SVP1_CAVPO
ID SVP1_CAVPO Reviewed; 396 AA.
AC P05995;
DT 01-NOV-1988, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 3.
DT 03-AUG-2022, entry version 93.
DE RecName: Full=Seminal vesicle major clotting proteins;
DE Contains:
DE RecName: Full=Seminal vesicle protein 1;
DE Short=SVP-1;
DE Contains:
DE RecName: Full=Seminal vesicle protein 3/4;
DE Short=SVP-3/4;
DE Flags: Precursor;
OS Cavia porcellus (Guinea pig).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Hystricomorpha; Caviidae;
OC Cavia.
OX NCBI_TaxID=10141;
RN [1]
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Testis;
RX PubMed=8702880; DOI=10.1074/jbc.271.35.21114;
RA Hagstrom J.E., Fautsch M.P., Perdok M., Vrabel A., Wieben E.D.;
RT "Exons lost and found. Unusual evolution of a seminal vesicle
RT transglutaminase substrate.";
RL J. Biol. Chem. 271:21114-21119(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Testis;
RX PubMed=9305940; DOI=10.1074/jbc.272.39.24691;
RA Fautsch M.P., Perdok M.M., Wieben E.D.;
RT "Production of SVP-1/-3/-4 in guinea pig testis. Characterization of novel
RT transcripts containing long 5'-untranslated regions and multiple upstream
RT AUG codons.";
RL J. Biol. Chem. 272:24691-24695(1997).
RN [3]
RP NUCLEOTIDE SEQUENCE OF 7-396.
RX PubMed=2691882; DOI=10.1210/mend-3-11-1797;
RA Hagstrom J.E., Harvey S., Madden B., McCormick D., Wieben E.D.;
RT "Androgens affect the processing of secretory protein precursors in the
RT guinea pig seminal vesicle. II. Identification of conserved sites for
RT protein processing.";
RL Mol. Endocrinol. 3:1797-1806(1989).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 194-396, AND PARTIAL PROTEIN SEQUENCE.
RX PubMed=3477802; DOI=10.1073/pnas.84.19.6712;
RA Moore J.T., Hagstrom J., McCormick D.J., Harvey S., Madden B., Holicky E.,
RA Stanford D.R., Wieben E.D.;
RT "The major clotting protein from guinea pig seminal vesicle contains eight
RT repeats of a 24-amino acid domain.";
RL Proc. Natl. Acad. Sci. U.S.A. 84:6712-6714(1987).
CC -!- FUNCTION: SVP-1 serves as substrate in the formation of the copulatory
CC plug. SVP-3 and SVP-4 may also contribute to the clot.
CC -!- SUBCELLULAR LOCATION: Secreted.
CC -!- PTM: SVP-3 may be a post-translationally modified form of SVP-4.
CC -!- PTM: Covalent clotting of SVP-1 is catalyzed by a transglutaminase
CC secreted by the anterior prostate through the formation of gamma-
CC glutamyl-epsilon-lysine cross-links. The conserved 2 Lys and 1 Gln
CC residues per functional unit seem to be the residues involved in the
CC formation of those cross-links.
CC -!- MISCELLANEOUS: SVP-1, SVP-3, and SVP-4 are 3 of the 4 major secretory
CC proteins, secreted by the guinea pig seminal vesicle epithelium (sve).
CC -!- MISCELLANEOUS: SVP-1 contains 8 and a half repeats of 24 amino acid
CC clotting domain. SVP-3/4 also contains 4 repeats of a 24 amino acid
CC domain, but which is unrelated to that of SVP-1.
CC -!- SIMILARITY: To the SVP-2 precursor, particularly in regions where
CC protein processing must occur. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAB82089.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=AAB82090.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; U59711; AAB06044.1; -; Genomic_DNA.
DR EMBL; AF001982; AAC53395.1; -; mRNA.
DR EMBL; AF002657; AAB82089.1; ALT_INIT; mRNA.
DR EMBL; AF002658; AAB82090.1; ALT_INIT; mRNA.
DR EMBL; M33295; AAA37054.1; -; mRNA.
DR EMBL; J02968; AAA37048.1; -; mRNA.
DR PIR; B41405; A33889.
DR RefSeq; NP_001166201.1; NM_001172730.1.
DR AlphaFoldDB; P05995; -.
DR STRING; 10141.ENSCPOP00000006002; -.
DR GeneID; 100379263; -.
DR KEGG; cpoc:100379263; -.
DR CTD; 41491; -.
DR eggNOG; ENOG502SZ79; Eukaryota.
DR OrthoDB; 926342at2759; -.
DR Proteomes; UP000005447; Unassembled WGS sequence.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0042628; P:mating plug formation; IEA:UniProtKB-KW.
DR InterPro; IPR002098; SVP_I.
DR PROSITE; PS00313; SVP_I; 8.
PE 1: Evidence at protein level;
KW Cleavage on pair of basic residues; Copulatory plug;
KW Direct protein sequencing; Reference proteome; Repeat; Secreted; Signal.
FT SIGNAL 1..21
FT CHAIN 22..176
FT /note="Seminal vesicle protein 3/4"
FT /id="PRO_0000022442"
FT PROPEP 177..192
FT /evidence="ECO:0000255"
FT /id="PRO_0000022443"
FT CHAIN 193..396
FT /note="Seminal vesicle protein 1"
FT /id="PRO_0000022444"
FT REPEAT 65..88
FT /note="SVP-3/-4 repeat"
FT REPEAT 89..112
FT /note="SVP-3/-4 repeat"
FT REPEAT 113..136
FT /note="SVP-3/-4 repeat"
FT REPEAT 137..157
FT /note="SVP-3/-4 repeat; truncated"
FT REPEAT 194..217
FT /note="SVP-1 clotting 1"
FT REPEAT 218..241
FT /note="SVP-1 clotting 2"
FT REPEAT 242..265
FT /note="SVP-1 clotting 3"
FT REPEAT 266..289
FT /note="SVP-1 clotting 4"
FT REPEAT 290..313
FT /note="SVP-1 clotting 5"
FT REPEAT 314..337
FT /note="SVP-1 clotting 6"
FT REPEAT 338..361
FT /note="SVP-1 clotting 7"
FT REPEAT 362..385
FT /note="SVP-1 clotting 8"
FT REPEAT 386..396
FT /note="SVP-1 clotting 9; truncated"
FT REGION 45..178
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 194..396
FT /note="9 X tandem repeats of SVP-1 like motif"
FT REGION 377..396
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 59..175
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 396 AA; 43941 MW; 8E7C3CB5EB04AA01 CRC64;
MKSTIFFILS LLLMLENQAA GRRLSGSAGA QDPVISRVWA KSQDMEEAVS GSGLTAEGGR
GSDREESVGE RVSLRQEEFE KGHIRSSVEE PEGEHVSVRR EHLEKSHIRH NVEEPEGERV
SVRREHLEKS HIRHSAEEPE GERVSVRHER VEKTHKRFHD DSVEESDSAS SVDHRKKGHI
RFKRQDPIAA LAAIEGQDAV KDSLWVKGQA SSEERFSVKG QDLVKGHLQM KGQSSLAERF
SVTGQDSVKG RLQMKGQDTL AERFSMTGQD SVKSRLQMKG QDSLSERFSM TGQDSVKGRL
QMKGQSSLAE RFSVTGQDSV KGRLQMKGKD TLAERFSVTG QDSVKGRLQM KGHDLLEERF
SVSGQDSVKG LARIKGQESV QSGFSVKGQG SLKGLI
