TEST2_RAT
ID TEST2_RAT Reviewed; 333 AA.
AC P15242; P15243;
DT 01-APR-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 2.
DT 03-AUG-2022, entry version 150.
DE RecName: Full=Testin-2;
DE AltName: Full=CMB-23;
DE Contains:
DE RecName: Full=Testin-1;
DE AltName: Full=CMB-22;
DE Flags: Precursor;
GN Name=Testin;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Testis;
RX PubMed=7711203; DOI=10.1095/biolreprod52.2.340;
RA Grima J., Zhu L., Zong S.D., Catterall J.F., Bardin C.W., Cheng C.Y.;
RT "Rat testin is a newly identified component of the junctional complexes in
RT various tissues whose mRNA is predominantly expressed in the testis and
RT ovary.";
RL Biol. Reprod. 52:340-355(1995).
RN [2]
RP PROTEIN SEQUENCE OF 18-49.
RC STRAIN=Sprague-Dawley; TISSUE=Sertoli cell;
RX PubMed=2592382; DOI=10.1016/s0021-9258(19)30092-4;
RA Cheng C.Y., Grima J., Stahler M.S., Lockshin R.A.;
RT "Testins are structurally related Sertoli cell proteins whose secretion is
RT tightly coupled to the presence of germ cells.";
RL J. Biol. Chem. 264:21386-21393(1989).
RN [3]
RP LACK OF PROTEASE ACTIVITY.
RX PubMed=8447824; DOI=10.1006/bbrc.1993.1206;
RA Cheng C.Y., Morris I., Bardin C.W.;
RT "Testins are structurally related to the mouse cysteine proteinase
RT precursor but devoid of any protease/anti-protease activity.";
RL Biochem. Biophys. Res. Commun. 191:224-231(1993).
CC -!- SUBCELLULAR LOCATION: Secreted.
CC -!- TISSUE SPECIFICITY: Sertoli cells.
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; U16858; AAC52162.1; -; mRNA.
DR PIR; I52525; I52525.
DR PIR; PC1251; PC1251.
DR RefSeq; NP_775155.1; NM_173132.2.
DR RefSeq; XP_008769650.1; XM_008771428.2.
DR AlphaFoldDB; P15242; -.
DR SMR; P15242; -.
DR STRING; 10116.ENSRNOP00000024467; -.
DR MEROPS; C01.972; -.
DR GlyGen; P15242; 1 site.
DR PaxDb; P15242; -.
DR Ensembl; ENSRNOT00000024467; ENSRNOP00000024467; ENSRNOG00000018028.
DR GeneID; 286916; -.
DR KEGG; rno:286916; -.
DR UCSC; RGD:708447; rat.
DR CTD; 286916; -.
DR RGD; 708447; Testin.
DR eggNOG; KOG1543; Eukaryota.
DR GeneTree; ENSGT00940000153321; -.
DR HOGENOM; CLU_012184_1_2_1; -.
DR InParanoid; P15242; -.
DR OMA; SIRGHED; -.
DR OrthoDB; 1275401at2759; -.
DR PhylomeDB; P15242; -.
DR TreeFam; TF313739; -.
DR Reactome; R-RNO-1474228; Degradation of the extracellular matrix.
DR Reactome; R-RNO-1592389; Activation of Matrix Metalloproteinases.
DR Reactome; R-RNO-1679131; Trafficking and processing of endosomal TLR.
DR Reactome; R-RNO-2022090; Assembly of collagen fibrils and other multimeric structures.
DR Reactome; R-RNO-2132295; MHC class II antigen presentation.
DR Reactome; R-RNO-8939242; RUNX1 regulates transcription of genes involved in differentiation of keratinocytes.
DR PRO; PR:P15242; -.
DR Proteomes; UP000002494; Chromosome 17.
DR Bgee; ENSRNOG00000018028; Expressed in ovary and 6 other tissues.
DR Genevisible; P15242; RN.
DR GO; GO:0030054; C:cell junction; IDA:RGD.
DR GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR GO; GO:0005764; C:lysosome; IBA:GO_Central.
DR GO; GO:0004197; F:cysteine-type endopeptidase activity; IBA:GO_Central.
DR GO; GO:0006955; P:immune response; IBA:GO_Central.
DR GO; GO:0051603; P:proteolysis involved in protein catabolic process; IBA:GO_Central.
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 1: Evidence at protein level;
KW Direct protein sequencing; Disulfide bond; Glycoprotein;
KW Reference proteome; Secreted; Signal.
FT SIGNAL 1..17
FT /evidence="ECO:0000269|PubMed:2592382"
FT CHAIN 18..333
FT /note="Testin-2"
FT /id="PRO_0000026291"
FT CHAIN 20..333
FT /note="Testin-1"
FT /id="PRO_0000026292"
FT ACT_SITE 276
FT /evidence="ECO:0000250"
FT ACT_SITE 300
FT /evidence="ECO:0000250"
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"
FT DISULFID 169..211
FT /evidence="ECO:0000250"
FT DISULFID 269..322
FT /evidence="ECO:0000250"
SQ SEQUENCE 333 AA; 38033 MW; B4426BD8B2B66A2E CRC64;
MIAVLFLAIL CLEVDSTAPT PDPSLDVEWN EWRTKHGKTY NMNEERLKRA VWEKNFKMIE
LHNWEYLEGR HDFTMAMNAF GDLTNIEFVK MMTGFQRQKI KKTHIFQDHQ FLYVPKRVDW
RQLGYVTPVK NQGHCASSWA FSATGSLEGQ MFRKTERLIP LSEQNLLDCM GSNVTHGCSG
GFMQYAFQYV KDNGGLATEE SYPYRGQGRE CRYHAENSAA NVRDFVQIPG SEEALMKAVA
KVGPISVAVD ASHGSFQFYG SGIYYEPQCK RVHLNHAVLV VGYGFEGEES DGNSFWLVKN
SWGEEWGMKG YMKLAKDWSN HCGIATYSTY PIV
