SFP1_BOVIN
ID SFP1_BOVIN Reviewed; 134 AA.
AC P02784;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1991, sequence version 2.
DT 03-AUG-2022, entry version 155.
DE RecName: Full=Seminal plasma protein PDC-109;
DE AltName: Full=BSP-A1 and BSP-A2;
DE AltName: Full=Seminal vesicle secretory protein 109;
DE Short=SVSP109;
DE Flags: Precursor;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=3229283; DOI=10.1089/dna.1988.7.595;
RA Kemme M., Scheit K.H.;
RT "Cloning and sequence analysis of a cDNA from seminal vesicle tissue
RT encoding the precursor of the major protein of bull semen.";
RL DNA 7:595-599(1988).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC TISSUE=Lung;
RX PubMed=1932121; DOI=10.1016/0167-4781(91)90113-z;
RA Braeuer C., Scheit K.H.;
RT "Characterization of the gene for the bovine seminal vesicle secretory
RT protein SVSP109.";
RL Biochim. Biophys. Acta 1090:259-260(1991).
RN [3]
RP NUCLEOTIDE SEQUENCE.
RA Braeuer C.C., Kleine Kuhlmann J.J., Hanes J.J., Scheit K.K.;
RL Submitted (MAY-1994) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP PROTEIN SEQUENCE OF 26-134, AND DISULFIDE BONDS.
RX PubMed=6870895; DOI=10.1016/0006-291x(83)91078-1;
RA Esch F.S., Ling N.C., Boehlen P., Ying S.Y., Guillemin R.;
RT "Primary structure of PDC-109, a major protein constituent of bovine
RT seminal plasma.";
RL Biochem. Biophys. Res. Commun. 113:861-867(1983).
RN [5]
RP GLYCOSYLATION AT THR-36.
RX PubMed=8070564; DOI=10.1016/0014-5793(94)00768-3;
RA Calvete J.J., Raida M., Sanz L., Wempe F., Scheit K.H., Romero A.,
RA Toepfer-Petersen E.;
RT "Localization and structural characterization of an oligosaccharide O-
RT linked to bovine PDC-109. Quantitation of the glycoprotein in seminal
RT plasma and on the surface of ejaculated and capacitated spermatozoa.";
RL FEBS Lett. 350:203-206(1994).
RN [6]
RP GLYCOSYLATION AT THR-36, AND STRUCTURE OF CARBOHYDRATE ON THR-36.
RX PubMed=8654577; DOI=10.1016/0014-5793(96)00448-6;
RA Gerwig G.L., Calvete J.J., Toepfer-Petersen E., Vliegenthart J.F.G.;
RT "The structure of the O-linked carbohydrate chain of bovine seminal plasma
RT protein PDC-109 revised by H-NMR spectroscopy A correction.";
RL FEBS Lett. 387:99-100(1996).
RN [7]
RP STRUCTURE BY NMR OF 95-134.
RX PubMed=1993183; DOI=10.1021/bi00220a032;
RA Constantine K.L., Ramesh V., Banyai L., Trexler M., Patthy L., Llinas M.;
RT "Sequence-specific 1H NMR assignments and structural characterization of
RT bovine seminal fluid protein PDC-109 domain b.";
RL Biochemistry 30:1663-1672(1991).
RN [8]
RP STRUCTURE BY NMR OF 95-134.
RX PubMed=1731074; DOI=10.1016/0022-2836(92)90731-x;
RA Constantine K.L., Madrid M., Banyai L., Trexler M., Patthy L., Llinas M.;
RT "Refined solution structure and ligand-binding properties of PDC-109 domain
RT b. A collagen-binding type II domain.";
RL J. Mol. Biol. 223:281-298(1992).
CC -!- FUNCTION: Could enhance the fertilizing capacity of bull spermatozoa
CC upon interaction with heparin-like glycosaminoglycans present in the
CC female genital tract. Exhibits both simulatory and inhibitory actions
CC on the release of pituitary gonadotropins.
CC -!- SUBUNIT: Homodimer.
CC -!- SUBCELLULAR LOCATION: Secreted.
CC -!- TISSUE SPECIFICITY: Major component of seminal plasma.
CC -!- PTM: O-linked glycan consists of Gal-GalNAc disaccharide which is
CC modified with a sialic acid residue (macro- and/or microheterogeneity
CC account for differences between BSP-A1 and BSP-A2).
CC {ECO:0000269|PubMed:8070564}.
CC -!- SIMILARITY: Belongs to the seminal plasma protein family.
CC {ECO:0000305}.
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DR EMBL; M22244; AAA30766.1; -; mRNA.
DR EMBL; X60495; CAA43021.1; -; Genomic_DNA.
DR EMBL; X60496; CAA43021.1; JOINED; Genomic_DNA.
DR EMBL; X60497; CAA43021.1; JOINED; Genomic_DNA.
