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O76217 (PE1_ANOGA) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 75. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Peritrophin-1
Alternative name(s):
AgAper-1
Peritrophic matrix protein 1
Peritrophin A
Gene names
Name:Aper1
ORF Names:AGAP006795
OrganismAnopheles gambiae (African malaria mosquito) [Reference proteome]
Taxonomic identifier7165 [NCBI]
Taxonomic lineageEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraNematoceraCulicoideaCulicidaeAnophelinaeAnopheles

Protein attributes

Sequence length153 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at transcript level

General annotation (Comments)

Function

Binds chitin but not cellulose. May be involved in the spatial organization of PM. Ref.1

Tissue specificity

Adult peritrophic membrane. Ref.1

Developmental stage

Expressed in adult but not larval guts, whole pupae or whole bodies minus gut.

Post-translational modification

Glycosylated.

Sequence similarities

Contains 2 chitin-binding type-2 domains.

Ontologies

Keywords
   DomainRepeat
Signal
   LigandChitin-binding
   PTMDisulfide bond
Glycoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processchitin metabolic process

Inferred from electronic annotation. Source: InterPro

   Cellular_componentextracellular region

Inferred from electronic annotation. Source: InterPro

   Molecular_functionchitin binding

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 1717 Potential
Chain18 – 153136Peritrophin-1
PRO_0000023612

Regions

Domain18 – 7962Chitin-binding type-2 1
Domain92 – 15362Chitin-binding type-2 2

Amino acid modifications

Glycosylation631N-linked (GlcNAc...) Potential
Disulfide bond56 ↔ 69 By similarity
Disulfide bond130 ↔ 143 By similarity

Natural variations

Natural variant71L → V in strain: 4aRR, PEST.
Natural variant191D → V in strain: 4aRR, PEST.
Natural variant281E → K in strain: L3-5.
Natural variant371P → S in strain: L3-5.
Natural variant551K → Q in strain: Yaounde Yd41.
Natural variant731A → S in strain: Yaounde Yd21, Yaounde Yd35, Yaounde Yd41.
Natural variant881A → V in strain: G3.
Natural variant891P → S in strain: 4aRR, PEST.

Sequences

Sequence LengthMass (Da)Tools
O76217 [UniParc].

Last modified July 5, 2005. Version 2.
Checksum: 2207D5130F487338

FASTA15316,791
        10         20         30         40         50         60 
MKVSASLVLL LAAAVLADDR CPPQDDPEQP PVLLAHPTDC DKFLICNHGT PVVSKCPPGL 

        70         80         90        100        110        120 
LWNDSQKQCD YPAQAQCAPG VTPNTEPAPK PSPNCPPEYD PDHMVYIPHE TDCGKYYICD 

