CRIS2_MOUSE
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 03-AUG-2022, entry version 159.
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 therebye
CC regulate 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_001204071.1.
DR RefSeq; NP_033446.1; NM_009420.2.
DR PDB; 2A05; NMR; -; A=189-243.
DR PDBsum; 2A05; -.
DR AlphaFoldDB; P16563; -.
DR SMR; P16563; -.
DR STRING; 10090.ENSMUSP00000024724; -.
DR iPTMnet; P16563; -.
DR PhosphoSitePlus; P16563; -.
DR PaxDb; P16563; -.
DR PRIDE; P16563; -.
DR ProteomicsDB; 284172; -.
DR Antibodypedia; 30834; 237 antibodies from 37 providers.
DR DNASU; 22024; -.
DR Ensembl; ENSMUST00000024724; ENSMUSP00000024724; ENSMUSG00000023930.
DR Ensembl; ENSMUST00000232709; ENSMUSP00000156411; ENSMUSG00000023930.
DR Ensembl; ENSMUST00000233529; ENSMUSP00000156818; ENSMUSG00000023930.
DR GeneID; 22024; -.
DR KEGG; mmu:22024; -.
DR UCSC; uc008coj.2; mouse.
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; KCKATCR; -.
DR OrthoDB; 1528782at2759; -.
DR PhylomeDB; P16563; -.
DR TreeFam; TF316148; -.
DR BioGRID-ORCS; 22024; 1 hit in 71 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 tissues.
DR ExpressionAtlas; P16563; baseline and differential.
DR Genevisible; P16563; MM.
DR GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR GO; GO:0098609; P:cell-cell adhesion; ISO:MGI.
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 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
