CAT8_MOUSE
ID CAT8_MOUSE Reviewed; 333 AA.
AC Q9JI81; Q6NV96;
DT 25-OCT-2017, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 151.
DE RecName: Full=Cathepsin 8 {ECO:0000312|MGI:MGI:1860275};
DE EC=3.4.22.- {ECO:0000305};
DE AltName: Full=Cathepsin 2 {ECO:0000303|PubMed:11829493};
DE Flags: Precursor;
GN Name=Cts8 {ECO:0000312|MGI:MGI:1860275};
GN Synonyms=Cts2 {ECO:0000303|PubMed:11829493, ECO:0000312|MGI:MGI:1860275},
GN Epcs68 {ECO:0000303|PubMed:10885754}, Epcs70 {ECO:0000312|EMBL:AAH68241.1};
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090 {ECO:0000312|EMBL:BAC33768.1};
RN [1] {ECO:0000312|EMBL:AAF81277.1}
RP NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RX PubMed=10885754; DOI=10.1006/dbio.2000.9705;
RA Hemberger M., Himmelbauer H., Ruschmann J., Zeitz C., Fundele R.;
RT "cDNA subtraction cloning reveals novel genes whose temporal and spatial
RT expression indicates association with trophoblast invasion.";
RL Dev. Biol. 222:158-169(2000).
RN [2] {ECO:0000312|EMBL:AAK00509.1}
RP NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RC STRAIN=C57BL/6J {ECO:0000312|EMBL:AAK00509.1};
RC TISSUE=Placenta {ECO:0000312|EMBL:AAK00509.1};
RX PubMed=11829493; DOI=10.1006/geno.2002.6696;
RA Deussing J., Kouadio M., Rehman S., Werber I., Schwinde A., Peters C.;
RT "Identification and characterization of a dense cluster of placenta-
RT specific cysteine peptidase genes and related genes on mouse chromosome
RT 13.";
RL Genomics 79:225-240(2002).
RN [3] {ECO:0000312|EMBL:BAC33768.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J {ECO:0000312|EMBL:BAC33768.1};
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [4] {ECO:0000312|Proteomes:UP000000589}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J {ECO:0000312|Proteomes:UP000000589};
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [5] {ECO:0000312|EMBL:EDL41315.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [6] {ECO:0000312|EMBL:AAH68241.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Embryo;
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 [7] {ECO:0000305}
RP FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND DEVELOPMENTAL
RP STAGE.
RX PubMed=18776147; DOI=10.1242/dev.025627;
RA Screen M., Dean W., Cross J.C., Hemberger M.;
RT "Cathepsin proteases have distinct roles in trophoblast function and
RT vascular remodelling.";
RL Development 135:3311-3320(2008).
CC -!- FUNCTION: Probable protease (By similarity). In placenta, plays a role
CC in promoting giant cell differentiation (PubMed:18776147). Also plays a
CC role in placental spiral artery remodeling by direct degradation of
CC smooth muscle alpha-actin (PubMed:18776147).
CC {ECO:0000250|UniProtKB:O60911, ECO:0000269|PubMed:18776147}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:18776147}. Lysosome
CC {ECO:0000269|PubMed:18776147}. Endosome {ECO:0000269|PubMed:18776147}.
CC Note=Localizes to the cytoplasm with a punctate staining pattern
CC indicative of a predominant lysosomal and endosomal localization.
CC {ECO:0000269|PubMed:18776147}.
CC -!- TISSUE SPECIFICITY: Expressed in placenta (PubMed:11829493,
CC PubMed:10885754, PubMed:18776147). Highly expressed in a subset of
CC trophoblast giant cells in the parietal yolk sac and at the outside of
CC the ectoplacental cone (PubMed:10885754). Expressed at highest level in
CC liver with lesser amounts in testis, kidney, heart, lung and brain
CC (PubMed:10885754). Not detected in spleen and skeletal muscle
CC (PubMed:10885754, PubMed:11829493). Not detected in blood, heart,
CC brain, testis, liver, lung, kidney, thymus or uterus (PubMed:11829493).
