ACR4L_ARATH
ID ACR4L_ARATH Reviewed; 895 AA.
AC Q9LX29;
DT 01-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 155.
DE RecName: Full=Serine/threonine-protein kinase-like protein ACR4;
DE EC=2.7.11.1;
DE AltName: Full=Protein CRINKLY 4;
DE Short=AtCR4;
DE Flags: Precursor;
GN Name=ACR4; OrderedLocusNames=At3g59420; ORFNames=F25L23.280;
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], FUNCTION, DISRUPTION PHENOTYPE, TISSUE
RP SPECIFICITY, DEVELOPMENTAL STAGE, AND SUBCELLULAR LOCATION.
RC STRAIN=cv. Columbia;
RX PubMed=11978870; DOI=10.1093/pcp/pcf052;
RA Tanaka H., Watanabe M., Watanabe D., Tanaka T., Machida C., Machida Y.;
RT "ACR4, a putative receptor kinase gene of Arabidopsis thaliana, that is
RT expressed in the outer cell layers of embryos and plants, is involved in
RT proper embryogenesis.";
RL Plant Cell Physiol. 43:419-428(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130713; DOI=10.1038/35048706;
RA Salanoubat M., Lemcke K., Rieger M., Ansorge W., Unseld M., Fartmann B.,
RA Valle G., Bloecker H., Perez-Alonso M., Obermaier B., Delseny M.,
RA Boutry M., Grivell L.A., Mache R., Puigdomenech P., De Simone V.,
RA Choisne N., Artiguenave F., Robert C., Brottier P., Wincker P.,
RA Cattolico L., Weissenbach J., Saurin W., Quetier F., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Benes V., Wurmbach E., Drzonek H.,
RA Erfle H., Jordan N., Bangert S., Wiedelmann R., Kranz H., Voss H.,
RA Holland R., Brandt P., Nyakatura G., Vezzi A., D'Angelo M., Pallavicini A.,
RA Toppo S., Simionati B., Conrad A., Hornischer K., Kauer G., Loehnert T.-H.,
RA Nordsiek G., Reichelt J., Scharfe M., Schoen O., Bargues M., Terol J.,
RA Climent J., Navarro P., Collado C., Perez-Perez A., Ottenwaelder B.,
RA Duchemin D., Cooke R., Laudie M., Berger-Llauro C., Purnelle B., Masuy D.,
RA de Haan M., Maarse A.C., Alcaraz J.-P., Cottet A., Casacuberta E.,
RA Monfort A., Argiriou A., Flores M., Liguori R., Vitale D., Mannhaupt G.,
RA Haase D., Schoof H., Rudd S., Zaccaria P., Mewes H.-W., Mayer K.F.X.,
RA Kaul S., Town C.D., Koo H.L., Tallon L.J., Jenkins J., Rooney T., Rizzo M.,
RA Walts A., Utterback T., Fujii C.Y., Shea T.P., Creasy T.H., Haas B.,
RA Maiti R., Wu D., Peterson J., Van Aken S., Pai G., Militscher J.,
RA Sellers P., Gill J.E., Feldblyum T.V., Preuss D., Lin X., Nierman W.C.,
RA Salzberg S.L., White O., Venter J.C., Fraser C.M., Kaneko T., Nakamura Y.,
RA Sato S., Kato T., Asamizu E., Sasamoto S., Kimura T., Idesawa K.,
RA Kawashima K., Kishida Y., Kiyokawa C., Kohara M., Matsumoto M., Matsuno A.,
RA Muraki A., Nakayama S., Nakazaki N., Shinpo S., Takeuchi C., Wada T.,
RA Watanabe A., Yamada M., Yasuda M., Tabata S.;
RT "Sequence and analysis of chromosome 3 of the plant Arabidopsis thaliana.";
RL Nature 408:820-822(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 FUNCTION, DISRUPTION PHENOTYPE, CATALYTIC ACTIVITY, MUTAGENESIS OF LYS-540,
RP SUBCELLULAR LOCATION, AND DEVELOPMENTAL STAGE.
RX PubMed=12900442; DOI=10.1242/dev.00634;
RA Gifford M.L., Dean S., Ingram G.C.;
RT "The Arabidopsis ACR4 gene plays a role in cell layer organisation during
RT ovule integument and sepal margin development.";
RL Development 130:4249-4258(2003).
