2.A.21.6.6
Urea transporter, UreA of 693 aas and ~17 TMSs. A three-dimensional model of UreA which, combined with mutagenesis studies, led to the identification of residues important for binding,
recognition and translocation of urea, and in the sorting of UreA to the membrane. Residues W82,
Y106, A110, T133, N275, D286, Y388, Y437 and S446, located in transmembrane helixes 2, 3, 7 and 11,
were found to be involved in the binding, recognition and/or translocation of urea and the sorting
of UreA to the membrane. Y106, A110, T133 and Y437 seem to play a role in substrate selectivity,
while S446 is necessary for proper sorting of UreA to the membrane (Sanguinetti et al. 2014). A pair of non-optimal codons are necessary for the correct biosynthesis of UreA (Sanguinetti et al. 2019).
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| Accession Number: | E5CZT5 |
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| Protein Name: | Urea active transporter |
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| Length: | 693 |
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| Molecular Weight: | 74235.00 |
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| Species: | Emericella nidulans [162425] |
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| Number of TMSs: | 17 |
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| Location1 / Topology2 / Orientation3: |
Membrane1 / Multi-pass membrane protein2 |
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| Substrate |
urea |
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1: MVAVIAAPDE AGVETVTFTA PLTQGFGYGI IIGLGFAFAL VMIFITWSLK RYQHEIITSE
61: MFSTAGRSVK SGLVASAVVS SWTWAATLLQ SSAVAYQYGT SGPFFYASGA TVQIILFATL
121: AIELKRRAPN AHTFLEAIRA RYGTVVHLVF IVFCLMTNIL VTAMLLTGGA AVLNSMTGVP
181: VVAACFLLPI GVVLYTLFGG IKATFITDYM HTVVIVVIIF IFAFSAYASN DRLGSPGKVY
241: DLLVQAALRN PVSGNAEGSY LTMRSKDGGI FWVINLVGNF GTVFLDNGYY NKAIAAHPVH
301: AFPGYVIGGL CWFAIPWLCA TTMGLSALAL EGTRRIASVD VTAGLVLPFA SVELLGYSGA
361: VCTTLMIFMA VTSAFSAQLI AVSSILTYDI YQAYINPAAK GKRLVWVSHL SCVVFAIAMA
421: AFATGLHYAG IGMGYLYLLM GVIISSAVFP GAMTLVWKGQ NWIAAAASPV LGLAMSLVAW
481: LVTTKTEYGV FTVETTGANY PMLAGNVAAL LSPVVFSPVL TYLFGPQNYD YESMRAIRKV
541: DDSDVAAAAH VDLELIPGAS NTNSSPSQQQ QEEEEIRKLN KAAFISRCLT VGMVICFLIL
601: WPIPMYGSGY VFSKKFFTGW VVVGIIWLFG TAFGVILFPL WEGRSSIKRV GKLMLLDAMG
661: RQWKSSALVG QGDEESEESG SGAVTPSEKI VAK