ID   SFP4_BOVIN              Reviewed;         183 AA.
AC   P81019; O97868;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-2000, sequence version 2.
DT   25-MAY-2022, entry version 118.
DE   RecName: Full=Seminal plasma protein BSP-30 kDa;
DE            Short=BSP-30K;
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].
RA   Salois D., Menard M., Paquette Y., Manjunath P.;
RT   "Complete mRNA sequence of bovine seminal plasma 30K protein (BSP-30K).";
RL   Submitted (APR-1998) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   PROTEIN SEQUENCE OF 26-183, AND GLYCOSYLATION AT THR-36; THR-46; THR-57;
RP   THR-58; THR-59 AND THR-64.
RC   TISSUE=Seminal plasma;
RX   PubMed=8980140; DOI=10.1016/s0014-5793(96)01310-5;
RA   Calvete J.J., Mann K., Sanz L., Raida M., Toepfer-Petersen E.;
RT   "The primary structure of BSP-30K, a major lipid-, gelatin-, and heparin-
RT   binding glycoprotein of bovine seminal plasma.";
RL   FEBS Lett. 399:147-152(1996).
CC   -!- FUNCTION: Binds to spermatozoa upon ejaculation and may play a role in
CC       sperm capacitation. Displays heparin-, gelatin- and phospholipid-
CC       binding activities.
CC   -!- SUBCELLULAR LOCATION: Secreted.
CC   -!- SIMILARITY: Belongs to the seminal plasma protein family.
CC       {ECO:0000305}.
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DR   EMBL; AF057133; AAD17519.1; -; mRNA.
DR   RefSeq; NP_777267.1; NM_174842.2.
DR   AlphaFoldDB; P81019; -.
DR   SMR; P81019; -.
DR   STRING; 9913.ENSBTAP00000052231; -.
DR   iPTMnet; P81019; -.
DR   PaxDb; P81019; -.
DR   Ensembl; ENSBTAT00000054953; ENSBTAP00000052231; ENSBTAG00000018882.
DR   GeneID; 317699; -.
DR   KEGG; bta:317699; -.
DR   CTD; 317699; -.
DR   VEuPathDB; HostDB:ENSBTAG00000018882; -.
DR   eggNOG; KOG1565; Eukaryota.
DR   GeneTree; ENSGT00940000164580; -.
DR   HOGENOM; CLU_126630_0_0_1; -.
DR   InParanoid; P81019; -.
DR   OMA; VEKPHED; -.
DR   OrthoDB; 1429125at2759; -.
DR   TreeFam; TF343543; -.
DR   Proteomes; UP000009136; Chromosome 18.
DR   Bgee; ENSBTAG00000018882; Expressed in mammary gland fat and 12 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; 1.
DR   DisProt; DP00669; -.
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   Pfam; PF00040; fn2; 2.
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; Glycoprotein;
KW   Heparin-binding; Reference proteome; Repeat; Secreted; Signal.
FT   SIGNAL          1..25
FT                   /evidence="ECO:0000269|PubMed:8980140"
FT   CHAIN           26..183
FT                   /note="Seminal plasma protein BSP-30 kDa"
FT                   /id="PRO_0000019233"
FT   DOMAIN          92..136
FT                   /note="Fibronectin type-II 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00479"
FT   DOMAIN          137..183
FT                   /note="Fibronectin type-II 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00479"
FT   REGION          23..47
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CARBOHYD        36
FT                   /note="O-linked (GalNAc...) threonine"
FT                   /evidence="ECO:0000269|PubMed:8980140"
FT   CARBOHYD        46
FT                   /note="O-linked (GalNAc...) threonine"
FT                   /evidence="ECO:0000269|PubMed:8980140"
FT   CARBOHYD        57
FT                   /note="O-linked (GalNAc...) threonine"
FT                   /evidence="ECO:0000269|PubMed:8980140"
FT   CARBOHYD        58
FT                   /note="O-linked (GalNAc...) threonine"
FT                   /evidence="ECO:0000269|PubMed:8980140"
FT   CARBOHYD        59
FT                   /note="O-linked (GalNAc...) threonine"
FT                   /evidence="ECO:0000269|PubMed:8980140"
FT   CARBOHYD        64
FT                   /note="O-linked (GalNAc...) threonine"
FT                   /evidence="ECO:0000269|PubMed:8980140"
FT   DISULFID        97..121
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00479"
FT   DISULFID        111..134
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00479"
FT   DISULFID        142..168
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00479"
FT   DISULFID        156..183
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00479"
FT   CONFLICT        38
FT                   /note="P -> S (in Ref. 2; AA sequence)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   183 AA;  21269 MW;  82615DFFB3AB42EA CRC64;
     MAPLVGLFLI WAGASVFQQL HPVNGGDIPD PGSKPTPPGM ADELPTETYD LPPEIYTTTF
     LPRTIYPQEE MPYDDKPFPS LLSKANDLNA VFEGPACAFP FTYKGKKYYM CTRKNSVLLW
     CSLDTEYQGN WKFCTERDEP ECVFPFIYRK KSYESCTRVH SFFWRRWCSL TSNYDRDKAW
     KYC