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A7XQ02

- MLX56_MORAL

UniProt

A7XQ02 - MLX56_MORAL

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Protein

Mulatexin

Gene
N/A
Organism
Morus alba (White mulberry)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli

Functioni

Chitin-binding protein which slows larval growth when consumed by the lepidopteran species S.ricini and M.brassica, but not when consumed by the mulberry specialist B.mori. Lacks chitinase activity.1 Publication

GO - Molecular functioni

  1. chitin binding Source: UniProtKB-KW

GO - Biological processi

  1. cell wall macromolecule catabolic process Source: InterPro
  2. defense response to insect Source: UniProtKB
Complete GO annotation...

Keywords - Biological processi

Plant defense

Keywords - Ligandi

Chitin-binding

Protein family/group databases

CAZyiCBM18. Carbohydrate-Binding Module Family 18.
GH19. Glycoside Hydrolase Family 19.

Names & Taxonomyi

Protein namesi
Recommended name:
Mulatexin1 Publication
Short name:
MLX561 Publication
Alternative name(s):
Latex proteinImported
OrganismiMorus alba (White mulberry)
Taxonomic identifieri3498 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsfabidsRosalesMoraceaeMorus

Subcellular locationi

Secreted 1 Publication

GO - Cellular componenti

  1. extracellular region Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 21211 PublicationSequence AnalysisAdd
BLAST
Chaini22 – 415394Mulatexin1 PublicationPRO_0000401103Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi26 ↔ 41By similarityPROSITE-ProRule annotation
Disulfide bondi35 ↔ 47By similarityPROSITE-ProRule annotation
Disulfide bondi40 ↔ 54By similarityPROSITE-ProRule annotation
Disulfide bondi60 ↔ 64By similarityPROSITE-ProRule annotation
Disulfide bondi128 ↔ 143By similarityPROSITE-ProRule annotation
Disulfide bondi137 ↔ 149By similarityPROSITE-ProRule annotation
Disulfide bondi142 ↔ 156By similarityPROSITE-ProRule annotation
Disulfide bondi161 ↔ 165By similarityPROSITE-ProRule annotation
Glycosylationi264 – 2641N-linked (GlcNAc...)Sequence Analysis

Post-translational modificationi

Glycosylated.1 Publication

Keywords - PTMi

Disulfide bond, Glycoprotein

Structurei

3D structure databases

ProteinModelPortaliA7XQ02.
SMRiA7XQ02. Positions 122-168, 181-410.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini23 – 6644Chitin-binding type-1 1PROSITE-ProRule annotationAdd
BLAST
Domaini125 – 16743Chitin-binding type-1 2PROSITE-ProRule annotationAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi68 – 13972Pro-richSequence AnalysisAdd
BLAST

Sequence similaritiesi

Contains 2 chitin-binding type-1 domains.PROSITE-ProRule annotation

Keywords - Domaini

Repeat, Signal

Family and domain databases

Gene3Di3.30.60.10. 2 hits.
InterProiIPR001002. Chitin-bd_1.
IPR018371. Chitin-binding_1_CS.
IPR000726. Glyco_hydro_19_cat.
IPR023346. Lysozyme-like_dom.
[Graphical view]
PfamiPF00187. Chitin_bind_1. 2 hits.
PF00182. Glyco_hydro_19. 1 hit.
[Graphical view]
ProDomiPD000609. Chitin_bd_1. 2 hits.
[Graphical view] [Entries sharing at least one domain]
SMARTiSM00270. ChtBD1. 2 hits.
[Graphical view]
SUPFAMiSSF53955. SSF53955. 1 hit.
SSF57016. SSF57016. 2 hits.
PROSITEiPS00026. CHIT_BIND_I_1. 1 hit.
PS50941. CHIT_BIND_I_2. 2 hits.
PS00773. CHITINASE_19_1. 1 hit.
PS00774. CHITINASE_19_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

A7XQ02-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MKFRTLLIIF SLVFLLEIVS ASEPQCGRDA GGALCHGNLC CSHWGFCGTT
60 70 80 90 100
AIYCDVDQGC QSQCWSSPPP PSPPPPPPSP PPPSPPPPSP PPPSPPPPSP
110 120 130 140 150
PPPSPPPPSP PPPSPPPPGG PERPDHRCGR ALGNPPCNPG RCCSIHNWCG
160 170 180 190 200
STAAYCRGSS CQYQCWNSLL SALISNGNNA ISKIISKSVF DEMFKHMKDC
210 220 230 240 250
PSKGFYSYDA FIIATTSFPH FGTTGDITTR KRELAAFFAQ TSLATTGQRF
260 270 280 290 300
DSQDLYVWGY CHINETTNGN DNDYCTSAHW PCPSGKKYNS RGAVQLTHNY
310 320 330 340 350
NYGLAGEALG LDLINNPDLV ATDPVISFKT AIWFWMAQHD NKLSCHDILI
360 370 380 390 400
NANSGYVIGN IIKNSGYQNG LITNTISTMR GIGYYKRYCD MLGVSYGDNL
410
DSWYDQTHFS EVARM
Length:415
Mass (Da):45,148
Last modified:April 29, 2008 - v2
Checksum:i3555EA15320D6457
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
EF535852 mRNA. Translation: ABS86614.2.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
EF535852 mRNA. Translation: ABS86614.2 .

3D structure databases

ProteinModelPortali A7XQ02.
SMRi A7XQ02. Positions 122-168, 181-410.
ModBasei Search...
MobiDBi Search...

Protein family/group databases

CAZyi CBM18. Carbohydrate-Binding Module Family 18.
GH19. Glycoside Hydrolase Family 19.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Family and domain databases

Gene3Di 3.30.60.10. 2 hits.
InterProi IPR001002. Chitin-bd_1.
IPR018371. Chitin-binding_1_CS.
IPR000726. Glyco_hydro_19_cat.
IPR023346. Lysozyme-like_dom.
[Graphical view ]
Pfami PF00187. Chitin_bind_1. 2 hits.
PF00182. Glyco_hydro_19. 1 hit.
[Graphical view ]
ProDomi PD000609. Chitin_bd_1. 2 hits.
[Graphical view ] [Entries sharing at least one domain ]
SMARTi SM00270. ChtBD1. 2 hits.
[Graphical view ]
SUPFAMi SSF53955. SSF53955. 1 hit.
SSF57016. SSF57016. 2 hits.
PROSITEi PS00026. CHIT_BIND_I_1. 1 hit.
PS50941. CHIT_BIND_I_2. 2 hits.
PS00773. CHITINASE_19_1. 1 hit.
PS00774. CHITINASE_19_2. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  1. "A unique latex protein, MLX56, defends mulberry trees from insects."
    Wasano N., Konno K., Nakamura M., Hirayama C., Hattori M., Tateishi K.
    Phytochemistry 70:880-888(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 22-30, FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, GLYCOSYLATION.
    Strain: cv. Shin-ichinose1 Publication.
    Tissue: Latex1 Publication.

Entry informationi

Entry nameiMLX56_MORAL
AccessioniPrimary (citable) accession number: A7XQ02
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 2, 2010
Last sequence update: April 29, 2008
Last modified: October 1, 2014
This is version 28 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Miscellaneousi

Miscellaneous

On the 2D-gel the determined MW of this protein is: 56 kDa.1 Publication

Keywords - Technical termi

Direct protein sequencing

Documents

  1. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3