ID   AQN1_PIG                Reviewed;         111 AA.
AC   P26322; O62626;
DT   01-MAY-1992, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1992, sequence version 1.
DT   25-MAY-2022, entry version 100.
DE   RecName: Full=Carbohydrate-binding protein AQN-1;
DE   AltName: Full=Spermadhesin AQN-1;
DE   AltName: Full=Zona pellucida-binding protein AQN-1;
OS   Sus scrofa (Pig).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX   NCBI_TaxID=9823;
RN   [1]
RP   PROTEIN SEQUENCE, AND DISULFIDE BONDS.
RC   TISSUE=Sperm;
RX   PubMed=1572364; DOI=10.1111/j.1432-1033.1992.tb16822.x;
RA   Sanz L., Calvete J.J., Mann K., Schaefer W., Schmid E.R.,
RA   Toepfer-Petersen E.;
RT   "The complete primary structure of the boar spermadhesin AQN-1, a
RT   carbohydrate-binding protein involved in fertilization.";
RL   Eur. J. Biochem. 205:645-652(1992).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Seminal vesicle;
RA   Ekhlasi-Hundrieser M., Toepfer-Petersen E.;
RL   Submitted (MAR-1998) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   PROTEIN SEQUENCE OF 1-32.
RC   TISSUE=Sperm;
RX   PubMed=1849093; DOI=10.1016/0014-5793(91)80233-s;
RA   Jonakova V., Sanz L., Calvete J.J., Henschen A., Cechova D.,
RA   Toepfer-Petersen E.;
RT   "Isolation and biochemical characterization of a zona pellucida-binding
RT   glycoprotein of boar spermatozoa.";
RL   FEBS Lett. 280:183-186(1991).
RN   [4]
RP   PROTEIN SEQUENCE OF 14-29; 52-57; 69-79; 80-88 AND 104-108.
RX   PubMed=8603690; DOI=10.1016/0014-5793(95)01513-2;
RA   Calvete J.J., Dostalova Z., Sanz L., Adermann K., Thole H.H.,
RA   Toepfer-Petersen E.;
RT   "Mapping the heparin-binding domain of boar spermadhesins.";
RL   FEBS Lett. 379:207-211(1996).
CC   -!- FUNCTION: AQN proteins mediate the binding of boar spermatozoa to
CC       component(s) of the egg's zona pellucida by a carbohydrate-binding
CC       mechanism. AQN proteins are secretory components of the male accessory
CC       glands being coated to the sperm surface at the time of ejaculation.
CC       They possess as well heparin-, serine-protease-inhibitor-binding
CC       capability.
CC   -!- SUBCELLULAR LOCATION: Secreted.
CC   -!- SIMILARITY: Belongs to the spermadhesin family. {ECO:0000305}.
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DR   EMBL; AJ004998; CAA06272.1; -; mRNA.
DR   PIR; S14300; S14300.
DR   PIR; S21211; S21211.
DR   AlphaFoldDB; P26322; -.
DR   SMR; P26322; -.
DR   STRING; 9823.ENSSSCP00000003226; -.
DR   PaxDb; P26322; -.
DR   PRIDE; P26322; -.
DR   eggNOG; ENOG502TD48; Eukaryota.
DR   Proteomes; UP000008227; Unplaced.
DR   Proteomes; UP000314985; Unplaced.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0008201; F:heparin binding; IEA:UniProtKB-KW.
DR   GO; GO:0007338; P:single fertilization; IEA:UniProtKB-KW.
DR   CDD; cd00041; CUB; 1.
DR   Gene3D; 2.60.120.290; -; 1.
DR   InterPro; IPR000859; CUB_dom.
DR   InterPro; IPR035914; Sperma_CUB_dom_sf.
DR   InterPro; IPR000124; Spermadhesin.
DR   Pfam; PF00431; CUB; 1.
DR   SMART; SM00042; CUB; 1.
DR   SUPFAM; SSF49854; SSF49854; 1.
DR   PROSITE; PS01180; CUB; 1.
DR   PROSITE; PS00985; SPERMADHESIN_1; 1.
DR   PROSITE; PS00986; SPERMADHESIN_2; 1.
PE   1: Evidence at protein level;
KW   Acetylation; Direct protein sequencing; Disulfide bond; Fertilization;
KW   Heparin-binding; Reference proteome; Secreted.
FT   CHAIN           1..111
FT                   /note="Carbohydrate-binding protein AQN-1"
FT                   /id="PRO_0000221453"
FT   DOMAIN          9..110
FT                   /note="CUB"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00059"
FT   MOD_RES         1
FT                   /note="N-acetylalanine"
FT                   /evidence="ECO:0000250|UniProtKB:P26776"
FT   DISULFID        9..30
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00059,
FT                   ECO:0000269|PubMed:1572364"
FT   DISULFID        53..74
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00059,
FT                   ECO:0000269|PubMed:1572364"
FT   CONFLICT        15..16
FT                   /note="NY -> DL (in Ref. 2 and 4)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   111 AA;  11882 MW;  7EDCCB52865E504B CRC64;
     AQNKGPHKCG GVLRNYSGRI STYEGPKTDC IWTILAKPGS RVFVAIPYLN LACGKEYVEV
     QDGLPGAGNY GKLCSGIGLT YQSSSNALSI KYSRTAGHSA SSFDIYYYGD S