ID   CRIS2_MOUSE             Reviewed;         243 AA.
AC   P16563;
DT   01-AUG-1990, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1990, sequence version 1.
DT   04-NOV-2026, entry version 178.
DE   RecName: Full=Cysteine-rich secretory protein 2;
DE            Short=CRISP-2;
DE   AltName: Full=Testis-specific protein TPX-1;
DE   Flags: Precursor;
GN   Name=Crisp2; Synonyms=Tpx-1, Tpx1;
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=Testis;
RX   PubMed=2613236; DOI=10.1016/0888-7543(89)90019-0;
RA   Kasahara M., Gutknecht J., Brew K., Spurr N., Goodfellow P.N.;
RT   "Cloning and mapping of a testis-specific gene with sequence similarity to
RT   a sperm-coating glycoprotein gene.";
RL   Genomics 5:527-534(1989).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Testis;
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   [3]
RP   INTERACTION WITH NSUN4.
RX   PubMed=19686095; DOI=10.1042/bc20090099;
RA   Jamsai D., Rijal S., Bianco D.M., O'Connor A.E., Merriner D.J., Smith S.J.,
RA   Gibbs G.M., O'Bryan M.K.;
RT   "A novel protein, sperm head and tail associated protein (SHTAP), interacts
RT   with cysteine-rich secretory protein 2 (CRISP2) during spermatogenesis in
RT   the mouse.";
RL   Biol. Cell 102:93-106(2010).
RN   [4]
RP   STRUCTURE BY NMR OF 189-243, FUNCTION, AND DISULFIDE BONDS.
RX   PubMed=16339766; DOI=10.1074/jbc.m506849200;
RA   Gibbs G.M., Scanlon M.J., Swarbrick J., Curtis S., Gallant E.,
RA   Dulhunty A.F., O'Bryan M.K.;
RT   "The cysteine-rich secretory protein domain of Tpx-1 is related to ion
RT   channel toxins and regulates ryanodine receptor Ca2+ signaling.";
RL   J. Biol. Chem. 281:4156-4163(2006).
CC   -!- FUNCTION: May regulate some ion channels' activity and thereby regulate
CC       calcium fluxes during sperm capacitation.
CC       {ECO:0000269|PubMed:16339766}.
CC   -!- SUBUNIT: Interacts with NSUN4 isoform 3. {ECO:0000269|PubMed:19686095}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305}.
CC   -!- TISSUE SPECIFICITY: Testis.
CC   -!- SIMILARITY: Belongs to the CRISP family. {ECO:0000305}.
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DR   EMBL; M25533; AAA40472.1; -; mRNA.
DR   EMBL; BC049615; AAH49615.1; -; mRNA.
DR   CCDS; CCDS28786.1; -.
DR   PIR; A33329; A33329.
DR   RefSeq; NP_001191000.1; NM_001204071.2.
DR   RefSeq; NP_033446.1; NM_009420.3.
DR   PDB; 2A05; NMR; -; A=189-243.
DR   AlphaFoldDB; P16563; -.
DR   SMR; P16563; -.
DR   FunCoup; P16563; 122.
DR   STRING; 10090.ENSMUSP00000156411; -.
DR   iPTMnet; P16563; -.
DR   PhosphoSitePlus; P16563; -.
DR   SwissPalm; P16563; -.
DR   PaxDb; 10090-ENSMUSP00000156411; -.
DR   ProteomicsDB; 284172; -.
DR   Antibodypedia; 30834; 247 antibodies from 37 providers.
DR   DNASU; 22024; -.
DR   Ensembl; ENSMUST00000024724.14; ENSMUSP00000024724.8; ENSMUSG00000023930.15.
DR   Ensembl; ENSMUST00000232709.2; ENSMUSP00000156411.2; ENSMUSG00000023930.15.
DR   Ensembl; ENSMUST00000233529.2; ENSMUSP00000156818.2; ENSMUSG00000023930.15.
DR   GeneID; 22024; -.
DR   KEGG; mmu:22024; -.
DR   UCSC; uc008coj.2; mouse.
DR   AGR; MGI:98815; -.
DR   CTD; 7180; -.
DR   MGI; MGI:98815; Crisp2.
DR   VEuPathDB; HostDB:ENSMUSG00000023930; -.
