BAME1_ARATH
ID BAME1_ARATH Reviewed; 1003 AA.
AC O49545;
DT 11-JAN-2011, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1998, sequence version 1.
DT 03-AUG-2022, entry version 178.
DE RecName: Full=Leucine-rich repeat receptor-like serine/threonine-protein kinase BAM1;
DE EC=2.7.11.1;
DE AltName: Full=Protein BARELY ANY MERISTEM 1;
DE Flags: Precursor;
GN Name=BAM1; OrderedLocusNames=At5g65700; ORFNames=F6H11.170, MPA24.5;
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=9628582; DOI=10.1093/dnares/5.1.41;
RA Sato S., Kaneko T., Kotani H., Nakamura Y., Asamizu E., Miyajima N.,
RA Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. IV. Sequence
RT features of the regions of 1,456,315 bp covered by nineteen physically
RT assigned P1 and TAC clones.";
RL DNA Res. 5:41-54(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130714; DOI=10.1038/35048507;
RA Tabata S., Kaneko T., Nakamura Y., Kotani H., Kato T., Asamizu E.,
RA Miyajima N., Sasamoto S., Kimura T., Hosouchi T., Kawashima K., Kohara M.,
RA Matsumoto M., Matsuno A., Muraki A., Nakayama S., Nakazaki N., Naruo K.,
RA Okumura S., Shinpo S., Takeuchi C., Wada T., Watanabe A., Yamada M.,
RA Yasuda M., Sato S., de la Bastide M., Huang E., Spiegel L., Gnoj L.,
RA O'Shaughnessy A., Preston R., Habermann K., Murray J., Johnson D.,
RA Rohlfing T., Nelson J., Stoneking T., Pepin K., Spieth J., Sekhon M.,
RA Armstrong J., Becker M., Belter E., Cordum H., Cordes M., Courtney L.,
RA Courtney W., Dante M., Du H., Edwards J., Fryman J., Haakensen B.,
RA Lamar E., Latreille P., Leonard S., Meyer R., Mulvaney E., Ozersky P.,
RA Riley A., Strowmatt C., Wagner-McPherson C., Wollam A., Yoakum M., Bell M.,
RA Dedhia N., Parnell L., Shah R., Rodriguez M., Hoon See L., Vil D.,
RA Baker J., Kirchoff K., Toth K., King L., Bahret A., Miller B., Marra M.A.,
RA Martienssen R., McCombie W.R., Wilson R.K., Murphy G., Bancroft I.,
RA Volckaert G., Wambutt R., Duesterhoeft A., Stiekema W., Pohl T.,
RA Entian K.-D., Terryn N., Hartley N., Bent E., Johnson S., Langham S.-A.,
RA McCullagh B., Robben J., Grymonprez B., Zimmermann W., Ramsperger U.,
RA Wedler H., Balke K., Wedler E., Peters S., van Staveren M., Dirkse W.,
RA Mooijman P., Klein Lankhorst R., Weitzenegger T., Bothe G., Rose M.,
RA Hauf J., Berneiser S., Hempel S., Feldpausch M., Lamberth S.,
RA Villarroel R., Gielen J., Ardiles W., Bents O., Lemcke K., Kolesov G.,
RA Mayer K.F.X., Rudd S., Schoof H., Schueller C., Zaccaria P., Mewes H.-W.,
RA Bevan M., Fransz P.F.;
RT "Sequence and analysis of chromosome 5 of the plant Arabidopsis thaliana.";
RL Nature 408:823-826(2000).
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=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 [5]
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 [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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 [7]
RP SUBCELLULAR LOCATION.
RC STRAIN=cv. La-0;
RX PubMed=14506206; DOI=10.1074/mcp.t300006-mcp200;
RA Nuehse T.S., Stensballe A., Jensen O.N., Peck S.C.;
RT "Large-scale analysis of in vivo phosphorylated membrane proteins by
RT immobilized metal ion affinity chromatography and mass spectrometry.";
RL Mol. Cell. Proteomics 2:1234-1243(2003).
RN [8]
RP FUNCTION, DISRUPTION PHENOTYPE, AND DEVELOPMENTAL STAGE.
RX PubMed=16751349; DOI=10.1105/tpc.105.036871;
RA Hord C.L.H., Chen C., Deyoung B.J., Clark S.E., Ma H.;
RT "The BAM1/BAM2 receptor-like kinases are important regulators of
RT Arabidopsis early anther development.";
RL Plant Cell 18:1667-1680(2006).
