RNAS9_HUMAN
ID RNAS9_HUMAN Reviewed; 205 AA.
AC P60153; A2RQR8; A8QJS1; Q5GAN7; Q6KG53;
DT 28-NOV-2003, integrated into UniProtKB/Swiss-Prot.
DT 28-NOV-2003, sequence version 1.
DT 03-AUG-2022, entry version 140.
DE RecName: Full=Inactive ribonuclease-like protein 9;
DE Flags: Precursor;
GN Name=RNASE9;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RX PubMed=15676279; DOI=10.1016/j.ygeno.2004.10.008;
RA Cho S., Beintema J.J., Zhang J.;
RT "The ribonuclease A superfamily of mammals and birds: identifying new
RT members and tracing evolutionary histories.";
RL Genomics 85:208-220(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), VARIANTS SER-148 AND PRO-204,
RP FUNCTION, AND TISSUE SPECIFICITY.
RC TISSUE=Epididymis;
RX PubMed=18992174; DOI=10.1186/1756-0500-1-111;
RA Liu J., Li J., Wang H., Zhang C., Li N., Lin Y., Liu J., Wang W.;
RT "Cloning, expression and location of RNase9 in human epididymis.";
RL BMC Res. Notes 1:111-111(2008).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), AND VARIANTS SER-148 AND
RP PRO-204.
RA Liu Q., Hamil K.G., Gao B., French F.S., Hall S.H., Zhang Y.-L.;
RT "Human RNASE9 transcript variants.";
RL Submitted (OCT-2006) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=12508121; DOI=10.1038/nature01348;
RA Heilig R., Eckenberg R., Petit J.-L., Fonknechten N., Da Silva C.,
RA Cattolico L., Levy M., Barbe V., De Berardinis V., Ureta-Vidal A.,
RA Pelletier E., Vico V., Anthouard V., Rowen L., Madan A., Qin S., Sun H.,
RA Du H., Pepin K., Artiguenave F., Robert C., Cruaud C., Bruels T.,
RA Jaillon O., Friedlander L., Samson G., Brottier P., Cure S., Segurens B.,
RA Aniere F., Samain S., Crespeau H., Abbasi N., Aiach N., Boscus D.,
RA Dickhoff R., Dors M., Dubois I., Friedman C., Gouyvenoux M., James R.,
RA Madan A., Mairey-Estrada B., Mangenot S., Martins N., Menard M., Oztas S.,
RA Ratcliffe A., Shaffer T., Trask B., Vacherie B., Bellemere C., Belser C.,
RA Besnard-Gonnet M., Bartol-Mavel D., Boutard M., Briez-Silla S.,
RA Combette S., Dufosse-Laurent V., Ferron C., Lechaplais C., Louesse C.,
RA Muselet D., Magdelenat G., Pateau E., Petit E., Sirvain-Trukniewicz P.,
RA Trybou A., Vega-Czarny N., Bataille E., Bluet E., Bordelais I., Dubois M.,
RA Dumont C., Guerin T., Haffray S., Hammadi R., Muanga J., Pellouin V.,
RA Robert D., Wunderle E., Gauguet G., Roy A., Sainte-Marthe L., Verdier J.,
RA Verdier-Discala C., Hillier L.W., Fulton L., McPherson J., Matsuda F.,
RA Wilson R., Scarpelli C., Gyapay G., Wincker P., Saurin W., Quetier F.,
RA Waterston R., Hood L., Weissenbach J.;
RT "The DNA sequence and analysis of human chromosome 14.";
RL Nature 421:601-607(2003).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANTS SER-148
RP AND PRO-204.
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [6]
RP PROTEIN SEQUENCE OF 27-36, FUNCTION, TISSUE SPECIFICITY, AND SIGNAL
RP SEQUENCE CLEAVAGE SITE.
RX PubMed=19137000; DOI=10.1038/aja.2008.30;
RA Cheng G.Z., Li J.Y., Li F., Wang H.Y., Shi G.X.;
RT "Human ribonuclease 9, a member of ribonuclease A superfamily, specifically
RT expressed in epididymis, is a novel sperm-binding protein.";
RL Asian J. Androl. 11:240-251(2009).
CC -!- FUNCTION: Does not exhibit any ribonuclease activity.
