ID   SVS2_RAT                Reviewed;         414 AA.
AC   P22006;
DT   01-AUG-1991, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1991, sequence version 1.
DT   25-MAY-2022, entry version 106.
DE   RecName: Full=Seminal vesicle secretory protein 2;
DE   AltName: Full=Seminal vesicle secretory protein II;
DE            Short=SVS II;
DE   Flags: Precursor;
GN   Name=Svs2;
OS   Rattus norvegicus (Rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Rattus.
OX   NCBI_TaxID=10116;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], PARTIAL PROTEIN SEQUENCE, AND
RP   PYROGLUTAMATE FORMATION AT GLN-23.
RX   PubMed=2351680; DOI=10.1016/s0021-9258(19)38756-3;
RA   Harris S.E., Harris M.A., Johnson C.M., Bean M.F., Dodd J.G., Matusik R.J.,
RA   Carr S.A., Crabb J.W.;
RT   "Structural characterization of the rat seminal vesicle secretion II
RT   protein and gene.";
RL   J. Biol. Chem. 265:9896-9903(1990).
CC   -!- FUNCTION: The rat seminal vesicle contains six major androgen-dependent
CC       secretory proteins referred to as SVS I-VI. The SVS I-III proteins
CC       appear to be components of the rat copulatory plug, with the SVS II
CC       protein being the major component.
CC   -!- PTM: The repeating unit appears to be involved in the formation of the
CC       copulatory plug via a transglutaminase reaction cross-linking glutamine
CC       and lysine residues.
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DR   EMBL; J05443; AAA42192.1; -; Genomic_DNA.
DR   PIR; A36443; A36443.
DR   AlphaFoldDB; P22006; -.
DR   STRING; 10116.ENSRNOP00000018420; -.
DR   PaxDb; P22006; -.
DR   PRIDE; P22006; -.
DR   RGD; 3790; Svs2.
DR   eggNOG; ENOG502T6BW; Eukaryota.
DR   InParanoid; P22006; -.
DR   PhylomeDB; P22006; -.
DR   Reactome; R-RNO-6803157; Antimicrobial peptides.
DR   PRO; PR:P22006; -.
DR   Proteomes; UP000002494; Unplaced.
DR   GO; GO:0001669; C:acrosomal vesicle; ISO:RGD.
DR   GO; GO:0005615; C:extracellular space; ISO:RGD.
DR   GO; GO:0032991; C:protein-containing complex; ISO:RGD.
DR   GO; GO:0008270; F:zinc ion binding; ISO:RGD.
DR   GO; GO:0019731; P:antibacterial humoral response; ISO:RGD.
DR   GO; GO:0061844; P:antimicrobial humoral immune response mediated by antimicrobial peptide; ISO:RGD.
DR   GO; GO:0050817; P:coagulation; ISO:RGD.
DR   GO; GO:0009566; P:fertilization; ISO:RGD.
DR   GO; GO:0031640; P:killing of cells of another organism; ISO:RGD.
DR   GO; GO:0042628; P:mating plug formation; IEA:UniProtKB-KW.
DR   GO; GO:0090281; P:negative regulation of calcium ion import; ISO:RGD.
DR   GO; GO:1901318; P:negative regulation of flagellated sperm motility; ISO:RGD.
DR   GO; GO:1900005; P:positive regulation of serine-type endopeptidase activity; ISO:RGD.
DR   GO; GO:0048240; P:sperm capacitation; ISO:RGD.
DR   InterPro; IPR018942; Seminal_vesicle_protein_repeat.
DR   InterPro; IPR002080; SVP_II_CS.
DR   Pfam; PF10578; SVS_QK; 17.
DR   PROSITE; PS00515; SVP_II; 12.
PE   1: Evidence at protein level;
KW   Copulatory plug; Direct protein sequencing; Pyrrolidone carboxylic acid;
KW   Reference proteome; Repeat; Signal.
FT   SIGNAL          1..22
FT   CHAIN           23..414
FT                   /note="Seminal vesicle secretory protein 2"
FT                   /id="PRO_0000022451"
FT   REPEAT          108..120
FT                   /note="1"
FT   REPEAT          127..139
FT                   /note="2"
FT   REPEAT          140..152
FT                   /note="3"
FT   REPEAT          153..165
FT                   /note="4"
FT   REPEAT          166..178
FT                   /note="5"
FT   REPEAT          179..191
FT                   /note="6"
FT   REPEAT          192..204
FT                   /note="7"
FT   REPEAT          205..217
FT                   /note="8"
FT   REPEAT          224..236
FT                   /note="9"
FT   REPEAT          237..249
FT                   /note="10"
FT   REPEAT          257..269
FT                   /note="11"
FT   REPEAT          275..287
FT                   /note="12"
FT   REPEAT          299..311
FT                   /note="13"
FT   REGION          108..311
FT                   /note="13 X 13 AA tandem repeats"
FT   REGION          170..228
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          240..294
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          306..369
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        306..325
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        327..341
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        342..369
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         23
FT                   /note="Pyrrolidone carboxylic acid"
FT                   /evidence="ECO:0000269|PubMed:2351680"
SQ   SEQUENCE   414 AA;  45539 MW;  C89E3FCE0C0EE92E CRC64;
     MKSSVFILSL FLLLERQAAV VGQYGGTKGH FQSSSSGFML GQKGHLNFGL KGGSEEAAEE
     SIFMQSQHQM FGQDGGDMAQ TSVSQEHTGV KGAAICRKGQ VSQLKSQESQ IKSFRQVKSS
     GQLKSGGSQL KSFGQVKSSE SQLKSFGQVK ASGSQLKSFG QVKASGSQLK SYGQMKSSGS
     QVKSFGQMKS SGSQVKSFGQ MKASESQIKS FGQRKSQGGQ LQSYGQMKSY GQTKSLESQA
     KSFGQVKSQS GQMKSSYGQR KSYGEETQLK SFDQDAQLKS YGQQKSQKQS SFSQVKSQSA
     QLKSFGQQKS LKGFSQQTQQ KGFAMDEDLS QVRKQFDDDD LSVQQKSTQQ MKTEEDLSQF
     GQQRQFGQER SQSYKGYLAQ YRKKLQEQQQ QKNFNQDNFF TKGGAGLYQA QLKG