RGI4_ARATH
ID RGI4_ARATH Reviewed; 1090 AA.
AC F4K6B8; Q0WLB3; Q8VYG7; Q9FKU3;
DT 10-FEB-2021, integrated into UniProtKB/Swiss-Prot.
DT 28-JUN-2011, sequence version 1.
DT 03-AUG-2022, entry version 82.
DE RecName: Full=Leucine-rich repeat receptor-like serine/threonine-protein kinase RGI4 {ECO:0000305|PubMed:27229312};
DE EC=2.7.11.1 {ECO:0000255|PROSITE-ProRule:PRU00159};
DE AltName: Full=Protein RECEPTOR OF RGF1 2 {ECO:0000303|PubMed:27229311};
DE AltName: Full=Protein RGF1 INSENSITIVE 4 {ECO:0000303|PubMed:27229312};
DE AltName: Full=Protein STERILITY-REGULATING KINASE MEMBER 2 {ECO:0000303|PubMed:23910659};
DE Flags: Precursor;
GN Name=RGI4 {ECO:0000303|PubMed:27229312};
GN Synonyms=RGFR2 {ECO:0000303|PubMed:27229311},
GN SKM2 {ECO:0000303|PubMed:23910659};
GN OrderedLocusNames=At5g56040 {ECO:0000312|Araport:AT5G56040};
GN ORFNames=MDA7.8 {ECO:0000312|EMBL:BAB09286.1};
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 [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=9679202; DOI=10.1093/dnares/5.2.131;
RA Kaneko T., Kotani H., Nakamura Y., Sato S., Asamizu E., Miyajima N.,
RA Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. V. Sequence
RT features of the regions of 1,381,565 bp covered by twenty one physically
RT assigned P1 and TAC clones.";
RL DNA Res. 5:131-145(1998).
RN [2]
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC STRAIN=cv. Columbia;
RX PubMed=14593172; DOI=10.1126/science.1088305;
RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA Ecker J.R.;
RT "Empirical analysis of transcriptional activity in the Arabidopsis
RT genome.";
RL Science 302:842-846(2003).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-1074 (ISOFORM 1).
RC STRAIN=cv. Columbia;
RA Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A.,
RA Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y.,
RA Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.,
RA Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y.,
RA Shinozaki K.;
RT "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
RL Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP FUNCTION, DISRUPTION PHENOTYPE, TISSUE SPECIFICITY, AND INDUCTION BY
RP HIGH-TEMPERATURE.
RX PubMed=23910659; DOI=10.1016/j.cub.2013.06.060;
RA Endo S., Shinohara H., Matsubayashi Y., Fukuda H.;
RT "A novel pollen-pistil interaction conferring high-temperature tolerance
RT during reproduction via CLE45 signaling.";
RL Curr. Biol. 23:1670-1676(2013).
RN [7]
RP FUNCTION, DISRUPTION PHENOTYPE, INTERACTION WITH RGF1; SERK1; SERK2 AND
RP BAK1/SERK3, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, GENE FAMILY, AND
RP 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, TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RC STRAIN=cv. Columbia;
RX PubMed=27354416; DOI=10.15252/embr.201642450;
RA Kang Y.H., Hardtke C.S.;
RT "Arabidopsis MAKR5 is a positive effector of BAM3-dependent CLE45
RT signaling.";
RL EMBO Rep. 17:1145-1154(2016).
CC -!- FUNCTION: Receptor with a serine/threonine-protein kinase activity (By
CC similarity). Together with SKM1, LRR-rich receptor-like kinase (LRR-
CC RLK) required for male fertility by the perception of CLE43 and CLE45
CC peptides and the transduction of their promoting action in pollen
CC tubes, especially under relatively high temperature (at 30 degrees
CC Celsius), thus conferring tolerance against high temperature probably
CC through the maintenance of mitochondrial activity (PubMed:23910659).
CC Seems to not be involved in the perception of CLE45 peptide in roots
CC (PubMed:27354416). Together with RGI1, RGI2, RGI3, RGI4 and RGI5, acts
CC as receptor of RGF1, a peptide hormone that maintains the postembryonic
CC root stem cell niche by regulating the expression levels and patterns
CC of the transcription factor PLETHORA (PLT) (PubMed:27229312,
CC PubMed:27229311). Links RGF1 signal with its downstream components
CC (PubMed:27229311). {ECO:0000250|UniProtKB:Q9ZWC8,
CC ECO:0000269|PubMed:23910659, ECO:0000269|PubMed:27229311,
CC ECO:0000269|PubMed:27229312, ECO:0000269|PubMed:27354416}.
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: Self-interacts (By similarity). Interacts with RGF1; this
CC interaction triggers its phosphorylation and ubiquitination and the
CC formation of heterodimers with SERK1 (PubMed:27229311).
