ID   RNS10_HORSE             Reviewed;         213 AA.
AC   Q70IB3; F6VMI8;
DT   07-FEB-2006, integrated into UniProtKB/Swiss-Prot.
DT   22-JAN-2014, sequence version 2.
DT   03-AUG-2022, entry version 85.
DE   RecName: Full=Inactive ribonuclease-like protein 10;
DE   AltName: Full=Protein Train A;
DE   Flags: Precursor;
GN   Name=RNASE10;
OS   Equus caballus (Horse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Perissodactyla; Equidae; Equus.
OX   NCBI_TaxID=9796;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Thoroughbred;
RX   PubMed=19892987; DOI=10.1126/science.1178158;
RA   Wade C.M., Giulotto E., Sigurdsson S., Zoli M., Gnerre S., Imsland F.,
RA   Lear T.L., Adelson D.L., Bailey E., Bellone R.R., Bloecker H., Distl O.,
RA   Edgar R.C., Garber M., Leeb T., Mauceli E., MacLeod J.N., Penedo M.C.T.,
RA   Raison J.M., Sharpe T., Vogel J., Andersson L., Antczak D.F., Biagi T.,
RA   Binns M.M., Chowdhary B.P., Coleman S.J., Della Valle G., Fryc S.,
RA   Guerin G., Hasegawa T., Hill E.W., Jurka J., Kiialainen A., Lindgren G.,
RA   Liu J., Magnani E., Mickelson J.R., Murray J., Nergadze S.G., Onofrio R.,
RA   Pedroni S., Piras M.F., Raudsepp T., Rocchi M., Roeed K.H., Ryder O.A.,
RA   Searle S., Skow L., Swinburne J.E., Syvaenen A.C., Tozaki T., Valberg S.J.,
RA   Vaudin M., White J.R., Zody M.C., Lander E.S., Lindblad-Toh K.;
RT   "Genome sequence, comparative analysis, and population genetics of the
RT   domestic horse.";
RL   Science 326:865-867(2009).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 1-165, AND TISSUE SPECIFICITY.
RC   TISSUE=Epididymis;
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).
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 (By similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
CC   -!- TISSUE SPECIFICITY: Male-specific expression in proximal caput of the
CC       epididymis. {ECO:0000269|PubMed:14561640}.
CC   -!- PTM: The N-terminus is blocked. Glycosylated (By similarity).
CC       {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the pancreatic ribonuclease family.
CC       {ECO:0000305}.
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DR   EMBL; AAWR02001632; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AJ580632; CAE45264.1; -; mRNA.
DR   RefSeq; NP_001157459.1; NM_001163987.1.
DR   RefSeq; XP_014588929.1; XM_014733443.1.
DR   AlphaFoldDB; Q70IB3; -.
DR   SMR; Q70IB3; -.
DR   STRING; 9796.ENSECAP00000001027; -.
DR   PaxDb; Q70IB3; -.
DR   Ensembl; ENSECAT00000001324; ENSECAP00000001027; ENSECAG00000001454.
DR   GeneID; 100033972; -.
DR   KEGG; ecb:100033972; -.
DR   CTD; 338879; -.
DR   GeneTree; ENSGT00730000111443; -.
DR   HOGENOM; CLU_1280301_0_0_1; -.
DR   InParanoid; Q70IB3; -.
DR   OMA; GQVTPHC; -.
DR   OrthoDB; 1349885at2759; -.
DR   TreeFam; TF337410; -.
DR   Proteomes; UP000002281; Chromosome 1.
DR   Bgee; ENSECAG00000001454; Expressed in oviduct epithelium and 10 other tissues.
DR   ExpressionAtlas; Q70IB3; baseline.
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:0034113; P:heterotypic cell-cell adhesion; ISS:UniProtKB.
DR   GO; GO:0022409; P:positive regulation of cell-cell adhesion; ISS:UniProtKB.
DR   GO; GO:1902093; P:positive regulation of flagellated sperm motility; ISS:UniProtKB.
DR   GO; GO:0080154; P:regulation of fertilization; ISS:UniProtKB.
DR   GO; GO:0007338; P:single fertilization; IEA:UniProtKB-KW.
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   2: Evidence at transcript level;
KW   Cell adhesion; Fertilization; Glycoprotein; Reference proteome; Secreted;
KW   Signal.
FT   SIGNAL          1..24
FT                   /evidence="ECO:0000255"
FT   CHAIN           25..213
FT                   /note="Inactive ribonuclease-like protein 10"
FT                   /id="PRO_0000045962"
FT   CARBOHYD        131
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   213 AA;  23942 MW;  3078C134895BB9BD CRC64;
     MKLTLVQIFF MMLLLLLGLG MGLGLGLQMA AAVLEDSDQS LNDFWSSDSQ EKAETTKEGD
     GTRTTETLLL SNKGVVQPVW PEETILAEDE VGGNKMLRAD ALFQSDKDYL RLDLMNRECN
     SLMAHKVKKR NHTCIPEYTF IHEELDTVKA VCKNPVVACD LKGAKCHKSS RPFDLTFCKL
     SKPGQVTPHC NYLTFIFEKF IIISCNDMKV KIT