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Protein

Inactive ribonuclease-like protein 10

Gene

Rnase10

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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.1 Publication

GO - Molecular functioni

  1. nucleic acid binding Source: InterPro

GO - Biological processi

  1. epithelial cell morphogenesis Source: MGI
  2. heterotypic cell-cell adhesion Source: UniProtKB
  3. male gonad development Source: MGI
  4. positive regulation of cell-cell adhesion Source: UniProtKB
  5. positive regulation of sperm motility Source: UniProtKB
  6. regulation of fertilization Source: UniProtKB
  7. seminiferous tubule development Source: MGI
  8. single fertilization Source: MGI
Complete GO annotation...

Keywords - Biological processi

Cell adhesion, Fertilization

Names & Taxonomyi

Protein namesi
Recommended name:
Inactive ribonuclease-like protein 10
Alternative name(s):
Protein Train A
Gene namesi
Name:Rnase10
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589 Componenti: Unplaced

Organism-specific databases

MGIiMGI:1922269. Rnase10.

Subcellular locationi

Secreted By similarity

GO - Cellular componenti

  1. extracellular region Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Secreted

Pathology & Biotechi

Disruption phenotypei

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.1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2424Sequence AnalysisAdd
BLAST
Chaini25 – 208184Inactive ribonuclease-like protein 10PRO_0000045964Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi125 – 1251N-linked (GlcNAc...)Sequence Analysis
Glycosylationi147 – 1471N-linked (GlcNAc...)Sequence Analysis

Post-translational modificationi

The N-terminus is blocked. Glycosylated (By similarity).By similarity

Keywords - PTMi

Glycoprotein

Proteomic databases

PRIDEiQ9D5A9.

Expressioni

Tissue specificityi

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

Developmental stagei

Expressed in mature epididymis.1 Publication

Gene expression databases

CleanExiMM_RNASE10.
GenevestigatoriQ9D5A9.

Structurei

3D structure databases

ProteinModelPortaliQ9D5A9.
SMRiQ9D5A9. Positions 70-208.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the pancreatic ribonuclease family.Curated

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiNOG46261.
HOVERGENiHBG080734.
InParanoidiQ9D5A9.
PhylomeDBiQ9D5A9.

Family and domain databases

Gene3Di3.10.130.10. 1 hit.
InterProiIPR029742. RNASE10.
IPR001427. RNaseA.
IPR023412. RNaseA_domain.
[Graphical view]
PANTHERiPTHR11437. PTHR11437. 1 hit.
PTHR11437:SF2. PTHR11437:SF2. 1 hit.
PfamiPF00074. RnaseA. 1 hit.
[Graphical view]
PRINTSiPR00794. RIBONUCLEASE.
ProDomiPD000535. RNaseA. 1 hit.
[Graphical view] [Entries sharing at least one domain]
SUPFAMiSSF54076. SSF54076. 1 hit.

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q9D5A9-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKVTLVHLLF MMLLLLLGLG LGLGLGLHMA AAVLEDQPLN EFWPSDSQNT
60 70 80 90 100
EEGEGIWTTE GLALGYKEMA QPVWPEEAVL SEDEVGGSRM LRAEPRFQSK
110 120 130 140 150
QDYLKFDLSV RDCNTMMAHK IKEPNQSCIN QYTFIHEDPN TVKAVCNGSL
160 170 180 190 200
VDCDLQGGKC YKSPRPFDLT LCKLAKPGQV TPNCHYLTYI TEKSIFMTCN

DKRQLETK
Length:208
Mass (Da):23,407
Last modified:May 31, 2001 - v1
Checksum:i383F776927F6067C
GO

Sequence cautioni

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

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti37 – 371Q → H in AAP43947 (PubMed:12920233).Curated
Sequence conflicti63 – 631A → T in AAP43947 (PubMed:12920233).Curated
Sequence conflicti128 – 1281C → S in AAP43947 (PubMed:12920233).Curated
Sequence conflicti156 – 1561Q → K in AAP43947 (PubMed:12920233).Curated
Sequence conflicti194 – 1941S → V in AAP43947 (PubMed:12920233).Curated
Sequence conflicti203 – 2031R → K in AAP43947 (PubMed:12920233).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY226990 mRNA. Translation: AAP43947.1. Different initiation.
AK015573 mRNA. Translation: BAB29898.1.
CCDSiCCDS49480.1.
RefSeqiNP_001156335.1. NM_001162863.1.
UniGeneiMm.318775.

Genome annotation databases

GeneIDi75019.
KEGGimmu:75019.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY226990 mRNA. Translation: AAP43947.1. Different initiation.
AK015573 mRNA. Translation: BAB29898.1.
CCDSiCCDS49480.1.
RefSeqiNP_001156335.1. NM_001162863.1.
UniGeneiMm.318775.

3D structure databases

ProteinModelPortaliQ9D5A9.
SMRiQ9D5A9. Positions 70-208.
ModBaseiSearch...
MobiDBiSearch...

Proteomic databases

PRIDEiQ9D5A9.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi75019.
KEGGimmu:75019.

Organism-specific databases

CTDi338879.
MGIiMGI:1922269. Rnase10.

Phylogenomic databases

eggNOGiNOG46261.
HOVERGENiHBG080734.
InParanoidiQ9D5A9.
PhylomeDBiQ9D5A9.

Miscellaneous databases

NextBioi342028.
PROiQ9D5A9.
SOURCEiSearch...

Gene expression databases

CleanExiMM_RNASE10.
GenevestigatoriQ9D5A9.

Family and domain databases

Gene3Di3.10.130.10. 1 hit.
InterProiIPR029742. RNASE10.
IPR001427. RNaseA.
IPR023412. RNaseA_domain.
[Graphical view]
PANTHERiPTHR11437. PTHR11437. 1 hit.
PTHR11437:SF2. PTHR11437:SF2. 1 hit.
PfamiPF00074. RnaseA. 1 hit.
[Graphical view]
PRINTSiPR00794. RIBONUCLEASE.
ProDomiPD000535. RNaseA. 1 hit.
[Graphical view] [Entries sharing at least one domain]
SUPFAMiSSF54076. SSF54076. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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(2002) [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.
    , 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(2004) [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(2003) [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(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, DISRUPTION PHENOTYPE, TISSUE SPECIFICITY.

Entry informationi

Entry nameiRNS10_MOUSE
AccessioniPrimary (citable) accession number: Q9D5A9
Secondary accession number(s): Q6XL64
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 6, 2006
Last sequence update: May 31, 2001
Last modified: March 31, 2015
This is version 94 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.