CC {ECO:0000269|PubMed:18992174, ECO:0000269|PubMed:19137000}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1; Synonyms=alpha1, alpha2, alpha12, beta2, beta12;
CC IsoId=P60153-1; Sequence=Displayed;
CC Name=2; Synonyms=alpha23, alpha123;
CC IsoId=P60153-2; Sequence=VSP_041856;
CC -!- TISSUE SPECIFICITY: At the mRNA level, widely expressed
CC (PubMed:18992174). At protein level, restricted to epididymis
CC (PubMed:19137000). Expressed in spermatozoa (sperm head and neck), with
CC higher levels on ejaculated and epididymal sperm than on testicular
CC sperm (at protein level). Expressed in the epithelial cells of the
CC epididymal tubule (at protein level). Not detected in muscle.
CC {ECO:0000269|PubMed:18992174, ECO:0000269|PubMed:19137000}.
CC -!- SIMILARITY: Belongs to the pancreatic ribonuclease family.
CC {ECO:0000305}.
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DR EMBL; AY665804; AAV87182.1; -; mRNA.
DR EMBL; EU414264; ACA49544.1; -; mRNA.
DR EMBL; AF382949; AAQ02792.1; -; mRNA.
DR EMBL; AY907670; AAX86045.1; -; mRNA.
DR EMBL; EF061296; ABP97451.1; -; mRNA.
DR EMBL; EF061297; ABP97452.1; -; mRNA.
DR EMBL; EF061298; ABP97453.1; -; mRNA.
DR EMBL; EF061299; ABP97454.1; -; mRNA.
DR EMBL; EF061300; ABP97455.1; -; mRNA.
DR EMBL; EF061301; ABP97456.1; -; mRNA.
DR EMBL; EF061302; ABP97457.1; -; mRNA.
DR EMBL; EF061303; ABP97458.1; -; mRNA.
DR EMBL; EF061304; ABP97459.1; -; mRNA.
DR EMBL; AL163195; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC130311; AAI30312.1; -; mRNA.
DR EMBL; BC130313; AAI30314.1; -; mRNA.
DR CCDS; CCDS32036.1; -. [P60153-1]
DR CCDS; CCDS53883.1; -. [P60153-2]
DR CCDS; CCDS55904.1; -. [P60153-2]
DR RefSeq; NP_001001673.2; NM_001001673.3. [P60153-1]
DR RefSeq; NP_001103826.1; NM_001110356.1. [P60153-1]
DR RefSeq; NP_001103827.1; NM_001110357.1. [P60153-1]
DR RefSeq; NP_001103828.1; NM_001110358.1. [P60153-2]
DR RefSeq; NP_001103829.1; NM_001110359.1. [P60153-2]
DR RefSeq; NP_001103830.1; NM_001110360.1. [P60153-2]
DR RefSeq; NP_001103831.1; NM_001110361.1. [P60153-2]
DR RefSeq; NP_001276039.1; NM_001289110.1. [P60153-1]
DR AlphaFoldDB; P60153; -.
DR SMR; P60153; -.
DR BioGRID; 133570; 3.
DR IntAct; P60153; 1.
DR STRING; 9606.ENSP00000384683; -.
DR GlyGen; P60153; 2 sites.
DR iPTMnet; P60153; -.
DR PhosphoSitePlus; P60153; -.
DR BioMuta; RNASE9; -.
DR DMDM; 38605140; -.
DR PaxDb; P60153; -.
DR PeptideAtlas; P60153; -.
DR PRIDE; P60153; -.
DR Antibodypedia; 175; 120 antibodies from 17 providers.
DR DNASU; 390443; -.
DR Ensembl; ENST00000338904.7; ENSP00000340162.3; ENSG00000188655.10. [P60153-1]
DR Ensembl; ENST00000404716.7; ENSP00000384683.3; ENSG00000188655.10. [P60153-2]
DR Ensembl; ENST00000429244.6; ENSP00000409504.2; ENSG00000188655.10. [P60153-1]
DR Ensembl; ENST00000553541.5; ENSP00000451285.1; ENSG00000188655.10. [P60153-1]
DR Ensembl; ENST00000553706.5; ENSP00000450570.1; ENSG00000188655.10. [P60153-2]
DR Ensembl; ENST00000554964.5; ENSP00000450599.1; ENSG00000188655.10. [P60153-1]
DR Ensembl; ENST00000555230.5; ENSP00000450800.1; ENSG00000188655.10. [P60153-1]
DR Ensembl; ENST00000556208.5; ENSP00000451160.1; ENSG00000188655.10. [P60153-2]
DR Ensembl; ENST00000557068.5; ENSP00000451565.1; ENSG00000188655.10. [P60153-1]
DR Ensembl; ENST00000557209.1; ENSP00000450987.1; ENSG00000188655.10. [P60153-2]
DR Ensembl; ENST00000611135.1; ENSP00000481786.1; ENSG00000188655.10. [P60153-2]
DR GeneID; 390443; -.
