SUB_ARATH
ID SUB_ARATH Reviewed; 768 AA.
AC Q8RWZ1; O04081; Q9SXA2;
DT 04-DEC-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2002, sequence version 1.
DT 03-AUG-2022, entry version 146.
DE RecName: Full=Protein STRUBBELIG;
DE AltName: Full=Leucine-rich repeat receptor kinase-like protein SUB;
DE AltName: Full=Protein SCRAMBLED;
DE Flags: Precursor;
GN Name=SUB; Synonyms=SCM; OrderedLocusNames=At1g11130;
GN ORFNames=T19D16.1, T19D16.8, T28P6.18;
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], MUTAGENESIS OF VAL-64; 288-GLN--ILE-768;
RP 337-TRP--ILE-768; GLY-506; LYS-525; GLU-539 AND ARG-599, LACK OF KINASE
RP ACTIVITY, AND TISSUE SPECIFICITY.
RC STRAIN=cv. Landsberg erecta;
RX PubMed=15951420; DOI=10.1073/pnas.0503526102;
RA Chevalier D., Batoux M., Fulton L., Pfister K., Yadav R.K.,
RA Schellenberg M., Schneitz K.;
RT "STRUBBELIG defines a receptor kinase-mediated signaling pathway regulating
RT organ development in Arabidopsis.";
RL Proc. Natl. Acad. Sci. U.S.A. 102:9074-9079(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130712; DOI=10.1038/35048500;
RA Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O.,
RA Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
RA Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
RA Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
RA Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
RA Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
RA Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
RA Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
RA Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A.,
RA Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
RA Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
RA Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
RA Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D.,
RA Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
RL Nature 408:816-820(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;
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, MUTAGENESIS OF 324-GLN--ILE-768, AND TISSUE SPECIFICITY.
RC STRAIN=cv. Wassilewskija;
RX PubMed=15618487; DOI=10.1126/science.1105373;
RA Kwak S.-H., Shen R., Schiefelbein J.;
RT "Positional signaling mediated by a receptor-like kinase in Arabidopsis.";
RL Science 307:1111-1113(2005).
RN [7]
RP FUNCTION.
RX PubMed=16317033; DOI=10.1093/jxb/erj037;
RA Dolan L.;
RT "Positional information and mobile transcriptional regulators determine
RT cell pattern in the Arabidopsis root epidermis.";
RL J. Exp. Bot. 57:51-54(2006).
RN [8]
RP FUNCTION, AND DEVELOPMENTAL STAGE.
RX PubMed=17027738; DOI=10.1016/j.ydbio.2006.09.009;
RA Kwak S.-H., Schiefelbein J.;
RT "The role of the SCRAMBLED receptor-like kinase in patterning the
RT Arabidopsis root epidermis.";
RL Dev. Biol. 302:118-131(2007).
RN [9]
RP LACK OF COMPLEMENTATION.
RC STRAIN=cv. Columbia;
RX PubMed=17397538; DOI=10.1186/1471-2229-7-16;
RA Eyueboglu B., Pfister K., Haberer G., Chevalier D., Fuchs A., Mayer K.F.X.,
RA Schneitz K.;
RT "Molecular characterisation of the STRUBBELIG-RECEPTOR FAMILY of genes
RT encoding putative leucine-rich repeat receptor-like kinases in Arabidopsis
RT thaliana.";
RL BMC Plant Biol. 7:16-16(2007).
RN [10]
RP FUNCTION, ACTIVITY REGULATION, AND SUBCELLULAR LOCATION.
RX PubMed=18771664; DOI=10.1016/j.ydbio.2008.08.010;
RA Yadav R.K., Fulton L., Batoux M., Schneitz K.;
RT "The Arabidopsis receptor-like kinase STRUBBELIG mediates inter-cell-layer
RT signaling during floral development.";
RL Dev. Biol. 323:261-270(2008).