       130        140        150 
PYGVELEQTC PSGLHWNPVV NYCDFPELAQ CEE 

« Hide

References

« Hide 'large scale' references
[1]"A type I peritrophic matrix protein from the malaria vector Anopheles gambiae binds to chitin. Cloning, expression, and characterization."
Shen Z., Jacobs-Lorena M.
J. Biol. Chem. 273:17665-17670(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, TISSUE SPECIFICITY.
Strain: G3.
Tissue: Midgut.
[2]"Anopheles peritrophic matrix protein-1 (AgAper-1) regulatory sequences mediate transgenic protein accumulation and secretion into the midgut lumen upon blood ingestion."
Abraham E.G., Donnelly-Doman M., Fujioka H., Ghosh A., Moreira L., Jacobs-Lorena M.
Submitted (SEP-2004) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[3]"Intraspecific nucleotide variation in Anopheles gambiae: new insights into the biology of malaria vectors."
Morlais I., Poncon N., Simard F., Cohuet A., Fontenille D.
Am. J. Trop. Med. Hyg. 71:795-802(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: 4aRR, L3-5, L3-51, Yaounde Yd21, Yaounde Yd35 and Yaounde Yd41.
[4]"The genome sequence of the malaria mosquito Anopheles gambiae."
Holt R.A., Subramanian G.M., Halpern A., Sutton G.G., Charlab R., Nusskern D.R., Wincker P., Clark A.G., Ribeiro J.M.C., Wides R., Salzberg S.L., Loftus B.J., Yandell M.D., Majoros W.H., Rusch D.B., Lai Z., Kraft C.L., Abril J.F. expand/collapse author list , Anthouard V., Arensburger P., Atkinson P.W., Baden H., de Berardinis V., Baldwin D., Benes V., Biedler J., Blass C., Bolanos R., Boscus D., Barnstead M., Cai S., Center A., Chaturverdi K., Christophides G.K., Chrystal M.A.M., Clamp M., Cravchik A., Curwen V., Dana A., Delcher A., Dew I., Evans C.A., Flanigan M., Grundschober-Freimoser A., Friedli L., Gu Z., Guan P., Guigo R., Hillenmeyer M.E., Hladun S.L., Hogan J.R., Hong Y.S., Hoover J., Jaillon O., Ke Z., Kodira C.D., Kokoza E., Koutsos A., Letunic I., Levitsky A.A., Liang Y., Lin J.-J., Lobo N.F., Lopez J.R., Malek J.A., McIntosh T.C., Meister S., Miller J.R., Mobarry C., Mongin E., Murphy S.D., O'Brochta D.A., Pfannkoch C., Qi R., Regier M.A., Remington K., Shao H., Sharakhova M.V., Sitter C.D., Shetty J., Smith T.J., Strong R., Sun J., Thomasova D., Ton L.Q., Topalis P., Tu Z.J., Unger M.F., Walenz B., Wang A.H., Wang J., Wang M., Wang X., Woodford K.J., Wortman J.R., Wu M., Yao A., Zdobnov E.M., Zhang H., Zhao Q., Zhao S., Zhu S.C., Zhimulev I., Coluzzi M., della Torre A., Roth C.W., Louis C., Kalush F., Mural R.J., Myers E.W., Adams M.D., Smith H.O., Broder S., Gardner M.J., Fraser C.M., Birney E., Bork P., Brey P.T., Venter J.C., Weissenbach J., Kafatos F.C., Collins F.H., Hoffman S.L.
Science 298:129-149(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: PEST.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF030431 mRNA. Translation: AAC39127.1.
AY750997 Genomic DNA. Translation: AAV31069.1.
AY344823 Genomic DNA. Translation: AAR02434.1.
AY344824 Genomic DNA. Translation: AAR02435.1.
AY344825 Genomic DNA. Translation: AAR02436.1.
AY344826 Genomic DNA. Translation: AAR02437.1.
AY344827 Genomic DNA. Translation: AAR02438.1.
AY344828 Genomic DNA. Translation: AAR02439.1.
AAAB01008807 Genomic DNA. Translation: EAA04177.3.

3D structure databases

ProteinModelPortalO76217.
ModBaseSearch...
MobiDBSearch...

Protein family/group databases

CAZyCBM14. Carbohydrate-Binding Module Family 14.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

KEGGaga:AgaP_AGAP006795.
VectorBaseAGAP006795. Anopheles gambiae.

Organism-specific databases

CTD1270270.

Phylogenomic databases

eggNOGNOG275071.
InParanoidO76217.
OrthoDBEOG73V6N7.

Family and domain databases

Gene3D2.170.140.10. 2 hits.
InterProIPR002557. Chitin-bd_dom.
[Graphical view]
PfamPF01607. CBM_14. 2 hits.
[Graphical view]
SMARTSM00494. ChtBD2. 2 hits.
[Graphical view]
SUPFAMSSF57625. SSF57625. 2 hits.
PROSITEPS50940. CHIT_BIND_II. 2 hits.
[Graphical view]
ProtoNetSearch...

Entry information

Entry namePE1_ANOGA
AccessionPrimary (citable) accession number: O76217
Secondary accession number(s): Q6VAW1 expand/collapse secondary AC list , Q6VAW2, Q6VAW4, Q6VAW5, Q6VAW6, Q7QID7
Entry history
Integrated into UniProtKB/Swiss-Prot: July 11, 2003
Last sequence update: July 5, 2005
Last modified: April 16, 2014
This is version 75 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)

Relevant documents

SIMILARITY comments

Index of protein domains and families