TEST2_MOUSE
ID TEST2_MOUSE Reviewed; 333 AA.
AC Q80UB0; Q3UKN7;
DT 17-APR-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 119.
DE RecName: Full=Testin-2;
DE Contains:
DE RecName: Full=Testin-1;
DE Flags: Precursor;
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;
RN [1] {ECO:0000305, ECO:0000312|EMBL:AAN63093.1}
RP NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
RC STRAIN=BALB/cJ {ECO:0000312|EMBL:AAN63093.1};
RC TISSUE=Testis {ECO:0000269|PubMed:12606342};
RX PubMed=12606342; DOI=10.1095/biolreprod.102.011205;
RA Cheng C.K., Cheung C.H., Lee W.M.;
RT "Mouse testin: complementary DNA cloning, genomic organization, and
RT characterization of its proximal promoter region.";
RL Biol. Reprod. 68:1376-1386(2003).
RN [2] {ECO:0000312|EMBL:BAE26764.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J {ECO:0000312|EMBL:BAE26764.1};
RC TISSUE=Placenta {ECO:0000312|EMBL:BAE26764.1};
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 [3] {ECO:0000312|EMBL:AAH61218.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=CD-1; TISSUE=Sertoli cell;
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).
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Expressed in testis and ovary. Low level in spleen,
CC epididymis, kidney, and uterus. Expressed in primary cultures of
CC Sertoli cells. {ECO:0000269|PubMed:12606342}.
CC -!- SIMILARITY: Belongs to the peptidase C1 family. {ECO:0000255|PROSITE-
CC ProRule:PRU10089, ECO:0000255|PROSITE-ProRule:PRU10090}.
CC -!- CAUTION: This protein is distinct from Tes/Testin which is a LIM domain
CC protein. {ECO:0000305}.
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DR EMBL; AY146988; AAN63093.1; -; mRNA.
DR EMBL; AK145933; BAE26764.1; -; mRNA.
DR EMBL; BC061218; AAH61218.1; -; mRNA.
DR CCDS; CCDS26583.1; -.
DR RefSeq; NP_835199.1; NM_178098.2.
DR AlphaFoldDB; Q80UB0; -.
DR SMR; Q80UB0; -.
DR BioGRID; 229551; 1.
DR STRING; 10090.ENSMUSP00000089157; -.
DR GlyGen; Q80UB0; 1 site.
DR PaxDb; Q80UB0; -.
DR PRIDE; Q80UB0; -.
DR DNASU; 214639; -.
DR Ensembl; ENSMUST00000091569; ENSMUSP00000089157; ENSMUSG00000050345.
DR GeneID; 214639; -.
DR KEGG; mmu:214639; -.
DR UCSC; uc007qvs.1; mouse.
DR MGI; MGI:1922258; 4930486L24Rik.
DR VEuPathDB; HostDB:ENSMUSG00000050345; -.
DR eggNOG; KOG1543; Eukaryota.
DR GeneTree; ENSGT00940000153321; -.
DR HOGENOM; CLU_012184_1_2_1; -.
DR InParanoid; Q80UB0; -.
DR OMA; IRNQGKC; -.
DR OrthoDB; 1275401at2759; -.
DR PhylomeDB; Q80UB0; -.
DR TreeFam; TF313739; -.
DR Reactome; R-MMU-1474228; Degradation of the extracellular matrix.
DR Reactome; R-MMU-1592389; Activation of Matrix Metalloproteinases.
DR Reactome; R-MMU-1679131; Trafficking and processing of endosomal TLR.
DR Reactome; R-MMU-2022090; Assembly of collagen fibrils and other multimeric structures.
DR Reactome; R-MMU-2132295; MHC class II antigen presentation.
DR Reactome; R-MMU-8939242; RUNX1 regulates transcription of genes involved in differentiation of keratinocytes.
DR BioGRID-ORCS; 214639; 6 hits in 72 CRISPR screens.
DR PRO; PR:Q80UB0; -.
DR Proteomes; UP000000589; Chromosome 13.
DR RNAct; Q80UB0; protein.
DR Bgee; ENSMUSG00000050345; Expressed in ectoplacental cone and 20 other tissues.
DR Genevisible; Q80UB0; MM.
DR GO; GO:0030054; C:cell junction; ISO: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:0043394; F:proteoglycan binding; ISO:MGI.
DR GO; GO:0097655; F:serpin family protein binding; ISO: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:0006508; P:proteolysis; ISO: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: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; IPR025661; Pept_asp_AS.
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; PS00640; THIOL_PROTEASE_ASN; 1.
DR PROSITE; PS00639; THIOL_PROTEASE_HIS; 1.
PE 2: Evidence at transcript level;
KW Disulfide bond; Glycoprotein; Reference proteome; Secreted; Signal.
FT SIGNAL 1..17
FT /evidence="ECO:0000250|UniProtKB:P15242"
FT CHAIN 18..333
FT /note="Testin-2"
FT /id="PRO_0000284681"
FT CHAIN 20..333
FT /note="Testin-1"
FT /id="PRO_0000284682"
FT ACT_SITE 276
FT /evidence="ECO:0000250|UniProtKB:P07711"
FT ACT_SITE 300
FT /evidence="ECO:0000250|UniProtKB:P07711"
FT SITE 138
FT /note="Ancestral active site"
FT CARBOHYD 173
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 135..178
FT /evidence="ECO:0000250|UniProtKB:P07711"
FT DISULFID 169..211
FT /evidence="ECO:0000250|UniProtKB:P07711"
FT DISULFID 269..322
FT /evidence="ECO:0000250|UniProtKB:P07711"
FT CONFLICT 208
FT /note="G -> D (in Ref. 2; BAE26764)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 333 AA; 38090 MW; 2B188C06000555F9 CRC64;
MIAVLFLAIL CLEIDSTAPT LDPSLDVQWN EWRTKHGKAY NVNEERLRRA VWEKNFKMIE
LHNWEYLEGK HDFTMTMNAF GDLTNTEFVK MMTGFRRQKI KRMHVFQDHQ FLYVPKYVDW
RMLGYVTPVK NQGYCASSWA FSATGSLEGQ MFKKTGRLVP LSEQNLLDCM GSNVTHDCSG
GFMQNAFQYV KDNGGLATEE SYPYIGPGRK CRYHAENSAA NVRDFVQIPG REEALMKAVA
KVGPISVAVD ASHDSFQFYD SGIYYEPQCK RVHLNHAVLV VGYGFEGEES DGNSYWLVKN
SWGEEWGMKG YIKIAKDWNN HCGIATLATY PIV
