CST8_HUMAN
ID CST8_HUMAN Reviewed; 142 AA.
AC O60676; Q2M2X6;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1998, sequence version 1.
DT 03-AUG-2022, entry version 165.
DE RecName: Full=Cystatin-8;
DE AltName: Full=Cystatin-related epididymal spermatogenic protein;
DE Flags: Precursor;
GN Name=CST8; Synonyms=CRES;
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].
RC TISSUE=Testis;
RX PubMed=7619504; DOI=10.1002/mrd.1080410107;
RA Cornwall G.A., Hann S.R.;
RT "Transient appearance of CRES protein during spermatogenesis and caput
RT epididymal sperm maturation.";
RL Mol. Reprod. Dev. 41:37-46(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=11780052; DOI=10.1038/414865a;
RA Deloukas P., Matthews L.H., Ashurst J.L., Burton J., Gilbert J.G.R.,
RA Jones M., Stavrides G., Almeida J.P., Babbage A.K., Bagguley C.L.,
RA Bailey J., Barlow K.F., Bates K.N., Beard L.M., Beare D.M., Beasley O.P.,
RA Bird C.P., Blakey S.E., Bridgeman A.M., Brown A.J., Buck D., Burrill W.D.,
RA Butler A.P., Carder C., Carter N.P., Chapman J.C., Clamp M., Clark G.,
RA Clark L.N., Clark S.Y., Clee C.M., Clegg S., Cobley V.E., Collier R.E.,
RA Connor R.E., Corby N.R., Coulson A., Coville G.J., Deadman R., Dhami P.D.,
RA Dunn M., Ellington A.G., Frankland J.A., Fraser A., French L., Garner P.,
RA Grafham D.V., Griffiths C., Griffiths M.N.D., Gwilliam R., Hall R.E.,
RA Hammond S., Harley J.L., Heath P.D., Ho S., Holden J.L., Howden P.J.,
RA Huckle E., Hunt A.R., Hunt S.E., Jekosch K., Johnson C.M., Johnson D.,
RA Kay M.P., Kimberley A.M., King A., Knights A., Laird G.K., Lawlor S.,
RA Lehvaeslaiho M.H., Leversha M.A., Lloyd C., Lloyd D.M., Lovell J.D.,
RA Marsh V.L., Martin S.L., McConnachie L.J., McLay K., McMurray A.A.,
RA Milne S.A., Mistry D., Moore M.J.F., Mullikin J.C., Nickerson T.,
RA Oliver K., Parker A., Patel R., Pearce T.A.V., Peck A.I.,
RA Phillimore B.J.C.T., Prathalingam S.R., Plumb R.W., Ramsay H., Rice C.M.,
RA Ross M.T., Scott C.E., Sehra H.K., Shownkeen R., Sims S., Skuce C.D.,
RA Smith M.L., Soderlund C., Steward C.A., Sulston J.E., Swann R.M.,
RA Sycamore N., Taylor R., Tee L., Thomas D.W., Thorpe A., Tracey A.,
RA Tromans A.C., Vaudin M., Wall M., Wallis J.M., Whitehead S.L.,
RA Whittaker P., Willey D.L., Williams L., Williams S.A., Wilming L.,
RA Wray P.W., Hubbard T., Durbin R.M., Bentley D.R., Beck S., Rogers J.;
RT "The DNA sequence and comparative analysis of human chromosome 20.";
RL Nature 414:865-871(2001).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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 [4]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-39.
RC TISSUE=Saliva;
RX PubMed=16740002; DOI=10.1021/pr050492k;
RA Ramachandran P., Boontheung P., Xie Y., Sondej M., Wong D.T., Loo J.A.;
RT "Identification of N-linked glycoproteins in human saliva by glycoprotein
RT capture and mass spectrometry.";
RL J. Proteome Res. 5:1493-1503(2006).
CC -!- FUNCTION: Performs a specialized role during sperm development and
CC maturation.
CC -!- SUBCELLULAR LOCATION: Secreted.
CC -!- TISSUE SPECIFICITY: Proximal caput region of the epididymis. Lower
CC expression in the testis. Within the testis it is localized to the
CC elongating spermatids, whereas within the epididymis it is exclusively
CC synthesized by the proximal caput epithelium.
CC -!- SIMILARITY: Belongs to the cystatin family. {ECO:0000305}.
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DR EMBL; AF059244; AAC14707.1; -; mRNA.
DR EMBL; AL109954; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC069496; AAH69496.1; -; mRNA.
DR EMBL; BC105113; AAI05114.1; -; mRNA.
