CRIS3_MOUSE
ID CRIS3_MOUSE Reviewed; 241 AA.
AC Q03402; A2RTK2;
DT 01-OCT-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1993, sequence version 1.
DT 03-AUG-2022, entry version 161.
DE RecName: Full=Cysteine-rich secretory protein 3;
DE Short=CRISP-3;
DE AltName: Full=Acidic epididymal glycoprotein 2;
DE AltName: Full=Sperm-coating glycoprotein 2;
DE Short=SCP 2;
DE Flags: Precursor;
GN Name=Crisp3; Synonyms=Aeg-2, Aeg2;
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;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Submandibular gland;
RX PubMed=1301383; DOI=10.1016/0303-7207(92)90207-m;
RA Mizuki N., Kasahara M.;
RT "Mouse submandibular glands express an androgen-regulated transcript
RT encoding an acidic epididymal glycoprotein-like molecule.";
RL Mol. Cell. Endocrinol. 89:25-32(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Submandibular gland;
RX PubMed=8319566; DOI=10.1210/endo.133.1.8319566;
RA Haendler B., Kraetzschmar J., Theuring F., Schleuning W.-D.;
RT "Transcripts for cysteine-rich secretory protein-1 (CRISP-1; DE/AEG) and
RT the novel related CRISP-3 are expressed under androgen control in the mouse
RT salivary gland.";
RL Endocrinology 133:192-198(1993).
RN [3]
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]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=FVB/N; TISSUE=Salivary gland;
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).
RN [5]
RP INTERACTION WITH KNG1.
RX PubMed=15461460; DOI=10.1021/bi048823e;
RA Udby L., Sorensen O.E., Pass J., Johnsen A.H., Behrendt N., Borregaard N.,
RA Kjeldsen L.;
RT "Cysteine-rich secretory protein 3 is a ligand of alpha1B-glycoprotein in
RT human plasma.";
RL Biochemistry 43:12877-12886(2004).
CC -!- FUNCTION: This protein is supposed to help spermatozoa undergo
CC functional maturation while they move from the testis to the ductus
CC deferens.
CC -!- SUBUNIT: Interacts with A1BG (By similarity). Interacts with KNG1
CC isoform LMW. {ECO:0000250, ECO:0000269|PubMed:15461460}.
CC -!- SUBCELLULAR LOCATION: Cytoplasmic vesicle, secretory vesicle.
CC Note=Stored in secretory granules of granular convoluted tubules cells.
CC -!- TISSUE SPECIFICITY: Expressed in submandibular gland.
CC -!- DEVELOPMENTAL STAGE: Exponential increase between days 25 and 30 after
CC birth.
CC -!- INDUCTION: By androgens.
CC -!- SIMILARITY: Belongs to the CRISP family. {ECO:0000305}.
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DR EMBL; M92850; AAA37186.1; -; mRNA.
DR EMBL; L05560; AAA37461.1; -; mRNA.
DR EMBL; CH466559; EDL23382.1; -; Genomic_DNA.
DR EMBL; BC022573; AAH22573.1; -; mRNA.
DR EMBL; BC132536; AAI32537.1; -; mRNA.
DR EMBL; BC132538; AAI32539.1; -; mRNA.
DR CCDS; CCDS28783.1; -.
DR PIR; B49202; B49202.
DR RefSeq; NP_033769.1; NM_009639.2.
DR AlphaFoldDB; Q03402; -.
DR SMR; Q03402; -.
DR STRING; 10090.ENSMUSP00000026499; -.
DR GlyGen; Q03402; 3 sites.
DR PhosphoSitePlus; Q03402; -.
DR MaxQB; Q03402; -.
DR PaxDb; Q03402; -.
DR PeptideAtlas; Q03402; -.
DR PRIDE; Q03402; -.
DR ProteomicsDB; 285333; -.
DR DNASU; 11572; -.