RN [9]
RP FUNCTION, DISRUPTION PHENOTYPE, TISSUE SPECIFICITY, AND DEVELOPMENTAL
RP STAGE.
RX PubMed=16367950; DOI=10.1111/j.1365-313x.2005.02592.x;
RA DeYoung B.J., Bickle K.L., Schrage K.J., Muskett P., Patel K., Clark S.E.;
RT "The CLAVATA1-related BAM1, BAM2 and BAM3 receptor kinase-like proteins are
RT required for meristem function in Arabidopsis.";
RL Plant J. 45:1-16(2006).
RN [10]
RP DISRUPTION PHENOTYPE, AND FUNCTION.
RX PubMed=18780746; DOI=10.1534/genetics.108.091108;
RA Deyoung B.J., Clark S.E.;
RT "BAM receptors regulate stem cell specification and organ development
RT through complex interactions with CLAVATA signaling.";
RL Genetics 180:895-904(2008).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-996, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19376835; DOI=10.1104/pp.109.138677;
RA Reiland S., Messerli G., Baerenfaller K., Gerrits B., Endler A.,
RA Grossmann J., Gruissem W., Baginsky S.;
RT "Large-scale Arabidopsis phosphoproteome profiling reveals novel
RT chloroplast kinase substrates and phosphorylation networks.";
RL Plant Physiol. 150:889-903(2009).
RN [12]
RP INTERACTION WITH MCLV3; CLE5; CLE11; CLE18; CLE19; CLE22; CLE25; CLE26;
RP CLE40; CLE41; CLE42; CLV1 AND BAM2, HOMODIMERIZATION, AND SUBCELLULAR
RP LOCATION.
RX PubMed=20626648; DOI=10.1111/j.1365-313x.2010.04295.x;
RA Guo Y., Han L., Hymes M., Denver R., Clark S.E.;
RT "CLAVATA2 forms a distinct CLE-binding receptor complex regulating
RT Arabidopsis stem cell specification.";
RL Plant J. 63:889-900(2010).
CC -!- FUNCTION: Necessary for male gametophyte development, as well as ovule
CC specification and function. Involved in cell-cell communication process
CC required during early anther development, and regulating cell division
CC and differentiation to organize cell layers. Required for the
CC development of high-ordered vascular strands within the leaf and a
CC correlated control of leaf shape, size and symmetry. May regulate the
CC CLV1-dependent CLV3-mediated signaling in meristems maintenance.
CC {ECO:0000269|PubMed:16367950, ECO:0000269|PubMed:16751349,
CC ECO:0000269|PubMed:18780746}.
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 -!- 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;
CC -!- SUBUNIT: Self-interacts and interacts with BAM2 and CLV1. Binds to the
CC CLV3, CLE5, CLE11, CLE18, CLE19, CLE22, CLE25, CLE26, CLE40, CLE41 and
CC CLE42 mature peptides, probably via its extracellular leucine-rich
CC repeat region. {ECO:0000269|PubMed:20626648}.
CC -!- INTERACTION:
CC O49545; F4I065: At1g49100; NbExp=2; IntAct=EBI-17069471, EBI-20654598;
CC O49545; A0A1I9LQ53: At3g50230; NbExp=3; IntAct=EBI-17069471, EBI-20654045;
CC O49545; O49545: BAM1; NbExp=2; IntAct=EBI-17069471, EBI-17069471;
CC O49545; Q9LJF3: BRL3; NbExp=2; IntAct=EBI-17069471, EBI-20651413;
CC O49545; C0LGW6: ERL1; NbExp=2; IntAct=EBI-17069471, EBI-16914248;
CC O49545; O64794: LRR-RLK; NbExp=2; IntAct=EBI-17069471, EBI-16887796;
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:14506206,
CC ECO:0000269|PubMed:20626648}; Single-pass type I membrane protein
CC {ECO:0000269|PubMed:14506206, ECO:0000269|PubMed:20626648}.
CC -!- TISSUE SPECIFICITY: Expressed in seedlings, roots, leaves,
CC inflorescences, flowers and siliques. {ECO:0000269|PubMed:16367950}.
CC -!- DEVELOPMENTAL STAGE: Expressed in a ring surrounding the center of
CC meristems extended in the cortex of developing stems and older
CC pedicels. Present in all developing floral organs, especially in
CC anthers and gynoecium. Observed in anthers at stage 2 in the
CC archesporial cells. At stage 3, localized in the primary sporogenous
CC and primary parietal cells. Subsequently preferentially expressed in
CC the sporogenous cells at anther stage 4. Later restricted to the
CC tapetum and pollen mother cells (PMCs) before disappearing
CC progressively. {ECO:0000269|PubMed:16367950,
CC ECO:0000269|PubMed:16751349}.
