Conserved Protein Domain Family
EFh_SPARC_SPARCL1

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cd16236: EFh_SPARC_SPARCL1 
EF-hand, extracellular calcium-binding (EC) motif, found in secreted protein, acidic and rich in cysteine-like 1 (SPARCL1)
SPARCL1, also termed SPARC-like protein 1, or high endothelial venule protein (Hevin), or MAST 9, or SC-1, or RAGS-1, or QR1, or ECM 2, is a diversely expressed and developmentally regulated extracellular matrix glycoprotein involved in tissue repair and remodeling via interaction with the surrounding extracellular matrix (ECM) proteins. It plays a pivotal role in the corneal wound healing. SPARCL1 may function as both a tumor suppressor and as a regulator of angiogenesis. It regulates cell migration/invasion and suppresses metastasis in many cancers, including prostate cancer, colorectal cancer, gastric cancer, and breast cancer. It can bind to collagens and be counter-adhesive to wild-type dermal fibroblasts, but do not influence rates of cell proliferation. Moreover, SPARCL1 contributes to neural development and participates in remodeling events associated with neuronal degeneration following neural injury. It can influence central nervous system (CNS) development and synaptic rearrangement. SPARCL1 is the closest family member to secreted protein acidic and rich in cysteine (SPARC), but does not compensate for the absence of SPARC in the CNS. SPARC contains an N-terminal acidic 52-residue segment followed by a follistatin-like (FS) domain, and an alpha-helical EC domain with 2 unusual calcium-binding EF-hands and the collagen-binding site. SPARCL1 shares the three primary domains contained within SPARC with an expanded N-terminal domain.
Statistics
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PSSM-Id: 320015
View PSSM: cd16236
Aligned: 3 rows
Threshold Bit Score: 190.197
Threshold Setting Gi: 194578959
Created: 18-Nov-2014
Updated: 18-Aug-2016
Structure
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Aligned Rows:
 
Feature 1:Ca binding site [ion binding site]
Evidence:

Sequence Alignment
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Format: Row Display: Color Bits: Type Selection:
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
Feature 1                                                                                        
gi 259016170 515 CTDFEVIQFPLRMRDWLKNILMQLYeansehagylnekqrnkvkkiyldekrllagdhpidlllrdfkknyhmYVYPVHW 594
gi 131764    527 CTDYEVNQFPLRMRDWLKNILMQYYerdqdtsafltekqrnkvkkiylnekrlvsgehpvelllhdfeknyhmYLYPVHW 606
gi 194578959 457 CVESELVQFPLRMRDWLKNVLLQLYehdsmspgfltakqrirvqkiyeserrlhagdhpveilqqdfeknynmYIYPVHW 536
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
Feature 1             #    #      #                      # # #      #         
gi 259016170 595 QFSELDQHPMDRVLTHSELAPLRASLVpMEHCITRFFEECDPNKDKHITLKEWGHCFGIKE 655
gi 131764    607 QFYQLDQHPVDRSLTHSELAPLRASLVpMEHCITRFFQECDGDQDKLITLKEWCHCFAIKE 667
gi 194578959 537 QFAQMDQHPSDRFLTHSELAPLRVPLVpMEHCTSVFFQMCDADKDKLVSFKEWCSCFGIKE 597

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