(data stored in SCRATCH zone)

EMBL: AM269952.PE30

AM269952.PE30        Location/Qualifiers
FT   CDS             62600..64339
FT                   /locus_tag="An01g01040"
FT                   /note="Function: Ank3 plays an important role in the
FT                   polarized distribution of many integral membrane proteins."
FT                   /note="Function: the ankyrin domain is supposed to mediate
FT                   protein-protein interactions."
FT                   /note="Localization: Ank3 is a broadly distributed
FT                   epithelial ankyrin and is the major ankyrin in the kidney
FT                   and other tissues."
FT                   /note="Remark: Ank3 is expressed in alternatively spliced
FT                   forms including forms that lack the NH2-terminal repeat
FT                   domain."
FT                   /note="Title: similarity to ankyrin 3 Ank3 - Mus musculus"
FT                   /note="See PMID 7615634"
FT                   /note="See PMID 9060470"
FT                   /db_xref="GOA:A2Q7K5"
FT                   /db_xref="InterPro:IPR002110"
FT                   /db_xref="InterPro:IPR020683"
FT                   /db_xref="InterPro:IPR036770"
FT                   /db_xref="UniProtKB/TrEMBL:A2Q7K5"
FT                   /inference="profile:COGS:COG0666"
FT                   /inference="profile:PFAM:PF00023"
FT                   /protein_id="CAK43481.1"
FT                   /translation="MSSDMDTQVSSGTEMGVSLPFLQAARQLNYDRLSLLIAEGHHPNR
FT                   RDENGYTALHRAILECPEDLTTVAMLLTYGANPHAVFKDRNSLREITPLHYAAIRGDVG
FT                   LVSLFLHHGKSDPAPRSLKYWTTPLEDAISNGHLTVVARFIEFFSSSQLLNKPSRGIDE
FT                   SIILSARLWYSKALSLLLEYKKHHLFPSPHGPDVLKHAFCEAIRSEACNSSVQGIGERA
FT                   GGPGDNTPSKCANLLLQAGVRFRDDEMDRLLSITCSNAHLIGVTRLLLNLGPKVTAHHI
FT                   TRAIESQSYHMVKIVTKYVITSAGEDAIKRDSEPDLIQYAASHGSLDTFEYLATELGTA
FT                   SSQSQPIATTESRKTPLIHYAVWGLRIDVVQHLLSTQGANVNEQDEYGHSPLMYAFDIA
FT                   QASDENPCLAIIQLLMQYGVDVKASSIEGLTALHLAVRLGITPAVQLLLSNGCDPNAKT
FT                   TTGSDLYLRRSPSSWSPETTARNRTPLHWAVDRLANVSYDVVRLLLHYGADMNAEDGNG
FT                   VTPLNLLLGEGWCINRAWESRMAVVNLFLTFGANIDIKDMSGITARQRIRQREAELCAP
FT                   VVD"
     MSSDMDTQVS SGTEMGVSLP FLQAARQLNY DRLSLLIAEG HHPNRRDENG YTALHRAILE        60
     CPEDLTTVAM LLTYGANPHA VFKDRNSLRE ITPLHYAAIR GDVGLVSLFL HHGKSDPAPR       120
     SLKYWTTPLE DAISNGHLTV VARFIEFFSS SQLLNKPSRG IDESIILSAR LWYSKALSLL       180
     LEYKKHHLFP SPHGPDVLKH AFCEAIRSEA CNSSVQGIGE RAGGPGDNTP SKCANLLLQA       240
     GVRFRDDEMD RLLSITCSNA HLIGVTRLLL NLGPKVTAHH ITRAIESQSY HMVKIVTKYV       300
     ITSAGEDAIK RDSEPDLIQY AASHGSLDTF EYLATELGTA SSQSQPIATT ESRKTPLIHY       360
     AVWGLRIDVV QHLLSTQGAN VNEQDEYGHS PLMYAFDIAQ ASDENPCLAI IQLLMQYGVD       420
     VKASSIEGLT ALHLAVRLGI TPAVQLLLSN GCDPNAKTTT GSDLYLRRSP SSWSPETTAR       480
     NRTPLHWAVD RLANVSYDVV RLLLHYGADM NAEDGNGVTP LNLLLGEGWC INRAWESRMA       540
     VVNLFLTFGA NIDIKDMSGI TARQRIRQRE AELCAPVVD                              579
//

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