CC {ECO:0000269|PubMed:10885754, ECO:0000269|PubMed:11829493,
CC ECO:0000269|PubMed:18776147}.
CC -!- DEVELOPMENTAL STAGE: Detected from 5.5 dpc in parietal trophoblast
CC giant cells (PubMed:18776147, PubMed:10885754). Detected at 8.5 dpc in
CC placenta, and shows increased expression level from 13.5 to 19.5 dpc
CC (PubMed:11829493). {ECO:0000269|PubMed:10885754,
CC ECO:0000269|PubMed:11829493, ECO:0000269|PubMed:18776147}.
CC -!- SIMILARITY: Belongs to the peptidase C1 family. {ECO:0000305}.
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DR EMBL; AF250840; AAF81277.1; -; mRNA.
DR EMBL; AY014780; AAK00509.1; -; mRNA.
DR EMBL; AK049474; BAC33768.1; -; mRNA.
DR EMBL; AC116797; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH466546; EDL41315.1; -; Genomic_DNA.
DR EMBL; BC068241; AAH68241.1; -; mRNA.
DR CCDS; CCDS26587.1; -.
DR RefSeq; NP_062414.3; NM_019541.3.
DR AlphaFoldDB; Q9JI81; -.
DR SMR; Q9JI81; -.
DR STRING; 10090.ENSMUSP00000021891; -.
DR MEROPS; C01.031; -.
DR GlyGen; Q9JI81; 2 sites.
DR MaxQB; Q9JI81; -.
DR PaxDb; Q9JI81; -.
DR PRIDE; Q9JI81; -.
DR ProteomicsDB; 265445; -.
DR DNASU; 56094; -.
DR Ensembl; ENSMUST00000021891; ENSMUSP00000021891; ENSMUSG00000057446.
DR GeneID; 56094; -.
DR KEGG; mmu:56094; -.
DR UCSC; uc007qwg.2; mouse.
DR CTD; 56094; -.
DR MGI; MGI:1860275; Cts8.
DR VEuPathDB; HostDB:ENSMUSG00000057446; -.
DR eggNOG; KOG1543; Eukaryota.
DR GeneTree; ENSGT00940000153321; -.
DR HOGENOM; CLU_012184_1_2_1; -.
DR InParanoid; Q9JI81; -.
DR OMA; FNEREGT; -.
DR OrthoDB; 1275401at2759; -.
DR PhylomeDB; Q9JI81; -.
DR TreeFam; TF313739; -.
DR BioGRID-ORCS; 56094; 3 hits in 71 CRISPR screens.
DR ChiTaRS; Cts8; mouse.
DR PRO; PR:Q9JI81; -.
DR Proteomes; UP000000589; Chromosome 13.
DR RNAct; Q9JI81; protein.
DR Bgee; ENSMUSG00000057446; Expressed in ectoplacental cone and 2 other tissues.
DR Genevisible; Q6NV96; MM.
DR GO; GO:0005576; C:extracellular region; IDA:MGI.
DR GO; GO:0005615; C:extracellular space; ISO:MGI.
DR GO; GO:0005794; C:Golgi apparatus; ISO:MGI.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; ISO:MGI.
DR GO; GO:0005764; C:lysosome; ISO:MGI.
DR GO; GO:0005771; C:multivesicular body; ISO:MGI.
DR GO; GO:0005886; C:plasma membrane; ISO:MGI.
DR GO; GO:0005518; F:collagen binding; ISO:MGI.
DR GO; GO:0004197; F:cysteine-type endopeptidase activity; ISO:MGI.
DR GO; GO:0008234; F:cysteine-type peptidase activity; ISO:MGI.
DR GO; GO:0001968; F:fibronectin binding; ISO:MGI.
DR GO; GO:0042393; F:histone binding; ISO:MGI.
DR GO; GO:0008233; F:peptidase activity; ISA:MGI.
DR GO; GO:0043394; F:proteoglycan binding; ISO:MGI.
DR GO; GO:0097655; F:serpin family protein binding; ISO:MGI.
DR GO; GO:0001974; P:blood vessel remodeling; IMP:MGI.