RN [5]
RP FUNCTION, DISRUPTION PHENOTYPE, MUTAGENESIS OF LYS-540, AND SUBCELLULAR
RP LOCATION.
RX PubMed=15255860; DOI=10.1111/j.1365-313x.2004.02132.x;
RA Watanabe M., Tanaka H., Watanabe D., Machida C., Machida Y.;
RT "The ACR4 receptor-like kinase is required for surface formation of
RT epidermis-related tissues in Arabidopsis thaliana.";
RL Plant J. 39:298-308(2004).
RN [6]
RP GENE FAMILY, CATALYTIC ACTIVITY, MUTAGENESIS OF LYS-540, DEVELOPMENTAL
RP STAGE, AND TISSUE SPECIFICITY.
RX PubMed=15549374; DOI=10.1007/s00425-004-1378-3;
RA Cao X., Li K., Suh S.-G., Guo T., Becraft P.W.;
RT "Molecular analysis of the CRINKLY4 gene family in Arabidopsis thaliana.";
RL Planta 220:645-657(2005).
RN [7]
RP FUNCTION, MUTAGENESIS OF CYS-221, AND SUBCELLULAR LOCATION.
RX PubMed=15772284; DOI=10.1105/tpc.104.029975;
RA Gifford M.L., Robertson F.C., Soares D.C., Ingram G.C.;
RT "ARABIDOPSIS CRINKLY4 function, internalization, and turnover are dependent
RT on the extracellular crinkly repeat domain.";
RL Plant Cell 17:1154-1166(2005).
RN [8]
RP FUNCTION, AUTOPHOSPHORYLATION, AND PHOSPHORYLATION BY ALE2.
RX PubMed=17376810; DOI=10.1242/dev.003533;
RA Tanaka H., Watanabe M., Sasabe M., Hiroe T., Tanaka T., Tsukaya H.,
RA Ikezaki M., Machida C., Machida Y.;
RT "Novel receptor-like kinase ALE2 controls shoot development by specifying
RT epidermis in Arabidopsis.";
RL Development 134:1643-1652(2007).
RN [9]
RP HOMODIMERIZATION, AND MUTAGENESIS OF ALA-433; GLY-438 AND ALA-452.
RX PubMed=18539132; DOI=10.1016/j.abb.2008.05.010;
RA Stokes K.D., Gururaj Rao A.;
RT "Dimerization properties of the transmembrane domains of Arabidopsis
RT CRINKLY4 receptor-like kinase and homologs.";
RL Arch. Biochem. Biophys. 477:219-226(2008).
RN [10]
RP FUNCTION, AND DEVELOPMENTAL STAGE.
RX PubMed=18948541; DOI=10.1126/science.1160158;
RA De Smet I., Vassileva V., De Rybel B., Levesque M.P., Grunewald W.,
RA Van Damme D., Van Noorden G., Naudts M., Van Isterdael G., De Clercq R.,
RA Wang J.Y., Meuli N., Vanneste S., Friml J., Hilson P., Juergens G.,
RA Ingram G.C., Inze D., Benfey P.N., Beeckman T.;
RT "Receptor-like kinase ACR4 restricts formative cell divisions in the
RT Arabidopsis root.";
RL Science 322:594-597(2008).
RN [11]
RP FUNCTION, AND INDUCTION BY CLE40.
RX PubMed=19398337; DOI=10.1016/j.cub.2009.03.060;
RA Stahl Y., Wink R.H., Ingram G.C., Simon R.;
RT "A signaling module controlling the stem cell niche in Arabidopsis root
RT meristems.";
RL Curr. Biol. 19:909-914(2009).
RN [12]
RP GENE FAMILY.
RX PubMed=19529822; DOI=10.1093/mp/ssn083;
RA Chae L., Sudat S., Dudoit S., Zhu T., Luan S.;
RT "Diverse transcriptional programs associated with environmental stress and
RT hormones in the Arabidopsis receptor-like kinase gene family.";
RL Mol. Plant 2:84-107(2009).
RN [13]
RP REVIEW.
