PSP1_PIG
ID PSP1_PIG Reviewed; 133 AA.
AC P35495;
DT 01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1996, sequence version 2.
DT 25-MAY-2022, entry version 126.
DE RecName: Full=Major seminal plasma glycoprotein PSP-I;
DE AltName: Full=SP3;
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].
RC TISSUE=Seminal vesicle;
RX PubMed=8397818; DOI=10.1089/dna.1993.12.605;
RA Kwok S.C.M., Yang D., Dai G., Soares M.J., Chen S., McMurtry J.P.;
RT "Molecular cloning and sequence analysis of two porcine seminal proteins,
RT PSP-I and PSP-II: new members of the spermadhesin family.";
RL DNA Cell Biol. 12:605-610(1993).
RN [2]
RP PROTEIN SEQUENCE OF 25-133.
RC TISSUE=Sperm;
RX PubMed=8269963; DOI=10.1111/j.1432-1033.1993.tb18426.x;
RA Calvete J.J., Solis D., Sanz L., Diaz-Maurino T., Schaefer W., Mann K.,
RA Toepfer-Petersen E.;
RT "Characterization of two glycosylated boar spermadhesins.";
RL Eur. J. Biochem. 218:719-725(1993).
RN [3]
RP PROTEIN SEQUENCE OF 25-133.
RC TISSUE=Sperm;
RX PubMed=1586165; DOI=10.1016/0003-9861(92)90528-5;
RA Rutherfurd K.J., Swiderek K.M., Green C.B., Chen S., Shively J.E.,
RA Kwok S.C.M.;
RT "Purification and characterization of PSP-I and PSP-II, two major proteins
RT from porcine seminal plasma.";
RL Arch. Biochem. Biophys. 295:352-359(1992).
RN [4]
RP PARTIAL PROTEIN SEQUENCE, DISULFIDE BONDS, GLYCOSYLATION AT ASN-71, AND
RP MASS SPECTROMETRY.
RC TISSUE=Sperm;
RX PubMed=7781775; DOI=10.1016/0014-5793(95)00452-f;
RA Calvete J.J., Mann K., Schaefer W., Raida M., Sanz L., Toepfer-Petersen E.;
RT "Boar spermadhesin PSP-II: location of posttranslational modifications,
RT heterodimer formation with PSP-I glycoforms and effect of dimerization on
RT the ligand-binding capabilities of the subunits.";
RL FEBS Lett. 365:179-182(1995).
RN [5]
RP PROTEIN SEQUENCE OF 28-34; 49-53; 71-78 AND 95-108.
RX PubMed=8603690; DOI=10.1016/0014-5793(95)01513-2;
RA Calvete J.J., Dostalova Z., Sanz L., Adermann K., Thole H.H.,
RA Toepfer-Petersen E.;
RT "Mapping the heparin-binding domain of boar spermadhesins.";
RL FEBS Lett. 379:207-211(1996).
RN [6]
RP STRUCTURE OF CARBOHYDRATE.
RX PubMed=10504403; DOI=10.1046/j.1432-1327.1999.00766.x;
RA Nimtz M., Grabenhorst E., Conradt H.S., Sanz L., Calvete J.J.;
RT "Structural characterization of the oligosaccharide chains of native and
RT crystallized boar seminal plasma spermadhesin PSP-I and PSP-II
RT glycoforms.";
RL Eur. J. Biochem. 265:703-718(1999).
RN [7]
RP X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS).
RX PubMed=9334740; DOI=10.1038/nsb1097-783;
RA Romero A., Romao M.J., Varela P.F., Koelln I., Dias J.M., Carvalho A.L.,
RA Sanz L., Toepfer-Petersen E., Calvete J.J.;
RT "The crystal structures of two spermadhesins reveal the CUB domain fold.";
RL Nat. Struct. Biol. 4:783-788(1997).
CC -!- FUNCTION: Not yet identified, major porcine seminal plasma protein. Can
CC bind soybean trypsin inhibitor after deglycosylation.
CC -!- SUBUNIT: Monomer or heterodimer with PSP-II (depending on the type of
CC glycosylation of PSP-I).
CC -!- SUBCELLULAR LOCATION: Secreted.
CC -!- TISSUE SPECIFICITY: Seminal plasma or sperm.