CC {ECO:0000250|UniProtKB:Q9SYQ8, ECO:0000269|PubMed:27229311}.
CC -!- INTERACTION:
CC F4K6B8; C0LGR6: At4g29180; NbExp=2; IntAct=EBI-1238236, EBI-20654480;
CC F4K6B8; O65440-2: BAM3; NbExp=2; IntAct=EBI-1238236, EBI-20653325;
CC F4K6B8; F4K6B8: RGI4; NbExp=2; IntAct=EBI-1238236, EBI-1238236;
CC F4K6B8; Q9LP77: RKL1; NbExp=2; IntAct=EBI-1238236, EBI-1544507;
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q9ZWC8};
CC Single-pass type I membrane protein {ECO:0000255}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=F4K6B8-1; Sequence=Displayed;
CC Name=2;
CC IsoId=F4K6B8-2; Sequence=VSP_060889, VSP_060890;
CC -!- TISSUE SPECIFICITY: Expressed in floers, pollen grains and stipules
CC (PubMed:23910659, PubMed:27229311). Present in roots (PubMed:27354416,
CC PubMed:27229311). {ECO:0000269|PubMed:23910659,
CC ECO:0000269|PubMed:27229311, ECO:0000269|PubMed:27354416}.
CC -!- DEVELOPMENTAL STAGE: Present throughout the root, starting from the
CC transition zone and including transition and elongation zones, but
CC absent from the meristem. {ECO:0000269|PubMed:27354416}.
CC -!- INDUCTION: Slightly induced in pollen upon high-temperature exposure
CC (HTE). {ECO:0000269|PubMed:23910659}.
CC -!- PTM: Autophosphorylated. {ECO:0000250|UniProtKB:O22476}.
CC -!- PTM: Phosphorylated and ubiquitinated upon interaction with RGF1, thus
CC leading to activation a subsequent degradation.
CC {ECO:0000250|UniProtKB:Q9LHP4}.
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). Insensitivity of pollen
CC tubes to CLE43 and, partially, to CLE45 peptides-mediated growth
CC stimulation (PubMed:23910659). Pollen tubes of plants missing both SKM1
CC and SKM2 are fully insensitive to CLE45 peptides (PubMed:23910659).
CC Quintuple mutants rgi1 rgi2 rgi3 rgi4 rgi5 display a consistent short
CC primary root phenotype with a small size of meristem associated with a
CC total insensitivity to RGF1 and undetectable levels of PLT1 and PLT2
CC (PubMed:27229312). {ECO:0000269|PubMed:23910659,
CC ECO:0000269|PubMed:27229311, 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=BAB09286.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=BAF02094.1; Type=Erroneous translation; Evidence={ECO:0000305};
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DR EMBL; AB011476; BAB09286.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002688; AED96713.1; -; Genomic_DNA.
DR EMBL; CP002688; AED96714.1; -; Genomic_DNA.
DR EMBL; AY072083; AAL59906.1; -; mRNA.
DR EMBL; FJ708803; ACN59394.1; -; mRNA.
DR EMBL; AK230293; BAF02094.1; ALT_SEQ; mRNA.
DR RefSeq; NP_001032080.1; NM_001037003.2. [F4K6B8-1]
DR RefSeq; NP_200415.2; NM_124986.3. [F4K6B8-2]
DR AlphaFoldDB; F4K6B8; -.
DR SMR; F4K6B8; -.
DR IntAct; F4K6B8; 43.
DR STRING; 3702.AT5G56040.2; -.
DR PaxDb; F4K6B8; -.
DR PRIDE; F4K6B8; -.
DR ProteomicsDB; 183811; -.
DR ProteomicsDB; 203984; -. [F4K6B8-1]
DR EnsemblPlants; AT5G56040.1; AT5G56040.1; AT5G56040. [F4K6B8-2]
DR EnsemblPlants; AT5G56040.2; AT5G56040.2; AT5G56040. [F4K6B8-1]
DR GeneID; 835702; -.
DR Gramene; AT5G56040.1; AT5G56040.1; AT5G56040. [F4K6B8-2]
DR Gramene; AT5G56040.2; AT5G56040.2; AT5G56040. [F4K6B8-1]
DR KEGG; ath:AT5G56040; -.
DR Araport; AT5G56040; -.
DR TAIR; locus:2161825; AT5G56040.
DR eggNOG; ENOG502QSU9; Eukaryota.
DR HOGENOM; CLU_000288_22_1_1; -.
DR InParanoid; F4K6B8; -.
DR OMA; DKSPCNW; -.
DR OrthoDB; 826997at2759; -.
DR PhylomeDB; F4K6B8; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; F4K6B8; baseline and differential.