RN [11]
RP FUNCTION, 3D-STRUCTURE MODELING, MUTAGENESIS OF CYS-57; VAL-64; CYS-66;
RP SER-69; SER-222; PRO-258; PRO-272; PRO-304; GLY-357; SER-466; PRO-473;
RP SER-545; ARG-599 AND LEU-633, AND DISULFIDE BOND.
RX PubMed=21603601; DOI=10.1371/journal.pone.0019730;
RA Vaddepalli P., Fulton L., Batoux M., Yadav R.K., Schneitz K.;
RT "Structure-function analysis of STRUBBELIG, an Arabidopsis atypical
RT receptor-like kinase involved in tissue morphogenesis.";
RL PLoS ONE 6:E19730-E19730(2011).
RN [12]
RP INTERACTION WITH AN.
RX PubMed=23368817; DOI=10.1186/1471-2229-13-16;
RA Bai Y., Vaddepalli P., Fulton L., Bhasin H., Hulskamp M., Schneitz K.;
RT "ANGUSTIFOLIA is a central component of tissue morphogenesis mediated by
RT the atypical receptor-like kinase STRUBBELIG.";
RL BMC Plant Biol. 13:16-16(2013).
CC -!- FUNCTION: Regulates the expression of transcription factors that define
CC the cell fates. Acts in a non-cell-autonomous fashion, functions in a
CC radial inside-out signaling process, and mediates cell morphogenesis
CC and cell fate across clonally distinct cell layers in floral primordia,
CC developing ovules, and root meristems. Seems to be required for the
CC regulation of cell shape and the orientation of the mitotic division
CC plane. Involved in root hair specification, in the formation of the
CC outer integument and the shape of organs such as carpels and petals and
CC is necessary for the shape and height of the stem. Non-functional SUB
CC proteins are retained in the endoplasmic reticulum and degraded by
CC endoplasmic reticulum-associated degradation (ERAD).
CC {ECO:0000269|PubMed:15618487, ECO:0000269|PubMed:16317033,
CC ECO:0000269|PubMed:17027738, ECO:0000269|PubMed:18771664,
CC ECO:0000269|PubMed:21603601}.
CC -!- ACTIVITY REGULATION: Regulated at the post-transcriptional level.
CC {ECO:0000269|PubMed:18771664}.
CC -!- SUBUNIT: Interacts (via intra-cellular domain) with AN; this
CC interaction is not required for correct subcellular localization and
CC recycling of SUB. {ECO:0000269|PubMed:23368817}.
CC -!- INTERACTION:
CC Q8RWZ1; O04567: At1g27190; NbExp=2; IntAct=EBI-17072125, EBI-1238687;
CC Q8RWZ1; C0LGI5: At1g69990; NbExp=3; IntAct=EBI-17072125, EBI-20651225;
CC Q8RWZ1; Q9ZQR3: At2g14510; NbExp=2; IntAct=EBI-17072125, EBI-20651957;
CC Q8RWZ1; Q8VYT3: At4g30520; NbExp=2; IntAct=EBI-17072125, EBI-16902452;
CC Q8RWZ1; Q9ASS4: At5g48380; NbExp=2; IntAct=EBI-17072125, EBI-6298290;
CC Q8RWZ1; Q94F62: BAK1; NbExp=4; IntAct=EBI-17072125, EBI-617138;
CC Q8RWZ1; O22476: BRI1; NbExp=2; IntAct=EBI-17072125, EBI-1797828;
CC Q8RWZ1; Q9ZWC8: BRL1; NbExp=2; IntAct=EBI-17072125, EBI-590903;
CC Q8RWZ1; Q42371: ERECTA; NbExp=3; IntAct=EBI-17072125, EBI-16940407;
CC Q8RWZ1; C0LGW6: ERL1; NbExp=4; IntAct=EBI-17072125, EBI-16914248;
CC Q8RWZ1; Q6XAT2: ERL2; NbExp=4; IntAct=EBI-17072125, EBI-16895926;
