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 13-FEB-2019, entry version 150. 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; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; 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., RA Beasley O.P., Bird C.P., Blakey S.E., Bridgeman A.M., Brown A.J., RA Buck D., Burrill W.D., Butler A.P., Carder C., Carter N.P., RA Chapman J.C., Clamp M., Clark G., Clark L.N., Clark S.Y., Clee C.M., RA Clegg S., Cobley V.E., Collier R.E., Connor R.E., Corby N.R., RA Coulson A., Coville G.J., Deadman R., Dhami P.D., Dunn M., RA 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., RA Rice C.M., Ross M.T., Scott C.E., Sehra H.K., Shownkeen R., Sims S., RA Skuce C.D., Smith M.L., Soderlund C., Steward C.A., Sulston J.E., RA Swann R.M., Sycamore N., Taylor R., Tee L., Thomas D.W., Thorpe A., RA Tracey A., Tromans A.C., Vaudin M., Wall M., Wallis J.M., RA Whitehead S.L., Whittaker P., Willey D.L., Williams L., Williams S.A., RA Wilming L., Wray P.W., Hubbard T., Durbin R.M., Bentley D.R., Beck S., RA 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 RT project: 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., RA Loo J.A.; RT "Identification of N-linked glycoproteins in human saliva by RT glycoprotein 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 CC exclusively synthesized by the proximal caput epithelium. CC -!- SIMILARITY: Belongs to the cystatin family. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC ----------------------------------------------------------------------- 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 UniGene; Hs.121602; -. DR ProteinModelPortal; O60676; -. DR SMR; O60676; -. DR BioGrid; 115358; 35. DR STRING; 9606.ENSP00000246012; -. DR MEROPS; I25.027; -. DR iPTMnet; O60676; -. DR PhosphoSitePlus; O60676; -. DR BioMuta; CST8; -. DR PaxDb; O60676; -. DR PeptideAtlas; O60676; -. DR PRIDE; O60676; -. DR ProteomicsDB; 49521; -. DR DNASU; 10047; -. DR Ensembl; ENST00000246012; ENSP00000246012; ENSG00000125815. DR GeneID; 10047; -. DR KEGG; hsa:10047; -. DR UCSC; uc002wth.3; human. DR CTD; 10047; -. DR DisGeNET; 10047; -. DR EuPathDB; HostDB:ENSG00000125815.8; -. DR GeneCards; CST8; -. DR HGNC; HGNC:2480; CST8. DR MIM; 608683; gene. DR neXtProt; NX_O60676; -. DR OpenTargets; ENSG00000125815; -. DR PharmGKB; PA26981; -. DR eggNOG; ENOG410IXH4; Eukaryota. DR eggNOG; ENOG41113F6; LUCA. DR GeneTree; ENSGT00940000162294; -. DR HOGENOM; HOG000231754; -. DR HOVERGEN; HBG095685; -. DR InParanoid; O60676; -. DR KO; K13904; -. DR OMA; KQCLWFA; -. DR OrthoDB; 1565344at2759; -. DR PhylomeDB; O60676; -. DR GeneWiki; CST8_(gene); -. DR GenomeRNAi; 10047; -. DR PRO; PR:O60676; -. DR Proteomes; UP000005640; Chromosome 20. DR Bgee; ENSG00000125815; Expressed in 12 organ(s), highest expression level in right testis. DR ExpressionAtlas; O60676; baseline and differential. DR Genevisible; O60676; HS. DR GO; GO:0009986; C:cell surface; IEA:Ensembl. DR GO; GO:0005737; C:cytoplasm; IEA:Ensembl. DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell. DR GO; GO:0004869; F:cysteine-type endopeptidase inhibitor activity; TAS:ProtInc. DR CDD; cd00042; CY; 1. DR InterPro; IPR027214; Cystatin. DR InterPro; IPR000010; Cystatin_dom. DR PANTHER; PTHR11413; PTHR11413; 1. DR Pfam; PF00031; Cystatin; 1. DR SMART; SM00043; CY; 1. PE 1: Evidence at protein level; KW Complete proteome; Disulfide bond; Glycoprotein; Polymorphism; KW Protease inhibitor; Reference proteome; Secreted; Signal; KW Thiol protease inhibitor. FT SIGNAL 1 21 {ECO:0000255}. FT CHAIN 22 142 Cystatin-8. FT /FTId=PRO_0000006653. FT MOTIF 77 81 Secondary area of contact. {ECO:0000255}. FT CARBOHYD 27 27 N-linked (GlcNAc...) asparagine. FT {ECO:0000255}. FT CARBOHYD 39 39 N-linked (GlcNAc...) asparagine. FT {ECO:0000269|PubMed:16740002}. FT DISULFID 95 105 {ECO:0000250}. FT DISULFID 119 139 {ECO:0000250}. FT VARIANT 52 52 A -> V (in dbSNP:rs35190670). FT /FTId=VAR_061130. FT VARIANT 142 142 A -> P (in dbSNP:rs1054633). FT /FTId=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 //