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1.A.17.1.18
TMEM16 of 735 aas and 10 TMSs.  Operates as a Ca2+-activated lipid scramblase. Each subunit of the homodimer contains a hydrophilic membrane-traversing cavity that is exposed to the lipid bilayer as a potential site of catalysis. This cavity harbours a conserved Ca2+-binding site, located within the hydrophobic core of the membrane. Mutations of residues involved in Ca2+ coordination affect both lipid scrambling in N. haematococca TMEM16 and ion conduction in the Cl- channel of TMEM16A. The structure reveals the general architecture of the family and its mode of Ca2+ activation (Brunner et al. 2014).

Accession Number:C7Z7K1
Protein Name:Predicted protein
Length:735
Molecular Weight:83110.00
Species:Nectria haematococca (strain 77-13-4 / ATCC MYA-4622 / FGSC 9596 / MPVI) [660122]
Number of TMSs:7
Substrate lipids

Cross database links:

Structure:
4WIS   4WIT     

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  • 2° Structure (Network Protein Sequence Analysis)

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Predict TMSs (Predict number of transmembrane segments)
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FASTA formatted sequence
1:	MSNLKDFSQP GSGQESNFGV DFVIHYKVPA AERDEAEAGF VQLIRALTTV GLATEVRHGE 
61:	NESLLVFVKV ASPDLFAKQV YRARLGDWLH GVRVSAPHND IAQALQDEPV VEAERLRLIY 
121:	LMITKPHNEG GAGVTPTNAK WKHVESIFPL HSHSFNKEWI KKWSSKYTLE QTDIDNIRDK 
181:	FGESVAFYFA FLRSYFRFLV IPSAFGFGAW LLLGQFSYLY ALLCGLWSVV FFEYWKKQEV 
241:	DLAVQWGVRG VSSIQQSRPE FEWEHEAEDP ITGEPVKVYP PMKRVKTQLL QIPFALACVV 
301:	ALGALIVTCN SLEVFINEVY SGPGKQYLGF LPTIFLVIGT PTISGVLMGA AEKLNAMENY 
361:	ATVDAHDAAL IQKQFVLNFM TSYMALFFTA FVYIPFGHIL HPFLNFWRAT AQTLTFSEKE 
421:	LPTREFQINP ARISNQMFYF TVTAQIVNFA TEVVVPYIKQ QAFQKAKQLK SGSKVQEDHE 
481:	EEAEFLQRVR EECTLEEYDV SGDYREMVMQ FGYVAMFSVA WPLAACCFLV NNWVELRSDA 
541:	LKIAISSRRP IPWRTDSIGP WLTALSFLSW LGSITSSAIV YLCSNSKNGT QGEASPLKAW 
601:	GLLLSILFAE HFYLVVQLAV RFVLSKLDSP GLQKERKERF QTKKRLLQEN LGQDAAEEAA 
661:	APGIEHSEKI TREALEEEAR QASIRGHGTP EEMFWQRQRG MQETIEIGRR MIEQQLAAGK 
721:	NGKKSAPAVP SEKAS