DR GO; GO:0030574; P:collagen catabolic process; ISO:MGI.
DR GO; GO:0039654; P:fusion of virus membrane with host endosome membrane; ISO:MGI.
DR GO; GO:0019064; P:fusion of virus membrane with host plasma membrane; ISO:MGI.
DR GO; GO:0006955; P:immune response; IBA:GO_Central.
DR GO; GO:0016540; P:protein autoprocessing; ISO:MGI.
DR GO; GO:0030163; P:protein catabolic process; IMP:MGI.
DR GO; GO:0006508; P:proteolysis; ISA:MGI.
DR GO; GO:0051603; P:proteolysis involved in protein catabolic process; ISO:MGI.
DR GO; GO:0019065; P:receptor-mediated endocytosis of virus by host cell; ISO:MGI.
DR GO; GO:0060707; P:trophoblast giant cell differentiation; IMP:MGI.
DR GO; GO:0046718; P:viral entry into host cell; ISO:MGI.
DR GO; GO:0031638; P:zymogen activation; ISO:MGI.
DR CDD; cd02248; Peptidase_C1A; 1.
DR InterPro; IPR038765; Papain-like_cys_pep_sf.
DR InterPro; IPR025660; Pept_his_AS.
DR InterPro; IPR000668; Peptidase_C1A_C.
DR InterPro; IPR039417; Peptidase_C1A_papain-like.
DR InterPro; IPR013201; Prot_inhib_I29.
DR Pfam; PF08246; Inhibitor_I29; 1.
DR Pfam; PF00112; Peptidase_C1; 1.
DR PRINTS; PR00705; PAPAIN.
DR SMART; SM00848; Inhibitor_I29; 1.
DR SMART; SM00645; Pept_C1; 1.
DR SUPFAM; SSF54001; SSF54001; 1.
DR PROSITE; PS00639; THIOL_PROTEASE_HIS; 1.
PE 2: Evidence at transcript level;
KW Disulfide bond; Endosome; Glycoprotein; Hydrolase; Lysosome; Protease;
KW Reference proteome; Secreted; Signal; Thiol protease; Zymogen.
FT SIGNAL 1..20
FT /evidence="ECO:0000255"
FT PROPEP 21..113
FT /note="Activation peptide"
FT /evidence="ECO:0000255"
FT /id="PRO_0000442172"
FT CHAIN 114..333
FT /note="Cathepsin 8"
FT /id="PRO_5008452492"
FT ACT_SITE 138
FT /evidence="ECO:0000250|UniProtKB:O60911"
FT ACT_SITE 276
FT /evidence="ECO:0000250|UniProtKB:O60911"
FT ACT_SITE 300
FT /evidence="ECO:0000250|UniProtKB:O60911"
FT CARBOHYD 39
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 72
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 135..178
FT /evidence="ECO:0000250|UniProtKB:O60911"
FT DISULFID 169..211
FT /evidence="ECO:0000250|UniProtKB:O60911"
FT DISULFID 269..322
FT /evidence="ECO:0000250|UniProtKB:O60911"
FT CONFLICT 14
FT /note="V -> A (in Ref. 6; AAH68241)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 333 AA; 37803 MW; 57648FD720A9614E CRC64;
MGPAVLLAIL CLGVAEVTQS SDPSLDSEWQ EWKRKFNKNY SMEEEGQKRA VWEENMKLVK
QHNIEYDQGK KNFTMDVNAF GDMTGEEYRK MLTDIPVPNF RKKKSIHQPI AGYLPKFVDW
RKRGCVTPVK NQGTCNSCWA FSAAGAIEGQ MFRKTGKLVP LSTQNLVDCS RLEGNFGCFK
GSTFLALKYV WKNRGLEAES TYPYKGTDGH CRYHPERSAA RITSFSFVSN SEKDLMRAVA
TIGPISVGID ARHKSFRLYR EGIYYEPKCS SNIINHSVLV VGYGYEGKES DGNKYWLIKN
SHGEQWGMNG YMKLARGRNN HCGIASYAVY PRV
