ID   SP1_HORSE               Reviewed;         120 AA.
AC   P81121;
DT   15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT   15-JUL-1998, sequence version 1.
DT   25-MAY-2022, entry version 87.
DE   RecName: Full=Seminal plasma protein HSP-1;
OS   Equus caballus (Horse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Perissodactyla; Equidae; Equus.
OX   NCBI_TaxID=9796;
RN   [1]
RP   PROTEIN SEQUENCE, AND GLYCOSYLATION AT THR-5; THR-12; THR-22 AND THR-27.
RC   TISSUE=Seminal plasma;
RX   PubMed=7654203; DOI=10.1042/bj3100615;
RA   Calvete J.J., Mann K., Schaefer W., Sanz L., Reinert M., Nessau S.,
RA   Raida M., Toepfer-Petersen E.;
RT   "Amino acid sequence of HSP-1, a major protein of stallion seminal plasma:
RT   effect of glycosylation on its heparin- and gelatin-binding capabilities.";
RL   Biochem. J. 310:615-622(1995).
RN   [2]
RP   SEQUENCE REVISION TO 67-69.
RC   TISSUE=Seminal plasma;
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: Could enhance the fertilizing capacity of spermatozoa upon
CC       interaction with heparin-like glycosaminoglycans present in the female
CC       genital tract.
CC   -!- SUBUNIT: One glycoform exists as a monomer while the other forms a
CC       heterotetramer with HSP-2 and binds heparin.
CC   -!- SUBCELLULAR LOCATION: Secreted.
CC   -!- TISSUE SPECIFICITY: Major component of seminal plasma.
CC   -!- PTM: O-glycosylated on Thr. There are two forms of HSP-1 which probably
CC       differ in the amount of sialylation of polysaccharide.
CC       {ECO:0000269|PubMed:7654203}.
CC   -!- SIMILARITY: Belongs to the seminal plasma protein family.
CC       {ECO:0000305}.
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DR   PIR; S58424; S58424.
DR   AlphaFoldDB; P81121; -.
DR   SMR; P81121; -.
DR   iPTMnet; P81121; -.
DR   PaxDb; P81121; -.
DR   HOGENOM; CLU_126630_0_0_1; -.
DR   Proteomes; UP000002281; Unplaced.
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; 1.
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; Glycoprotein;
KW   Heparin-binding; Reference proteome; Repeat; Secreted.
FT   CHAIN           1..120
FT                   /note="Seminal plasma protein HSP-1"
FT                   /id="PRO_0000158526"
FT   REPEAT          1..13
FT                   /note="1"
FT   REPEAT          16..28
FT                   /note="2"
FT   DOMAIN          29..73
FT                   /note="Fibronectin type-II 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00479"
FT   DOMAIN          74..120
FT                   /note="Fibronectin type-II 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00479"
FT   REGION          1..28
FT                   /note="2 X approximate repeats"
FT   CARBOHYD        5
FT                   /note="O-linked (GalNAc...) threonine"
FT                   /evidence="ECO:0000269|PubMed:7654203"
FT   CARBOHYD        12
FT                   /note="O-linked (GalNAc...) threonine"
FT                   /evidence="ECO:0000269|PubMed:7654203"
FT   CARBOHYD        22
FT                   /note="O-linked (GalNAc...) threonine"
FT                   /evidence="ECO:0000269|PubMed:7654203"
FT   CARBOHYD        27
FT                   /note="O-linked (GalNAc...) threonine"
FT                   /evidence="ECO:0000269|PubMed:7654203"
FT   DISULFID        34..58
FT   DISULFID        48..71
FT   DISULFID        79..105
FT   DISULFID        93..120
SQ   SEQUENCE   120 AA;  13905 MW;  AE22F0CA9481401C CRC64;
     DLQTTGADHS ATVNPDQQLI MTKHSATVTP ENKCVFPFNY RGYRYYDCTR TDSFYRWCSL
     TGTYSGSWKY CAATDYAKCA FPFVYRGQTY DRCTTDGSLF RISWCSVTPN YDHHGAWKYC