ID F1N2X7_BOVIN Unreviewed; 1616 AA.
AC F1N2X7;
DT 03-MAY-2011, integrated into UniProtKB/TrEMBL.
DT 10-APR-2019, sequence version 3.
DT 27-MAR-2024, entry version 87.
DE SubName: Full=Afadin, adherens junction formation factor {ECO:0000313|Ensembl:ENSBTAP00000007309.6};
GN Name=AFDN {ECO:0000313|Ensembl:ENSBTAP00000007309.6,
GN ECO:0000313|VGNC:VGNC:25709};
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913 {ECO:0000313|Ensembl:ENSBTAP00000007309.6, ECO:0000313|Proteomes:UP000009136};
RN [1] {ECO:0000313|Ensembl:ENSBTAP00000007309.6, ECO:0000313|Proteomes:UP000009136}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Hereford {ECO:0000313|Ensembl:ENSBTAP00000007309.6,
RC ECO:0000313|Proteomes:UP000009136};
RA Rosen B.D., Bickhart D.M., Koren S., Schnabel R.D., Hall R., Zimin A.,
RA Dreischer C., Schultheiss S., Schroeder S.G., Elsik C.G., Couldrey C.,
RA Liu G.E., Van Tassell C.P., Phillippy A.M., Smith T.P.L., Medrano J.F.;
RT "ARS-UCD1.2.";
RL Submitted (MAR-2018) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSBTAP00000007309.6}
RP IDENTIFICATION.
RC STRAIN=Hereford {ECO:0000313|Ensembl:ENSBTAP00000007309.6};
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
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DR Ensembl; ENSBTAT00000007309.6; ENSBTAP00000007309.6; ENSBTAG00000005557.6.
DR VEuPathDB; HostDB:ENSBTAG00000005557; -.
DR VGNC; VGNC:25709; AFDN.
DR eggNOG; KOG1892; Eukaryota.
DR GeneTree; ENSGT00940000155237; -.
DR HOGENOM; CLU_000594_1_0_1; -.
DR TreeFam; TF350731; -.
DR Proteomes; UP000009136; Chromosome 9.
DR Bgee; ENSBTAG00000005557; Expressed in zone of skin and 106 other cell types or tissues.
DR ExpressionAtlas; F1N2X7; baseline and differential.
DR GO; GO:0005911; C:cell-cell junction; IEA:InterPro.
DR GO; GO:0007155; P:cell adhesion; IEA:UniProtKB-KW.
DR GO; GO:0007165; P:signal transduction; IEA:InterPro.
DR CDD; cd22711; FHA_AFDN; 1.
DR CDD; cd15471; Myo5p-like_CBD_afadin; 1.
DR CDD; cd00992; PDZ_signaling; 1.
DR CDD; cd01781; RA2_Afadin; 1.
DR Gene3D; 2.30.42.10; -; 1.
DR Gene3D; 2.60.200.20; -; 1.
DR InterPro; IPR028842; Afadin.
DR InterPro; IPR037977; CBD_Afadin.
DR InterPro; IPR002710; Dilute_dom.
DR InterPro; IPR000253; FHA_dom.
DR InterPro; IPR001478; PDZ.
DR InterPro; IPR036034; PDZ_sf.
DR InterPro; IPR000159; RA_dom.
DR InterPro; IPR008984; SMAD_FHA_dom_sf.
DR InterPro; IPR029071; Ubiquitin-like_domsf.
DR PANTHER; PTHR10398; AFADIN; 1.
DR PANTHER; PTHR10398:SF2; AFADIN; 1.
DR Pfam; PF01843; DIL; 1.
DR Pfam; PF00498; FHA; 1.
DR Pfam; PF00595; PDZ; 1.
DR Pfam; PF00788; RA; 2.
DR SMART; SM01132; DIL; 1.
DR SMART; SM00240; FHA; 1.
DR SMART; SM00228; PDZ; 1.
DR SMART; SM00314; RA; 2.
DR SUPFAM; SSF50156; PDZ domain-like; 1.
DR SUPFAM; SSF49879; SMAD/FHA domain; 1.
DR SUPFAM; SSF54236; Ubiquitin-like; 2.
DR PROSITE; PS51126; DILUTE; 1.
DR PROSITE; PS50106; PDZ; 1.
DR PROSITE; PS50200; RA; 2.
PE 4: Predicted;
KW Cell adhesion {ECO:0000256|ARBA:ARBA00022889};
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Reference proteome {ECO:0000313|Proteomes:UP000009136}.
