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ESPB1_CANLF
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   25-MAY-2022, entry version 84.
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; 9612.ENSCAFP00000032923; -.
DR   PaxDb; Q9GL25; -.
DR   GeneID; 399530; -.
DR   KEGG; cfa:399530; -.
DR   CTD; 64100; -.
DR   eggNOG; KOG1565; Eukaryota.
DR   InParanoid; Q9GL25; -.
DR   OrthoDB; 1075463at2759; -.
DR   Proteomes; UP000002254; 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; -; 4.
DR   InterPro; IPR000562; FN_type2_dom.
DR   InterPro; IPR036943; FN_type2_sf.
DR   InterPro; IPR013806; Kringle-like.
DR   Pfam; PF00040; fn2; 4.
DR   SMART; SM00059; FN2; 4.
DR   SUPFAM; SSF57440; SSF57440; 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
 
 
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