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Protein

Testin-2

Gene

Testin

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei138 – 1381Ancestral active site
Active sitei276 – 2761By similarity
Active sitei300 – 3001By similarity

GO - Molecular functioni

Complete GO annotation...

Enzyme and pathway databases

ReactomeiR-RNO-1442490. Collagen degradation.
R-RNO-1474228. Degradation of the extracellular matrix.
R-RNO-1679131. Trafficking and processing of endosomal TLR.
R-RNO-2022090. Assembly of collagen fibrils and other multimeric structures.
R-RNO-2132295. MHC class II antigen presentation.

Protein family/group databases

MEROPSiC01.972.

Names & Taxonomyi

Protein namesi
Recommended name:
Testin-2
Alternative name(s):
CMB-23
Cleaved into the following chain:
Alternative name(s):
CMB-22
Gene namesi
Name:Testin
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Chromosome 17

Organism-specific databases

RGDi708447. Testin.

Subcellular locationi

GO - Cellular componenti

  • cell junction Source: RGD
  • extracellular region Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 17171 PublicationAdd
BLAST
Chaini18 – 333316Testin-2PRO_0000026291Add
BLAST
Chaini20 – 333314Testin-1PRO_0000026292Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi135 ↔ 178By similarity
Disulfide bondi169 ↔ 211By similarity
Glycosylationi173 – 1731N-linked (GlcNAc...)Sequence analysis
Disulfide bondi269 ↔ 322By similarity

Keywords - PTMi

Disulfide bond, Glycoprotein

Proteomic databases

PaxDbiP15242.
PRIDEiP15242.

Expressioni

Tissue specificityi

Sertoli cells.

Gene expression databases

GenevisibleiP15242. RN.

Interactioni

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000024467.

Structurei

3D structure databases

ProteinModelPortaliP15242.
SMRiP15242. Positions 20-333.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the peptidase C1 family.PROSITE-ProRule annotation

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiKOG1543. Eukaryota.
COG4870. LUCA.
GeneTreeiENSGT00760000118871.
HOGENOMiHOG000230774.
HOVERGENiHBG011513.
InParanoidiP15242.
OMAiNEEFLAY.
OrthoDBiEOG786H3P.
PhylomeDBiP15242.
TreeFamiTF313739.

Family and domain databases

InterProiIPR025661. Pept_asp_AS.
IPR025660. Pept_his_AS.
IPR013128. Peptidase_C1A.
IPR000668. Peptidase_C1A_C.
IPR013201. Prot_inhib_I29.
[Graphical view]
PANTHERiPTHR12411. PTHR12411. 1 hit.
PfamiPF08246. Inhibitor_I29. 1 hit.
PF00112. Peptidase_C1. 1 hit.
[Graphical view]
PRINTSiPR00705. PAPAIN.
SMARTiSM00848. Inhibitor_I29. 1 hit.
SM00645. Pept_C1. 1 hit.
[Graphical view]
PROSITEiPS00640. THIOL_PROTEASE_ASN. 1 hit.
PS00639. THIOL_PROTEASE_HIS. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P15242-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MIAVLFLAIL CLEVDSTAPT PDPSLDVEWN EWRTKHGKTY NMNEERLKRA
60 70 80 90 100
VWEKNFKMIE LHNWEYLEGR HDFTMAMNAF GDLTNIEFVK MMTGFQRQKI
110 120 130 140 150
KKTHIFQDHQ FLYVPKRVDW RQLGYVTPVK NQGHCASSWA FSATGSLEGQ
160 170 180 190 200
MFRKTERLIP LSEQNLLDCM GSNVTHGCSG GFMQYAFQYV KDNGGLATEE
210 220 230 240 250
SYPYRGQGRE CRYHAENSAA NVRDFVQIPG SEEALMKAVA KVGPISVAVD
260 270 280 290 300
ASHGSFQFYG SGIYYEPQCK RVHLNHAVLV VGYGFEGEES DGNSFWLVKN
310 320 330
SWGEEWGMKG YMKLAKDWSN HCGIATYSTY PIV
Length:333
Mass (Da):38,033
Last modified:November 1, 1995 - v2
Checksum:iB4426BD8B2B66A2E
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U16858 mRNA. Translation: AAC52162.1.
PIRiI52525.
PC1251.
RefSeqiNP_775155.1. NM_173132.2.
XP_008769650.1. XM_008771428.1.
UniGeneiRn.10029.

