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Q27289

- CTR1_ANOGA

UniProt

Q27289 - CTR1_ANOGA

Protein

Chymotrypsin-1

Gene

CHYM1

Organism
Anopheles gambiae (African malaria mosquito)
Status
Reviewed - Annotation score: 3 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 100 (01 Oct 2014)
      Sequence version 3 (26 Jun 2007)
      Previous versions | rss
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    Functioni

    Catalytic activityi

    Preferential cleavage: Tyr-|-Xaa, Trp-|-Xaa, Phe-|-Xaa, Leu-|-Xaa.PROSITE-ProRule annotation

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei74 – 741Charge relay systemBy similarity
    Active sitei119 – 1191Charge relay systemBy similarity
    Sitei206 – 2061Required for specificityBy similarity
    Active sitei212 – 2121Charge relay systemBy similarity

    GO - Molecular functioni

    1. serine-type endopeptidase activity Source: InterPro

    GO - Biological processi

    1. digestion Source: UniProtKB-KW

    Keywords - Molecular functioni

    Hydrolase, Protease, Serine protease

    Keywords - Biological processi

    Digestion

    Protein family/group databases

    MEROPSiS01.166.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Chymotrypsin-1 (EC:3.4.21.1)
    Alternative name(s):
    AnChym1
    Gene namesi
    Name:CHYM1
    ORF Names:AGAP006709
    OrganismiAnopheles gambiae (African malaria mosquito)
    Taxonomic identifieri7165 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraNematoceraCulicoideaCulicidaeAnophelinaeAnopheles
    ProteomesiUP000007062: Chromosome 2L

    Subcellular locationi

    Secreted 1 Publication

    GO - Cellular componenti

    1. extracellular region Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Secreted

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 1717Sequence AnalysisAdd
    BLAST
    Propeptidei18 – 3215Activation peptide1 PublicationPRO_0000027654Add
    BLAST
    Chaini33 – 259227Chymotrypsin-1PRO_0000027655Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Disulfide bondi59 ↔ 75PROSITE-ProRule annotation
    Disulfide bondi182 ↔ 198PROSITE-ProRule annotation
    Disulfide bondi208 ↔ 232PROSITE-ProRule annotation

    Keywords - PTMi

    Disulfide bond, Zymogen

    Expressioni

    Tissue specificityi

    After blood feeding, expression is induced in the midgut epithelium, followed by secretion into the midgut lumen.1 Publication

    Structurei

    3D structure databases

    ProteinModelPortaliQ27289.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini33 – 255223Peptidase S1PROSITE-ProRule annotationAdd
    BLAST

    Sequence similaritiesi

    Belongs to the peptidase S1 family.PROSITE-ProRule annotation
    Contains 1 peptidase S1 domain.PROSITE-ProRule annotation

    Keywords - Domaini

    Signal

    Phylogenomic databases

    eggNOGiCOG5640.
    HOGENOMiHOG000251820.
    InParanoidiQ27289.
    OMAiWGHTSAN.
    OrthoDBiEOG7MKW6Q.
    PhylomeDBiQ27289.

    Family and domain databases

    InterProiIPR001254. Peptidase_S1.
    IPR018114. Peptidase_S1_AS.
    IPR001314. Peptidase_S1A.
    IPR009003. Trypsin-like_Pept_dom.
    [Graphical view]
    PfamiPF00089. Trypsin. 1 hit.
    [Graphical view]
    PRINTSiPR00722. CHYMOTRYPSIN.
    SMARTiSM00020. Tryp_SPc. 1 hit.
    [Graphical view]
    SUPFAMiSSF50494. SSF50494. 1 hit.
    PROSITEiPS50240. TRYPSIN_DOM. 1 hit.
    PS00134. TRYPSIN_HIS. 1 hit.
    PS00135. TRYPSIN_SER. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

