ID   A29AB_DROSI             Reviewed;         234 AA.
AC   Q9U968;
DT   01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2000, sequence version 1.
DT   03-AUG-2022, entry version 91.
DE   RecName: Full=Accessory gland protein Acp29AB;
DE   Flags: Precursor;
GN   Name=Acp29AB;
OS   Drosophila simulans (Fruit fly).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC   Drosophilidae; Drosophila; Sophophora.
OX   NCBI_TaxID=7240;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=S9;
RX   PubMed=10353898; DOI=10.1093/genetics/152.2.543;
RA   Aguade M.;
RT   "Positive selection drives the evolution of the Acp29AB accessory gland
RT   protein in Drosophila.";
RL   Genetics 152:543-551(1999).
CC   -!- FUNCTION: Responsible for physiological and behavioral changes in mated
CC       female flies.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305}.
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DR   EMBL; AJ240552; CAB53227.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q9U968; -.
DR   SMR; Q9U968; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0030246; F:carbohydrate binding; IEA:UniProtKB-KW.
DR   GO; GO:0046693; P:sperm storage; IEA:EnsemblMetazoa.
DR   Gene3D; 3.10.100.10; -; 1.
DR   InterPro; IPR001304; C-type_lectin-like.
DR   InterPro; IPR016186; C-type_lectin-like/link_sf.
DR   InterPro; IPR016187; CTDL_fold.
DR   Pfam; PF00059; Lectin_C; 1.
DR   SMART; SM00034; CLECT; 1.
DR   SUPFAM; SSF56436; SSF56436; 1.
DR   PROSITE; PS50041; C_TYPE_LECTIN_2; 1.
PE   3: Inferred from homology;
KW   Behavior; Disulfide bond; Glycoprotein; Lectin; Secreted; Signal.
FT   SIGNAL          1..21
FT                   /evidence="ECO:0000255"
FT   CHAIN           22..234
FT                   /note="Accessory gland protein Acp29AB"
FT                   /id="PRO_0000017557"
FT   DOMAIN          137..234
FT                   /note="C-type lectin"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
FT   CARBOHYD        29
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        61
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        127
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        164
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        139..228
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
FT   DISULFID        207..220
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
SQ   SEQUENCE   234 AA;  26915 MW;  EE9C556E02EFED98 CRC64;
     MYATNLLYLL ALWNLWLVSG GQQDIPNGNA TLPSPQKPQN TIDQIGANQN YWFTYNALRQ
     NETLAIIDAM ESGIASSVLA FQAQMEIQLQ PLKIIMLHHA GNIKASNNIK MSRFEKVGSR
     YFHIEKNLTL TWFEAYVTCR EMNGHLANIR DEKELDGILA LAPNNSYWVD ISKLVEYGGT
     FVSTLTGREP IFVKWKPNQD KKKQHNCVYI YAKEMYYDEC FEKKSFVCQA NQWA