RX PubMed=20016993; DOI=10.1007/s00709-009-0095-y;
RA Wang G., Fiers M.;
RT "CLE peptide signaling during plant development.";
RL Protoplasma 240:33-43(2010).
RN [14]
RP INTERACTION WITH PP2A3, AND PHOSPHORYLATION AT SER-475.
RX PubMed=26792519; DOI=10.1073/pnas.1525122113;
RA Yue K., Sandal P., Williams E.L., Murphy E., Stes E., Nikonorova N.,
RA Ramakrishna P., Czyzewicz N., Montero-Morales L., Kumpf R., Lin Z.,
RA van de Cotte B., Iqbal M., Van Bel M., Van De Slijke E., Meyer M.R.,
RA Gadeyne A., Zipfel C., De Jaeger G., Van Montagu M., Van Damme D.,
RA Gevaert K., Rao A.G., Beeckman T., De Smet I.;
RT "PP2A-3 interacts with ACR4 and regulates formative cell division in the
RT Arabidopsis root.";
RL Proc. Natl. Acad. Sci. U.S.A. 113:1447-1452(2016).
CC -!- FUNCTION: Controls formative cell division in meristems, including root
CC tips and lateral root initiation zones of the pericycle, in response to
CC CLE40 signal. Acts with CLE40p peptide as a ligand-receptor pair in a
CC signal transduction pathway, coordinating movement of the root tip and
CC organization of cell divisions in the root meristem. Required during
CC embryogenesis and development, probably for the differentiation of
CC protoderm and epidermal cells. Involved in the regulation of cellular
CC organization during the development of sepal margins and ovule
CC integument outgrowth. Can phosphorylate ALE2.
CC {ECO:0000269|PubMed:11978870, ECO:0000269|PubMed:12900442,
CC ECO:0000269|PubMed:15255860, ECO:0000269|PubMed:15772284,
CC ECO:0000269|PubMed:17376810, ECO:0000269|PubMed:18948541,
CC ECO:0000269|PubMed:19398337}.
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:0000269|PubMed:12900442, ECO:0000269|PubMed:15549374};
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:0000269|PubMed:12900442,
CC ECO:0000269|PubMed:15549374};
CC -!- SUBUNIT: Homodimer (Probable). Interacts with PP2A3 (PubMed:26792519).
CC {ECO:0000269|PubMed:26792519, ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: Cell membrane; Single-pass type I membrane
CC protein. Endosome, multivesicular body membrane; Single-pass type I
CC membrane protein. Note=Also localized into protein export bodies.
CC Internalization may be involved in degradation of ACR4 for its rapid
CC turn-over. In the epidermis, mostly expressed in the lateral and basal
CC planes of cells.
CC -!- TISSUE SPECIFICITY: Expressed in seedlings, floral buds, siliques,
CC leaves, shoot apical meristems (SAM), and, to a lower extent, in roots.
CC {ECO:0000269|PubMed:11978870, ECO:0000269|PubMed:15549374}.
CC -!- DEVELOPMENTAL STAGE: First observed in all young embryo cells. At the
CC globular stage, restricted to apical region. Later confined to the
CC protoderm area leading to cotyledon primordia and the root apex. In
CC mature embryos, mostly localized in the L1 layer of the SAM, apical
CC regions of cotyledons and the root apex, and, to a lower extent, in
CC protoderm of other regions. In seedlings, expressed in developing
CC tissues of the shoot, including the SAM and epidermis of organs
CC primordia, especially in L1 layer cells. In roots, localized in
CC quiescent center (QC) central cells, columella initials and cells below
CC the QC, the lateral root cap (LRC) and the initial cells destined to
CC give rise to the root epidermal cell file and the LRC. Expressed in
CC epidermal emerged from under the LRC, with levels vanishing in
CC elongation zone. Specifically detected in the small daughter cells
CC after the first asymmetric pericycle cell division during lateral roots
CC emergence. Subsequently, the expression expands to the adjacent small
CC daughter cells from the second asymmetric cell division, resulting in a
CC central core-specific expression pattern. {ECO:0000269|PubMed:11978870,
CC ECO:0000269|PubMed:12900442, ECO:0000269|PubMed:15549374,
CC ECO:0000269|PubMed:18948541}.
CC -!- INDUCTION: By CLE40 in root quiescent center (QC).
