273
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 345
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 358
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 369
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 444
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 465
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 492
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 502
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 521
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 524
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 598
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 618
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 665
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 707
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT DISULFID 69..76
FT /evidence="ECO:0000250|UniProtKB:Q94AG2"
FT CONFLICT 79
FT /note="S -> P (in Ref. 1; CAD79349)"
FT /evidence="ECO:0000305"
FT CONFLICT 257
FT /note="S -> F (in Ref. 1; CAD79349)"
FT /evidence="ECO:0000305"
FT CONFLICT 369
FT /note="N -> D (in Ref. 1; CAD79349)"
FT /evidence="ECO:0000305"
FT CONFLICT 463
FT /note="I -> T (in Ref. 1; CAD79349)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1135 AA; 123612 MW; E267BA44BAE0E69C CRC64;
MSLQMPIPRK KALTVSHFSI TLSLFLAFFI SSTSASTNEV SALISWLHSS NSPPPSVFSG
WNPSDSDPCQ WPYITCSSSD NKLVTEINVV SVQLALPFPP NISSFTSLQK LVISNTNLTG
AISSEIGDCS ELIVIDLSSN SLVGEIPSSL GKLKNLQELC LNSNGLTGKI PPELGDCVSL
KNLEIFDNYL SENLPLELGK ISTLESIRAG GNSELSGKIP EEIGNCRNLK VLGLAATKIS
GSLPVSLGQL SKLQSLSVYS TMLSGEIPKE LGNCSELINL FLYDNDLSGT LPKELGKLQN
LEKMLLWQNN LHGPIPEEIG FMKSLNAIDL SMNYFSGTIP KSFGNLSNLQ ELMLSSNNIT
GSIPSILSNC TKLVQFQIDA NQISGLIPPE IGLLKELNIF LGWQNKLEGN IPDELAGCQN
LQALDLSQNY LTGSLPAGLF QLRNLTKLLL ISNAISGVIP LEIGNCTSLV RLRLVNNRIT
GEIPKGIGFL QNLSFLDLSE NNLSGPVPLE ISNCRQLQML NLSNNTLQGY LPLSLSSLTK
LQVLDVSSND LTGKIPDSLG HLISLNRLIL SKNSFNGEIP SSLGHCTNLQ LLDLSSNNIS
GTIPEELFDI QDLDIALNLS WNSLDGFIPE RISALNRLSV LDISHNMLSG DLSALSGLEN
LVSLNISHNR FSGYLPDSKV FRQLIGAEME GNNGLCSKGF RSCFVSNSSQ LTTQRGVHSH
RLRIAIGLLI SVTAVLAVLG VLAVIRAKQM IRDDNDSETG ENLWTWQFTP FQKLNFTVEH
VLKCLVEGNV IGKGCSGIVY KAEMPNREVI AVKKLWPVTV PNLNEKTKSS GVRDSFSAEV
KTLGSIRHKN IVRFLGCCWN KNTRLLMYDY MSNGSLGSLL HERSGVCSLG WEVRYKIILG
AAQGLAYLHH DCVPPIVHRD IKANNILIGP DFEPYIGDFG LAKLVDDGDF ARSSNTIAGS
YGYIAPEYGY SMKITEKSDV YSYGVVVLEV LTGKQPIDPT IPDGLHIVDW VKKIRDIQVI
DQGLQARPES EVEEMMQTLG VALLCINPIP EDRPTMKDVA AMLSEICQER EESMKVDGCS
GSCNNGRERG KDDSTSSVMQ QTAKYLRSSS TSFSASSLLY SSSSSATSNV RPNLK