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:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0042277; F:peptide binding; IPI:UniProtKB.
DR GO; GO:0001653; F:peptide receptor activity; IMP:UniProtKB.
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:0006468; P:protein phosphorylation; IEA:InterPro.
DR GO; GO:0080092; P:regulation of pollen tube growth; IMP:UniProtKB.
DR GO; GO:0010082; P:regulation of root meristem growth; IGI:TAIR.
DR GO; GO:0009266; P:response to temperature stimulus; IEP:UniProtKB.
DR Gene3D; 3.80.10.10; -; 5.
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; IPR008271; Ser/Thr_kinase_AS.
DR Pfam; PF13855; LRR_8; 2.
DR Pfam; PF08263; LRRNT_2; 1.
DR Pfam; PF00069; Pkinase; 1.
DR SMART; SM00369; LRR_TYP; 9.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF56112; SSF56112; 1.
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 Alternative splicing; ATP-binding; Cell membrane; Disulfide bond;
KW Glycoprotein; Kinase; Leucine-rich repeat; Membrane; Nucleotide-binding;
KW Phosphoprotein; Receptor; Reference proteome; Repeat;
KW Serine/threonine-protein kinase; Signal; Transferase; Transmembrane;
KW Transmembrane helix; Ubl conjugation.
FT SIGNAL 1..20
FT /evidence="ECO:0000255"
FT CHAIN 21..1090
FT /note="Leucine-rich repeat receptor-like serine/threonine-
FT protein kinase RGI4"
FT /id="PRO_5009954980"
FT TOPO_DOM 21..702
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 703..723
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 724..1090
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT REPEAT 36..59
FT /note="LRR 1"
FT /evidence="ECO:0000255"
FT REPEAT 95..119
FT /note="LRR 2"
FT /evidence="ECO:0000255"
FT REPEAT 120..143
FT /note="LRR 3"
FT /evidence="ECO:0000255"
FT REPEAT 145..166
FT /note="LRR 4"
FT /evidence="ECO:0000255"
FT REPEAT 168..191
FT /note="LRR 5"
FT /evidence="ECO:0000255"
FT REPEAT 216..240
FT /note="LRR 6"
FT /evidence="ECO:0000255"
FT REPEAT 242..264
FT /note="LRR 7"
FT /evidence="ECO:0000255"
FT REPEAT 265..288
FT /note="LRR 8"
FT /evidence="ECO:0000255"
FT REPEAT 289..312
FT /note="LRR 9"
FT /evidence="ECO:0000255"
FT REPEAT 314..335
FT /note="LRR 10"
FT /evidence="ECO:0000255"
FT REPEAT 336..360
FT /note="LRR 11"
FT /evidence="ECO:0000255"
FT REPEAT 362..386
FT /note="LRR 12"
FT /evidence="ECO:0000255"
FT REPEAT 408..432
FT /note="LRR 13"
FT /evidence="ECO:0000255"
FT REPEAT 434..456
FT /note="LRR 14"
FT /evidence="ECO:0000255"
FT REPEAT 457..480
FT /note="LRR 15"
FT /evidence="ECO:0000255"
FT REPEAT 481..504
FT /note="LRR 16"
FT /evidence="ECO:0000255"
FT REPEAT 506..526
FT /note="LRR 17"
FT /evidence="ECO:0000255"
FT REPEAT 527..550
FT /note="LRR 18"
FT /evidence="ECO:0000255"
FT REPEAT 551..574
FT /note="LRR 19"
FT /evidence="ECO:0000255"
FT REPEAT 576..598
FT /note="LRR 20"
FT /evidence="ECO:0000255"
FT REPEAT 600..622
FT /note="LRR 21"
FT /evidence="ECO:0000255"
FT REPEAT 623..646
FT /note="LRR 22"
FT /evidence="ECO:0000255"
FT REPEAT 647..670
FT /note="LRR 23"
FT /evidence="ECO:0000255"
FT DOMAIN 758..1040
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REPEAT 1037..1060
FT /note="LRR 24"
FT /evidence="ECO:0000255"
FT REGION 1054..1079
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 176..177
FT /note="Small peptide recognition"
FT /evidence="ECO:0000250|UniProtKB:C0LGR3"
FT MOTIF 198..201
FT /note="Small peptide recognition"
FT /evidence="ECO:0000250|UniProtKB:C0LGR3"
FT MOTIF 221..226
FT /note="Small peptide recognition"
FT /evidence="ECO:0000250|UniProtKB:C0LGR3"
FT MOTIF 249
