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P16563 (CRIS2_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified May 29, 2013. Version 109. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Cysteine-rich secretory protein 2

Short name=CRISP-2
Alternative name(s):
Testis-specific protein TPX-1
Gene names
Name:Crisp2
Synonyms:Tpx-1, Tpx1
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length243 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

May regulate some ion channels' activity and therebye regulate calcium fluxes during sperm capacitation. Ref.4

Subunit structure

Interacts with NSUN4 isoform 3. Ref.3

Subcellular location

Secreted Probable.

Tissue specificity

Testis.

Sequence similarities

Belongs to the CRISP family.

Contains 1 SCP domain.

Contains 1 ShKT domain.

Ontologies

Keywords
   Cellular componentSecreted
   DomainSignal
   PTMDisulfide bond
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Cellular_componentextracellular region

Inferred from electronic annotation. Source: UniProtKB-SubCell

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2222 Potential
Chain23 – 243221Cysteine-rich secretory protein 2
PRO_0000006266

Regions

Domain42 – 169128SCP
Domain205 – 23834ShKT

Amino acid modifications

Disulfide bond189 ↔ 196 Ref.4
Disulfide bond192 ↔ 201 Ref.4
Disulfide bond205 ↔ 238 Ref.4
Disulfide bond214 ↔ 232 Ref.4
Disulfide bond223 ↔ 236 Ref.4

Secondary structure

......... 243
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P16563 [UniParc].

Last modified August 1, 1990. Version 1.
Checksum: 6E707F569ACAA244

FASTA24327,605
        10         20         30         40         50         60 
MAWFQVMLFV FALLLRSPLT EGKDPDFTSL LTNQLQVQRE IVNKHNELRR SVNPTGSDIL 

        70         80         90        100        110        120 
KMEWSIQATT NAQKWANKCI LEHSSKDDRK INIRCGENLY MSTDPTLWST VIQSWYNENE 

       130        140        150        160        170        180 
DFVYGVGAKP NSAVGHYTQL VWYSSFKIGC GIAYCPNQDN LKYFYVCHYC PMGNNVMKKS 

       190        200        210        220        230        240 
TPYQQGTPCA SCPNNCENGL CTNSCDFEDL LSNCESLKTS AGCKHELLKT KCQATCLCED 


KIH 

« Hide

References

« Hide 'large scale' references
[1]"Cloning and mapping of a testis-specific gene with sequence similarity to a sperm-coating glycoprotein gene."
Kasahara M., Gutknecht J., Brew K., Spurr N., Goodfellow P.N.
Genomics 5:527-534(1989) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Testis.
[2]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Testis.
[3]"A novel protein, sperm head and tail associated protein (SHTAP), interacts with cysteine-rich secretory protein 2 (CRISP2) during spermatogenesis in the mouse."
Jamsai D., Rijal S., Bianco D.M., O'Connor A.E., Merriner D.J., Smith S.J., Gibbs G.M., O'Bryan M.K.
Biol. Cell 102:93-106(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH NSUN4.
[4]"The cysteine-rich secretory protein domain of Tpx-1 is related to ion channel toxins and regulates ryanodine receptor Ca2+ signaling."
Gibbs G.M., Scanlon M.J., Swarbrick J., Curtis S., Gallant E., Dulhunty A.F., O'Bryan M.K.
J. Biol. Chem. 281:4156-4163(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: STRUCTURE BY NMR OF 189-243, FUNCTION, DISULFIDE BONDS.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M25533 mRNA. Translation: AAA40472.1.
BC049615 mRNA. Translation: AAH49615.1.
IPIIPI00135918.
PIRA33329.
RefSeqNP_001191000.1. NM_001204071.1.
NP_033446.1. NM_009420.2.
UniGeneMm.1296.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2A05NMR-A189-243[»]
ProteinModelPortalP16563.
SMRP16563. Positions 26-243.
ModBaseSearch...

Protein-protein interaction databases

STRING10090.ENSMUSP00000024724.

PTM databases

PhosphoSiteP16563.

Proteomic databases

PaxDbP16563.
PRIDEP16563.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000024724; ENSMUSP00000024724; ENSMUSG00000023930.
GeneID22024.
KEGGmmu:22024.
UCSCuc008coj.2. mouse.

Organism-specific databases

CTD7180.
MGIMGI:98815. Crisp2.

Phylogenomic databases

eggNOGNOG312931.
GeneTreeENSGT00700000104242.
HOGENOMHOG000236338.
HOVERGENHBG004184.
InParanoidP16563.
OMACKHELLK.
OrthoDBEOG4XKV7K.

Gene expression databases

ArrayExpressP16563.
BgeeP16563.
CleanExMM_CRISP2.
GenevestigatorP16563.
GermOnlineENSMUSG00000023930. Mus musculus.

Family and domain databases

Gene3D3.40.33.10. 1 hit.
InterProIPR001283. Allrgn_V5/Tpx1.
IPR018244. Allrgn_V5/Tpx1_CS.
IPR014044. CAP_domain.
IPR013871. Cysteine_rich_secretory.
[Graphical view]
PANTHERPTHR10334. PTHR10334. 1 hit.
PfamPF00188. CAP. 1 hit.
PF08562. Crisp. 1 hit.
[Graphical view]
PRINTSPR00837. V5TPXLIKE.
SMARTSM00198. SCP. 1 hit.
[Graphical view]
SUPFAMSSF55797. SCP-like_extracellular. 1 hit.
PROSITEPS01009. CRISP_1. 1 hit.
PS01010. CRISP_2. 1 hit.
PS51670. SHKT. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP16563.
NextBio301760.
SOURCESearch...

Entry information

Entry nameCRIS2_MOUSE
AccessionPrimary (citable) accession number: P16563
Entry history
Integrated into UniProtKB/Swiss-Prot: August 1, 1990
Last sequence update: August 1, 1990
Last modified: May 29, 2013
This is version 109 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families