ID   RNS10_PIG               Reviewed;         213 AA.
AC   Q8SPJ0;
DT   07-FEB-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2002, sequence version 1.
DT   03-AUG-2022, entry version 96.
DE   RecName: Full=Inactive ribonuclease-like protein 10;
DE   AltName: Full=Protein Train A;
DE   Flags: Precursor;
GN   Name=RNASE10;
OS   Sus scrofa (Pig).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX   NCBI_TaxID=9823;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 32-45; 64-68; 96-108;
RP   151-159; 168-176; 177-191 AND 197-201, GLYCOSYLATION, TISSUE SPECIFICITY,
RP   AND SUBCELLULAR LOCATION.
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).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   TISSUE=Epididymis;
RA   Castella S., Uzbekova S., Dacheux J.-L.;
RT   "Sus Scrofa Train A gene sequencing.";
RL   Submitted (APR-2004) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   FUNCTION, AND SUBCELLULAR LOCATION.
RX   PubMed=15253924; DOI=10.1095/biolreprod.104.031666;
RA   Castella S., Benedetti H., de Llorens R., Dacheux J.-L., Dacheux F.;
RT   "Train A, an RNase A-like protein without RNase activity, is secreted and
RT   reabsorbed by the same epididymal cells under testicular control.";
RL   Biol. Reprod. 71:1677-1687(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 (By similarity). Does not have
CC       ribonuclease activity. {ECO:0000250, ECO:0000269|PubMed:15253924}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:14561640,
CC       ECO:0000269|PubMed:15253924}.
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.
CC       {ECO:0000269|PubMed:14561640}.
CC   -!- MISCELLANEOUS: Represents 34% of the proteins secreted by the
CC       epididymis and 89% of the proteins secreted by the proximal caput.
CC   -!- SIMILARITY: Belongs to the pancreatic ribonuclease family.
CC       {ECO:0000305}.
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DR   EMBL; AJ430467; CAD23253.1; -; mRNA.
DR   EMBL; AJ634916; CAG25552.1; -; Genomic_DNA.
DR   RefSeq; NP_001007112.1; NM_001007111.1.
DR   RefSeq; XP_005656364.1; XM_005656307.2.
DR   RefSeq; XP_005658175.1; XM_005658118.2.
DR   RefSeq; XP_013844514.1; XM_013989060.1.
DR   RefSeq; XP_013844515.1; XM_013989061.1.
DR   RefSeq; XP_013844516.1; XM_013989062.1.
DR   RefSeq; XP_013844517.1; XM_013989063.1.
DR   RefSeq; XP_013846715.1; XM_013991261.1.
DR   RefSeq; XP_013846716.1; XM_013991262.1.
DR   RefSeq; XP_013846717.1; XM_013991263.1.
DR   RefSeq; XP_013846718.1; XM_013991264.1.
DR   AlphaFoldDB; Q8SPJ0; -.
DR   SMR; Q8SPJ0; -.
DR   STRING; 9823.ENSSSCP00000002332; -.
DR   iPTMnet; Q8SPJ0; -.
DR   PaxDb; Q8SPJ0; -.
DR   PeptideAtlas; Q8SPJ0; -.
DR   PRIDE; Q8SPJ0; -.
DR   Ensembl; ENSSSCT00000002387; ENSSSCP00000002332; ENSSSCG00000002134.
DR   Ensembl; ENSSSCT00005036143; ENSSSCP00005022043; ENSSSCG00005022869.
DR   Ensembl; ENSSSCT00025006430; ENSSSCP00025002668; ENSSSCG00025004750.
DR   Ensembl; ENSSSCT00035001341; ENSSSCP00035000402; ENSSSCG00035001108.
DR   Ensembl; ENSSSCT00040023803; ENSSSCP00040010083; ENSSSCG00040017633.
DR   Ensembl; ENSSSCT00045007229; ENSSSCP00045004966; ENSSSCG00045004328.
DR   Ensembl; ENSSSCT00050004199; ENSSSCP00050001625; ENSSSCG00050003190.
DR   Ensembl; ENSSSCT00055031721; ENSSSCP00055025248; ENSSSCG00055016101.
DR   Ensembl; ENSSSCT00065082526; ENSSSCP00065035954; ENSSSCG00065060243.
DR   Ensembl; ENSSSCT00070039120; ENSSSCP00070032760; ENSSSCG00070019758.
DR   GeneID; 396701; -.
DR   KEGG; ssc:396701; -.
DR   CTD; 338879; -.
DR   eggNOG; ENOG502RPGF; Eukaryota.
DR   GeneTree; ENSGT00730000111443; -.
DR   HOGENOM; CLU_1280301_0_0_1; -.
DR   InParanoid; Q8SPJ0; -.
DR   OMA; GQVTPHC; -.
DR   OrthoDB; 1349885at2759; -.
DR   TreeFam; TF337410; -.
DR   Proteomes; UP000008227; Chromosome 7.
DR   Proteomes; UP000314985; Chromosome 7.
DR   Bgee; ENSSSCG00000002134; Expressed in epididymis and 3 other tissues.
DR   Genevisible; Q8SPJ0; SS.
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   1: Evidence at protein level;
KW   Cell adhesion; Direct protein sequencing; Fertilization; Glycoprotein;
KW   Reference proteome; Secreted; Signal.
FT   SIGNAL          1..24
FT                   /evidence="ECO:0000255"
FT   CHAIN           25..213
FT                   /note="Inactive ribonuclease-like protein 10"
FT                   /id="PRO_0000045965"
FT   CARBOHYD        128
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000305|PubMed:14561640"
SQ   SEQUENCE   213 AA;  23740 MW;  515ADA0B39A1AF02 CRC64;
     MKLTLVQFFF MMLLLLLGLG VGLGLGLQMA AAVLEESDQL LSEFQSSDSQ DKTQATKKGA
     GTRTMETLLL SDNVVMQPEE TILSEDEVGG NKMLRAQAFS QSYPNYLRSD LMDRECNTLM
     AKKMKPYNHT CISQYIFIHE EPDEIKAVCK SPPVACELKG GKCHKSARPF DLTFCKLSKP
     GQVTPHCNYV TFLLEKHILI SCNDMKVQVM SGS