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

    Q27289-1 [UniParc]FASTAAdd to Basket

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    MLRKVFAVVS VLLVVSAAKV TKLVLDDNYV NRVVGGEVAK NGSAPYQVSL    50
    QVPGWGHNCG GSLLNDRWVL TAAHCLVGHA PGDLMVLVGT NSLKEGGELL 100
    KVDKLLYHSR YNLPRFHNDI GLVRLEQPVR FSELVQSVEY SEKAVPANAT 150
    VRLTGWGHTS ANGPSPTLLQ SLNVVTLSNE DCNKKGGDPG YTDVGHLCTL 200
    TKTGEGACNG DSGGPLVYEG KLVGVVNFGV PCALGYPDGF ARVSYYHDWV 250
    RTTMANNSK 259
    Length:259
    Mass (Da):27,722
    Last modified:June 26, 2007 - v3
    Checksum:i3EF7D6F19EAAED23
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti9 – 113VSV → ASI in CAA79325. (PubMed:11453997)Curated
    Sequence conflicti9 – 113VSV → ASI in CAA83568. (PubMed:11453997)Curated
    Sequence conflicti21 – 211T → P in CAA79325. (PubMed:11453997)Curated
    Sequence conflicti21 – 211T → P in CAA83568. (PubMed:11453997)Curated
    Sequence conflicti28 – 281N → H in CAA79325. (PubMed:11453997)Curated
    Sequence conflicti28 – 281N → H in CAA83568. (PubMed:11453997)Curated
    Sequence conflicti130 – 1301R → Q in CAA79325. (PubMed:11453997)Curated
    Sequence conflicti130 – 1301R → Q in CAA83568. (PubMed:11453997)Curated
    Sequence conflicti158 – 1581H → R in CAA79325. (PubMed:11453997)Curated
    Sequence conflicti158 – 1581H → R in CAA83568. (PubMed:11453997)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    Z18887 mRNA. Translation: CAA79325.1.
    Z32645 Genomic DNA. Translation: CAA83568.1.
    AAAB01008807 Genomic DNA. Translation: EAA45497.2.
    PIRiS49129.
    RefSeqiXP_309033.2. XM_309033.4.

    Genome annotation databases

    EnsemblMetazoaiAGAP006709-RA; AGAP006709-PA; AGAP006709.
    GeneIDi1270348.
    KEGGiaga:AgaP_AGAP006709.
    VectorBaseiAGAP006709. Anopheles gambiae.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    Z18887 mRNA. Translation: CAA79325.1 .
    Z32645 Genomic DNA. Translation: CAA83568.1 .
    AAAB01008807 Genomic DNA. Translation: EAA45497.2 .
    PIRi S49129.
    RefSeqi XP_309033.2. XM_309033.4.

    3D structure databases

    ProteinModelPortali Q27289.
    ModBasei Search...
    MobiDBi Search...

    Protein family/group databases

    MEROPSi S01.166.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblMetazoai AGAP006709-RA ; AGAP006709-PA ; AGAP006709 .
    GeneIDi 1270348.
    KEGGi aga:AgaP_AGAP006709.
    VectorBasei AGAP006709. Anopheles gambiae.

    Organism-specific databases

    CTDi 1270348.

    Phylogenomic databases

    eggNOGi COG5640.
    HOGENOMi HOG000251820.
    InParanoidi Q27289.
    OMAi WGHTSAN.
    OrthoDBi EOG7MKW6Q.
    PhylomeDBi Q27289.

    Family and domain databases

    InterProi IPR001254. Peptidase_S1.
    IPR018114. Peptidase_S1_AS.
    IPR001314. Peptidase_S1A.
    IPR009003. Trypsin-like_Pept_dom.
    [Graphical view ]
    Pfami PF00089. Trypsin. 1 hit.
    [Graphical view ]
    PRINTSi PR00722. CHYMOTRYPSIN.
    SMARTi SM00020. Tryp_SPc. 1 hit.
    [Graphical view ]
    SUPFAMi SSF50494. SSF50494. 1 hit.
    PROSITEi PS50240. TRYPSIN_DOM. 1 hit.
    PS00134. TRYPSIN_HIS. 1 hit.
    PS00135. TRYPSIN_SER. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Blood digestion in the malaria mosquito Anopheles gambiae: molecular cloning and biochemical characterization of two inducible chymotrypsins."
      Vizioli J., Catteruccia F., della Torre A., Reckmann I., Mueller H.M.
      Eur. J. Biochem. 268:4027-4035(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], PROTEIN SEQUENCE OF 33-42, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
      Strain: Suakoko.
      Tissue: Midgut.
    2. "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.
      , 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.

    Entry informationi

    Entry nameiCTR1_ANOGA
    AccessioniPrimary (citable) accession number: Q27289
    Secondary accession number(s): Q7PF17
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 1, 1997
    Last sequence update: June 26, 2007
    Last modified: October 1, 2014
    This is version 100 of the entry and version 3 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. Peptidase families
      Classification of peptidase families and list of entries
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3