DR Ensembl; ENSMUST00000026499; ENSMUSP00000026499; ENSMUSG00000025433.
DR GeneID; 11572; -.
DR KEGG; mmu:11572; -.
DR UCSC; uc008cog.1; mouse.
DR CTD; 10321; -.
DR MGI; MGI:102552; Crisp3.
DR VEuPathDB; HostDB:ENSMUSG00000025433; -.
DR eggNOG; KOG3017; Eukaryota.
DR GeneTree; ENSGT00940000162013; -.
DR HOGENOM; CLU_035730_2_1_1; -.
DR InParanoid; Q03402; -.
DR OMA; CPITDHS; -.
DR OrthoDB; 1528782at2759; -.
DR PhylomeDB; Q03402; -.
DR TreeFam; TF316148; -.
DR BioGRID-ORCS; 11572; 1 hit in 72 CRISPR screens.
DR ChiTaRS; Crisp3; mouse.
DR PRO; PR:Q03402; -.
DR Proteomes; UP000000589; Chromosome 17.
DR RNAct; Q03402; protein.
DR Bgee; ENSMUSG00000025433; Expressed in submandibular gland and 29 other tissues.
DR Genevisible; Q03402; MM.
DR GO; GO:0005576; C:extracellular region; ISO:MGI.
DR GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR GO; GO:0042581; C:specific granule; ISO:MGI.
DR GO; GO:0030133; C:transport vesicle; IEA:UniProtKB-SubCell.
DR Gene3D; 1.10.10.740; -; 1.
DR Gene3D; 3.40.33.10; -; 1.
DR InterPro; IPR018244; Allrgn_V5/Tpx1_CS.
DR InterPro; IPR014044; CAP_domain.
DR InterPro; IPR035940; CAP_sf.
DR InterPro; IPR042076; Crisp-like_dom.
DR InterPro; IPR001283; CRISP-related.
DR InterPro; IPR013871; Cysteine_rich_secretory.
DR InterPro; IPR003582; ShKT_dom.
DR PANTHER; PTHR10334; PTHR10334; 1.
DR Pfam; PF00188; CAP; 1.
DR Pfam; PF08562; Crisp; 1.
DR PRINTS; PR00837; V5TPXLIKE.
DR SMART; SM00198; SCP; 1.
DR SUPFAM; SSF55797; SSF55797; 1.
DR PROSITE; PS01009; CRISP_1; 1.
DR PROSITE; PS01010; CRISP_2; 1.
DR PROSITE; PS51670; SHKT; 1.
PE 1: Evidence at protein level;
KW Cytoplasmic vesicle; Disulfide bond; Glycoprotein; Reference proteome;
KW Signal.
FT SIGNAL 1..19
FT CHAIN 20..241
FT /note="Cysteine-rich secretory protein 3"
FT /id="PRO_0000006269"
FT DOMAIN 44..170
FT /note="SCP"
FT DOMAIN 210..241
FT /note="ShKT"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01005"
FT CARBOHYD 118
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 132
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 175
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 194..201
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01005"
FT DISULFID 197..206
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01005"
FT DISULFID 210..241
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01005"
FT DISULFID 219..235
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01005"
FT DISULFID 226..239
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01005"
SQ SEQUENCE 241 AA; 27314 MW; D903788B4E4001EF CRC64;
MALMLVLFFL AAVLPPSLLQ DNSQENSLEK LSTSKKSVQE EIVSKHNQLR RKVSPSGSDL
LNMEWNYDAQ VNAQQRADKC TFSHSPIELR TTNLKCGENL FMSSYLVPWS SVIQGWYNES
KGLIFGVGPK QNVSVVGHHT QVVWKSNLQV ACGVAECPEN PLRYFYVCRY CPVLNYSGHY
PSRPYLAYTA RAPCASCPDR CEDGLCTKSC QYKDMSFWCK RLEYVCKHPG LKKRCLATCQ
C
