3FO5


Conserved Protein Domain Family
START_STARD14_15-like

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cd08873: START_STARD14_15-like 
Click on image for an interactive view with Cn3D
Lipid-binding START domain of mammalian STARDT14, -15, and related proteins
This subfamily includes the steroidogenic acute regulatory protein (StAR)-related lipid transfer (START) domains of mammalian brown fat-inducible STARD14 (also known as Acyl-Coenzyme A Thioesterase 11 or ACOT11, BFIT, THEA, THEM1, KIAA0707, and MGC25974), STARD15/ACOT12 (also known as cytoplasmic acetyl-CoA hydrolase/CACH, THEAL, and MGC105114), and related domains. The START domain family belongs to the SRPBCC (START/RHO_alpha_C/PITP/Bet_v1/CoxG/CalC) domain superfamily of proteins that bind hydrophobic ligands. SRPBCC domains have a deep hydrophobic ligand-binding pocket. STARD14/ACOT11 and STARD15/ACOT12 are type II acetyl-CoA thioesterases; they catalyze the hydrolysis of acyl-CoAs to free fatty acid and CoASH. Human STARD14 displays acetyl-CoA thioesterase activity towards medium(C12)- and long(C16)-chain fatty acyl-CoA substrates. Rat CACH hydrolyzes acetyl-CoA to acetate and CoA. In addition to having a START domain, STARD14 and STARD15 each have two tandem copies of the hotdog domain. There are two splice variants of human STARD14, named BFIT1 and BFIT2, which differ in their C-termini. Human BFIT2 is equivalent to mouse mBFIT/Acot11, whose transcription is increased two fold in obesity-resistant mice compared with obesity-prone mice. Human STARD15 may have roles in cholesterol metabolism and in beta-oxidation.
Statistics
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PSSM-Id: 176882
View PSSM: cd08873
Aligned: 3 rows
Threshold Bit Score: 427.784
Threshold Setting Gi: 198431964
Created: 30-Jul-2009
Updated: 2-Oct-2020
Structure
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Program:
Drawing:
Aligned Rows:
 
Conserved site includes 50 residues -Click on image for an interactive view with Cn3D
Feature 1:lipid binding site [chemical binding site]
Evidence:
  • Comment:based on the START domain of human ACOT11/STARD14 and related START domains with structure
  • Structure:3FO5_A; human ACOT11/STARD14 START domain binds pentaethylene glycol and glycerol, contacts at 4A
    View structure with Cn3D
  • Comment:The specific ligand of the ACOT11/STARD14 domain is unknown; pentaethylene glycol is a remnant of the crystallography process.

Sequence Alignment
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Format: Row Display: Color Bits: Type Selection:
Feature 1                                                                    ##      #       ## #
3FO5_A        11 RRYREASARKKIRLDRKYIVScKQTEVPLSVPWDPSNQVYLSYNNVSSLKMLVAKdnWVLSSEisqVRLYTLEDdkFLSF 90  human
Q8WYK0       312 RRYRGAIARKRIRLGRKYVIS-HKEEVPLCIHWDISKQASLSDSNVEALKKLAAKrgWEVTSTvekIKIYTLEEhdVLSV 390 human
XP_002121692 369 RRQKEAAARRKIRLDRRYILS-LQRNDRLSVAWSRTNAMYLCYGNITALSRIAGKsdWTVAASttsVTLCTREQdgVLSF 447 Ciona intestinalis
Feature 1         #            #   #     #  ##              ##                 # ####   #  # # # 
3FO5_A        91 HMEMVVHV--DAAQAFLLLSDLRQRPEWDK-------------HYRSVELVQQVDEDDAIYHVTSPALgghTKPQDFVIL 155 human
Q8WYK0       391 WVEKHVGS--PAHLAYRLLSDFTKRPLWDP-------------HFVSCEVIDWVSEDDQLYHITCPILn-dDKPKDLVVL 454 human
XP_002121692 448 CVTLKPQTelCASDVFDVLKNPFKRVEWDPltficsafheifvRGRSCDEVKRIGDEDGIYHTVMKSQt-sEVPNDFVLL 526 Ciona intestinalis
Feature 1                        #                # #### #           # # ##### ### ### ###    #  
3FO5_A       156 ASRRKPCDNGDPYVIALRSVTLPTHRETPEYRRGETLCSGFCLWREgDQLTKVSYYNQATPGVLNYVTTNVAGLSSEFYT 235 human
Q8WYK0       455 VSRRKPLKDGNTYTVAVKSVILPSVPPSPQYIRSEIICAGFLIHAIdSNSCIVSYFNHMSASILPYFAGNLGGWSKSIEE 534 human
XP_002121692 527 VSDRRPATDSDPYKVAFRSVTHDRVPQTTGFSRTEVACAGFVIRQDcGTCTEISYYNETNPKLVSYVTCDLAGLGALYCR 606 Ciona intestinalis
Feature 1        ##  #       
3FO5_A       236 TFKACEQFLLDN 247 human
Q8WYK0       535 TAASCIQFLENP 546 human
XP_002121692 607 VFHCLENYLVTN 618 Ciona intestinalis

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