CRIS1_MOUSE
ID CRIS1_MOUSE Reviewed; 244 AA.
AC Q03401;
DT 01-OCT-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1993, sequence version 1.
DT 03-AUG-2022, entry version 155.
DE RecName: Full=Cysteine-rich secretory protein 1;
DE Short=CRISP-1;
DE AltName: Full=Acidic epididymal glycoprotein 1;
DE AltName: Full=Sperm-coating glycoprotein 1;
DE Short=SCP 1;
DE Flags: Precursor;
GN Name=Crisp1; Synonyms=Aeg-1, Aeg1;
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).
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 -!- SUBCELLULAR LOCATION: Cytoplasmic vesicle, secretory vesicle.
CC Note=Stored in secretory granules of granular convoluted tubules cells.
CC -!- TISSUE SPECIFICITY: Mainly found in the cauda epididymis where it is
CC synthesized by the principal cells and secreted into the lumen. Binds
CC to the heads of spermatozoa. Also expressed in the 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; M92849; AAA37185.1; -; mRNA.
DR EMBL; L05559; AAA37460.1; -; mRNA.
DR CCDS; CCDS28784.1; -.
DR PIR; A49202; A49202.
DR RefSeq; NP_033768.3; NM_009638.3.
DR AlphaFoldDB; Q03401; -.
DR SMR; Q03401; -.
DR STRING; 10090.ENSMUSP00000026498; -.
DR GlyGen; Q03401; 1 site.
DR iPTMnet; Q03401; -.
DR PhosphoSitePlus; Q03401; -.
DR PaxDb; Q03401; -.
DR PeptideAtlas; Q03401; -.
DR PRIDE; Q03401; -.
DR ProteomicsDB; 284171; -.
DR DNASU; 11571; -.
DR Ensembl; ENSMUST00000026498; ENSMUSP00000026498; ENSMUSG00000025431.
DR GeneID; 11571; -.
DR KEGG; mmu:11571; -.
DR UCSC; uc008coh.2; mouse.
DR CTD; 167; -.
DR MGI; MGI:102553; Crisp1.
DR VEuPathDB; HostDB:ENSMUSG00000025431; -.
DR eggNOG; KOG3017; Eukaryota.
DR GeneTree; ENSGT00940000162013; -.
DR HOGENOM; CLU_035730_2_1_1; -.
DR InParanoid; Q03401; -.
DR OMA; IWNSSYK; -.
DR OrthoDB; 1528782at2759; -.
DR PhylomeDB; Q03401; -.
DR TreeFam; TF316148; -.
DR BioGRID-ORCS; 11571; 0 hits in 72 CRISPR screens.
DR ChiTaRS; Crisp1; mouse.
DR PRO; PR:Q03401; -.
DR Proteomes; UP000000589; Chromosome 17.
DR RNAct; Q03401; protein.
DR Bgee; ENSMUSG00000025431; Expressed in parotid gland and 44 other tissues.
DR ExpressionAtlas; Q03401; baseline and differential.
DR Genevisible; Q03401; MM.
DR GO; GO:0005576; C:extracellular region; ISS: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 CDD; cd05383; CAP_CRISP; 1.
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; IPR034117; SCP_CRISP.
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 2: Evidence at transcript level;
KW Cytoplasmic vesicle; Disulfide bond; Glycoprotein; Reference proteome;
KW Signal.
FT SIGNAL 1..19
FT CHAIN 20..244
FT /note="Cysteine-rich secretory protein 1"
FT /id="PRO_0000006262"
FT DOMAIN 44..170
FT /note="SCP"
FT DOMAIN 206..239
FT /note="ShKT"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01005"
FT CARBOHYD 145
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 190..197
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01005"
FT DISULFID 193..202
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01005"
FT DISULFID 206..239
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01005"
FT DISULFID 215..233
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01005"
FT DISULFID 224..237
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01005"
SQ SEQUENCE 244 AA; 27680 MW; D00DD0348F85781F CRC64;
MALMLVLFFL AAVLPPSLLQ DSSQENRLEK LSTTKMSVQE EIVSKHNQLR RMVSPSGSDL
LKMEWNYDAQ VNAQQWADKC TFSHSPIELR TTNLRCGENL FMSSYLASWS SAIQGWYNEY
KDLTYDVGPK QPDSVVGHYT QVVWNSTFQV ACGVAECPKN PLRYYYVCHY CPVGNYQGRL
YTPYTAGEPC ASCPDHCEDG LCTNSCGHED KYTNCKYLKK MLSCEHELLK KGCKATCLCE
GKIH
