ID H2RDP8_PANTR Unreviewed; 1651 AA.
AC H2RDP8; A0A2J8KHF3;
DT 21-MAR-2012, integrated into UniProtKB/TrEMBL.
DT 28-FEB-2018, sequence version 2.
DT 27-MAR-2024, entry version 70.
DE SubName: Full=Afadin, adherens junction formation factor {ECO:0000313|Ensembl:ENSPTRP00000059182.3};
GN Name=AFDN {ECO:0000313|Ensembl:ENSPTRP00000059182.3,
GN ECO:0000313|VGNC:VGNC:14790};
OS Pan troglodytes (Chimpanzee).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Pan.
OX NCBI_TaxID=9598 {ECO:0000313|Ensembl:ENSPTRP00000059182.3, ECO:0000313|Proteomes:UP000002277};
RN [1] {ECO:0000313|Ensembl:ENSPTRP00000059182.3, ECO:0000313|Proteomes:UP000002277}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16136131; DOI=10.1038/nature04072;
RG Chimpanzee sequencing and analysis consortium;
RT "Initial sequence of the chimpanzee genome and comparison with the human
RT genome.";
RL Nature 437:69-87(2005).
RN [2] {ECO:0000313|Ensembl:ENSPTRP00000059182.3}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
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DR EMBL; AACZ04062706; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC202803; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; XP_016812143.1; XM_016956654.1.
DR PaxDb; 9598-ENSPTRP00000059182; -.
DR Ensembl; ENSPTRT00000067597.3; ENSPTRP00000059182.3; ENSPTRG00000018810.7.
DR VGNC; VGNC:14790; AFDN.
DR eggNOG; KOG1892; Eukaryota.
DR GeneTree; ENSGT00940000155237; -.
DR HOGENOM; CLU_000594_1_0_1; -.
DR TreeFam; TF350731; -.
DR Proteomes; UP000002277; Chromosome 6.
DR Bgee; ENSPTRG00000018810; Expressed in lung and 21 other cell types or tissues.
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; 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:UP000002277}.
FT DOMAIN 39..133
FT /note="Ras-associating"
FT /evidence="ECO:0000259|PROSITE:PS50200"
FT DOMAIN 246..348
FT /note="Ras-associating"
FT /evidence="ECO:0000259|PROSITE:PS50200"
FT DOMAIN 668..908
FT /note="Dilute"
FT /evidence="ECO:0000259|PROSITE:PS51126"
FT DOMAIN 1007..1093
FT /note="PDZ"
FT /evidence="ECO:0000259|PROSITE:PS50106"
FT REGION 128..194
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 349..378
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 534..570
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1107..1223
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1235..1528
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1569..1651
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 143..194
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 349..369
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 544..568
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1129..1145
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1154..1169
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1171..1209
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1274..1300
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1302..1340
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1360..1375
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1406..1442
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1443..1492
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1514..1528
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1590..1651
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1651 AA; 187730 MW; D3F56A18F65A1BA2 CRC64;
MSAGGRDEER RKLADIIHHW NANRLDLFEI SQPTEDLEFH GVMRFYFQDK AAGNFATKCI
RVSSTATTQD VIETLAEKFR PDMRMLSSPK YSLYEVHVSG ERRLDIDEKP LVVQLNWNKD
DREGRFVLKN ENDAIPPKKA QSNGPEKQEK EGVIQNFKRT LSKKEKKEKK KREKEALRQA
SDKDDRPFQG EDVENSRLAA EVYKDMPETS FTRTISNPEV VMKRRRQQKL EKRMQEFRSS
DGRPDSGGTL RIYADSLKPN IPYKTILLST TDPADFAVAE ALEKYGLEKE NPKDYCIARV
MLPPGAQHSD EKGAKEIILD DDECPLQIFR EWPSDKGILV FQLKRRPPDH IPKKTKKHLE
GKTPKGKERA DGSGYGSTLP PEKLPYLVEL SPGRRNHFAY YNYHTYEDGS DSRDKPKLYR
LQLSVTEVGT EKLDDNSIQL FGPGIQPHHC DLTNMDGVVT VTPRSMDAET YVEGQRISET
TMLQSGMKVQ FGASHVFKFV DPSQDHALAK RSVDGGLMVK GPRHKPGIVQ ETTFDLGGDI
HSGTALPTSK STTRLDSDRV SSASSTAERG MVKPMIRVEQ QPDYRRQESR TQDVSGPELI
LPASIEFRES SEDSFLSAII NYTNSSTVHF KLSPTYVLYM ACRYVLSNQY RPDISPTERT
HKVIAVVNKM VSMMEGVIQK QKNIAGALAF WMANASELLN FIKQDRDLSR ITLDAQDVLA
HLVQMAFKYL VHCLQSELNN YMPAFLDDPE ENSLQRPKID DVLHTLTGAM SLLRRCRVNA
ALTIQLFSQL FHFINMWLFN RLVTDPDSGL CSHYWGAIIR QQLGHIEAWA EKQGLELAAD
CHLSRIVQAT TLLTMDKYAP DDIPNINSTC FKLNSLQLQA LLQNYHCAPD EPFIPTDLIE
NVVTVAENTA DELARSDGRE VQLEEDPDLQ LPFLLPEDGY SCDVVRNIPN GLQEFLDPLC
QRGFCRLIPH TRSPGTWTIY FEGADYESHL LRENTELAQP LRKEPEIITV TLKKQNGMGL
SIVAAKGAGQ DKLGIYVKSV VKGGAADVDG RLAAGDQLLS VDGRSLVGLS QERAAELMTR
TSSVVTLEVA KQGAIYHGLA TLLNQPSPMM QRISDRRGSG KPRPKSEGFE LYNNSTQNGS
PESPQLPWAE YSEPKKLPGD DRLMKNRADH RSSPNVANQP PSPGGKSAYA SGTTAKITSV
STGNLCTEEQ TPPPRPEAYP IPTQTYTREY FTFPASKSQD RMAPPQNQWP NYEEKPHMHT
DSNHSSIAIQ RVTRSQEELR EDKAYQLERH RIEAAMDRKS DSDMWINQSS SLDSSTSSQE
HLNHSSKSVT PASTLTKSGP GRWKTPAAIP ATPVAISQPI RTDLPPPPPP PPVHYAGDFD
GMSMDLPLPP PPSTNQIGLP SAQVAAAERK KREEHQRWYE KEKARLEEER ERKRREQERK
LGQMRTQSLN PAPFSPLTAQ QMKPEKPSTL QRPQETVIRE LQPQQQPRTI ERRDLQYITV
SKEELSSGDS LSPDPWKRDA KEKLEKQQQM HIVDMLSKEI QELQSKPDRS AEESDRLRKL
MLEWQFQKRL QESKQKDEDD EEEEEDDVDT MLIMQRLEAE RRARDEERRR QQQLEEMRKR
EAEDRARQEE ERRRQEEERT KRDAEEKVMV L
//
