Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

Q9D5A9

- RNS10_MOUSE

UniProt

Q9D5A9 - RNS10_MOUSE

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

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

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: Unplaced

Organism-specific databases

MGIiMGI:1922269. Rnase10.

Subcellular locationi

Secreted By similarity

GO - Cellular componenti

  1. extracellular region Source: UniProtKB-KW
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 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.
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: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 IPR029742. RNASE10.
IPR001427. RNaseA.
IPR023412. RNaseA_domain.
[Graphical view ]
PANTHERi PTHR11437. PTHR11437. 1 hit.
PTHR11437:SF2. PTHR11437:SF2. 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

« 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(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 29, 2014
This is version 92 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