CC -!- DISRUPTION PHENOTYPE: Rescues partially CLV3 disruption. When
CC associated with BAM2 disruption, abnormal anthers at a very early stage
CC and later lack of endothecium, middle and tapetum layers. Loss of stem
CC cells at the shoot and flower meristems. {ECO:0000269|PubMed:16367950,
CC ECO:0000269|PubMed:16751349, ECO:0000269|PubMed:18780746}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein
CC kinase family. {ECO:0000255|PROSITE-ProRule:PRU00159}.
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DR EMBL; AB010075; BAB10677.1; -; Genomic_DNA.
DR EMBL; AL021684; CAA16688.1; -; Genomic_DNA.
DR EMBL; CP002688; AED98091.1; -; Genomic_DNA.
DR EMBL; CP002688; AED98092.1; -; Genomic_DNA.
DR EMBL; AY099814; AAM20665.1; -; mRNA.
DR EMBL; BT008810; AAP68249.1; -; mRNA.
DR EMBL; FJ708816; ACN59407.1; -; mRNA.
DR EMBL; AK226485; BAE98627.1; -; mRNA.
DR PIR; T05898; T05898.
DR RefSeq; NP_001190624.1; NM_001203695.1.
DR RefSeq; NP_201371.1; NM_125967.5.
DR AlphaFoldDB; O49545; -.
DR SMR; O49545; -.
DR BioGRID; 21941; 88.
DR IntAct; O49545; 90.
DR STRING; 3702.AT5G65700.2; -.
DR iPTMnet; O49545; -.
DR PaxDb; O49545; -.
DR PRIDE; O49545; -.
DR ProteomicsDB; 241122; -.
DR EnsemblPlants; AT5G65700.1; AT5G65700.1; AT5G65700.
DR EnsemblPlants; AT5G65700.2; AT5G65700.2; AT5G65700.
DR GeneID; 836699; -.
DR Gramene; AT5G65700.1; AT5G65700.1; AT5G65700.
DR Gramene; AT5G65700.2; AT5G65700.2; AT5G65700.
DR KEGG; ath:AT5G65700; -.
DR Araport; AT5G65700; -.
DR TAIR; locus:2169965; AT5G65700.
DR eggNOG; ENOG502QQRQ; Eukaryota.
DR HOGENOM; CLU_000288_22_1_1; -.
DR InParanoid; O49545; -.
DR OMA; KDHHQPT; -.
DR OrthoDB; 154810at2759; -.
DR PhylomeDB; O49545; -.
DR PRO; PR:O49545; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; O49545; baseline and differential.
DR Genevisible; O49545; AT.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; HDA:TAIR.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0043621; F:protein self-association; IDA: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:0033612; F:receptor serine/threonine kinase binding; IPI:UniProtKB.
DR GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW.
DR GO; GO:0048437; P:floral organ development; IGI:TAIR.
DR GO; GO:0048229; P:gametophyte development; IGI:TAIR.
DR GO; GO:0009755; P:hormone-mediated signaling pathway; IBA:GO_Central.
DR GO; GO:0006468; P:protein phosphorylation; IEA:InterPro.
DR GO; GO:0010075; P:regulation of meristem growth; IGI:TAIR.
DR GO; GO:0009934; P:regulation of meristem structural organization; IGI:TAIR.
DR Gene3D; 3.80.10.10; -; 3.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR001611; Leu-rich_rpt.
DR InterPro; IPR025875; Leu-rich_rpt_4.
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; IPR008271; Ser/Thr_kinase_AS.
DR Pfam; PF00560; LRR_1; 1.
DR Pfam; PF12799; LRR_4; 1.
DR Pfam; PF08263; LRRNT_2; 1.
DR Pfam; PF00069; Pkinase; 1.
DR SMART; SM00369; LRR_TYP; 7.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF56112; SSF56112; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Cell membrane; Developmental protein; Differentiation;
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.
