ID A0A2K6M070_RHIBE Unreviewed; 1814 AA.
AC A0A2K6M070;
DT 28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT 28-MAR-2018, sequence version 1.
DT 27-MAR-2024, entry version 29.
DE SubName: Full=Afadin, adherens junction formation factor {ECO:0000313|Ensembl:ENSRBIP00000029168.1};
GN Name=AFDN {ECO:0000313|Ensembl:ENSRBIP00000029168.1};
OS Rhinopithecus bieti (Black snub-nosed monkey) (Pygathrix bieti).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Colobinae; Rhinopithecus.
OX NCBI_TaxID=61621 {ECO:0000313|Ensembl:ENSRBIP00000029168.1, ECO:0000313|Proteomes:UP000233180};
RN [1] {ECO:0000313|Ensembl:ENSRBIP00000029168.1, ECO:0000313|Proteomes:UP000233180}
RP NUCLEOTIDE SEQUENCE.
RA Wu, C.-I. and Zhang, Y.;
RT "Genome of Rhinopithecus bieti.";
RL Submitted (JUN-2016) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSRBIP00000029168.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
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DR STRING; 61621.ENSRBIP00000029168; -.
DR Ensembl; ENSRBIT00000053118.1; ENSRBIP00000029168.1; ENSRBIG00000038335.1.
DR GeneTree; ENSGT00940000155237; -.
DR Proteomes; UP000233180; Unplaced.
DR GO; GO:0005911; C:cell-cell junction; IEA:InterPro.
DR GO; GO:0005829; C:cytosol; IEA:Ensembl.
DR GO; GO:0016607; C:nuclear speck; IEA:Ensembl.
DR GO; GO:0005886; C:plasma membrane; IEA:Ensembl.
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; cd01782; RA1_Afadin; 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 Reference proteome {ECO:0000313|Proteomes:UP000233180}.
FT DOMAIN 22..116
FT /note="Ras-associating"
FT /evidence="ECO:0000259|PROSITE:PS50200"
FT DOMAIN 229..331
FT /note="Ras-associating"
FT /evidence="ECO:0000259|PROSITE:PS50200"
FT DOMAIN 651..898
FT /note="Dilute"
FT /evidence="ECO:0000259|PROSITE:PS51126"
FT DOMAIN 997..1083
FT /note="PDZ"
FT /evidence="ECO:0000259|PROSITE:PS50106"
FT REGION 111..177
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 332..361
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 522..578
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1097..1213
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1225..1518
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1559..1814
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 126..177
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 332..352
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 527..551
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1120..1135
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1144..1159
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1161..1199
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1264..1290
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1292..1330
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1350..1365
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1396..1432
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1433..1482
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1504..1518
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1580..1666
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1672..1701
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1752..1766
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1783..1798
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1799..1814
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1814 AA; 205817 MW; E699DC4555BFCA72 CRC64;
MLQNLKRFEC QRDTQRRNDL EFHGVMRFYF QDKAAGNFAT KCIRVSSTAT TQDVIETLAE
KFRPDMRMLS SPKYSLYEVH VSGERRLDID EKPLVVQLNW NKDDREGRFV LKNENDAIPP
KKAQSNGPEK QEKEGVIQNF KRTLSKKEKK EKKKREKEAL RQASDKDDRP FQGEDVENSR
LAAEVYKDMP ETSFTRTISN PEVVMKRRRQ QKLEKRMQEF RSSDGRPDSG GTLRIYADSL
KPNIPYKTIL LSTTDPADFA VAEALEKYGL EKENPKDYCI ARVMLPPGAQ HSDEKGAKEI
ILDDDECPLQ IFREWPSDKG ILVFQLKRRP PDHIPKKTKK HLEGKTPKGK ERADGSGYGS
ALPPEKLPYL VELSPGRRNH FAYYNYHTYE DGSDSRDKPK LYRLQLSVTE VGTEKLDDSS
IQLFGPGIQP HHCDLTNMDG VVTVTPRSMD AETYVEGQRI SETTMLQSGM KVQFGASHVF
KFVDPSQDHA LAKRSVDGGL MVKGPRHKPG IVQETTFDLG GDIHSGTALP TSKSTTRLDS
DRVSSASSTA ERGMVKPMIR VEQQPDYRRQ ESRTQDASGP ELILPASIEF RESSEDSFLS
AIINYTNSST VHFKLSPTYV LYMACRYVLS NQYRPDISPP ERTHKVIAVV NKMVSMMEGV
IQEVDQVDQK QKNIAGALAF WMANASELLN FIKQDRDLSR ITLDAQDVLA HLVQMAFKYL
VHCLQSELNN YMPAFLDDPE ENSLQRPKID DVLHTLTGAM SLLRRCRVNA ALTIQLFSQL
FHFINMWLFN RLVTDPDSGL CSHYWGAIIR QQLGHIEAWA EKQGLELAAD CHLSRIVQAT
TLLTMDKYAP DDIPNINSTC FKLNSLQLQA LLQNYHCAPD EPFIPTDLIE NVVAVAENTA
DELARSDGRE VQLEEDPDLQ LPFLLPEDGY SCDVVRNIPN GLQEFLDPLC QRGFCRLIPH
TRSPGTWTIY FEGADYESHF LRENTELAQP LRKEPEIITV TLKKQNGMGL SIVAAKGAGQ
DKLGIYVKSV VKGGAADVDG RLAAGDQLLS VDGRSLVGLS QERAAELMTR TSSVVTLEVA
KQGAIYHGLA TLLNQPSPMM QRISDRRGSG KPRPKSEGFE LYNNSAQNGS PESPQLPWAE
YSEPKKLPGD DRLMKNRADH RSSPNVANQP PSPGGKSAYA SGTTAKITSV STGNLCTEEQ
TPPPRPEAYP IPTQTYTREY FTFPASKSQD RMAPPQNQWP NYEEKPHMHT DSNHSSIAIQ
RVTRSQEELR EDKAYQLERH RIEAAMDRKS DSDMWINQSS SLDSSTSSQE HLNHSSKSVT
PASTLTKSGP GRWKTPAAIP ATPVAVSQPI RTDLPPPPPP PPIHYAGDFD GISMDLPLPP
PPSTNQIGLP SAQVAAAERK KREEHQRWYE KEKARLEEER ERKRREQERK LGQMRTQSLN
PAPFSPLTTQ QMKPEKPSTL QRPQETVIRE LQPQQQPRTI ERRDLQYITV SKEELSSGDS
LSPDPWKRDA KEKLEKQQQM HIVDMLSKEI QELQSKPDRS AEESDRLRKL MLEWQFQKRL
QESKQKDEDD EEEEDDDVDT MLIMQRLEAE RRARLQDEER RRQQQLEEMR KREAEDRARQ
EEERRRQEEE RTKRDAEEKR RQEEGYYSRL EAERRRQHDE AARRLLEPEA PGLCRPPLPR
DYEPPSPSPA PGAPPPPPQR NASYLKTQAL SPDSLFTAKF VAYNEEEEEE DCSLAGPNSY
PGSAGAAVGA HDAYRDAKEK RSKSQDADLP GSSGAPENLT FKERQRLFSQ GQDVSNKVKA
SRKLTELENE LNTK
//
