Conserved Protein Domain Family
C1_TNS2-like

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cd20826: C1_TNS2-like 
protein kinase C conserved region 1 (C1 domain) found in tensin-2 like (TNS2-like) proteins
The TNS2-like group includes TNS2, and variants of TNS1 and TNS3. Tensin-2 (TNS2), also called C1 domain-containing phosphatase and tensin (C1-TEN), or tensin-like C1 domain-containing phosphatase (TENC1), is an essential component for the maintenance of glomerular basement membrane (GBM) structures. It regulates cell motility and proliferation. It may have phosphatase activity. TNS2 reduces AKT1 phosphorylation, lowers AKT1 kinase activity and interferes with AKT1 signaling. Tensin-1 (TNS1) plays a role in fibrillar adhesion formation. It may be involved in cell migration, cartilage development and in linking signal transduction pathways to the cytoskeleton. Tensin-3 (TNS3), also called tensin-like SH2 domain-containing protein 1 (TENS1), or tumor endothelial marker 6 (TEM6), may play a role in actin remodeling. It is involved in the dissociation of the integrin-tensin-actin complex. Typical TNS1 and TNS3 do not contain C1 domains, but some isoforms/variants do. Members of this family contain an N-terminal region with a zinc finger (C1 domain), a protein tyrosine phosphatase (PTP)-like domain and a protein kinase 2 (C2) domain, and a C-terminal region with SH2 and pTyr binding (PTB) domains. This model corresponds to C1 domain. The C1 domain is a cysteine-rich zinc binding domain that does not bind DNA nor possess structural similarity to conventional zinc finger domains; it contains two separate Zn(2+)-binding sites.
Statistics
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PSSM-Id: 410376
Aligned: 22 rows
Threshold Bit Score: 70.1093
Created: 4-Nov-2019
Updated: 25-Oct-2021
Structure
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Aligned Rows:
 
Zn binding site
Feature 1: Zn binding site [ion binding site], 8 residue positions
Conserved feature residue pattern:H C C C C H C CClick to see conserved feature residue pattern help
Evidence:
  • Comment:Two non-consecutive sets of zinc-binding residues form two separate metal-binding sites.
  • Comment:Based on the structure evidence that Rattus norvegicus ROCK2 binds two Zn2+ ions

Sequence Alignment
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Format: Row Display: Color Bits: Type Selection:
Feature 1           #              #  #             #  #    #  #       #   
Q63HR2         30 EPHSFREKVFRKk-pPVCAVCKVTIDg---TGVSCRVCKVATHRKCEAKVtsaCQAL 82   human
XP_024308847   19 KTHRFKVKTFKKv--KPCGICRQVITq---EGCTCKVCSFSCHRKCQAKVaapCVPP 70   human
BAD92232       29 SLHAFKNKAFKKs--KVCGVCKQIIDg---QGISCRACKYSCHKKCEAKVvipCGVQ 80   human
OAJ32754     1423 MGHFFTNRQYYKp--TDCSICHEALWdtknHGMECTACKMICHKTCRPQVdtsCQDI 1477 Batrachochytrium dendrobatidis JEL423
XP_012557710   65 MLHNFKTRPVNKyapQVCHLCRKMVWn---CTKVCSGCNFTCHVECQPMVlkhCLTL 118  Hydra vulgaris
XP_027043375   73 CDHVFKSDLLAVl--EKCGFCGQEIDs---FGKICEGCNFHCHDKCEKMVkeqCSRQ 124  Pocillopora damicornis
PVD37944        7 LRHQFRLYHFRRp--HTCFVCKQLVLn---QGSACEVCKYICHRKCETQVmttCVPQ 58   Pomacea canaliculata
XP_029639805   94 IVHNFQPHRVVQp--HQCLVCKKIIWn---QGSSCVDCHIICHRKCETEVmttCTPT 145  common octopus
XP_013414683   16 RRHSFKSKQLKKp--KTCEVCRHFIWt---QGSVCKVCKYVCHFQCESQVvtaCNPP 67   Lingula anatina
XP_023214750    8 WEHYFRPAGFRRp--RSCDFCKRMLRd---RGHRCAECLYCCHPDCRPKViapCSPS 59   bark scorpion

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