DR EMBL; BC105119; AAI05120.1; -; mRNA.
DR CCDS; CCDS13156.1; -.
DR RefSeq; NP_001268659.1; NM_001281730.1.
DR RefSeq; NP_005483.1; NM_005492.3.
DR AlphaFoldDB; O60676; -.
DR SMR; O60676; -.
DR BioGRID; 115358; 48.
DR STRING; 9606.ENSP00000246012; -.
DR MEROPS; I25.027; -.
DR GlyGen; O60676; 2 sites.
DR iPTMnet; O60676; -.
DR PhosphoSitePlus; O60676; -.
DR BioMuta; CST8; -.
DR MassIVE; O60676; -.
DR PaxDb; O60676; -.
DR PeptideAtlas; O60676; -.
DR PRIDE; O60676; -.
DR ProteomicsDB; 49521; -.
DR Antibodypedia; 1474; 235 antibodies from 32 providers.
DR DNASU; 10047; -.
DR Ensembl; ENST00000246012.2; ENSP00000246012.1; ENSG00000125815.9.
DR GeneID; 10047; -.
DR KEGG; hsa:10047; -.
DR MANE-Select; ENST00000246012.2; ENSP00000246012.1; NM_005492.4; NP_005483.1.
DR UCSC; uc002wth.3; human.
DR CTD; 10047; -.
DR DisGeNET; 10047; -.
DR GeneCards; CST8; -.
DR HGNC; HGNC:2480; CST8.
DR HPA; ENSG00000125815; Tissue enriched (testis).
DR MIM; 608683; gene.
DR neXtProt; NX_O60676; -.
DR OpenTargets; ENSG00000125815; -.
DR PharmGKB; PA26981; -.
DR VEuPathDB; HostDB:ENSG00000125815; -.
DR eggNOG; ENOG502T6MT; Eukaryota.
DR GeneTree; ENSGT00940000162294; -.
DR InParanoid; O60676; -.
DR OMA; YFIDVEI; -.
DR OrthoDB; 1565344at2759; -.
DR PhylomeDB; O60676; -.
DR PathwayCommons; O60676; -.
DR BioGRID-ORCS; 10047; 14 hits in 1063 CRISPR screens.
DR GeneWiki; CST8_(gene); -.
DR GenomeRNAi; 10047; -.
DR Pharos; O60676; Tbio.
DR PRO; PR:O60676; -.
DR Proteomes; UP000005640; Chromosome 20.
DR RNAct; O60676; protein.
DR Bgee; ENSG00000125815; Expressed in right testis and 24 other tissues.
DR ExpressionAtlas; O60676; baseline and differential.
DR Genevisible; O60676; HS.
DR GO; GO:0009986; C:cell surface; IBA:GO_Central.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005576; C:extracellular region; IBA:GO_Central.
DR GO; GO:0004869; F:cysteine-type endopeptidase inhibitor activity; TAS:ProtInc.
DR CDD; cd00042; CY; 1.
DR InterPro; IPR000010; Cystatin_dom.
DR InterPro; IPR046350; Cystatin_sf.
DR Pfam; PF00031; Cystatin; 1.
DR SMART; SM00043; CY; 1.
DR SUPFAM; SSF54403; SSF54403; 1.
PE 1: Evidence at protein level;
KW Disulfide bond; Glycoprotein; Protease inhibitor; Reference proteome;
KW Secreted; Signal; Thiol protease inhibitor.
FT SIGNAL 1..21
FT /evidence="ECO:0000255"
FT CHAIN 22..142
FT /note="Cystatin-8"
FT /id="PRO_0000006653"
FT MOTIF 77..81
FT /note="Secondary area of contact"
FT /evidence="ECO:0000255"
FT CARBOHYD 27
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 39
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:16740002"
FT DISULFID 95..105
FT /evidence="ECO:0000250"
FT DISULFID 119..139
FT /evidence="ECO:0000250"
FT VARIANT 52
FT /note="A -> V (in dbSNP:rs35190670)"
FT /id="VAR_061130"
FT VARIANT 142
FT /note="A -> P (in dbSNP:rs1054633)"
FT /id="VAR_014527"
SQ SEQUENCE 142 AA; 16275 MW; 9A3512757E0F4ECD CRC64;
MPRCRWLSLI LLTIPLALVA RKDPKKNETG VLRKLKPVNA SNANVKQCLW FAMQEYNKES
EDKYVFLVVK TLQAQLQVTN LLEYLIDVEI ARSDCRKPLS TNEICAIQEN SKLKRKLSCS
FLVGALPWNG EFTVMEKKCE DA