CC {ECO:0000269|PubMed:19398337}.
CC -!- PTM: Autophosphorylated and phosphorylated by ALE2.
CC {ECO:0000269|PubMed:17376810}.
CC -!- DISRUPTION PHENOTYPE: Reduced fertility due to abnormal embryogenesis
CC and integument formation. Abnormal seed coat and leaves epidermis, with
CC transient fusion between adjacent developing leaves and reduced
CC hydrophobicity of leaf surfaces. {ECO:0000269|PubMed:11978870,
CC ECO:0000269|PubMed:12900442, ECO:0000269|PubMed:15255860}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein
CC kinase family. {ECO:0000255|PROSITE-ProRule:PRU00159}.
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; AB074762; BAB91132.1; -; mRNA.
DR EMBL; AL356014; CAB91612.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE79920.1; -; Genomic_DNA.
DR PIR; T49010; T49010.
DR RefSeq; NP_191501.1; NM_115804.4.
DR PDB; 7A0J; X-ray; 1.95 A; AAA/BBB/CCC/DDD=30-335.
DR PDBsum; 7A0J; -.
DR AlphaFoldDB; Q9LX29; -.
DR SMR; Q9LX29; -.
DR BioGRID; 10426; 2.
DR STRING; 3702.AT3G59420.1; -.
DR PaxDb; Q9LX29; -.
DR PRIDE; Q9LX29; -.
DR ProteomicsDB; 244760; -.
DR EnsemblPlants; AT3G59420.1; AT3G59420.1; AT3G59420.
DR GeneID; 825111; -.
DR Gramene; AT3G59420.1; AT3G59420.1; AT3G59420.
DR KEGG; ath:AT3G59420; -.
DR Araport; AT3G59420; -.
DR TAIR; locus:2081227; AT3G59420.
DR eggNOG; ENOG502QUN0; Eukaryota.
DR HOGENOM; CLU_009948_0_0_1; -.
DR InParanoid; Q9LX29; -.
DR OMA; TPAHFPF; -.
DR OrthoDB; 684563at2759; -.
DR PhylomeDB; Q9LX29; -.
DR PRO; PR:Q9LX29; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q9LX29; baseline and differential.
DR Genevisible; Q9LX29; AT.
DR GO; GO:0009986; C:cell surface; IDA:TAIR.
DR GO; GO:0030139; C:endocytic vesicle; IDA:TAIR.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0032585; C:multivesicular body membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; IDA:TAIR.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0042803; F:protein homodimerization activity; 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:0019199; F:transmembrane receptor protein kinase activity; ISS:TAIR.
DR GO; GO:0009793; P:embryo development ending in seed dormancy; IMP:TAIR.
DR GO; GO:0048439; P:flower morphogenesis; IEA:EnsemblPlants.
DR GO; GO:0010311; P:lateral root formation; IMP:TAIR.
DR GO; GO:0090627; P:plant epidermal cell differentiation; IEA:EnsemblPlants.
DR GO; GO:0046777; P:protein autophosphorylation; IEA:EnsemblPlants.
DR GO; GO:0009786; P:regulation of asymmetric cell division; IMP:TAIR.
DR GO; GO:0048829; P:root cap development; IMP:TAIR.
DR GO; GO:0048364; P:root development; IMP:TAIR.
DR Gene3D; 2.130.10.30; -; 2.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR009091; RCC1/BLIP-II.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR InterPro; IPR001368; TNFR/NGFR_Cys_rich_reg.
DR Pfam; PF00069; Pkinase; 1.
DR SMART; SM00220; S_TKc; 1.
DR SMART; SM00208; TNFR; 1.
DR SUPFAM; SSF50985; SSF50985; 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.
DR PROSITE; PS50050; TNFR_NGFR_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; ATP-binding; Cell membrane; Developmental protein;
KW Disulfide bond; Endosome; Glycoprotein; Kinase; Membrane;
KW Nucleotide-binding; Phosphoprotein; Receptor; Reference proteome; Repeat;
KW Serine/threonine-protein kinase; Signal; Transferase; Transmembrane;
KW Transmembrane helix.