DR   eggNOG; KOG3017; Eukaryota.
DR   GeneTree; ENSGT00940000156439; -.
DR   HOGENOM; CLU_035730_2_1_1; -.
DR   InParanoid; P16563; -.
DR   OMA; AAIQNWY; -.
DR   OrthoDB; 737510at2759; -.
DR   PhylomeDB; P16563; -.
DR   Reactome; R-MMU-6798695; Neutrophil degranulation.
DR   BioGRID-ORCS; 22024; 1 hit in 76 CRISPR screens.
DR   EvolutionaryTrace; P16563; -.
DR   PRO; PR:P16563; -.
DR   Proteomes; UP000000589; Chromosome 17.
DR   RNAct; P16563; protein.
DR   Bgee; ENSMUSG00000023930; Expressed in seminiferous tubule of testis and 32 other cell types or tissues.
DR   ExpressionAtlas; P16563; baseline and differential.
DR   GO; GO:0005576; C:extracellular region; IBA:GO_Central.
DR   GO; GO:0060090; F:molecular adaptor activity; IBA:GO_Central.
DR   GO; GO:0098609; P:cell-cell adhesion; ISO:GO_Central.
DR   CDD; cd05383; CAP_CRISP; 1.
DR   FunFam; 1.10.10.740:FF:000001; Cysteine-rich secretory protein 2; 1.
DR   FunFam; 3.40.33.10:FF:000005; Cysteine-rich secretory protein 2; 1.
DR   Gene3D; 3.40.33.10; CAP; 1.
DR   Gene3D; 1.10.10.740; Crisp domain; 1.
DR   InterPro; IPR018244; Allrgn_V5/Tpx1_CS.
DR   InterPro; IPR014044; CAP_dom.
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; CYSTEINE-RICH SECRETORY PROTEIN-RELATED; 1.
DR   Pfam; PF00188; CAP; 1.
DR   Pfam; PF08562; Crisp; 1.
DR   PRINTS; PR00837; V5TPXLIKE.
DR   SMART; SM00198; SCP; 1.
DR   SUPFAM; SSF57546; Crisp domain-like; 1.
DR   SUPFAM; SSF55797; PR-1-like; 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   3D-structure; Disulfide bond; Reference proteome; Secreted; Signal.
FT   SIGNAL          1..22
FT                   /evidence="ECO:0000255"
FT   CHAIN           23..243
FT                   /note="Cysteine-rich secretory protein 2"
FT                   /id="PRO_0000006266"
FT   DOMAIN          42..169
FT                   /note="SCP"
FT   DOMAIN          205..238
FT                   /note="ShKT"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01005"
FT   DISULFID        189..196
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01005,
FT                   ECO:0000269|PubMed:16339766"
FT   DISULFID        192..201
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01005,
FT                   ECO:0000269|PubMed:16339766"
FT   DISULFID        205..238
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01005,
FT                   ECO:0000269|PubMed:16339766"
FT   DISULFID        214..232
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01005,
FT                   ECO:0000269|PubMed:16339766"
FT   DISULFID        223..236
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01005,
FT                   ECO:0000269|PubMed:16339766"
FT   STRAND          197..200
FT                   /evidence="ECO:0007829|PDB:2A05"
FT   HELIX           214..220
FT                   /evidence="ECO:0007829|PDB:2A05"
FT   HELIX           228..231
FT                   /evidence="ECO:0007829|PDB:2A05"
FT   HELIX           233..236
FT                   /evidence="ECO:0007829|PDB:2A05"
SQ   SEQUENCE   243 AA;  27605 MW;  6E707F569ACAA244 CRC64;
     MAWFQVMLFV FALLLRSPLT EGKDPDFTSL LTNQLQVQRE IVNKHNELRR SVNPTGSDIL
     KMEWSIQATT NAQKWANKCI LEHSSKDDRK INIRCGENLY MSTDPTLWST VIQSWYNENE
     DFVYGVGAKP NSAVGHYTQL VWYSSFKIGC GIAYCPNQDN LKYFYVCHYC PMGNNVMKKS
     TPYQQGTPCA SCPNNCENGL CTNSCDFEDL LSNCESLKTS AGCKHELLKT KCQATCLCED
     KIH
//