ID   AWN_HORSE               Reviewed;         133 AA.
AC   P80720; P80948;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1997, sequence version 1.
DT   25-MAY-2022, entry version 73.
DE   RecName: Full=Carbohydrate-binding protein AWN;
DE   AltName: Full=Seminal plasma protein HSP-7;
DE   AltName: Full=Spermadhesin AWN;
DE   AltName: Full=Zona pellucida-binding protein AWN;
OS   Equus caballus (Horse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Perissodactyla; Equidae; Equus.
OX   NCBI_TaxID=9796;
RN   [1]
RP   PROTEIN SEQUENCE, AND DISULFIDE BONDS.
RC   TISSUE=Sperm;
RX   PubMed=9022691; DOI=10.1111/j.1432-1033.1996.0636r.x;
RA   Reinert M., Calvete J.J., Sanz L., Mann K., Toepfer-Petersen E.;
RT   "Primary structure of stallion seminal plasma protein HSP-7, a zona-
RT   pellucida-binding protein of the spermadhesin family.";
RL   Eur. J. Biochem. 242:636-640(1996).
RN   [2]
RP   PROTEIN SEQUENCE OF 1-14.
RC   TISSUE=Seminal plasma;
RX   PubMed=7654203; DOI=10.1042/bj3100615;
RA   Calvete J.J., Mann K., Schaefer W., Sanz L., Reinert M., Nessau S.,
RA   Raida M., Toepfer-Petersen E.;
RT   "Amino acid sequence of HSP-1, a major protein of stallion seminal plasma:
RT   effect of glycosylation on its heparin- and gelatin-binding capabilities.";
RL   Biochem. J. 310:615-622(1995).
CC   -!- FUNCTION: Mediates the binding of spermatozoa to component(s) of the
CC       egg's zona pellucida by a carbohydrate-binding mechanism. It is a
CC       secretory component of the male accessory glands being coated to the
CC       sperm surface at the time of ejaculation.
CC   -!- SUBCELLULAR LOCATION: Secreted. Note=Predominantly localized on the
CC       membrane overlying the acrosomal cap region of the sperm head.
CC   -!- SIMILARITY: Belongs to the spermadhesin family. {ECO:0000305}.
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DR   AlphaFoldDB; P80720; -.
DR   SMR; P80720; -.
DR   Proteomes; UP000002281; Unplaced.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
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   Reference proteome; Secreted.
FT   CHAIN           1..133
FT                   /note="Carbohydrate-binding protein AWN"
FT                   /id="PRO_0000221455"
FT   DOMAIN          9..110
FT                   /note="CUB"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00059"
FT   REGION          73..110
FT                   /note="Heparin-binding"
FT                   /evidence="ECO:0000250"
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:9022691"
FT   DISULFID        53..74
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00059,
FT                   ECO:0000269|PubMed:9022691"
SQ   SEQUENCE   133 AA;  14774 MW;  4D9EB081985E888B CRC64;
     AWNRRSRSCG GVLRDPPGKI FNSDGPQKDC VWTIKVKPHF HVVIAIPPLN LSCGKEYVEL
     LDGPPGSEII GKICGGISLV FRSSSNIATI KYLRTSGQRA SPFHIYYYAD PEGPLPFPYF
     ERQTIIATEK NIP