Conserved Protein Domain Family
EFh_SPARC_TICN

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cd16232: EFh_SPARC_TICN 
EF-hand, extracellular calcium-binding (EC) motif, found in testicans
Testicans are nervous system-expressed proteoglycans that play important roles in the regulation of protease activity, as well as in the determination of age at menarche. Testican-1 (TICN1, also termed protein SPOCK) is a secreted chimeric proteoglycan that is highly expressed in brain and carries both chondroitin and heparan sulfate glycosaminoglycan side chains. It has been implicated in autoimmune disease. It also acts as a regulator of bone morphogenetic protein (BMP) signaling and show critical functions in the nervous system. Testican-2 (TICN2, also termed protein SPOCK2) is an extracellular heparan sulphate proteoglycan highly expressed in brain. It may play regulatory roles in the development of the central nervous system. It also participates in diverse steps of neurogenesis. TICN1, but not TICN2, inhibits cathepsin L. TICN1 also inhibits attachment and neurite outgrowth in cultures of N2A neuroblastoma cells, While TICN2 is able to inhibit neurite outgrowth from primary cerebellar cells. Testicans contain an N-terminal signal peptide, a testican-specific domain followed by a follistatin-like (FS) domain, an extracellular calcium-binding (EC) domain including a pair of EF hands, a thyroglobulin-like domain (TY), and a C-terminal region with two putative glycosaminoglycan attachment sites. The substitution of a ligating Asp residue by Tyr orTyr in the +Y position of EF hand 2 in testican-2 could prevent Ca2+ binding to this site and also cause EF-hand 1 to bind one Ca2+ with low affinity. The substitution of a ligating Asp residue by Phe or Tyr in the +Y position of EF-hand 2 in testicans could prevent Ca2+ binding to this site and also cause EF-hand 1 to bind one Ca2+ ion with low affinity.
Statistics
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PSSM-Id: 320011
View PSSM: cd16232
Aligned: 14 rows
Threshold Bit Score: 148.287
Threshold Setting Gi: 560126870
Created: 18-Nov-2014
Updated: 18-Aug-2016
Structure
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Aligned Rows:
 
Feature 1:putative Ca binding site [ion binding site]
Evidence:
  • Comment:Based on the structure evidence how the first EF-hand motif in Homo sapiens SPARC (1SRA) binds Ca2+ ion.
  • Comment:Unlike other members in SPARC family, the substitution of a ligating Asp residue in the +Y position of EF hand 2 in testicans could prevent Ca2+ binding to this site and also cause EF-hand 1 to bind one Ca2+ with low affinity.
  • Citation:PMID 8119487
  • Citation:PMID 9323035

Sequence Alignment
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Format: Row Display: Color Bits: Type Selection:
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
Feature 1                                                                            #   #      #
gi 24212500  199 CTGQDLADLGDRLRDWFQLLHENSKqngsassvagp---------asgldkslgasCKDSIGWMFSKLDTSADLFLDQTE 269
gi 524872404 197 CTTSEFSQMRTRMMGWFHLLHGQDHlakkqagnikhfhkhvsvkkelrehdgnrceCFKSAMWQFNQMDKNGDDHLNEFE 276
gi 675383903 175 CNENELKAMGDRLLDWFSVVMADHRrgqsrrrsf-------------rlshtqlpdCKPEVSWMFQHLDTDGDLKLSLQE 241
gi 669327419 154 CTEKQLVTIEDLLVRWFTSLRMQSTnaeavsl------------------pkhhirCQPDVGWMFAQLDGNHDGHLEHDE 215
gi 541041205 115 CGEQELHRIGGRLLQWFIEMHKVSGadvevss------------------qkrdveCRPDVAWMFEQWDGNNDGELSVKE 176
gi 560126870  85 CSHAELISMGGRLLQWFSDMHRIHTgrektl-------------------pahkiaCRNDVAWMFEQWDGDNDGLLSKDE 145
gi 373219462  40 CTRSELMRMGGRLVKWFKDVHAQESgadhtl-------------------klhsvpCRVEVGWMFNQWDGNQDGKLSKAE 100
gi 229290057 113 CSTEELEDMGNRLLEWFKVLRKNEEkekpdtn------------------knvqicYEPAVGWMFSKLDVNFDLFLSKKE 174
gi 442620572 428 CKPQQLTAIGNRLLDWFSVIMADSKkrrqhsqk---------------skahfppaCKTEAKWMFGHLDLNNDGQLSLQE 492
gi 67473703  201 CSDLEFREVANRLRDWFKALHESGSqnkktktllrpe--------rsrfdtsilpiCKDSLGWMFNRLDTNYDLLLDQSE 272
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
Feature 1                                                   
gi 24212500  270 LAAINLDKYEVCIRPFFNSC--DTYKDGRVSTAEWCFCFWREK 310
gi 524872404 277 MSVMEENSMEPCMRPYLTSC--DRNADGKLSSDEWCCCFANVV 317
gi 675383903 242 LYDLENDDQEHCLRPYLLDC--DVERDLVLSPYEWCSCFDKSQ 282
gi 669327419 216 LYTLDHEKYKNCIHHFLDQC--DLNQDAQLSLDEWCDCFEWAG 256
gi 541041205 177 LAPLESDANEKCLKAFIDRCdtDPGNDDVITLEEWCDCFAWAD 219
gi 560126870 146 LMPLEGNGRESCLAQFIDMCd-DMVVDGQISVDEWCDCFSFAD 187
gi 373219462 101 LRPIERGGNEACVEEFIDMCd-DMVVDGSISVDEWCDCFTFSD 142
gi 229290057 175 LSLIEYDEYEHCITPFIDRC--DRIKDGILSANEWCSCFEEAS 215
gi 442620572 493 MYDLEHDQNERCIKPFIDTC--DLDTDSSINTREWCRCFEKTD 533
gi 67473703  273 LRSIYLDKNEQCTKAFFNSC--DTYKDSLISNNEWCYCFQRQQ 313

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