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Protein

Mulatexin

Gene
N/A
Organism
Morus alba (White mulberry)
Status
Reviewed-Annotation score: 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

GO - Biological processi

  • cell wall macromolecule catabolic process Source: InterPro
  • 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

GO - Cellular componenti

  • 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 ↔ 41PROSITE-ProRule annotationBy similarity
Disulfide bondi35 ↔ 47PROSITE-ProRule annotationBy similarity
Disulfide bondi40 ↔ 54PROSITE-ProRule annotationBy similarity
Disulfide bondi60 ↔ 64PROSITE-ProRule annotationBy similarity
Disulfide bondi128 ↔ 143PROSITE-ProRule annotationBy similarity
Disulfide bondi137 ↔ 149PROSITE-ProRule annotationBy similarity
Disulfide bondi142 ↔ 156PROSITE-ProRule annotationBy similarity
Disulfide bondi161 ↔ 165PROSITE-ProRule annotationBy similarity
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:
EMBLi
GenBanki
DDBJi
Links Updated
EF535852 mRNA. Translation: ABS86614.2.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
EF535852 mRNA. Translation: ABS86614.2.

3D structure databases

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

Protein family/group databases

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

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

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]
ProtoNetiSearch...

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: May 27, 2015
This is version 30 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.