PSP2_PIG
ID PSP2_PIG Reviewed; 137 AA.
AC P35496;
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-II;
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 22-34.
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 [3]
RP PARTIAL PROTEIN SEQUENCE, DISULFIDE BONDS, GLYCOSYLATION AT ASN-119, 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 [4]
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 [5]
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 -!- SUBUNIT: Monomer or heterodimer with PSP-I (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=12410; Mass_error=8; Method=MALDI;
CC Evidence={ECO:0000269|PubMed:7781775};
CC -!- SIMILARITY: Belongs to the spermadhesin family. {ECO:0000305}.
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DR EMBL; U02627; AAC48400.1; -; mRNA.
DR PIR; S65875; S65875.
DR RefSeq; NP_999001.1; NM_213836.1.
DR PDB; 1SPP; X-ray; 2.40 A; B=22-137.
DR PDBsum; 1SPP; -.
DR AlphaFoldDB; P35496; -.
DR SMR; P35496; -.
DR MINT; P35496; -.
DR STRING; 9823.ENSSSCP00000003225; -.
DR GlyConnect; 361; 39 N-Linked glycans (1 site).
DR PaxDb; P35496; -.
DR PeptideAtlas; P35496; -.
DR PRIDE; P35496; -.
DR GeneID; 396817; -.
DR KEGG; ssc:396817; -.
DR CTD; 396817; -.
DR eggNOG; ENOG502TD48; Eukaryota.
DR OrthoDB; 1512831at2759; -.
DR EvolutionaryTrace; P35496; -.
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..21
FT /evidence="ECO:0000269|PubMed:1586165"
FT CHAIN 22..137
FT /note="Major seminal plasma glycoprotein PSP-II"
FT /id="PRO_0000033189"
FT DOMAIN 30..131
FT /note="CUB"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00059"
FT CARBOHYD 119
FT /note="N-linked (GlcNAc...) (complex) asparagine"
FT /evidence="ECO:0000269|PubMed:7781775"
FT /id="CAR_000148"
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 STRAND 23..25
FT /evidence="ECO:0007829|PDB:1SPP"
FT HELIX 26..29
FT /evidence="ECO:0007829|PDB:1SPP"
FT STRAND 32..34
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 62..71
FT /evidence="ECO:0007829|PDB:1SPP"
FT STRAND 77..85
FT /evidence="ECO:0007829|PDB:1SPP"
FT STRAND 90..103
FT /evidence="ECO:0007829|PDB:1SPP"
FT STRAND 105..117
FT /evidence="ECO:0007829|PDB:1SPP"
FT STRAND 125..131
FT /evidence="ECO:0007829|PDB:1SPP"
SQ SEQUENCE 137 AA; 14816 MW; FD4C26A97DAF5D23 CRC64;
MKLGTAIPWA LLLSTATLVS TARINGPDEC GRVIKDTSGS ISNTDRQKNL CTWTILMKPD
QKVRMAIPYL NLACGKEYVE VFDGLLSGPS YGKLCAGAAI VFLSTANTMT IKYNRISGNS
SSPFLIYFYG SSPGSEY
