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Q9D5A9

- RNS10_MOUSE

UniProt

Q9D5A9 - RNS10_MOUSE

Protein

Inactive ribonuclease-like protein 10

Gene

Rnase10

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 91 (01 Oct 2014)
      Sequence version 1 (01 Jun 2001)
      Previous versions | rss
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    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. endoribonuclease activity, producing 3'-phosphomonoesters Source: InterPro
    2. 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

    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: Unplaced

    Organism-specific databases

    MGIiMGI:1922269. Rnase10.

    Subcellular locationi

    Secreted By similarity

    GO - Cellular componenti

    1. extracellular region Source: UniProtKB-SubCell

    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 113-202.
    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.
    InterProiIPR001427. RNaseA.
    IPR023412. RNaseA_domain.
    [Graphical view]
    PANTHERiPTHR11437. PTHR11437. 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

    MKVTLVHLLF MMLLLLLGLG LGLGLGLHMA AAVLEDQPLN EFWPSDSQNT    50
    EEGEGIWTTE GLALGYKEMA QPVWPEEAVL SEDEVGGSRM LRAEPRFQSK 100
    QDYLKFDLSV RDCNTMMAHK IKEPNQSCIN QYTFIHEDPN TVKAVCNGSL 150
    VDCDLQGGKC YKSPRPFDLT LCKLAKPGQV TPNCHYLTYI TEKSIFMTCN 200
    DKRQLETK 208
    Length:208
    Mass (Da):23,407
    Last modified:June 1, 2001 - v1
    Checksum:i383F776927F6067C
    GO

    Sequence cautioni

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

    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:
    EMBL
    GenBank
    DDBJ
    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:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AY226990 mRNA. Translation: AAP43947.1 . Different initiation.
    AK015573 mRNA. Translation: BAB29898.1 .
    CCDSi CCDS49480.1.
    RefSeqi NP_001156335.1. NM_001162863.1.
    UniGenei Mm.318775.

    3D structure databases

    ProteinModelPortali Q9D5A9.
    SMRi Q9D5A9. Positions 113-202.
    ModBasei Search...
    MobiDBi Search...

    Proteomic databases

    PRIDEi Q9D5A9.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    GeneIDi 75019.
    KEGGi mmu:75019.

    Organism-specific databases

    CTDi 338879.
    MGIi MGI:1922269. Rnase10.

    Phylogenomic databases

    eggNOGi NOG46261.
    HOVERGENi HBG080734.
    InParanoidi Q9D5A9.
    PhylomeDBi Q9D5A9.

    Miscellaneous databases

    NextBioi 342028.
    PROi Q9D5A9.
    SOURCEi Search...

    Gene expression databases

    CleanExi MM_RNASE10.
    Genevestigatori Q9D5A9.

    Family and domain databases

    Gene3Di 3.10.130.10. 1 hit.
    InterProi IPR001427. RNaseA.
    IPR023412. RNaseA_domain.
    [Graphical view ]
    PANTHERi PTHR11437. PTHR11437. 1 hit.
    Pfami PF00074. RnaseA. 1 hit.
    [Graphical view ]
    PRINTSi PR00794. RIBONUCLEASE.
    ProDomi PD000535. RNaseA. 1 hit.
    [Graphical view ] [Entries sharing at least one domain ]
    SUPFAMi SSF54076. SSF54076. 1 hit.
    ProtoNeti Search...

    Publicationsi

    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.
      , 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.

    Entry informationi

    Entry nameiRNS10_MOUSE
    AccessioniPrimary (citable) accession number: Q9D5A9
    Secondary accession number(s): Q6XL64
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: February 7, 2006
    Last sequence update: June 1, 2001
    Last modified: October 1, 2014
    This is version 91 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