CU20_MANSE
ID CU20_MANSE Reviewed; 200 AA.
AC Q8T635;
DT 05-JUL-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2002, sequence version 1.
DT 25-MAY-2022, entry version 37.
DE RecName: Full=Pupal cuticle protein 20;
DE AltName: Full=MS-PCP20;
DE Short=MsCP20;
DE Flags: Precursor;
GN Name=PCP20;
OS Manduca sexta (Tobacco hawkmoth) (Tobacco hornworm).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Lepidoptera; Glossata; Ditrysia; Bombycoidea;
OC Sphingidae; Sphinginae; Sphingini; Manduca.
OX NCBI_TaxID=7130 {ECO:0000312|EMBL:AAL90881.1};
RN [1] {ECO:0000305}
RP NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 19-200, 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 19-40, 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 larval 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: Present at low levels early in the fifth larval
CC stadium, followed by a large increase in abundance prior to pupal
CC ecdysis. {ECO:0000269|PubMed:12609518}.
CC -!- MASS SPECTROMETRY: Mass=17894; Method=MALDI;
CC Evidence={ECO:0000269|PubMed:12609518};
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DR EMBL; AF487520; AAL90881.1; -; mRNA.
DR AlphaFoldDB; Q8T635; -.
DR GO; GO:0042302; F:structural constituent of cuticle; IEA:UniProtKB-KW.
DR InterPro; IPR031311; CHIT_BIND_RR_consensus.
DR InterPro; IPR000618; Insect_cuticle.
DR Pfam; PF00379; Chitin_bind_4; 1.
DR PRINTS; PR00947; CUTICLE.
DR PROSITE; PS00233; CHIT_BIND_RR_1; 1.
DR PROSITE; PS51155; CHIT_BIND_RR_2; 1.
PE 1: Evidence at protein level;
KW Cuticle; Direct protein sequencing; Signal.
FT SIGNAL 1..18
FT /evidence="ECO:0000269|PubMed:10646967,
FT ECO:0000269|PubMed:12609518"
FT CHAIN 19..200
FT /note="Pupal cuticle protein 20"
FT /evidence="ECO:0000269|PubMed:12609518"
FT /id="PRO_0000006410"
FT DOMAIN 93..162
FT /note="Chitin-binding type R&R"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00497"
FT REGION 100..119
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 177..200
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CONFLICT 154
FT /note="L -> V (in Ref. 1; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 165
FT /note="P -> I (in Ref. 1; AA sequence)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 200 AA; 19481 MW; FE8B0A54E41414E8 CRC64;
MATILLVLTA VLIAVGSCGR LEPQYLPPRP GNGFGGGAGS GGNAGLGGGA GGSGAGAGGF
GGSGAGAYGG SGGSHGGGAQ IPITSFENVN NGDGSYHFSY ETGNGISAQE SGAPRAPGPE
GLAVTAEGAF SYRTPDGQQI ALTYTADENG FHPLGPHLPT PPPIPEEILR SIEFNRQNPS
SEGSYNGGNG GSGGSNGYHY