SVS3A_MOUSE
ID SVS3A_MOUSE Reviewed; 265 AA.
AC F2Z472; F2Z467; Q8VI13; Q9JKD2;
DT 31-JAN-2018, integrated into UniProtKB/Swiss-Prot.
DT 31-MAY-2011, sequence version 1.
DT 03-AUG-2022, entry version 65.
DE RecName: Full=Seminal vesicle secretory protein 3A {ECO:0000312|MGI:MGI:1927635};
DE AltName: Full=Seminal vesicle secretory protein III {ECO:0000303|PubMed:11723121};
DE Short=SVS III {ECO:0000303|PubMed:11723121};
DE Flags: Precursor;
GN Name=Svs3a {ECO:0000312|MGI:MGI:1927635};
GN Synonyms=Svs3 {ECO:0000312|MGI:MGI:1927635};
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090 {ECO:0000312|Proteomes:UP000000589};
RN [1] {ECO:0000312|EMBL:AAF61258.1}
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORM 1), FUNCTION, SUBCELLULAR
RP LOCATION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, INDUCTION,
RP GLYCOSYLATION, TRANSGLUTAMINATION, REPEATS, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RC TISSUE=Seminal vesicle {ECO:0000303|PubMed:11723121};
RX PubMed=11723121; DOI=10.1074/jbc.m107578200;
RA Lin H.J., Luo C.W., Chen Y.H.;
RT "Localization of the transglutaminase cross-linking site in SVS III, a
RT novel glycoprotein secreted from mouse seminal vesicle.";
RL J. Biol. Chem. 277:3632-3639(2002).
RN [2] {ECO:0000312|Proteomes:UP000000589}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [3] {ECO:0000312|EMBL:EDL06372.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [4] {ECO:0000312|EMBL:AAI31997.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
CC -!- FUNCTION: Component of the copulatory plug.
CC {ECO:0000269|PubMed:11723121}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:11723121}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=F2Z472-1; Sequence=Displayed;
CC Name=2;
CC IsoId=F2Z472-2; Sequence=VSP_059284;
CC -!- TISSUE SPECIFICITY: Highly expressed in the seminal vesicle where it is
CC detected in luminal epithelium of the mucosa folds, and also in luminal
CC fluid (at protein level). Not detected in other tissues tested.
CC {ECO:0000269|PubMed:11723121}.
CC -!- DEVELOPMENTAL STAGE: First detected at 3 weeks of age. Expression
CC increases through to 6 weeks of age and remains high thereafter.
CC {ECO:0000269|PubMed:11723121}.
CC -!- INDUCTION: Up-regulated in response to androgens.
CC {ECO:0000269|PubMed:11723121}.
CC -!- PTM: Glycosylated. {ECO:0000269|PubMed:11723121}.
CC -!- PTM: Covalently cross-linked by transglutaminase, which is important
CC for the formation of the gelatinous copulatory plug. Five repeats of Q-
CC X-K-(S/T) in the central region of the protein serve as the
CC transglutaminase substrate site(s). {ECO:0000269|PubMed:11723121}.
CC -!- MISCELLANEOUS: [Isoform 2]: May be due to competing acceptor splice
CC site. {ECO:0000305}.
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DR EMBL; AF242220; AAF61258.1; -; mRNA.
DR EMBL; AF323459; AAL37256.1; -; Genomic_DNA.
DR EMBL; AL590429; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH466551; EDL06372.1; -; Genomic_DNA.
DR EMBL; CH466551; EDL06375.1; -; Genomic_DNA.
DR EMBL; BC131996; AAI31997.1; -; mRNA.
DR EMBL; BC131998; AAI31999.1; -; mRNA.
DR CCDS; CCDS17030.1; -. [F2Z472-1]
DR CCDS; CCDS79860.1; -. [F2Z472-2]
DR RefSeq; NP_001298043.1; NM_001311114.1. [F2Z472-2]
DR RefSeq; NP_067338.2; NM_021363.2. [F2Z472-1]
DR AlphaFoldDB; F2Z472; -.
DR STRING; 10090.ENSMUSP00000017147; -.
DR PaxDb; F2Z472; -.
DR PRIDE; F2Z472; -.
