ID   CUD4_LOCMI              Reviewed;         116 AA.
AC   P21799;
DT   01-MAY-1991, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1994, sequence version 3.
DT   25-MAY-2022, entry version 60.
DE   RecName: Full=Endocuticle structural glycoprotein ABD-4;
OS   Locusta migratoria (Migratory locust).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Polyneoptera; Orthoptera; Caelifera; Acrididea; Acridomorpha;
OC   Acridoidea; Acrididae; Oedipodinae; Locusta.
OX   NCBI_TaxID=7004;
RN   [1]
RP   PROTEIN SEQUENCE, PYROGLUTAMATE FORMATION AT GLN-1, AMIDATION AT PRO-116,
RP   AND GLYCOSYLATION AT THR-90; THR-107 AND THR-111.
RX   PubMed=1997327; DOI=10.1111/j.1432-1033.1991.tb15730.x;
RA   Talbo G., Hoejrup P., Rahbek-Nielsen H., Andersen S.O., Roepstorff P.;
RT   "Determination of the covalent structure of an N- and C-terminally blocked
RT   glycoprotein from endocuticle of Locusta migratoria. Combined use of plasma
RT   desorption mass spectrometry and Edman degradation to study post-
RT   translationally modified proteins.";
RL   Eur. J. Biochem. 195:495-504(1991).
CC   -!- FUNCTION: Component of the soft endocuticle of migratory locust.
CC   -!- PTM: 3 variants exists that arise from a sequential glycosylation with
CC       N-acetylgalactosamine at three (ABD-4A), two (ABD-4B) or one (ABD-4C)
CC       threonine residues. {ECO:0000269|PubMed:1997327}.
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DR   PIR; S14261; S14261.
DR   AlphaFoldDB; P21799; -.
DR   iPTMnet; P21799; -.
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   Amidation; Cuticle; Direct protein sequencing; Glycoprotein;
KW   Pyrrolidone carboxylic acid.
FT   CHAIN           1..116
FT                   /note="Endocuticle structural glycoprotein ABD-4"
FT                   /id="PRO_0000196116"
FT   DOMAIN          20..92
FT                   /note="Chitin-binding type R&R"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00497"
FT   REGION          78..97
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         1
FT                   /note="Pyrrolidone carboxylic acid"
FT                   /evidence="ECO:0000269|PubMed:1997327"
FT   MOD_RES         116
FT                   /note="Proline amide"
FT                   /evidence="ECO:0000269|PubMed:1997327"
FT   CARBOHYD        90
FT                   /note="O-linked (GalNAc) threonine; in ADB-4A, ABD-4B and
FT                   ABD-4C"
FT                   /evidence="ECO:0000269|PubMed:1997327"
FT   CARBOHYD        107
FT                   /note="O-linked (GalNAc) threonine; in ADB-4A and ABD-4B"
FT                   /evidence="ECO:0000269|PubMed:1997327"
FT   CARBOHYD        111
FT                   /note="O-linked (GalNAc) threonine; in ADB-4A"
FT                   /evidence="ECO:0000269|PubMed:1997327"
SQ   SEQUENCE   116 AA;  12476 MW;  E5ABF6C65E313E61 CRC64;
     QAPSDKVIPI ISQNEVRNPD GSYQWNYETG NGIKADETGT LKKGSKPDEG DFIVAQGSFS
     YTGPDGTAYQ VQYSADDENG FVPQGAHFPT PPPIPPAIQR ALDYLATLPP TPEARP