ID ESPB1_CANLF Reviewed; 245 AA.
AC Q9GL25; Q9GL26;
DT 23-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 27-MAR-2024, entry version 91.
DE RecName: Full=Epididymal sperm-binding protein 1;
DE AltName: Full=CeE12;
DE AltName: Full=E12a;
DE AltName: Full=Epididymal secretory protein 12;
DE Flags: Precursor;
GN Name=ELSPBP1; Synonyms=E12;
OS Canis lupus familiaris (Dog) (Canis familiaris).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Caniformia; Canidae; Canis.
OX NCBI_TaxID=9615;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=11144225;
RX DOI=10.1002/1098-2795(200101)58:1<88::aid-mrd12>3.0.co;2-d;
RA Saalmann A., Muenz S., Ellerbrock K., Ivell R., Kirchhoff C.;
RT "Novel sperm-binding proteins of epididymal origin contain four fibronectin
RT type II-modules.";
RL Mol. Reprod. Dev. 58:88-100(2001).
CC -!- FUNCTION: Binds to spermatozoa upon ejaculation and may play a role in
CC sperm capacitation. Has phosphorylcholine-binding activity (By
CC similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:11144225}.
CC -!- TISSUE SPECIFICITY: Detected in epididymal duct epithelium, cauda
CC epididymidal fluid and on sperm membrane (at protein level).
CC {ECO:0000269|PubMed:11144225}.
CC -!- SIMILARITY: Belongs to the seminal plasma protein family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAC14265.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AJ278477; CAC14266.1; -; mRNA.
DR EMBL; AJ278477; CAC14265.1; ALT_INIT; mRNA.
DR RefSeq; NP_001002931.1; NM_001002931.1.
DR AlphaFoldDB; Q9GL25; -.
DR SMR; Q9GL25; -.
DR STRING; 9615.ENSCAFP00000006026; -.
DR PaxDb; 9612-ENSCAFP00000032923; -.
DR GeneID; 399530; -.
DR KEGG; cfa:399530; -.
DR CTD; 64100; -.
DR eggNOG; KOG1565; Eukaryota.
DR InParanoid; Q9GL25; -.
DR OrthoDB; 2896418at2759; -.
DR Proteomes; UP000002254; Unplaced.
DR Proteomes; UP000694429; Unplaced.
DR Proteomes; UP000694542; Unplaced.
DR Proteomes; UP000805418; Unplaced.
DR GO; GO:0009986; C:cell surface; IBA:GO_Central.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0008201; F:heparin binding; IBA:GO_Central.
DR GO; GO:0007338; P:single fertilization; IEA:UniProtKB-KW.
DR GO; GO:0048240; P:sperm capacitation; IBA:GO_Central.
DR CDD; cd00062; FN2; 3.
DR Gene3D; 2.10.10.10; Fibronectin, type II, collagen-binding; 4.
DR InterPro; IPR000562; FN_type2_dom.
DR InterPro; IPR036943; FN_type2_sf.
DR InterPro; IPR013806; Kringle-like.
DR PANTHER; PTHR22918:SF2; EPIDIDYMAL SPERM-BINDING PROTEIN 1; 1.
DR PANTHER; PTHR22918; SEMINAL PLASMA PROTEIN; 1.
DR Pfam; PF00040; fn2; 4.
DR PRINTS; PR00013; FNTYPEII.
DR SMART; SM00059; FN2; 4.
DR SUPFAM; SSF57440; Kringle-like; 4.
DR PROSITE; PS00023; FN2_1; 2.
DR PROSITE; PS51092; FN2_2; 4.
PE 1: Evidence at protein level;
KW Disulfide bond; Fertilization; Reference proteome; Repeat; Secreted;
KW Signal.
FT SIGNAL 1..23
FT /evidence="ECO:0000255"
FT CHAIN 24..245
FT /note="Epididymal sperm-binding protein 1"
FT /id="PRO_0000308248"
FT DOMAIN 46..90
FT /note="Fibronectin type-II 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00479"
FT DOMAIN 91..139
FT /note="Fibronectin type-II 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00479"
FT DOMAIN 146..192
FT /note="Fibronectin type-II 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00479"
FT DOMAIN 199..245
FT /note="Fibronectin type-II 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00479"
FT DISULFID 51..75
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00479"
FT DISULFID 65..88
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00479"
FT DISULFID 96..122
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00479"
FT DISULFID 110..137
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00479"
FT DISULFID 151..175
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00479"
FT DISULFID 165..190
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00479"
FT DISULFID 204..230
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00479"
FT DISULFID 218..245
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00479"
SQ SEQUENCE 245 AA; 28746 MW; DBDF6A6B540D5010 CRC64;
MNPWSSYLLG WTTFLLYFYE TSGKIPNLSS LGKHEFTKPW ISIKEDQKDS CVFPFVYKGS
SYFSCIKTNS FSPWCATRAV YNGQWKFCMA DDYPRCIFPF IFRGKSHNSC ITEGSFLRRL
WCSVTSSFDE NQQWKYCETN EYGGNSFSKP CIFPSIFRNS TIFECMEDEN NKLWCPTTEN
MDEDGKWSLC ADTRISSLVP GFPCHFPFSY KNKNYYNCIG KGTKENLTWC ATSYNYDRDH
TWVYC
//
