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2.A.53.2.5
Prestin, the outer hair cell voltage-sensitive motor protein (voltage sensitivity depends on intracellular Cl- and HCO3- which may bind to prestin). Prestin transports anions including formate and oxalate; transport and voltage-sensing capabilities are independent functions of the same protein (Bai et al., 2009). Prestin-mediated electromotility is a dual-step process: transport of anions by an alternate access cycle, followed by an anion-dependent transition generating electromotility (Schaechinger et al., 2011; McGuire et al., 2011).  A three-dimensional molecular dynamics model of prestin predicted that it contains eight transmembrane spanning segments and two helical re-entry loops. Tyrosyl residues recognize anions, with residues Y367, Y486, Y501 and Y508 contributing to anion binding through anion-pi interactions. Such interactions, sensitive to voltage and mechanical stimulation, confer a capability to perform electromechanical and mechanoelectric conversions (Lovas et al. 2015).

Accession Number:Q99NH7
Protein Name:SLC26A5 aka PRES
Length:744
Molecular Weight:81321.00
Species:Mus musculus (Mouse) [10090]
Number of TMSs:11
Location1 / Topology2 / Orientation3: Cell membrane1 / Multi-pass membrane protein2
Substrate formate, Oxalate

Cross database links:

Genevestigator: Q99NH7
HEGENOM: HBG446299
Pfam: PF01740    PF00916   

Gene Ontology

GO:0016323 C:basolateral plasma membrane
GO:0016021 C:integral to membrane
GO:0003774 F:motor activity
GO:0008271 F:secondary active sulfate transmembrane tran...
GO:0030507 F:spectrin binding
GO:0008360 P:regulation of cell shape
GO:0042391 P:regulation of membrane potential
GO:0007605 P:sensory perception of sound
GO:0008272 P:sulfate transport
GO:0055085 P:transmembrane transport

References (1)

[1] “Expression of prestin, a membrane motor protein, in the mammalian auditory and vestibular periphery.”  Dougherty G.W.et.al.   14553901

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Predict TMSs (Predict number of transmembrane segments)
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FASTA formatted sequence
1:	MDHAEENEIP AETQRYYVER PIFSHPVLQE RLHVKDKVTE SIGDKLKQAF TCTPKKIRNI 
61:	IYMFLPITKW LPAYKFKEYV LGDLVSGIST GVLQLPQGLA FAMLAAVPPV FGLYSSFYPV 
121:	IMYCFFGTSR HISIGPFAVI SLMIGGVAVR LVPDDIVIPG GVNATNGTEA RDALRVKVAM 
181:	SVTLLSGIIQ FCLGVCRFGF VAIYLTEPLV RGFTTAAAVH VFTSMLKYLF GVKTKRYSGI 
241:	FSVVYSTVAV LQNVKNLNVC SLGVGLMVFG LLLGGKEFNE RFKEKLPAPI PLEFFAVVMG 
301:	TGISAGFNLH ESYSVDVVGT LPLGLLPPAN PDTSLFHLVY VDAIAIAIVG FSVTISMAKT 
361:	LANKHGYQVD GNQELIALGI CNSIGSLFQT FSISCSLSRS LVQEGTGGKT QLAGCLASLM 
421:	ILLVILATGF LFESLPQAVL SAIVIVNLKG MFMQFSDLPF FWRTSKIEPT IWLTTFVSSL 
481:	FLGLDYGLIT AVIIALLTVI YRTQSPSYKV LGQLPDTDVY IDIDAYEEVK EIPGIKIFQI 
541:	NAPIYYANSD LYSSALKRKT GVNPALIMGA RRKAMRKYAK EVGNANVANA TVVKVDAEVD 
601:	GENATKPEEE DDEVKFPPIV IKTTFPEELQ RFLPQGENVH TVILDFTQVN FVDSVGVKTL 
661:	AGIVKEYGDV GIYVYLAGCS PQVVNDLTRN NFFENPALKE LLFHSIHDAV LGSQVREAMA 
721:	EQEATASLPQ EDMEPNATPT TPEA