PB1_PIG
ID PB1_PIG Reviewed; 130 AA.
AC P80964; O46615;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 27-JAN-2003, sequence version 2.
DT 03-AUG-2022, entry version 105.
DE RecName: Full=Seminal plasma protein pB1;
DE AltName: Full=Protein DQH;
DE AltName: Full=pAIF-1;
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].
RX PubMed=10206662;
RX DOI=10.1002/(sici)1098-2795(199903)52:3<303::aid-mrd8>3.0.co;2-7;
RA Plucienniczak G., Jagiello A., Plucienniczak A., Holody D., Strzezek J.;
RT "Cloning of complementary DNA encoding the pB1 component of the 54-
RT kilodalton glycoprotein of boar seminal plasma.";
RL Mol. Reprod. Dev. 52:303-309(1999).
RN [2]
RP PROTEIN SEQUENCE OF 26-130.
RC STRAIN=Wild boar;
RX PubMed=9166899; DOI=10.1016/s0014-5793(97)00344-x;
RA Calvete J.J., Raida M., Gentzel M., Urbanke C., Sanz L.,
RA Toepfer-Petersen E.;
RT "Isolation and characterization of heparin- and phosphorylcholine-binding
RT proteins of boar and stallion seminal plasma. Primary structure of porcine
RT pB1.";
RL FEBS Lett. 407:201-206(1997).
CC -!- FUNCTION: May form a complex with spermadhesin AQN-1 which possesses
CC phosphorylcholine-binding activity.
CC -!- SUBCELLULAR LOCATION: Secreted.
CC -!- TISSUE SPECIFICITY: Component of seminal plasma.
CC -!- SIMILARITY: Belongs to the seminal plasma protein family.
CC {ECO:0000305}.
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DR EMBL; AF047026; AAD11581.1; -; mRNA.
DR PIR; A58837; A58837.
DR RefSeq; NP_998997.1; NM_213832.1.
DR AlphaFoldDB; P80964; -.
DR SMR; P80964; -.
DR BioGRID; 1148955; 1.
DR STRING; 9823.ENSSSCP00000003307; -.
DR PaxDb; P80964; -.
DR PRIDE; P80964; -.
DR GeneID; 396806; -.
DR KEGG; ssc:396806; -.
DR CTD; 100034140; -.
DR eggNOG; KOG1565; Eukaryota.
DR HOGENOM; CLU_126630_0_0_1; -.
DR InParanoid; P80964; -.
DR OrthoDB; 1429125at2759; -.
DR TreeFam; TF343543; -.
DR Proteomes; UP000008227; Unplaced.
DR Proteomes; UP000314985; Unplaced.
DR Genevisible; P80964; SS.
DR GO; GO:0009986; C:cell surface; IBA:GO_Central.
DR GO; GO:0005615; C:extracellular space; IEA:InterPro.
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; 2.
DR Gene3D; 2.10.10.10; -; 2.
DR InterPro; IPR000562; FN_type2_dom.
DR InterPro; IPR036943; FN_type2_sf.
DR InterPro; IPR013806; Kringle-like.
DR InterPro; IPR016356; Seminal_plasma_PDC-109-like.
DR Pfam; PF00040; fn2; 2.
DR PIRSF; PIRSF002541; Seminal_plasma_PDC-109; 1.
DR SMART; SM00059; FN2; 2.
DR SUPFAM; SSF57440; SSF57440; 2.
DR PROSITE; PS00023; FN2_1; 1.
DR PROSITE; PS51092; FN2_2; 2.
PE 1: Evidence at protein level;
KW Direct protein sequencing; Disulfide bond; Fertilization;
KW Reference proteome; Repeat; Secreted; Signal.
FT SIGNAL 1..25
FT /evidence="ECO:0000269|PubMed:9166899"
FT CHAIN 26..130
FT /note="Seminal plasma protein pB1"
FT /id="PRO_0000019234"
FT DOMAIN 39..83
FT /note="Fibronectin type-II 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00479"
FT DOMAIN 84..130
FT /note="Fibronectin type-II 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00479"
FT DISULFID 44..68
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00479"
FT DISULFID 58..81
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00479"
FT DISULFID 89..115
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00479"
FT DISULFID 103..130
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00479"
FT CONFLICT 78
FT /note="W -> P (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 84
FT /note="T -> Q (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 116
FT /note="P -> T (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 123
FT /note="Q -> R (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 128
FT /note="R -> K (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 130 AA; 15373 MW; 96DF171A45459DE6 CRC64;
MAPRLGIFLL WAGVSVFLPL DPVNGDQHLP GRFLTPAITS DDKCVFPFIY KGNLYFDCTL
HDSTYYWCSV TTYYMKRWRY CRSTDYARCA LPFIFRGKEY DSCIKEGSVF SKYWCPVTPN
YDQDRAWRYC