FT SIGNAL 1..19
FT /evidence="ECO:0000255"
FT CHAIN 20..1003
FT /note="Leucine-rich repeat receptor-like serine/threonine-
FT protein kinase BAM1"
FT /id="PRO_0000403352"
FT TOPO_DOM 20..640
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 641..661
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 662..1003
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REPEAT 68..92
FT /note="LRR 1"
FT REPEAT 93..116
FT /note="LRR 2"
FT REPEAT 117..140
FT /note="LRR 3"
FT REPEAT 142..165
FT /note="LRR 4"
FT REPEAT 166..191
FT /note="LRR 5"
FT REPEAT 193..213
FT /note="LRR 6"
FT REPEAT 215..238
FT /note="LRR 7"
FT REPEAT 239..262
FT /note="LRR 8"
FT REPEAT 263..285
FT /note="LRR 9"
FT REPEAT 286..310
FT /note="LRR 10"
FT REPEAT 312..334
FT /note="LRR 11"
FT REPEAT 335..358
FT /note="LRR 12"
FT REPEAT 359..382
FT /note="LRR 13"
FT REPEAT 385..406
FT /note="LRR 14"
FT REPEAT 407..430
FT /note="LRR 15"
FT REPEAT 432..454
FT /note="LRR 16"
FT REPEAT 455..480
FT /note="LRR 17"
FT REPEAT 482..502
FT /note="LRR 18"
FT REPEAT 503..526
FT /note="LRR 19"
FT REPEAT 527..550
FT /note="LRR 20"
FT REPEAT 551..574
FT /note="LRR 21"
FT REPEAT 575..598
FT /note="LRR 22"
FT DOMAIN 694..971
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 969..1003
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 979..1003
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 820
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 700..708
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 722
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT MOD_RES 686
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:O22476"
FT MOD_RES 769
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:O22476"
FT MOD_RES 807
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:C0LGT6"
FT MOD_RES 855
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9M0G7"
FT MOD_RES 863
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:C0LGT6"
FT MOD_RES 870
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:Q9M0G7"
FT MOD_RES 871
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9M0G7"
FT MOD_RES 996
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19376835"
FT CARBOHYD 80
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 97
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 123
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 130
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 153
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 164
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 212
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 237
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 312
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 346
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 420
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 477
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 557
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 586
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 601
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 1003 AA; 109203 MW; E7577BC093F76228 CRC64;
MKLFLLLLFL LHISHTFTAS RPISEFRALL SLKTSLTGAG DDKNSPLSSW KVSTSFCTWI
GVTCDVSRRH VTSLDLSGLN LSGTLSPDVS HLRLLQNLSL AENLISGPIP PEISSLSGLR
HLNLSNNVFN GSFPDEISSG LVNLRVLDVY NNNLTGDLPV SVTNLTQLRH LHLGGNYFAG
KIPPSYGSWP VIEYLAVSGN ELVGKIPPEI GNLTTLRELY IGYYNAFEDG LPPEIGNLSE
LVRFDGANCG LTGEIPPEIG KLQKLDTLFL QVNVFSGPLT WELGTLSSLK SMDLSNNMFT
GEIPASFAEL KNLTLLNLFR NKLHGEIPEF IGDLPELEVL QLWENNFTGS IPQKLGENGK
LNLVDLSSNK LTGTLPPNMC SGNKLETLIT LGNFLFGSIP DSLGKCESLT RIRMGENFLN
GSIPKGLFGL PKLTQVELQD NYLSGELPVA GGVSVNLGQI SLSNNQLSGP LPPAIGNFTG
VQKLLLDGNK FQGPIPSEVG KLQQLSKIDF SHNLFSGRIA PEISRCKLLT FVDLSRNELS
GEIPNEITAM KILNYLNLSR NHLVGSIPGS ISSMQSLTSL DFSYNNLSGL VPGTGQFSYF
NYTSFLGNPD LCGPYLGPCK DGVAKGGHQS HSKGPLSASM KLLLVLGLLV CSIAFAVVAI
IKARSLKKAS ESRAWRLTAF QRLDFTCDDV LDSLKEDNII GKGGAGIVYK GVMPNGDLVA
VKRLAAMSRG SSHDHGFNAE IQTLGRIRHR HIVRLLGFCS NHETNLLVYE YMPNGSLGEV
LHGKKGGHLH WDTRYKIALE AAKGLCYLHH DCSPLIVHRD VKSNNILLDS NFEAHVADFG
LAKFLQDSGT SECMSAIAGS YGYIAPEYAY TLKVDEKSDV YSFGVVLLEL VTGRKPVGEF
GDGVDIVQWV RKMTDSNKDS VLKVLDPRLS SIPIHEVTHV FYVAMLCVEE QAVERPTMRE
VVQILTEIPK LPPSKDQPMT ESAPESELSP KSGVQSPPDL LNL