Genome annotation databases

EnsembliENSRNOT00000024467; ENSRNOP00000024467; ENSRNOG00000018028.
GeneIDi286916.
KEGGirno:286916.
UCSCiRGD:708447. rat.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U16858 mRNA. Translation: AAC52162.1.
PIRiI52525.
PC1251.
RefSeqiNP_775155.1. NM_173132.2.
XP_008769650.1. XM_008771428.1.
UniGeneiRn.10029.

3D structure databases

ProteinModelPortaliP15242.
SMRiP15242. Positions 20-333.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000024467.

Protein family/group databases

MEROPSiC01.972.

Proteomic databases

PaxDbiP15242.
PRIDEiP15242.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSRNOT00000024467; ENSRNOP00000024467; ENSRNOG00000018028.
GeneIDi286916.
KEGGirno:286916.
UCSCiRGD:708447. rat.

Organism-specific databases

CTDi286916.
RGDi708447. Testin.

Phylogenomic databases

eggNOGiKOG1543. Eukaryota.
COG4870. LUCA.
GeneTreeiENSGT00760000118871.
HOGENOMiHOG000230774.
HOVERGENiHBG011513.
InParanoidiP15242.
OMAiNEEFLAY.
OrthoDBiEOG786H3P.
PhylomeDBiP15242.
TreeFamiTF313739.

Enzyme and pathway databases

ReactomeiR-RNO-1442490. Collagen degradation.
R-RNO-1474228. Degradation of the extracellular matrix.
R-RNO-1679131. Trafficking and processing of endosomal TLR.
R-RNO-2022090. Assembly of collagen fibrils and other multimeric structures.
R-RNO-2132295. MHC class II antigen presentation.

Miscellaneous databases

PROiP15242.

Gene expression databases

GenevisibleiP15242. RN.

Family and domain databases

InterProiIPR025661. Pept_asp_AS.
IPR025660. Pept_his_AS.
IPR013128. Peptidase_C1A.
IPR000668. Peptidase_C1A_C.
IPR013201. Prot_inhib_I29.
[Graphical view]
PANTHERiPTHR12411. PTHR12411. 1 hit.
PfamiPF08246. Inhibitor_I29. 1 hit.
PF00112. Peptidase_C1. 1 hit.
[Graphical view]
PRINTSiPR00705. PAPAIN.
SMARTiSM00848. Inhibitor_I29. 1 hit.
SM00645. Pept_C1. 1 hit.
[Graphical view]
PROSITEiPS00640. THIOL_PROTEASE_ASN. 1 hit.
PS00639. THIOL_PROTEASE_HIS. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. "Rat testin is a newly identified component of the junctional complexes in various tissues whose mRNA is predominantly expressed in the testis and ovary."
    Grima J., Zhu L., Zong S.D., Catterall J.F., Bardin C.W., Cheng C.Y.
    Biol. Reprod. 52:340-355(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Testis.
  2. "Testins are structurally related Sertoli cell proteins whose secretion is tightly coupled to the presence of germ cells."
    Cheng C.Y., Grima J., Stahler M.S., Lockshin R.A.
    J. Biol. Chem. 264:21386-21393(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 18-49.
    Strain: Sprague-Dawley.
    Tissue: Sertoli cell.
  3. "Testins are structurally related to the mouse cysteine proteinase precursor but devoid of any protease/anti-protease activity."
    Cheng C.Y., Morris I., Bardin C.W.
    Biochem. Biophys. Res. Commun. 191:224-231(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: LACK OF PROTEASE ACTIVITY.

Entry informationi

Entry nameiTEST2_RAT
AccessioniPrimary (citable) accession number: P15242
Secondary accession number(s): P15243
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 1, 1990
Last sequence update: November 1, 1995
Last modified: June 8, 2016
This is version 118 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Caution

This protein is distinct from Tes/Testin which is a LIM domain protein.Curated

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Peptidase families
    Classification of peptidase families and list of entries
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.