ID U3J9P6_ANAPP Unreviewed; 1720 AA.
AC U3J9P6;
DT 13-NOV-2013, integrated into UniProtKB/TrEMBL.
DT 05-JUN-2019, sequence version 2.
DT 27-MAR-2024, entry version 49.
DE SubName: Full=Afadin, adherens junction formation factor {ECO:0000313|Ensembl:ENSAPLP00000016224.2};
GN Name=AFDN {ECO:0000313|Ensembl:ENSAPLP00000016224.2};
OS Anas platyrhynchos platyrhynchos (Northern mallard).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Anseriformes; Anatidae;
OC Anatinae; Anas.
OX NCBI_TaxID=8840 {ECO:0000313|Ensembl:ENSAPLP00000016224.2, ECO:0000313|Proteomes:UP000016666};
RN [1] {ECO:0000313|Ensembl:ENSAPLP00000016224.2, ECO:0000313|Proteomes:UP000016666}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Hou Z.-C., Zhou Z.-K., Zhu F., Hou S.-S.;
RT "A new Pekin duck reference genome.";
RL Submitted (OCT-2017) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSAPLP00000016224.2}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
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DR Ensembl; ENSAPLT00000017037.2; ENSAPLP00000016224.2; ENSAPLG00000002298.2.
DR GeneTree; ENSGT00940000155237; -.
DR Proteomes; UP000016666; Chromosome 3.
DR GO; GO:0005911; C:cell-cell junction; IEA:InterPro.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-KW.
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 Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Reference proteome {ECO:0000313|Proteomes:UP000016666}.
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 611..858
FT /note="Dilute"
FT /evidence="ECO:0000259|PROSITE:PS51126"
FT DOMAIN 957..1043
FT /note="PDZ"
FT /evidence="ECO:0000259|PROSITE:PS50106"
FT REGION 86..148
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 309..333
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 484..513
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1055..1164
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1180..1207
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1249..1507
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1520..1702
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 102..148
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 309..328
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 489..512
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1072..1090
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1097..1112
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1114..1151
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1252..1281
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1290..1305
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1308..1324
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1355..1391
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1408..1443
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1465..1480
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1492..1507
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1567..1642
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1661..1676
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1720 AA; 195762 MW; 5E8E5681741883B7 CRC64;
MRFYFQDKAA GNFATKCIRV SSTATTQDVI ETLAEKFRPD MRMLSSPKYS LYEVHVSGEE
RRLDVDEKPL VVQLNWNKDD REGRFVLKNE NDTLPPKKAQ SNGPEKQEKE GVIQNFKRTL
SKKEKKEKKR REKEALRQAS DKDDRFLHGD DIENSRLAAE VYKDMPETSF TRTISNPEVV
MKRRRQQKLE KRMQEFRSSD GRPDSGGTLR IYADSLKPNI PYKTILLSTT DTADFAVIEA
LEKYGLEKEN PKDYCIARVM LPPGAQHSDD KGAKESILDD DECPLQIFRE WPSDKGILVF
QLKRRPPDYV PKKSKKTADG KPLKGKDRVD GSGYGSCLPP EKLPYLVELS PDGSDSRDKP
KLYRLQLSVT AVGTEKFDEN SIQLFGPGIQ PHHCDLTNMD GVVTVTPRNI DAETYVEGQR
ISETTMLQSG MKVQFGSSHV FKFVDPTQDH IIPKRPIDAS LMVKGPRHKT GAVQETTFDL
EGDVHSGTAL PVSKSTSRLD GDRTSSASST AERGMVKPMI RIEQQDYRRQ DSRSQDTHGP
ELILPASIEF RESSEDAFLS AIINYTNSST VHFKLSPTYV LYMTCRYVLS SQYRPDITPT
ERTHKVIAIV NKMVNMMEGV IQEVDQVDQK QKNIAGALAF WMANASELLN FIKQDRDLSR
ITVDAQDVLA HLVQMAFKYL VHCLQSELNN YMPAFLDDPE ENNPQRPKID DVLHTLTGAM
SLLRRCRVNA ALTIQLFSQL FHFINMWLFN RLVTAPDSGL CSHYWGAIVR QQLGHIEAWA
EKQGLELAAD CHLSRIVQAT TLLTMDKYSH ADVPNINSTC FKLNSLQLQA LLQNYHCAPD
EPLIPTELIE NVVTVAENTA DELARSDGRE VQLEEDPDLQ LPFLLPEDGY SCDVVRNVPS
GLQEFLDPLC QRGFCRLIPH PRSPGTWTIY FEGADYESHL SHENAELAQP LRKEPEIITV
TLKKQNGMGL SIVAAKGAGQ DKLGIYVKSV VKGGAADVDG RLAAGDQLLS VDGRSLVGLS
QERAAELMTR TGSVVTLEVA KQGAIYHGLA TLLNQPSPMM QRGKPRPKSE GFELYNNSTQ
NGSPESPQLP WTEYSEPKKL PGDDRLMKNR ADHRSSPNVA NQPPSPGGKN AYASGTTTKI
TSVSTGNLCT EEETLPPRPE AYPIPTQTYT REYFTFPASK SQDRMGPAQS QWPSYEEKPQ
VQAESNHSIN STMQRVARSQ EELRDKVFQP DRNRLEVVIR KDVEYIDRKS DSDQWMNSSV
DSSTSSQEHL NHSSKPVSPG SCLTKSGPGR WKTPATSQPT PVAISQPIRT DLPPPPPPPP
VHYAAEFDEP QMDLPLPPPP LPNQIGTQAS SQVAAAERKK REEHQRWYEK EKARLEEERE
RKRREQERKL GQMRSQPLIP AQPVVPPVSL QQVKSEKPST LQRPQETVIR ELQPQQQPRT
IERRDLQYIT ISKEELSSSD SLSPDPWKRD AKEKLEKQQQ MHIVDMLSKE IQDLQNKPDR
TAEENDRLRK LMLEWQFQKR LQESKQKDED DDEEEDDDVD TMLIMQRLEA ERRARQTAVP
AISVLDLLQD EERRRQQQLE EMRKREAEDR ARQEEERRQQ EEERTRREAE EKRRQEEEYY
NRLEAERRRQ HDEAERRLLE PDEPGINSYT GSTGATVGAH EVYRDPRDKR SKSQDTDLPG
APENLTFRER QRLFSQGQDV SNKVKASRKL MELENELNTK
//