DR ProteomicsDB; 254728; -. [F2Z472-1]
DR ProteomicsDB; 254729; -. [F2Z472-2]
DR Ensembl; ENSMUST00000017147; ENSMUSP00000017147; ENSMUSG00000017003. [F2Z472-1]
DR Ensembl; ENSMUST00000109370; ENSMUSP00000104995; ENSMUSG00000017003. [F2Z472-2]
DR GeneID; 64335; -.
DR KEGG; mmu:64335; -.
DR UCSC; uc008nuf.2; mouse. [F2Z472-1]
DR CTD; 64335; -.
DR MGI; MGI:1927635; Svs3a.
DR VEuPathDB; HostDB:ENSMUSG00000017003; -.
DR GeneTree; ENSGT00940000162560; -.
DR HOGENOM; CLU_1049563_0_0_1; -.
DR InParanoid; F2Z472; -.
DR OMA; QHAYSQD; -.
DR OrthoDB; 1237854at2759; -.
DR PhylomeDB; F2Z472; -.
DR TreeFam; TF338974; -.
DR BioGRID-ORCS; 64335; 1 hit in 40 CRISPR screens.
DR ChiTaRS; Svs3a; mouse.
DR PRO; PR:F2Z472; -.
DR Proteomes; UP000000589; Chromosome 2.
DR RNAct; F2Z472; protein.
DR Bgee; ENSMUSG00000017003; Expressed in seminal vesicle and 8 other tissues.
DR Genevisible; F2Z472; MM.
DR GO; GO:0005576; C:extracellular region; IDA:MGI.
DR GO; GO:0005615; C:extracellular space; ISO:MGI.
DR GO; GO:0032991; C:protein-containing complex; ISO:MGI.
DR GO; GO:0002020; F:protease binding; ISO:MGI.
DR GO; GO:0008270; F:zinc ion binding; ISO:MGI.
DR GO; GO:0042628; P:mating plug formation; IDA:MGI.
DR GO; GO:0048240; P:sperm capacitation; IBA:GO_Central.
PE 1: Evidence at protein level;
KW Alternative splicing; Copulatory plug; Glycoprotein; Reference proteome;
KW Repeat; Secreted; Signal.
FT SIGNAL 1..20
FT /evidence="ECO:0000255"
FT CHAIN 21..265
FT /note="Seminal vesicle secretory protein 3A"
FT /id="PRO_5003291021"
FT REPEAT 116..119
FT /note="1"
FT /evidence="ECO:0000305|PubMed:11723121"
FT REPEAT 122..125
FT /note="2"
FT /evidence="ECO:0000305|PubMed:11723121"
FT REPEAT 129..132
FT /note="3"
FT /evidence="ECO:0000305|PubMed:11723121"
FT REPEAT 136..139
FT /note="4"
FT /evidence="ECO:0000305|PubMed:11723121"
FT REPEAT 142..145
FT /note="5"
FT /evidence="ECO:0000305|PubMed:11723121"
FT REGION 116..145
FT /note="5 X 4 AA tandem repeats of Q-X-K-[ST]"
FT /evidence="ECO:0000305|PubMed:11723121"
FT VAR_SEQ 25
FT /note="Missing (in isoform 2)"
FT /id="VSP_059284"
FT CONFLICT 71
FT /note="E -> A (in Ref. 1; AAF61258, 4; AAI31997/AAI31999
FT and 3; AAL37256/EDL06372/EDL06375)"
FT /evidence="ECO:0000305"
FT CONFLICT 217
FT /note="R -> H (in Ref. 1; AAF61258 and 4; AAI31997/
FT AAI31999)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 265 AA; 29967 MW; A736C961C029FE84 CRC64;
MKSIFFSLSL LLLLEKKAAG IELYAGGTKG HFLVKTSPLM FIGKNQFLYG HKEEQEEAPE
ESIFVQTKHH EYGQDADADM GGALSSQELT SLKEDIVCEE EDELAQQKSQ LPSQSQIKSQ
TQVKSYAAQL KSQPGQLKTI GQVKSQTMLK SHGAPLKSFK ARLNLREDIP QQVKGRGYGL
AEDLAQVRQQ PAKVHRLKGK HRQSRKTAAF YPQFRRRSRP YPRYFVQFQE QLQGSVHHTK
SFYPGPGMCY CPRGGVILYQ DAFTD