CC Q8RWZ1; Q9C8I6: IOS1; NbExp=3; IntAct=EBI-17072125, EBI-16924837;
CC Q8RWZ1; Q9ZVD4: LRR-RLK; NbExp=2; IntAct=EBI-17072125, EBI-20651739;
CC Q8RWZ1; Q9C7S5: PSY1R; NbExp=2; IntAct=EBI-17072125, EBI-16904988;
CC Q8RWZ1; Q9ZRF9: RPK1; NbExp=2; IntAct=EBI-17072125, EBI-1238953;
CC Q8RWZ1; Q94AG2: SERK1; NbExp=4; IntAct=EBI-17072125, EBI-1555537;
CC Q8RWZ1; Q9SKG5: SERK4; NbExp=4; IntAct=EBI-17072125, EBI-6290483;
CC Q8RWZ1; Q6R2K3: SRF3; NbExp=2; IntAct=EBI-17072125, EBI-20651925;
CC Q8RWZ1; Q6R2K1: SRF5; NbExp=2; IntAct=EBI-17072125, EBI-20651875;
CC Q8RWZ1; Q9C8M9: SRF6; NbExp=2; IntAct=EBI-17072125, EBI-16954301;
CC Q8RWZ1; Q8RWZ1: SUB; NbExp=2; IntAct=EBI-17072125, EBI-17072125;
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Single-pass membrane
CC protein {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Expressed in leaves, stems, inflorescences, flower
CC buds and developing root epidermis. {ECO:0000269|PubMed:15618487,
CC ECO:0000269|PubMed:15951420}.
CC -!- DEVELOPMENTAL STAGE: Required for epidermal patterning during
CC postembryonic root development, but not involved in hypocotyl
CC development. {ECO:0000269|PubMed:17027738}.
CC -!- DOMAIN: The protein kinase domain is catalytically inactive, but
CC nevertheless important for SUB function.
CC -!- MISCELLANEOUS: Cannot be functionally replaced by the SRF1 to SRF8
CC proteins.
CC -!- MISCELLANEOUS: The sub/scm phenotype is sensitive to ecotype and is
CC greatly reduced in cv. Columbia background.
CC -!- MISCELLANEOUS: Phosphorylation of Thr-486, Thr-494 or Ser-656 is not
CC required for SUB function. {ECO:0000305|PubMed:21603601}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein
CC kinase family. {ECO:0000255|PROSITE-ProRule:PRU00159}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAB65472.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=AAD50000.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AF399923; AAQ03031.1; -; mRNA.
DR EMBL; AC007259; AAD50000.1; ALT_INIT; Genomic_DNA.
DR EMBL; U95973; AAB65472.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002684; AEE28690.1; -; Genomic_DNA.
DR EMBL; AY091019; AAM14041.1; -; mRNA.
DR EMBL; AY117318; AAM51393.1; -; mRNA.
DR EMBL; AK227100; BAE99152.1; -; mRNA.
DR PIR; D86245; D86245.
DR RefSeq; NP_172580.2; NM_100986.4.
DR AlphaFoldDB; Q8RWZ1; -.
DR SMR; Q8RWZ1; -.
DR BioGRID; 22894; 33.
DR IntAct; Q8RWZ1; 32.
DR STRING; 3702.AT1G11130.1; -.
DR iPTMnet; Q8RWZ1; -.
DR PaxDb; Q8RWZ1; -.
DR PRIDE; Q8RWZ1; -.
DR ProteomicsDB; 245352; -.
DR EnsemblPlants; AT1G11130.1; AT1G11130.1; AT1G11130.
DR GeneID; 837654; -.
DR Gramene; AT1G11130.1; AT1G11130.1; AT1G11130.
DR KEGG; ath:AT1G11130; -.
DR Araport; AT1G11130; -.
DR TAIR; locus:2202084; AT1G11130.
DR eggNOG; KOG1187; Eukaryota.
DR HOGENOM; CLU_000288_92_2_1; -.
DR InParanoid; Q8RWZ1; -.
DR OMA; MDVRVVK; -.
DR OrthoDB; 684563at2759; -.
