ID  F1MAD2;
PN  InaD-like protein;
GN  Patj;
OS  10116;
SL  Nucleus Position: SL-0198;
SL  Comments: Cell junction, tight junction {ECO:0000250|UniProtKB:Q8NI35}. Apical cell membrane {ECO:0000250|UniProtKB:Q8NI35}; Peripheral membrane protein {ECO:0000250|UniProtKB:Q8NI35}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:Q63ZW7}. Note=Localizes to the apical region at the start of epithelial cell polarization then locates to tight junctions as polarization is completed (By similarity). Localized in the paranodal region of myelinating Schwann cells (By similarity). Localized to the leading edge of the actin cortex of migrating epithelia cells (By similarity). {ECO:0000250|UniProtKB:E2QYC9, ECO:0000250|UniProtKB:Q63ZW7, ECO:0000250|UniProtKB:Q8NI35}.
DR  UNIPROT: F1MAD2;
DR  PDB: 3UIT;
DR  Pfam: PF09045;
DR  Pfam: PF00595;
DR  PROSITE: PS51022;
DR  PROSITE: PS50106;
DE  Function: Scaffolding protein that facilitates the localization of proteins to the cell membrane (By similarity). Required for the correct formation of tight junctions and epithelial apico-basal polarity (By similarity). Positively regulates epithelial cell microtubule elongation and cell migration, possibly via facilitating localization of PRKCI/aPKC and PAR3D/PAR3 at the leading edge of migrating cells (By similarity). Plays a role in the correct reorientation of the microtubule-organizing center during epithelial migration (By similarity). May regulate the surface expression and/or function of ASIC3 in sensory neurons (By similarity). May recruit ARHGEF18 to apical cell-cell boundaries (By similarity). {ECO:0000250|UniProtKB:E2QYC9, ECO:0000250|UniProtKB:Q63ZW7, ECO:0000250|UniProtKB:Q8NI35}.
DE  Reference Proteome: Yes;
GO  GO:0045177;
GO  GO:0016324;
GO  GO:0005923;
GO  GO:0005737;
GO  GO:0048471;
GO  GO:0032991;
GO  GO:0035003;
GO  GO:0070160;
GO  GO:0035089;
GO  GO:0120192;
TP  Membrane Topology: Peripheral; Source: UniProt - By Similarity {ECO:0000250|UniProtKB:Q8NI35};
SQ  MPENPAAEKMQVLQVLDRLRGKLQEKGDTTQNEKLSAFYETLKSPLFNQILTLQQSIKQLKGQLSHIPSDCSANFDFSRK
SQ  GLLVFTDGSITNGNAHRPCSSITASESLPWTQRSGNEDFTSVIQQMAQGRHIEYIDIERPSTGGLGFSVVALRSQSLGLI
SQ  DIFVKEVHPGSVADRDQRLKENDQILAINDTPLDQNISHQQAIALLQQATGSLRLVVAREVGHTQSRTSTSSADTTLPET
SQ  VRWGHTEDVELINDGSGLGFGIVGGKSSGVVVRTIVPGGLADRDGRLQTGDHILKIGSTNVQGMTSEQVAQVLRNCGNSV
SQ  RMLVARDPVGEIAVTPPTPASLPVALPVVATRTLGSDSSPFETYNVELVKKDGQSLGIRIVGYVGTAHPGEASGIYVKSI
SQ  IPGSAAYHNGQIQVNDKIVAVDGVNIQGFANQDVVEVLRNAGQVVHLTLVRRKTSLSASPFEQPSSREAVAEPPEVPELT
SQ  GSLKPETNSRMEAEEIGERLDNLRKDTVQALEKPDVYPEDIPGCPENELKSRWENLLGPDYEVMVATLDTQIADDEELQK
SQ  YSKLLPIHTLRLGMEVDSFDGHHYISSIAPGGPVDTLNLLQPEDELLEVNGVQLYGKSRREAVSFLKEVPPPFTLVCCRR
SQ  LFDDEASVDEPRTVEPSLLEAEVDRSVDVSTEDDDGELALWSPEVKTVELVKDCKGLGFSILDYQDPLDPMRSVIVIRSL
SQ  VADGVAERSGELLPGDRLVSVNEFSLDNATLAEAVEVLKAVPPGVVHLGICKPLVEEEKEEKEEHFIFHSNNNGDNSESP
SQ  ETVHEIHSSLILEAPQGFRDEPYLEELVDEPFLDLGKSLQFQQKDMDSSSEAWEMHEFLSPRLERRGEEREMLVDEEYEI
SQ  YQDRLRDMEAHPPPPHIREPTSASPRLDLQAGPQWLHADLSGGEILECHDTESMMTAYPQEMQDYSFSTTDMMKETFGLD
SQ  SRPPMPSSEGNGQHGRFDDLEHLHSLVSHGLDLGMMTPSDLQGPGVLVDLPAVTQRREQEELPLYRLPSARVVTKPSSHV
SQ  GMVSSRHANAACELPEREEGEGEETPNFSHWGPPRIVEIFREPNVSLGISIVGGQTVIKRLKNGEELKGIFIKQVLEDSP
SQ  AGKTKALKTGDKILEVSGVDLQNASHAEAVEAIKSAGNPVVFVVQSLSSTPRVIPSVNNKGKTPPQNQDQNTQEKKAKRH
SQ  GTAPPPMKLPPPYRAPSADTEESEEDSALTDKKIRQRYADLPGELHIIELEKDKNGLGLSLAGNKDRSRMSIFVVGINPD
SQ  GPAAADGRMRVGDELLEINNQILYGRSHQNASAIIKTAPTRVKLVFIRNEDAVNQMAVAPFPVPSHSPSPVEDLGGTEPV
SQ  SSEEDSSVDAKPLPERESSKPEDLTQAVDDSMVAEQEKASESPDSAARQMKQPGYSAQVSSSSQEIPSAPAPLCQSTHAD
SQ  VTGSGNFQAPLSVDPAPLSVDPATCPIVPGQEMIIEISKGRSGLGLSIVGGKDTPLDAIVIHEVYEEGAAARDGRLWAGD
SQ  QILEVNGVDLRSSSHEEAITALRQTPQKVRLVIYRDEAQYRDEENLEVFLVDLQKKTGRGLGLSIVGKRSGSGVFISDIV
SQ  KGGAADLDGRLIRGDQILSVNGEDVRQASQETVATILKCVQGLVQLEIGRLRAGSWASSRKTSQNSQGDQHSAHSSCRPS
SQ  FAPVITSLQNLVGTKRSSDPPQKCTEEEPRTVEIIRELSDALGVSIAGGKGSPLGDIPIFIAMIQANGVAARTQKLKVGD
SQ  RIVSINGQPLDGLSHTDAVNLLKNAFGRIILQVVADTNISAIATQLEMMSAGSQLGSPTADRHPQDPEELLQRTAD
//