RNS10_MOUSE
ID RNS10_MOUSE Reviewed; 208 AA.
AC Q9D5A9; Q6XL64;
DT 07-FEB-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 123.
DE RecName: Full=Inactive ribonuclease-like protein 10;
DE AltName: Full=Protein Train A;
DE Flags: Precursor;
GN Name=Rnase10;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], DEVELOPMENTAL STAGE, AND TISSUE SPECIFICITY.
RC STRAIN=FVB/N; TISSUE=Epididymis;
RX PubMed=12920233; DOI=10.1210/me.2003-0008;
RA Penttinen J., Pujianto D.A., Sipilae P., Huhtaniemi I., Poutanen M.;
RT "Discovery in silico and characterization in vitro of novel genes
RT exclusively expressed in the mouse epididymis.";
RL Mol. Endocrinol. 17:2138-2151(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Testis;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3]
RP TISSUE SPECIFICITY.
RX PubMed=14561640; DOI=10.1095/biolreprod.103.022459;
RA Castella S., Fouchecourt S., Teixeira-Gomes A.P., Vinh J., Belghazi M.,
RA Dacheux F., Dacheux J.-L.;
RT "Identification of a member of a new RNase A family specifically secreted
RT by epididymal caput epithelium.";
RL Biol. Reprod. 70:319-328(2004).
RN [4]
RP FUNCTION, DISRUPTION PHENOTYPE, AND TISSUE SPECIFICITY.
RX PubMed=22750516; DOI=10.1096/fj.12-205211;
RA Krutskikh A., Poliandri A., Cabrera-Sharp V., Dacheux J.L., Poutanen M.,
RA Huhtaniemi I.;
RT "Epididymal protein Rnase10 is required for post-testicular sperm
RT maturation and male fertility.";
RL FASEB J. 26:4198-4209(2012).
CC -!- FUNCTION: Secreted proximal epididymal protein required for post-
CC testicular sperm maturation and male fertility. May be involved in
CC sperm adhesion to the egg zona pellucida. Does not have ribonuclease
CC activity. {ECO:0000269|PubMed:22750516}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Male-specific expression in proximal caput of the
CC epididymis (at protein level). {ECO:0000269|PubMed:12920233,
CC ECO:0000269|PubMed:14561640, ECO:0000269|PubMed:22750516}.
CC -!- DEVELOPMENTAL STAGE: Expressed in mature epididymis.
CC {ECO:0000269|PubMed:12920233}.
CC -!- PTM: The N-terminus is blocked. Glycosylated (By similarity).
CC {ECO:0000250}.
CC -!- DISRUPTION PHENOTYPE: Mice are viable, anatomically normal and reach
CC adulthood but display impaired fertility consequent to an inability of
CC the spermatozoa to ascend the uterotubal junction (UTJ) canal of the
CC female reproductive tract and gain the site of fertilization.
CC Spermatozoa fail to establish a strong association with either
CC epididymal epithelial cells, the zona pellucida of oocytes or oviductal
CC epithelial cells, yet they are capable of fertilizing eggs in vitro.
CC {ECO:0000269|PubMed:22750516}.
CC -!- SIMILARITY: Belongs to the pancreatic ribonuclease family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAP43947.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AY226990; AAP43947.1; ALT_INIT; mRNA.
DR EMBL; AK015573; BAB29898.1; -; mRNA.
DR CCDS; CCDS49480.1; -.
DR RefSeq; NP_001156335.1; NM_001162863.1.
DR AlphaFoldDB; Q9D5A9; -.
DR SMR; Q9D5A9; -.
DR STRING; 10090.ENSMUSP00000022424; -.
DR GlyGen; Q9D5A9; 2 sites.
DR PaxDb; Q9D5A9; -.
DR PRIDE; Q9D5A9; -.
DR ProteomicsDB; 260824; -.
DR DNASU; 75019; -.
DR GeneID; 75019; -.
DR KEGG; mmu:75019; -.
DR CTD; 338879; -.
DR MGI; MGI:1922269; Rnase10.
DR eggNOG; ENOG502RPGF; Eukaryota.
DR InParanoid; Q9D5A9; -.
DR PhylomeDB; Q9D5A9; -.
DR BioGRID-ORCS; 75019; 3 hits in 73 CRISPR screens.
DR ChiTaRS; Rnase10; mouse.
DR PRO; PR:Q9D5A9; -.
DR Proteomes; UP000000589; Unplaced.
DR RNAct; Q9D5A9; protein.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR GO; GO:0050830; P:defense response to Gram-positive bacterium; IBA:GO_Central.
DR GO; GO:0003382; P:epithelial cell morphogenesis; IGI:MGI.
DR GO; GO:0034113; P:heterotypic cell-cell adhesion; IMP:UniProtKB.
DR GO; GO:0008584; P:male gonad development; IGI:MGI.
DR GO; GO:0022409; P:positive regulation of cell-cell adhesion; IMP:UniProtKB.
DR GO; GO:1902093; P:positive regulation of flagellated sperm motility; IMP:UniProtKB.
DR GO; GO:0080154; P:regulation of fertilization; IMP:UniProtKB.
DR GO; GO:0072520; P:seminiferous tubule development; IGI:MGI.
DR GO; GO:0007338; P:single fertilization; IGI:MGI.
DR Gene3D; 3.10.130.10; -; 1.
DR InterPro; IPR029742; RNASE10.
DR InterPro; IPR001427; RNaseA.
DR InterPro; IPR036816; RNaseA-like_dom_sf.
DR InterPro; IPR023412; RNaseA_domain.
DR PANTHER; PTHR11437; PTHR11437; 1.
DR PANTHER; PTHR11437:SF2; PTHR11437:SF2; 1.
DR Pfam; PF00074; RnaseA; 1.
DR PRINTS; PR00794; RIBONUCLEASE.
DR SMART; SM00092; RNAse_Pc; 1.
DR SUPFAM; SSF54076; SSF54076; 1.
PE 1: Evidence at protein level;
KW Cell adhesion; Fertilization; Glycoprotein; Reference proteome; Secreted;
KW Signal.
FT SIGNAL 1..24
FT /evidence="ECO:0000255"
FT CHAIN 25..208
FT /note="Inactive ribonuclease-like protein 10"
FT /id="PRO_0000045964"
FT CARBOHYD 125
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 147
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CONFLICT 37
FT /note="Q -> H (in Ref. 1; AAP43947)"
FT /evidence="ECO:0000305"
FT CONFLICT 63
FT /note="A -> T (in Ref. 1; AAP43947)"
FT /evidence="ECO:0000305"
FT CONFLICT 128
FT /note="C -> S (in Ref. 1; AAP43947)"
FT /evidence="ECO:0000305"
FT CONFLICT 156
FT /note="Q -> K (in Ref. 1; AAP43947)"
FT /evidence="ECO:0000305"
FT CONFLICT 194
FT /note="S -> V (in Ref. 1; AAP43947)"
FT /evidence="ECO:0000305"
FT CONFLICT 203
FT /note="R -> K (in Ref. 1; AAP43947)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 208 AA; 23407 MW; 383F776927F6067C CRC64;
MKVTLVHLLF MMLLLLLGLG LGLGLGLHMA AAVLEDQPLN EFWPSDSQNT EEGEGIWTTE
GLALGYKEMA QPVWPEEAVL SEDEVGGSRM LRAEPRFQSK QDYLKFDLSV RDCNTMMAHK
IKEPNQSCIN QYTFIHEDPN TVKAVCNGSL VDCDLQGGKC YKSPRPFDLT LCKLAKPGQV
TPNCHYLTYI TEKSIFMTCN DKRQLETK
