ID   SP23_TENMO              Reviewed;         182 AA.
AC   Q27022; Q27012;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   25-MAY-2022, entry version 53.
DE   RecName: Full=Spermatophorin SP23;
DE   Flags: Precursor;
GN   Name=SP23;
OS   Tenebrio molitor (Yellow mealworm beetle).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Coleoptera; Polyphaga; Cucujiformia;
OC   Tenebrionidae; Tenebrio.
OX   NCBI_TaxID=7067;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND PROTEIN SEQUENCE OF 8-20.
RC   TISSUE=Bean-shaped accessory gland;
RX   PubMed=1527013; DOI=10.1016/s0021-9258(19)37039-5;
RA   Paesen G.C., Schwartz M.B., Peferoen M., Weyda F., Happ G.M.;
RT   "Amino acid sequence of Sp23, a structural protein of the spermatophore of
RT   the mealworm beetle, Tenebrio molitor.";
RL   J. Biol. Chem. 267:18852-18857(1992).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=8972909; DOI=10.1016/s0378-1119(96)00372-1;
RA   Feng X., Happ G.M.;
RT   "Isolation and sequencing of the gene encoding Sp23, a structural protein
RT   of spermatophore of the mealworm beetle, Tenebrio molitor.";
RL   Gene 179:257-262(1996).
CC   -!- FUNCTION: Structural protein of a layer within the wall of the
CC       spermatophore produced probably by cell type 4 of the bean-shaped gland
CC       (BAG). Fixation in the spermatophore seems to require covalent cross-
CC       linking of spermatophorins.
CC   -!- SUBCELLULAR LOCATION: Secreted.
CC   -!- TISSUE SPECIFICITY: Spermatophore.
CC   -!- DEVELOPMENTAL STAGE: Expressed at the beginning of the adult stage,
CC       about four days after the pupal peak of ecdysteroids.
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DR   EMBL; M92928; AAA18165.1; -; mRNA.
DR   EMBL; U39658; AAC47422.1; -; Genomic_DNA.
DR   PIR; A44157; A44157.
DR   PIR; JC5233; JC5233.
DR   AlphaFoldDB; Q27022; -.
DR   SMR; Q27022; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
PE   1: Evidence at protein level;
KW   Direct protein sequencing; Repeat; Secreted; Signal.
FT   SIGNAL          1..7
FT                   /evidence="ECO:0000269|PubMed:1527013"
FT   CHAIN           8..182
FT                   /note="Spermatophorin SP23"
FT                   /id="PRO_0000022388"
FT   REGION          1..26
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          56..79
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          101..136
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        60..79
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        104..133
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CONFLICT        61
FT                   /note="K -> R (in Ref. 2; AAC47422)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        110
FT                   /note="P -> A (in Ref. 2; AAC47422)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        127
FT                   /note="Missing (in Ref. 2)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   182 AA;  20570 MW;  D84F0F95ACC16E3C CRC64;
     MVASIAGEEE PAAEKSQQSP DHFQPYRPYY YPPYRGYPIT YPYPYPHGYP KPYHNFQTIA
     KPNEGPTDQP EANSANSIEE GGVSKRLFIE PIFNLFRPRP RDPIVVNQAP PPPPVIYQAP
     PPPPPPPIFQ QAPPTIYQQP SPTIIQQAPQ PSVTKLVYSQ PEPSHSVIYQ TQPKTELVYL
     NQ