DR PhylomeDB; Q8RWZ1; -.
DR PRO; PR:Q8RWZ1; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q8RWZ1; baseline and differential.
DR Genevisible; Q8RWZ1; AT.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IDA:TAIR.
DR GO; GO:0009506; C:plasmodesma; 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:0004672; F:protein kinase activity; IEA:InterPro.
DR GO; GO:0000902; P:cell morphogenesis; IMP:TAIR.
DR GO; GO:0048437; P:floral organ development; IMP:TAIR.
DR GO; GO:0048366; P:leaf development; IMP:TAIR.
DR GO; GO:0010305; P:leaf vascular tissue pattern formation; IMP:TAIR.
DR GO; GO:0048481; P:plant ovule development; IMP:TAIR.
DR GO; GO:0010059; P:positive regulation of atrichoblast fate specification; IMP:TAIR.
DR GO; GO:0010063; P:positive regulation of trichoblast fate specification; IMP:TAIR.
DR GO; GO:0006468; P:protein phosphorylation; IBA:GO_Central.
DR GO; GO:0042127; P:regulation of cell population proliferation; IMP:TAIR.
DR GO; GO:0010071; P:root meristem specification; IMP:TAIR.
DR GO; GO:0048367; P:shoot system development; TAS:TAIR.
DR Gene3D; 3.80.10.10; -; 2.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR001611; Leu-rich_rpt.
DR InterPro; IPR032675; LRR_dom_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR Pfam; PF13855; LRR_8; 1.
DR Pfam; PF00069; Pkinase; 1.
DR SUPFAM; SSF56112; SSF56112; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Cell membrane; Disulfide bond; Glycoprotein;
KW Leucine-rich repeat; Membrane; Nucleotide-binding; Receptor;
KW Reference proteome; Repeat; Signal; Transmembrane; Transmembrane helix.
FT SIGNAL 1..24
FT /evidence="ECO:0000255"
FT CHAIN 25..768
FT /note="Protein STRUBBELIG"
FT /id="PRO_0000311840"
FT TOPO_DOM 25..341
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 342..362
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 363..768
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REPEAT 94..115
FT /note="LRR 1"
FT REPEAT 116..139
FT /note="LRR 2"
FT REPEAT 140..162
FT /note="LRR 3"
FT REPEAT 164..186
FT /note="LRR 4"
FT REPEAT 188..210
FT /note="LRR 5"
FT REPEAT 211..231
FT /note="LRR 6"
FT DOMAIN 497..768
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 241..334
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 385..477
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 245..302
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 308..334
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 440..477
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 503..511
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 525
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT CARBOHYD 70
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 119
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 243
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 57..66
FT /evidence="ECO:0000305|PubMed:21603601"
FT MUTAGEN 57
FT /note="C->Y: In sub-10; loss of function. Loss of function;
FT when associated with Y-66."
FT /evidence="ECO:0000269|PubMed:21603601"
FT MUTAGEN 64
FT /note="V->M: In sub-3; loss of function."
FT /evidence="ECO:0000269|PubMed:15951420,
FT ECO:0000269|PubMed:21603601"
FT MUTAGEN 66
FT /note="C->Y: Loss of function. Loss of function; when
FT associated with Y-57."
FT /evidence="ECO:0000269|PubMed:21603601"
FT MUTAGEN 69
FT /note="S->L: In sub-11; no phenotypic effect."
FT /evidence="ECO:0000269|PubMed:21603601"
FT MUTAGEN 222
FT /note="S->L: In sub-12; no phenotypic effect."
FT /evidence="ECO:0000269|PubMed:21603601"
FT MUTAGEN 258
FT /note="P->L: In sub-13; no phenotypic effect."
FT /evidence="ECO:0000269|PubMed:21603601"
FT MUTAGEN 272
FT /note="P->S: In sub-14; no phenotypic effect."
FT /evidence="ECO:0000269|PubMed:21603601"
FT MUTAGEN 288..768
FT /note="Missing: In sub-5; loss of function."