FT SIGNAL 1..29
FT /evidence="ECO:0000255"
FT CHAIN 30..895
FT /note="Serine/threonine-protein kinase-like protein ACR4"
FT /id="PRO_0000382750"
FT TOPO_DOM 30..434
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 435..455
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 456..895
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REPEAT 38..73
FT /note="1"
FT REPEAT 77..112
FT /note="2"
FT REPEAT 130..167
FT /note="3"
FT REPEAT 169..202
FT /note="4"
FT REPEAT 210..245
FT /note="5"
FT REPEAT 262..296
FT /note="6"
FT REPEAT 301..339
FT /note="7"
FT REPEAT 346..395
FT /note="TNFR-Cys"
FT DOMAIN 512..789
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 38..339
FT /note="7 X 36 AA repeats"
FT REGION 818..895
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 824..853
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 854..875
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 641
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 518..526
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 540
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000305"
FT MOD_RES 475
FT /note="Phosphoserine"
FT CARBOHYD 158
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 196
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 290
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 398
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 410
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 347..370
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00206"
FT DISULFID 373..387
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00206"
FT DISULFID 377..395
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00206"
FT MUTAGEN 221
FT /note="C->Y: In acr4-7; abnormal embryogenesis, and reduced
FT internalization into vesicles."
FT /evidence="ECO:0000269|PubMed:15772284"
FT MUTAGEN 433
FT /note="A->F: Enhanced dimerization."
FT /evidence="ECO:0000269|PubMed:18539132"
FT MUTAGEN 438
FT /note="G->V: Enhanced dimerization."
FT /evidence="ECO:0000269|PubMed:18539132"
FT MUTAGEN 452
FT /note="A->C: Unchanged dimerization."
FT /evidence="ECO:0000269|PubMed:18539132"
FT MUTAGEN 540
FT /note="K->L,M,W: Loss of kinase activity."
FT /evidence="ECO:0000269|PubMed:12900442,
FT ECO:0000269|PubMed:15255860, ECO:0000269|PubMed:15549374"
SQ SEQUENCE 895 AA; 98181 MW; 1B6BD5BB5F0B9DFC CRC64;
MRMFETRARE WILLVKLVLF TSIWQLASAL GSMSSIAISY GEGGSVFCGL KSDGSHLVVC
YGSNSAILYG TPGHLQFIGL TGGDGFMCGL LMLSHQPYCW GNSAFIQMGV PQPMTKGAEY
LEVSAGDYHL CGLRKPIVGR RKNSNIISSS LVDCWGYNMT RNFVFDKQLH SLSAGSEFNC
ALSSKDKSVF CWGDENSSQV ISLIPKEKKF QKIAAGGYHV CGILDGLESR VLCWGKSLEF
EEEVTGTSTE EKILDLPPKE PLLAVVGGKF YACGIKRYDH SAVCWGFFVN RSTPAPTGIG
FYDLAAGNYF TCGVLTGTSM SPVCWGLGFP ASIPLAVSPG LCIDTPCPPG THELSNQENS
PCKFTGSHIC LPCSTSCPPG MYQKSVCTER SDQVCVYNCS SCSSHDCSSN CSSSATSGGK
EKGKFWSLQL PIATAEIGFA LFLVAVVSIT AALYIRYRLR NCRCSENDTR SSKDSAFTKD
NGKIRPDLDE LQKRRRARVF TYEELEKAAD GFKEESIVGK GSFSCVYKGV LRDGTTVAVK
RAIMSSDKQK NSNEFRTELD LLSRLNHAHL LSLLGYCEEC GERLLVYEFM AHGSLHNHLH
GKNKALKEQL DWVKRVTIAV QAARGIEYLH GYACPPVIHR DIKSSNILID EEHNARVADF
GLSLLGPVDS GSPLAELPAG TLGYLDPEYY RLHYLTTKSD VYSFGVLLLE ILSGRKAIDM
HYEEGNIVEW AVPLIKAGDI NALLDPVLKH PSEIEALKRI VSVACKCVRM RGKDRPSMDK
VTTALERALA QLMGNPSSEQ PILPTEVVLG SSRMHKKSWR IGSKRSGSEN TEFRGGSWIT
FPSVTSSQRR KSSASEGDVA EEEDEGRKQQ EALRSLEEEI GPASPGQSLF LHHNF
