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Q9D5A9 (RNS10_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 88. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | 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:
Inactive ribonuclease-like protein 10
Alternative name(s):
Protein Train A
Gene names
Name:Rnase10
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length208 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Secreted proximal epididymal protein required for post-testicular sperm maturation and male fertility. May be involved in sperm adhesion to the egg zona pellucida. Does not have ribonuclease activity. Ref.4

Subcellular location

Secreted By similarity.

Tissue specificity

Male-specific expression in proximal caput of the epididymis (at protein level). Ref.1 Ref.3 Ref.4

Developmental stage

Expressed in mature epididymis. Ref.1

Post-translational modification

The N-terminus is blocked. Glycosylated By similarity.

Disruption phenotype

Mice are viable, anatomically normal and reach adulthood but display impaired fertility consequent to an inability of the spermatozoa to ascend the uterotubal junction (UTJ) canal of the female reproductive tract and gain the site of fertilization. Spermatozoa fail to establish a strong association with either epididymal epithelial cells, the zona pellucida of oocytes or oviductal epithelial cells, yet they are capable of fertilizing eggs in vitro. Ref.4

Sequence similarities

Belongs to the pancreatic ribonuclease family.

Sequence caution

The sequence AAP43947.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2424 Potential
Chain25 – 208184Inactive ribonuclease-like protein 10
PRO_0000045964

Amino acid modifications

Glycosylation1251N-linked (GlcNAc...) Potential
Glycosylation1471N-linked (GlcNAc...) Potential

Experimental info

Sequence conflict371Q → H in AAP43947. Ref.1
Sequence conflict631A → T in AAP43947. Ref.1
Sequence conflict1281C → S in AAP43947. Ref.1
Sequence conflict1561Q → K in AAP43947. Ref.1
Sequence conflict1941S → V in AAP43947. Ref.1
Sequence conflict2031R → K in AAP43947. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Q9D5A9 [UniParc].

Last modified June 1, 2001. Version 1.
Checksum: 383F776927F6067C

FASTA20823,407
        10         20         30         40         50         60 
MKVTLVHLLF MMLLLLLGLG LGLGLGLHMA AAVLEDQPLN EFWPSDSQNT EEGEGIWTTE 

        70         80         90        100        110        120 
GLALGYKEMA QPVWPEEAVL SEDEVGGSRM LRAEPRFQSK QDYLKFDLSV RDCNTMMAHK 

       130        140        150        160        170        180 
IKEPNQSCIN QYTFIHEDPN TVKAVCNGSL VDCDLQGGKC YKSPRPFDLT LCKLAKPGQV 

       190        200 
TPNCHYLTYI TEKSIFMTCN DKRQLETK 

« Hide

References

« Hide 'large scale' references
[1]"Discovery in silico and characterization in vitro of novel genes exclusively expressed in the mouse epididymis."
Penttinen J., Pujianto D.A., Sipilae P., Huhtaniemi I., Poutanen M.
Mol. Endocrinol. 17:2138-2151(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], DEVELOPMENTAL STAGE, TISSUE SPECIFICITY.
Strain: FVB/N.
Tissue: Epididymis.
[2]"The transcriptional landscape of the mammalian genome."
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. expand/collapse author list , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: C57BL/6J.
Tissue: Testis.
[3]"Identification of a member of a new RNase A family specifically secreted by epididymal caput epithelium."
Castella S., Fouchecourt S., Teixeira-Gomes A.P., Vinh J., Belghazi M., Dacheux F., Dacheux J.-L.
Biol. Reprod. 70:319-328(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: TISSUE SPECIFICITY.
[4]"Epididymal protein Rnase10 is required for post-testicular sperm maturation and male fertility."
Krutskikh A., Poliandri A., Cabrera-Sharp V., Dacheux J.L., Poutanen M., Huhtaniemi I.
FASEB J. 26:4198-4209(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, DISRUPTION PHENOTYPE, TISSUE SPECIFICITY.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AY226990 mRNA. Translation: AAP43947.1. Different initiation.
AK015573 mRNA. Translation: BAB29898.1.
RefSeqNP_001156335.1. NM_001162863.1.
UniGeneMm.318775.

3D structure databases

ProteinModelPortalQ9D5A9.
SMRQ9D5A9. Positions 70-208.
ModBaseSearch...
MobiDBSearch...

Proteomic databases

PRIDEQ9D5A9.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID75019.
KEGGmmu:75019.

Organism-specific databases

CTD338879.
MGIMGI:1922269. Rnase10.

Phylogenomic databases

eggNOGNOG46261.
HOVERGENHBG080734.
InParanoidQ9D5A9.
PhylomeDBQ9D5A9.

Gene expression databases

CleanExMM_RNASE10.
GenevestigatorQ9D5A9.

Family and domain databases

Gene3D3.10.130.10. 1 hit.
InterProIPR001427. RNaseA.
IPR023412. RNaseA_domain.
[Graphical view]
PANTHERPTHR11437. PTHR11437. 1 hit.
PfamPF00074. RnaseA. 1 hit.
[Graphical view]
PRINTSPR00794. RIBONUCLEASE.
ProDomPD000535. RNaseA. 1 hit.
[Graphical view] [Entries sharing at least one domain]
SUPFAMSSF54076. SSF54076. 1 hit.
ProtoNetSearch...

Other

NextBio342028.
PROQ9D5A9.
SOURCESearch...

Entry information

Entry nameRNS10_MOUSE
AccessionPrimary (citable) accession number: Q9D5A9
Secondary accession number(s): Q6XL64
Entry history
Integrated into UniProtKB/Swiss-Prot: February 7, 2006
Last sequence update: June 1, 2001
Last modified: April 16, 2014
This is version 88 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

MGD cross-references

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