FT /note="Small peptide recognition"
FT /evidence="ECO:0000250|UniProtKB:C0LGR3"
FT MOTIF 269..273
FT /note="CLE45 peptide binding"
FT /evidence="ECO:0000250|UniProtKB:O65440"
FT MOTIF 271..273
FT /note="Small peptide recognition"
FT /evidence="ECO:0000250|UniProtKB:C0LGR3"
FT MOTIF 319..322
FT /note="Small peptide recognition"
FT /evidence="ECO:0000250|UniProtKB:C0LGR3"
FT MOTIF 341..343
FT /note="Small peptide recognition"
FT /evidence="ECO:0000250|UniProtKB:C0LGR3"
FT MOTIF 389..393
FT /note="Small peptide recognition"
FT /evidence="ECO:0000250|UniProtKB:C0LGR3"
FT MOTIF 415..418
FT /note="Small peptide recognition"
FT /evidence="ECO:0000250|UniProtKB:C0LGR3"
FT MOTIF 437..441
FT /note="Small peptide recognition"
FT /evidence="ECO:0000250|UniProtKB:C0LGR3"
FT MOTIF 461..463
FT /note="Small peptide recognition"
FT /evidence="ECO:0000250|UniProtKB:C0LGR3"
FT ACT_SITE 882
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 764..772
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 786
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT SITE 786
FT /note="Essential for autophosphorylation activity"
FT /evidence="ECO:0000250|UniProtKB:Q9LHP4"
FT MOD_RES 829
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:O22476"
FT MOD_RES 869
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:C0LGT6"
FT MOD_RES 932
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:C0LGT6"
FT CARBOHYD 43
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 107
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 263
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 359
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 420
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 434
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 455
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 606
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 653
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT DISULFID 60..67
FT /evidence="ECO:0000250|UniProtKB:Q94AG2"
FT VAR_SEQ 936..953
FT /note="EHASMQHITEKSDVYSYG -> GKIQNFDFNVINLSISKY (in isoform
FT 2)"
FT /id="VSP_060889"
FT VAR_SEQ 954..1090
FT /note="Missing (in isoform 2)"
FT /id="VSP_060890"
FT CONFLICT 948
FT /note="D -> G (in Ref. 5; BAF02094)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1090 AA; 119331 MW; 011FD4BC2B74DCBA CRC64;
MPRNPRFCFF LFLLFHSSLF FSIPCFSIDE QGLALLSWKS QLNISGDALS SWKASESNPC
QWVGIKCNER GQVSEIQLQV MDFQGPLPAT NLRQIKSLTL LSLTSVNLTG SIPKELGDLS
ELEVLDLADN SLSGEIPVDI FKLKKLKILS LNTNNLEGVI PSELGNLVNL IELTLFDNKL
AGEIPRTIGE LKNLEIFRAG GNKNLRGELP WEIGNCESLV TLGLAETSLS GRLPASIGNL
KKVQTIALYT SLLSGPIPDE IGNCTELQNL YLYQNSISGS IPVSMGRLKK LQSLLLWQNN
LVGKIPTELG TCPELFLVDL SENLLTGNIP RSFGNLPNLQ ELQLSVNQLS GTIPEELANC
TKLTHLEIDN NQISGEIPPL IGKLTSLTMF FAWQNQLTGI IPESLSQCQE LQAIDLSYNN
LSGSIPNGIF EIRNLTKLLL LSNYLSGFIP PDIGNCTNLY RLRLNGNRLA GNIPAEIGNL
KNLNFIDISE NRLIGNIPPE ISGCTSLEFV DLHSNGLTGG LPGTLPKSLQ FIDLSDNSLT
GSLPTGIGSL TELTKLNLAK NRFSGEIPRE ISSCRSLQLL NLGDNGFTGE IPNELGRIPS
LAISLNLSCN HFTGEIPSRF SSLTNLGTLD VSHNKLAGNL NVLADLQNLV SLNISFNEFS
GELPNTLFFR KLPLSVLESN KGLFISTRPE NGIQTRHRSA VKVTMSILVA ASVVLVLMAV
YTLVKAQRIT GKQEELDSWE VTLYQKLDFS IDDIVKNLTS ANVIGTGSSG VVYRVTIPSG
ETLAVKKMWS KEENRAFNSE INTLGSIRHR NIIRLLGWCS NRNLKLLFYD YLPNGSLSSL
LHGAGKGSGG ADWEARYDVV LGVAHALAYL HHDCLPPILH GDVKAMNVLL GSRFESYLAD
FGLAKIVSGE GVTDGDSSKL SNRPPLAGSY GYMAPEHASM QHITEKSDVY SYGVVLLEVL
TGKHPLDPDL PGGAHLVQWV RDHLAGKKDP REILDPRLRG RADPIMHEML QTLAVSFLCV
SNKASDRPMM KDIVAMLKEI RQFDMDRSES DMIKGGKCEK WQPQPLPPEK IVSTPRGSSN
CSFAYSDESV
