AWN_PIG
ID AWN_PIG Reviewed; 153 AA.
AC P26776; Q712L0;
DT 01-AUG-1992, integrated into UniProtKB/Swiss-Prot.
DT 07-MAR-2006, sequence version 2.
DT 25-MAY-2022, entry version 97.
DE RecName: Full=Carbohydrate-binding protein AWN;
DE AltName: Full=Sperm-associated protein AWN;
DE AltName: Full=Spermadhesin AWN;
DE AltName: Full=Zona pellucida-binding protein AWN;
DE Flags: Precursor;
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 NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Seminal vesicle;
RA Ekhlasi-Hundrieser M., Toepfer-Petersen E.;
RL Submitted (APR-1999) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP PROTEIN SEQUENCE OF 21-153, ACETYLATION AT ALA-21, AND DISULFIDE BONDS.
RC TISSUE=Sperm;
RX PubMed=1555646; DOI=10.1016/0014-5793(92)80848-b;
RA Sanz L., Calvete J.J., Mann K., Schaefer W., Schmid E.R., Amselgruber W.,
RA Sinowatz F., Ehrhard M., Toepfer-Petersen E.;
RT "The complete primary structure of the spermadhesin AWN, a zona pellucida-
RT binding protein isolated from boar spermatozoa.";
RL FEBS Lett. 300:213-218(1992).
RN [3]
RP PARTIAL PROTEIN SEQUENCE.
RC TISSUE=Sperm;
RX PubMed=1540644; DOI=10.1016/0167-4838(92)90382-n;
RA Sanz L., Calvete J.J., Schaefer W., Mann K., Toepfer-Petersen E.;
RT "Isolation and biochemical characterization of two isoforms of a boar sperm
RT zona pellucida-binding protein.";
RL Biochim. Biophys. Acta 1119:127-132(1992).
RN [4]
RP PROTEIN SEQUENCE OF 21-33; 42-52; 72-77; 94-107 AND 121-129, AND
RP IDENTIFICATION OF HEPARIN-BINDING DOMAIN.
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: AWN proteins mediate the binding of boar spermatozoa to
CC component(s) of the egg's zona pellucida by a carbohydrate-binding
CC mechanism. Awn 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. Note=Predominantly localized on the
CC membrane overlying the acrosomal cap region of the sperm head.
CC -!- PTM: Partial N-acetylation differentiates isoforms AWN-1 (not
CC acetylated) and AWN-2 (acetylated).
CC -!- SIMILARITY: Belongs to the spermadhesin family. {ECO:0000305}.
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DR EMBL; AJ238538; CAB43872.1; -; mRNA.
DR PIR; S21114; S21114.
DR RefSeq; NP_998994.1; NM_213829.1.
DR AlphaFoldDB; P26776; -.
DR SMR; P26776; -.
DR BioGRID; 1148934; 1.
DR STRING; 9823.ENSSSCP00000003227; -.
DR iPTMnet; P26776; -.
DR PaxDb; P26776; -.
DR GeneID; 396783; -.
DR CTD; 396783; -.
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; Signal.
FT SIGNAL 1..20
FT /evidence="ECO:0000269|PubMed:1555646,
FT ECO:0000269|PubMed:8603690"
FT CHAIN 21..153
FT /note="Carbohydrate-binding protein AWN"
FT /id="PRO_0000221456"
FT DOMAIN 29..130
FT /note="CUB"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00059"
FT REGION 93..130
FT /note="Heparin-binding"
FT MOD_RES 21
FT /note="N-acetylalanine"
FT /evidence="ECO:0000269|PubMed:1555646"
FT DISULFID 29..50
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00059,
FT ECO:0000269|PubMed:1555646"
FT DISULFID 73..94
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00059,
FT ECO:0000269|PubMed:1555646"
FT CONFLICT 112
FT /note="Y -> R (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 118
FT /note="Q -> H (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 136
FT /note="Q -> P (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 141
FT /note="D -> E (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 153 AA; 16730 MW; BD6DEFEFD442A59E CRC64;
MKLAAPSLAL LLSTATLVSG AWNRRSRSCG GVLRDPPGKI FNSDGPQKDC VWTIKVKPHF
HVVLAIPPLN LSCGKEYVEL LDGPPGSEII GKICGGISLV FRSSSNIATI KYLRTSGQRA
SPFHIYYYAD PEGPLQFPYF DRQTIIATEK NIP
