ID G1KHR9_ANOCA Unreviewed; 1774 AA.
AC G1KHR9;
DT 19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT 29-SEP-2021, sequence version 3.
DT 27-MAR-2024, entry version 80.
DE SubName: Full=Afadin, adherens junction formation factor {ECO:0000313|Ensembl:ENSACAP00000008247.4};
GN Name=AFDN {ECO:0000313|Ensembl:ENSACAP00000008247.4};
OS Anolis carolinensis (Green anole) (American chameleon).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC Iguania; Dactyloidae; Anolis.
OX NCBI_TaxID=28377 {ECO:0000313|Ensembl:ENSACAP00000008247.4, ECO:0000313|Proteomes:UP000001646};
RN [1] {ECO:0000313|Ensembl:ENSACAP00000008247.4, ECO:0000313|Proteomes:UP000001646}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JBL SC #1 {ECO:0000313|Ensembl:ENSACAP00000008247.4,
RC ECO:0000313|Proteomes:UP000001646};
RG The Genome Sequencing Platform;
RA Di Palma F., Alfoldi J., Heiman D., Young S., Grabherr M., Johnson J.,
RA Lander E.S., Lindblad-Toh K.;
RT "The Genome Sequence of Anolis carolinensis (Green Anole Lizard).";
RL Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSACAP00000008247.4}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
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DR STRING; 28377.ENSACAP00000008247; -.
DR Ensembl; ENSACAT00000008424.4; ENSACAP00000008247.4; ENSACAG00000008269.4.
DR eggNOG; KOG1892; Eukaryota.
DR GeneTree; ENSGT00940000155237; -.
DR TreeFam; TF350731; -.
DR Proteomes; UP000001646; Chromosome 1.
DR Bgee; ENSACAG00000008269; Expressed in testis and 13 other cell types or tissues.
DR ExpressionAtlas; G1KHR9; baseline.
DR GO; GO:0005912; C:adherens junction; IBA:GO_Central.
DR GO; GO:0050839; F:cell adhesion molecule binding; IBA:GO_Central.
DR GO; GO:0007155; P:cell adhesion; IEA:UniProtKB-KW.
DR GO; GO:0032880; P:regulation of protein localization; IBA:GO_Central.
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:UP000001646}.
FT DOMAIN 44..139
FT /note="Ras-associating"
FT /evidence="ECO:0000259|PROSITE:PS50200"
FT DOMAIN 250..352
FT /note="Ras-associating"
FT /evidence="ECO:0000259|PROSITE:PS50200"
FT DOMAIN 670..917
FT /note="Dilute"
FT /evidence="ECO:0000259|PROSITE:PS51126"
FT DOMAIN 1016..1102
FT /note="PDZ"
FT /evidence="ECO:0000259|PROSITE:PS50106"
FT REGION 134..197
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 357..381
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 546..568
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1116..1198
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1245..1270
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1315..1549
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1587..1740
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 140..154
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 156..197
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 357..373
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1139..1154
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1162..1177
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1179..1198
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1245..1264
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1318..1354
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1375..1389
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1422..1458
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1472..1510
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1532..1547
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1608..1697
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1774 AA; 202293 MW; D1FECEE37217BDAC CRC64;
MSGGGGGGGS REEERRKLAD IINHWNANRL DLFEISPPTE DLEFHGVMRF YFQDRAAGNF
ATKCIRVSST ATTQDVIETL AEKFRPDMRM LSSPKYSLYE VHVSGEERRL DIDEKPLVVQ
LNWNKDDREG RFVLKNENDA LPPKTQSNGP EKQEKEGVIQ NFKRTLSKKE KKEKKRREKE
ALRQALDNDG PFHGDDIENS RLAAEVYKDM PETSFTRTIS NPEVVMKRRR QQKLEKRMQE
FRSSDGRPDS GGTLRIYADS LKPNIPYKTI LLSTTDTADF AVIEALEKYG LEKENPKDYC
IARVMLPPGA QHSDDKGAKE SILDDDECPL QIFREWPSDK GILVFQLKRR PPDYVPKKLK
KQVDGKPLKG KERVDGSSYG SSLPPEKLPY LVELSPGRRN HFAYYNYHTY EDGSDSRDKP
KLYRLQLSVT EVGTEKLDEN SIQLFGPGIQ PHHCDLTNMD GVVTVTPRNI DAETYVEGQR
ISETTMLQSG MKVQFGTSHV FKFVDPVQDH IPKGRLDAGH MVKSSRIKAG AVQETTFDLE
GDIHSGTGLS TSKSTNRLDS DRMSTSSTAE RGMVKPMIRI EQQQDYRRQD GRPQDLHGPE
LILPASIEFR ETSEDAFLSA IINYTNSSTV HFKLSPTYVL YMTCRYVLSS QYRPDISPAE
RTHKVIAIVN KMVSMMEGVI QEVDQVDQKQ KNIAGALAFW MANASELLNF IKQDRDLSRI
TLDAQDVLAH LVQMAFKYLV HCLQSELNNY MPAFLDDPEE NSPQRPKIDD VLHTLTGAMS
LLRRCRVNAA LTIQLFSQLF HFINMWLFNR LVTDPDSGLC SHYWGAIIRQ QLGHIEAWAE
KQGLELAADC HLSRIVQATT LLTMDKYLPE DIPNINSTCF KLNSLQLHAL LQNYHCAPDE
PFIPTELIEN VVAVAENTAD ELARSDGREV QLEEDPDLQL PFLLPEDGYS CDVVRNIPNG
LQEFLDPLCQ RGFCRLTPHP RSPGTWTIYF EGADYENHLL QDNADLAQPL RKEPEIITVT
LKKQNGMGLS IVAAKGAGQD KLGIYVKSVV KGGAADADGR LAAGDQLLSV DGRSLVGLSQ
ERAAELMTRT GSVVTLEVAK QGAIYHGLAT LLNQPSPMMQ RVSDRRGSGK PRPKSEGFEL
YNNSAQNGSP ESPQPWPEYN EPKKLPGDDR LMKNRADHRS SPNVANQPPS PGTKNAYAAG
TTNKITSVST GNLCTEEQIL PPRPEAYPIP TQTYTREYFT FPASKSQDRM GPAQNQWSSY
EEKAQVPEES NHYISAAMQR VTRSQEELRD DKVYHPERNR LEVVIRKDVE YIDRKSDSDP
WMNSSVDSST SSQEHLNHSS KSIPPGSSLT KSGPGRWKTP IVPQPLSLAP AQSNRTDLPP
PPPPPPVHYA AEFDGLQMDL PLPPPPPPSS QLGPQASSQA AAAERKKREE HQRWYEKEKA
RLEEERDRKR REQERKLGQM RAQPLIPTQP LLPPASVQQV KPEKPSTLQR SQETVIRELQ
PQQQPRTIER RDLQYITISK EELSSSDSLS PDPWKRDAKE KLEKQQQMHI VDMLSKEIQE
LQNKPDRTAE ENDRLRKLML EWQFQKRLQE SKQKDEDEDD EEDDDIDTML IMQRLEAERR
ARLQDEERRR QQQLEEMRKR EAEDRARQEE ERRRQEEERT KREAEQKRRQ EEEYYNRLEA
ERRRQHDEAE RRLLEPDEPG INYTGSTGAI VGSHEPYQDP REKNSKSQDT ELPGAPENLT
FRERQRLFSQ GQDVSNKVKA SRKLMELENE LNTK
//
