ID   ESPB1_PIG               Reviewed;         223 AA.
AC   Q7YR83; Q7YR82;
DT   23-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2003, sequence version 1.
DT   25-MAY-2022, entry version 70.
DE   RecName: Full=Epididymal sperm-binding protein 1;
DE   AltName: Full=Epididymal secretory protein 12;
DE   Flags: Precursor;
GN   Name=ELSPBP1; Synonyms=E12;
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] (ISOFORMS 1 AND 2), PROTEIN SEQUENCE OF 24-37,
RP   PHOSPHORYLCHOLINE-BINDING, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RC   TISSUE=Epididymis;
RX   PubMed=17307309; DOI=10.1016/j.gene.2007.01.002;
RA   Ekhlasi-Hundrieser M., Schaefer B., Philipp U., Kuiper H., Leeb T.,
RA   Mehta M., Kirchhoff C., Toepfer-Petersen E.;
RT   "Sperm-binding fibronectin type II-module proteins are genetically linked
RT   and functionally related.";
RL   Gene 392:253-265(2007).
CC   -!- FUNCTION: Binds to spermatozoa upon ejaculation and may play a role in
CC       sperm capacitation. Has phosphorylcholine-binding activity.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:17307309}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q7YR83-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q7YR83-2; Sequence=VSP_028929;
CC   -!- TISSUE SPECIFICITY: Detected in epididymal duct epithelium and on sperm
CC       membrane (at protein level). {ECO:0000269|PubMed:17307309}.
CC   -!- PTM: Not N-glycosylated.
CC   -!- SIMILARITY: Belongs to the seminal plasma protein family.
CC       {ECO:0000305}.
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DR   EMBL; AJ539176; CAD62254.1; -; mRNA.
DR   EMBL; AJ539177; CAD62255.1; -; mRNA.
DR   RefSeq; NP_999569.1; NM_214404.1. [Q7YR83-1]
DR   AlphaFoldDB; Q7YR83; -.
DR   SMR; Q7YR83; -.
DR   STRING; 9823.ENSSSCP00000003383; -.
DR   PaxDb; Q7YR83; -.
DR   PeptideAtlas; Q7YR83; -.
DR   PRIDE; Q7YR83; -.
DR   GeneID; 399529; -.
DR   KEGG; ssc:399529; -.
DR   CTD; 64100; -.
DR   eggNOG; KOG1565; Eukaryota.
DR   InParanoid; Q7YR83; -.
DR   OrthoDB; 1075463at2759; -.
DR   Proteomes; UP000008227; Unplaced.
DR   Proteomes; UP000314985; 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   Alternative splicing; Direct protein sequencing; Disulfide bond;
KW   Fertilization; Reference proteome; Repeat; Secreted; Signal.
FT   SIGNAL          1..23
FT                   /evidence="ECO:0000255"
FT   CHAIN           24..223
FT                   /note="Epididymal sperm-binding protein 1"
FT                   /id="PRO_5000070518"
FT   DOMAIN          24..68
FT                   /note="Fibronectin type-II 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00479"
FT   DOMAIN          69..117
FT                   /note="Fibronectin type-II 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00479"
FT   DOMAIN          124..170
FT                   /note="Fibronectin type-II 3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00479"
FT   DOMAIN          177..223
FT                   /note="Fibronectin type-II 4"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00479"
FT   DISULFID        29..53
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00479"
FT   DISULFID        43..66
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00479"
FT   DISULFID        74..100
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00479"
FT   DISULFID        88..115
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00479"
FT   DISULFID        129..153
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00479"
FT   DISULFID        143..168
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00479"
FT   DISULFID        182..208
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00479"
FT   DISULFID        196..223
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00479"
FT   VAR_SEQ         119..172
FT                   /note="EYGGNSFSKPCIFPSKYRNHIISECLEDESNKLWCPTTENMDMDGKWSLCAD
FT                   TR -> G (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:17307309"
FT                   /id="VSP_028929"
FT   CONFLICT        4
FT                   /note="R -> W (in Ref. 1; CAD62255)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        21
FT                   /note="T -> A (in Ref. 1; CAD62255)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   223 AA;  26200 MW;  0FCE37524971435C CRC64;
     MNRRSSYLLG CTAFILYSYE TSGDTKDSCV FPFNYKGFTY FSCTRTNSLS PWCATRAVYD
     GQWKYCLIED YPRCVFPFIY RGRSHRNCIV EGSFFGKLWC SVTSSFDEKQ QWKYCEINEY
     GGNSFSKPCI FPSKYRNHII SECLEDESNK LWCPTTENMD MDGKWSLCAD TRISSLVPGF
     PCHFPFNYKN KNYFNCTTKG SKENLLWCAT SYNYDQDHTW VYC