FT DOMAIN 1..92
FT /note="Ras-associating"
FT /evidence="ECO:0000259|PROSITE:PS50200"
FT DOMAIN 205..307
FT /note="Ras-associating"
FT /evidence="ECO:0000259|PROSITE:PS50200"
FT DOMAIN 627..874
FT /note="Dilute"
FT /evidence="ECO:0000259|PROSITE:PS51126"
FT DOMAIN 973..1059
FT /note="PDZ"
FT /evidence="ECO:0000259|PROSITE:PS50106"
FT REGION 89..155
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 303..338
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 507..527
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1073..1156
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1168..1430
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1569..1616
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 1468..1495
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 102..155
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 303..326
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 512..527
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1096..1113
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1120..1138
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1139..1156
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1187..1211
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1240..1265
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1269..1306
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1318..1333
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1358..1394
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1616 AA; 181663 MW; A5608A91D63ADF8E CRC64;
MRFYFQDKAA GNFATKCIRV SSTATTQDVL ETLAEKFRPD MRMLSSPKYS LYEVHVSGEE
RRLDIDEKPL VVQLNWNKDD REGRFVLKNE NDAVPAKKAQ SNGPEKQEKE GVIQNFKRTL
SKKEKKEKKK REKEAVRQAS EKDDRPFSGD DTENSRLAAE VYKDMPETSF TRTISNPEVV
MKRRRQQKLE RRMQEFRSSD GRPDSGGTLR IYADSLKPNI PYKTILLSTT DPADFAVAEA
LEKYGLEKEN PRDYCIARVM LPPGAQHSDE KGAKEVILDD DECPLQIFRE WPSDRGILVF
QLKRRPPDHI PKKSKKHTDG KPLQGKERAD GSAYGSALPP EKLPYLVELS PGRRNHSACY
SSHASEDGSD SRDKPKLYRL QLSVTEVGTE KFDDSSIQLF GSGIQPHHCD LTNMDGVVTV
TPRSMDAETY VDGQRISETT MLQSGMKVQF GASHVFKFVD PSQDHTLPKR SVDGGLTVKG
PRHKSGIVQE TTFDLGGDVH SGMALPASKS TARLDSDRTP STSSTAERGM VKPMVRVEQQ
LDYRRQDSRT QDAPGPDLIL PASIEFRESS EDSFLSAIIN YTNSSTVHFK LSPTYVLYMA
CRYVLSSQYR PDVSPAERTH KVMAIVNKMV SMMEGVIQEV DQVDQKQKNI AGALAFWMAN
ASELLNFIKQ DRDLSRITLD AQDVLAHLVQ MAFKYLVHCL QSELNNYMPA FLDDPEEDSL
QRPKIDDVLH TLTGAMSLLR RCRVNAALTI QLFSQLFHFI NMWLFNRLVT DPESGLCSHY
WGAILRQQLG HVEAWAEKQG LELAADCHLS RIVQATTLLT MDKYAPDDIP NINSTCFKLN
SLQLQALLQN YHCAPDEPFV PADLIANVVA VAENTADELA RSDGREVRLE EDPDLQLPFL
LPEDGYSCDV VRNVPSGLQE FLDPLCQRGF CRLIPHPRSP GTWTIYFEGA DYESHLLREN
TELAQPLRKE PEIITVTLKK QNGMGLSIVA AKGAGQDKLG IYVKSVVKGG AADVDGRLAA
GDQLLSVDGR SLVGLSQERA AELMTRTSSV VTLEVAKQGA IYHGLATLLN QPSPMMQRIS
ERRGSGKPRP KSEGFELYNN SAQNGSPESP QTPWAEYSEP KKLPGDDRLT KHRADHRSSP
NVANQPPSPG GKSAYASGTA AKITSVSTGN LCAEEQTPPP RPEAYPIPTQ TSTREYFTFP
ASKSQDRVAP PQSQWLGFEE KPHVLADGNH SSAAVQRVTR SQEELREDAY HPERQRPEAA
ADRRSDGSDA WPTQGSSLGS GASSQEHLGP PSKAGTPAST LTKSGPGRWK TPAASPPMRT
DPALPPPPPP GSYAGEADAD ADSPPPPAAT AAGQAQAAAE RKKREEQQRW YEKEKARLDE
ERERRRREQE RRLGQLRAPA PPPAPARAPD TVIRELQPQQ QPRTIERRDL QYITVSREEL
ASGDSLSPDP WKRDAREKLE KQQQLHIVDL LSREIQELQG KAERSAEESD RLRKLLLEWQ
FQKRLQESKQ KDEDDEEEED DDVDTVLLMQ RLEAERRARQ TAMPAISVLD LLPARLFWWR
ATSPSFRLQD EERRRQQQLE EMRTREAEER ARQEEQRRRQ EDERVRREAE DKVLVL
//