FT /evidence="ECO:0000269|PubMed:15951420"
FT MUTAGEN 304
FT /note="P->L: In sub-15; loss of function."
FT /evidence="ECO:0000269|PubMed:21603601"
FT MUTAGEN 324..768
FT /note="Missing: In scm-1; loss of function."
FT /evidence="ECO:0000269|PubMed:15618487"
FT MUTAGEN 337..768
FT /note="Missing: In sub-2; loss of function."
FT /evidence="ECO:0000269|PubMed:15951420"
FT MUTAGEN 357
FT /note="G->S: In sub-16; no phenotypic effect."
FT /evidence="ECO:0000269|PubMed:21603601"
FT MUTAGEN 466
FT /note="S->L: In sub-17; no phenotypic effect."
FT /evidence="ECO:0000269|PubMed:21603601"
FT MUTAGEN 473
FT /note="P->L: In sub-18; no phenotypic effect."
FT /evidence="ECO:0000269|PubMed:21603601"
FT MUTAGEN 506
FT /note="G->A: No phenotypic effect."
FT /evidence="ECO:0000269|PubMed:15951420"
FT MUTAGEN 525
FT /note="K->E: No phenotypic effect."
FT /evidence="ECO:0000269|PubMed:15951420"
FT MUTAGEN 539
FT /note="E->A: No phenotypic effect."
FT /evidence="ECO:0000269|PubMed:15951420"
FT MUTAGEN 545
FT /note="S->F: In sub-19; loss of function."
FT /evidence="ECO:0000269|PubMed:21603601"
FT MUTAGEN 599
FT /note="R->C: In sub-4; loss of function."
FT /evidence="ECO:0000269|PubMed:15951420,
FT ECO:0000269|PubMed:21603601"
FT MUTAGEN 633
FT /note="L->F: In sub-20; no phenotypic effect."
FT /evidence="ECO:0000269|PubMed:21603601"
SQ SEQUENCE 768 AA; 84460 MW; D7702FC30A8EFFCE CRC64;
MSFTRWEVFF GLSVLALTMP FSAGVTNLRD VSAINNLYIT LGAPSLHHWL AFGGDPCGEK
WQGVVCDSSN ITEIRIPGMK VGGGLSDTLA DFSSIQVMDF SSNHISGTIP QALPSSIRNL
SLSSNRFTGN IPFTLSFLSD LSELSLGSNL LSGEIPDYFQ QLSKLTKLDL SSNILEGHLP
SSMGDLASLK ILYLQDNKLT GTLDVIEDLF LTDLNVENNL FSGPIPPNLL KIPNFKKDGT
PFNTSIITPP PPPVVDPPPA THRAPPVPRI PPVSGVPPAP FAPFAPLQPQ QHPPPSPPLV
WSPPSSDNGG GDPWNSVSGQ PTLQISPPSG SGSGKFWSTQ RIILVVSSVA IIVLVSGLCV
TLWRCCRSKI YNRYYSGARK DLQRPYFNKP PSQPTPTMGK VSREPMVKPF DGYGAGDRKY
GYPMPQRAEE SRRAMPPTSY YNKDVNTPQK PLQQPPRQFQ SNDTASKRAA HFPPGLNSSS
SATVFTIASL QQYTNNFSEE NIIGEGSIGN VYRAELRHGK FLAVKKLSNT INRTQSDGEF
LNLVSNVLKL KRGHILELLG YCNEFGQRLL VYEYCPNGSL QDALHLDRKL HKKLTWNVRI
NIALGASKAL QFLHEVCQPP VVHQNFKSSK VLLDGKLSVR VADSGLAYML PPRPTSQMAG
YAAPEVEYGS YTCQSDVFSL GVVMLELLTG RRPFDRTRPR GHQTLAQWAI PRLHDIDALT
RMVDPSLHGA YPMKSLSRFA DIISRSLQME PGFRPPISEI VQDLQHMI