CC -!- MASS SPECTROMETRY: Mass=11982; Mass_error=4; Method=MALDI;
CC Evidence={ECO:0000269|PubMed:7781775};
CC -!- SIMILARITY: Belongs to the spermadhesin family. {ECO:0000305}.
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DR EMBL; U02626; AAC48399.1; -; mRNA.
DR RefSeq; NP_999002.1; NM_213837.1.
DR PDB; 1SPP; X-ray; 2.40 A; A=25-133.
DR PDBsum; 1SPP; -.
DR AlphaFoldDB; P35495; -.
DR SMR; P35495; -.
DR BioGRID; 1148964; 1.
DR MINT; P35495; -.
DR STRING; 9823.ENSSSCP00000003223; -.
DR GlyConnect; 360; 36 N-Linked glycans (1 site).
DR PaxDb; P35495; -.
DR PeptideAtlas; P35495; -.
DR Ensembl; ENSSSCT00045021213; ENSSSCP00045014595; ENSSSCG00045012414.
DR GeneID; 396818; -.
DR KEGG; ssc:396818; -.
DR CTD; 396818; -.
DR eggNOG; ENOG502TD48; Eukaryota.
DR OrthoDB; 1512831at2759; -.
DR EvolutionaryTrace; P35495; -.
DR Proteomes; UP000008227; Unplaced.
DR Proteomes; UP000314985; Unplaced.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0007338; P:single fertilization; IEA:InterPro.
DR CDD; cd00041; CUB; 1.
DR Gene3D; 2.60.120.290; -; 1.
DR InterPro; IPR000859; CUB_dom.
DR InterPro; IPR035914; Sperma_CUB_dom_sf.
DR InterPro; IPR000124; Spermadhesin.
DR Pfam; PF00431; CUB; 1.
DR SMART; SM00042; CUB; 1.
DR SUPFAM; SSF49854; SSF49854; 1.
DR PROSITE; PS01180; CUB; 1.
DR PROSITE; PS00985; SPERMADHESIN_1; 1.
DR PROSITE; PS00986; SPERMADHESIN_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Direct protein sequencing; Disulfide bond; Glycoprotein;
KW Reference proteome; Secreted; Signal.
FT SIGNAL 1..24
FT /evidence="ECO:0000269|PubMed:1586165,
FT ECO:0000269|PubMed:8269963"
FT CHAIN 25..133
FT /note="Major seminal plasma glycoprotein PSP-I"
FT /id="PRO_0000033188"
FT DOMAIN 30..130
FT /note="CUB"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00059"
FT CARBOHYD 71
FT /note="N-linked (GlcNAc...) (complex) asparagine"
FT /evidence="ECO:0000269|PubMed:7781775"
FT /id="CAR_000189"
FT DISULFID 30..51
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00059,
FT ECO:0000269|PubMed:7781775"
FT DISULFID 74..95
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00059,
FT ECO:0000269|PubMed:7781775"
FT CONFLICT 81
FT /note="I -> V (in Ref. 3; AA sequence)"
FT /evidence="ECO:0000305"
FT STRAND 32..35
FT /evidence="ECO:0007829|PDB:1SPP"
FT STRAND 37..42
FT /evidence="ECO:0007829|PDB:1SPP"
FT STRAND 49..56
FT /evidence="ECO:0007829|PDB:1SPP"
FT STRAND 61..71
FT /evidence="ECO:0007829|PDB:1SPP"
FT TURN 74..76
FT /evidence="ECO:0007829|PDB:1SPP"
FT STRAND 77..85
FT /evidence="ECO:0007829|PDB:1SPP"
FT STRAND 90..104
FT /evidence="ECO:0007829|PDB:1SPP"
FT STRAND 109..114
FT /evidence="ECO:0007829|PDB:1SPP"
FT STRAND 124..130
FT /evidence="ECO:0007829|PDB:1SPP"
SQ SEQUENCE 133 AA; 14501 MW; 94B5B42EEEED14C9 CRC64;
MKLGSAIPWA LLFSTATLIS TGWGLDYHAC GGRLTDDYGT IFTYKGPKTE CVWTLQVDPK
YKLLVSIPTL NLTCGKEYVE ILEGAPGSKS LGKFCEGLSI LNRGSSGMTV KYKRDSGHPA
SPYEIIFLRD SQG
