(data stored in ACNUC7421 zone)

SWISSPROT: CU27_MANSE

ID   CU27_MANSE              Reviewed;         180 AA.
AC   Q8T4J9;
DT   05-JUL-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2002, sequence version 1.
DT   11-DEC-2019, entry version 38.
DE   RecName: Full=Pupal cuticle protein 27;
DE   AltName: Full=MS-PCP27;
DE            Short=MsCP27;
DE   Flags: Precursor;
GN   Name=PCP27;
OS   Manduca sexta (Tobacco hawkmoth) (Tobacco hornworm).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Holometabola; Lepidoptera; Glossata; Ditrysia; Bombycoidea;
OC   Sphingidae; Sphinginae; Sphingini; Manduca.
OX   NCBI_TaxID=7130 {ECO:0000312|EMBL:AAL92478.1};
RN   [1] {ECO:0000305}
RP   NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 16-180, FUNCTION,
RP   SUBCELLULAR LOCATION, DEVELOPMENTAL STAGE, AND MASS SPECTROMETRY.
RC   TISSUE=Pharate pupal cuticle {ECO:0000269|PubMed:12609518};
RX   PubMed=12609518; DOI=10.1016/s0965-1748(02)00247-3;
RA   Suderman R.J., Andersen S.O., Hopkins T.L., Kanost M.R., Kramer K.J.;
RT   "Characterization and cDNA cloning of three major proteins from pharate
RT   pupal cuticle of Manduca sexta.";
RL   Insect Biochem. Mol. Biol. 33:331-343(2003).
RN   [2] {ECO:0000305}
RP   PROTEIN SEQUENCE OF 16-39, AND SUBCELLULAR LOCATION.
RC   TISSUE=Pharate pupal cuticle {ECO:0000269|PubMed:10646967};
RX   PubMed=10646967; DOI=10.1016/s0965-1748(99)00091-0;
RA   Hopkins T.L., Krchma L.J., Ahmad S.A., Kramer K.J.;
RT   "Pupal cuticle proteins of Manduca sexta: characterization and profiles
RT   during sclerotization.";
RL   Insect Biochem. Mol. Biol. 30:19-27(2000).
CC   -!- FUNCTION: Component of the pupal abdominal endocuticle. May have
CC       important role in the pharate pupal cuticle structure.
CC       {ECO:0000269|PubMed:12609518, ECO:0000303|PubMed:10646967}.
CC   -!- SUBCELLULAR LOCATION: Note=Synthesized in the epidermis during the
CC       larval-pupal transformation and then secreted into the pharate pupal
CC       cuticle. {ECO:0000269|PubMed:10646967, ECO:0000269|PubMed:12609518}.
CC   -!- DEVELOPMENTAL STAGE: Expression is increased to a peak level just
CC       before pupal ecdysis. {ECO:0000269|PubMed:12609518}.
CC   -!- MASS SPECTROMETRY: Mass=17623; Method=MALDI;
CC       Evidence={ECO:0000269|PubMed:12609518};
DR   EMBL; AY083171; AAL92478.1; -; mRNA.
DR   HOGENOM; HOG000219175; -.
DR   GO; GO:0042302; F:structural constituent of cuticle; IEA:UniProtKB-KW.
DR   InterPro; IPR000618; Insect_cuticle.
DR   Pfam; PF00379; Chitin_bind_4; 1.
DR   PRINTS; PR00947; CUTICLE.
DR   PROSITE; PS51155; CHIT_BIND_RR_2; 1.
PE   1: Evidence at protein level;
DR   PRODOM; Q8T4J9.
DR   SWISS-2DPAGE; Q8T4J9.
KW   Cuticle; Direct protein sequencing; Signal.
FT   SIGNAL          1..15
FT                   /evidence="ECO:0000269|PubMed:10646967,
FT                   ECO:0000269|PubMed:12609518"
FT   CHAIN           16..180
FT                   /note="Pupal cuticle protein 27"
FT                   /evidence="ECO:0000269|PubMed:12609518"
FT                   /id="PRO_0000006411"
FT   DOMAIN          69..129
FT                   /note="Chitin-binding type R&R"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00497"
FT   CONFLICT        30
FT                   /note="S -> P (in Ref. 1; AA sequence)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        39
FT                   /note="G -> S (in Ref. 2; AA sequence)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        164
FT                   /note="S -> N (in Ref. 1; AA sequence)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   180 AA;  19028 MW;  9F39E103FC1C6B5B CRC64;
     MNLIIYVTII ALTSAAELPS RNYIPQDQGS GPYPGPHGGI GGDTGNRRPQ QDAEKNSNVV
     KQEQEISDSG NYHFGFETSN GIRAEEAGGP EQAQGGYSYK GDDGQTYTLI YTSGEGGFKP
     QGEHLPVAPP TPEAILIALQ QNERDEAAGI FDDGQYHPEN NGQSRPGASA GAGTGSGYHY
//

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