DR KEGG; hsa:390443; -.
DR UCSC; uc001vxq.4; human. [P60153-1]
DR CTD; 390443; -.
DR GeneCards; RNASE9; -.
DR HGNC; HGNC:20673; RNASE9.
DR HPA; ENSG00000188655; Tissue enriched (epididymis).
DR MIM; 614014; gene.
DR neXtProt; NX_P60153; -.
DR OpenTargets; ENSG00000188655; -.
DR PharmGKB; PA134887351; -.
DR VEuPathDB; HostDB:ENSG00000188655; -.
DR eggNOG; ENOG502TDU6; Eukaryota.
DR GeneTree; ENSGT00390000013952; -.
DR HOGENOM; CLU_1464451_0_0_1; -.
DR InParanoid; P60153; -.
DR OrthoDB; 1271649at2759; -.
DR PhylomeDB; P60153; -.
DR TreeFam; TF338401; -.
DR PathwayCommons; P60153; -.
DR SignaLink; P60153; -.
DR BioGRID-ORCS; 390443; 27 hits in 1058 CRISPR screens.
DR GenomeRNAi; 390443; -.
DR Pharos; P60153; Tbio.
DR PRO; PR:P60153; -.
DR Proteomes; UP000005640; Chromosome 14.
DR RNAct; P60153; protein.
DR Bgee; ENSG00000188655; Expressed in skin of abdomen and 5 other tissues.
DR ExpressionAtlas; P60153; baseline and differential.
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 Gene3D; 3.10.130.10; -; 1.
DR InterPro; IPR029741; RNASE9.
DR InterPro; IPR001427; RNaseA.
DR InterPro; IPR036816; RNaseA-like_dom_sf.
DR InterPro; IPR023412; RNaseA_domain.
DR PANTHER; PTHR11437; PTHR11437; 1.
DR PANTHER; PTHR11437:SF14; PTHR11437:SF14; 1.
DR Pfam; PF00074; RnaseA; 1.
DR SUPFAM; SSF54076; SSF54076; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Direct protein sequencing; Disulfide bond;
KW Glycoprotein; Reference proteome; Secreted; Signal.
FT SIGNAL 1..26
FT /evidence="ECO:0000269|PubMed:19137000"
FT CHAIN 27..205
FT /note="Inactive ribonuclease-like protein 9"
FT /id="PRO_0000030951"
FT CARBOHYD 131
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 143
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 116..168
FT /evidence="ECO:0000250"
FT DISULFID 123..130
FT /evidence="ECO:0000250"
FT VAR_SEQ 1
FT /note="M -> MSAGKM (in isoform 2)"
FT /evidence="ECO:0000303|Ref.3"
FT /id="VSP_041856"
FT VARIANT 148
FT /note="F -> S (in dbSNP:rs12590446)"
FT /evidence="ECO:0000269|PubMed:15489334,
FT ECO:0000269|PubMed:18992174, ECO:0000269|Ref.3"
FT /id="VAR_052197"
FT VARIANT 204
FT /note="S -> P (in dbSNP:rs1243647)"
FT /evidence="ECO:0000269|PubMed:15489334,
FT ECO:0000269|PubMed:18992174, ECO:0000269|Ref.3"
FT /id="VAR_034473"
SQ SEQUENCE 205 AA; 24307 MW; EDE63F0727282BF6 CRC64;
MMRTLITTHP LPLLLLPQQL LQLVQFQEVD TDFDFPEEDK KEEFEECLEK FFSTGPARPP
TKEKVKRRVL IEPGMPLNHI EYCNHEIMGK NVYYKHRWVA EHYFLLMQYD ELQKICYNRF
VPCKNGIRKC NRSKGLVEGV YCNLTEAFEI PACKYESLYR KGYVLITCSW QNEMQKRIPH
TINDLVEPPE HRSFLSEDGV FVISP