DR EMBL; X60498; CAA43021.1; JOINED; Genomic_DNA.
DR EMBL; X60960; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; Z33621; CAA83915.1; -; Genomic_DNA.
DR PIR; S18404; WTBO.
DR RefSeq; NP_001001145.1; NM_001001145.1.
DR PDB; 1H8P; X-ray; 1.82 A; A/B=26-134.
DR PDB; 1PDC; NMR; -; A=90-134.
DR PDBsum; 1H8P; -.
DR PDBsum; 1PDC; -.
DR AlphaFoldDB; P02784; -.
DR BMRB; P02784; -.
DR SMR; P02784; -.
DR STRING; 9913.ENSBTAP00000051819; -.
DR GlyConnect; 553; 2 O-Linked glycans (1 site).
DR PaxDb; P02784; -.
DR Ensembl; ENSBTAT00000055955; ENSBTAP00000051819; ENSBTAG00000023434.
DR GeneID; 407187; -.
DR KEGG; bta:407187; -.
DR CTD; 100034140; -.
DR VEuPathDB; HostDB:ENSBTAG00000023434; -.
DR eggNOG; KOG1565; Eukaryota.
DR GeneTree; ENSGT00940000164580; -.
DR HOGENOM; CLU_126630_0_0_1; -.
DR InParanoid; P02784; -.
DR OMA; PDNKCVF; -.
DR OrthoDB; 1429125at2759; -.
DR TreeFam; TF343543; -.
DR EvolutionaryTrace; P02784; -.
DR Proteomes; UP000009136; Chromosome 18.
DR Bgee; ENSBTAG00000023434; Expressed in mammary gland fat and 14 other tissues.
DR GO; GO:0009986; C:cell surface; IBA:GO_Central.
DR GO; GO:0005615; C:extracellular space; IDA:CAFA.
DR GO; GO:0008201; F:heparin binding; IBA:GO_Central.
DR GO; GO:0033700; P:phospholipid efflux; IDA:CAFA.
DR GO; GO:1902492; P:positive regulation of sperm capacitation; IDA:CAFA.
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; 2.
DR PROSITE; PS51092; FN2_2; 2.
PE 1: Evidence at protein level;
KW 3D-structure; Direct protein sequencing; Disulfide bond; Fertilization;
KW Glycoprotein; Reference proteome; Repeat; Secreted; Signal.
FT SIGNAL 1..25
FT /evidence="ECO:0000269|PubMed:6870895"
FT CHAIN 26..134
FT /note="Seminal plasma protein PDC-109"
FT /id="PRO_0000019231"
FT DOMAIN 44..88
FT /note="Fibronectin type-II 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00479"
FT DOMAIN 89..134
FT /note="Fibronectin type-II 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00479"
FT CARBOHYD 36
FT /note="O-linked (GalNAc...) threonine"
FT /evidence="ECO:0000269|PubMed:8070564,
FT ECO:0000269|PubMed:8654577"
FT /id="CAR_000071"
FT DISULFID 49..73
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00479,
FT ECO:0000269|PubMed:6870895"
FT DISULFID 63..86
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00479,
FT ECO:0000269|PubMed:6870895"
FT DISULFID 94..119
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00479,
FT ECO:0000269|PubMed:6870895"
FT DISULFID 108..134
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00479,
FT ECO:0000269|PubMed:6870895"
FT STRAND 51..55
FT /evidence="ECO:0007829|PDB:1H8P"
FT STRAND 58..62
FT /evidence="ECO:0007829|PDB:1H8P"
FT STRAND 68..70
FT /evidence="ECO:0007829|PDB:1H8P"
FT STRAND 72..78
FT /evidence="ECO:0007829|PDB:1H8P"
FT STRAND 83..85
FT /evidence="ECO:0007829|PDB:1H8P"
FT HELIX 88..90
FT /evidence="ECO:0007829|PDB:1H8P"
FT STRAND 96..100
FT /evidence="ECO:0007829|PDB:1H8P"
FT STRAND 103..107
FT /evidence="ECO:0007829|PDB:1H8P"
FT STRAND 114..116
FT /evidence="ECO:0007829|PDB:1H8P"
FT STRAND 118..124
FT /evidence="ECO:0007829|PDB:1H8P"
FT HELIX 125..128
FT /evidence="ECO:0007829|PDB:1H8P"
FT STRAND 131..133
FT /evidence="ECO:0007829|PDB:1H8P"
SQ SEQUENCE 134 AA; 15481 MW; AD55FB8969B32224 CRC64;
MALQLGLFLI WAGVSVFLQL DPVNGDQDEG VSTEPTQDGP AELPEDEECV FPFVYRNRKH
FDCTVHGSLF PWCSLDADYV GRWKYCAQRD YAKCVFPFIY GGKKYETCTK IGSMWMSWCS
LSPNYDKDRA WKYC
