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Database: UniProt
Entry: A0A455BNK8_PHYMC
LinkDB: A0A455BNK8_PHYMC
Original site: A0A455BNK8_PHYMC 
ID   A0A455BNK8_PHYMC        Unreviewed;      1791 AA.
AC   A0A455BNK8;
DT   05-JUN-2019, integrated into UniProtKB/TrEMBL.
DT   05-JUN-2019, sequence version 1.
DT   27-MAR-2024, entry version 20.
DE   SubName: Full=Afadin isoform X2 {ECO:0000313|RefSeq:XP_028350560.1};
GN   Name=AFDN {ECO:0000313|RefSeq:XP_028350560.1};
OS   Physeter macrocephalus (Sperm whale) (Physeter catodon).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Whippomorpha; Cetacea; Odontoceti;
OC   Physeteridae; Physeter.
OX   NCBI_TaxID=9755 {ECO:0000313|Proteomes:UP000248484, ECO:0000313|RefSeq:XP_028350560.1};
RN   [1] {ECO:0000313|RefSeq:XP_028350560.1}
RP   IDENTIFICATION.
RC   TISSUE=Muscle {ECO:0000313|RefSeq:XP_028350560.1};
RG   RefSeq;
RL   Submitted (NOV-2023) to UniProtKB.
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DR   RefSeq; XP_028350560.1; XM_028494759.2.
DR   Proteomes; UP000248484; Chromosome 10.
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; 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:UP000248484}.
FT   DOMAIN          39..134
FT                   /note="Ras-associating"
FT                   /evidence="ECO:0000259|PROSITE:PS50200"
FT   DOMAIN          247..349
FT                   /note="Ras-associating"
FT                   /evidence="ECO:0000259|PROSITE:PS50200"
FT   DOMAIN          654..894
FT                   /note="Dilute"
FT                   /evidence="ECO:0000259|PROSITE:PS51126"
FT   DOMAIN          993..1079
FT                   /note="PDZ"
FT                   /evidence="ECO:0000259|PROSITE:PS50106"
FT   REGION          130..196
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          352..379
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          525..585
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1093..1176
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1188..1207
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1218..1487
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1533..1791
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          1496..1523
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        144..196
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        352..370
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        531..545
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1116..1131
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1140..1155
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1233..1247
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1260..1286
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1291..1327
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1372..1408
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1414..1435
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1579..1647
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1656..1674
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1763..1791
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1791 AA;  201342 MW;  24DBDA1028D21222 CRC64;
     MSAGGRDEER RKLADIIQHW NANRLDLFEI SQPTEDLEFH GVMRFYFQDK AAGNFATKCI
     RVSSTATTQD VLETLAEKFR PDMRMLSSPK YSLYEVHVSG EERRLDIDEK PLVVQLNWNK
     DDREGRFVLK NENDAIPAKK AQSNGPEKQE KEGVIQNFKR TLSKKEKKEK KKREKEAMRQ
     ASDRDDRPFH GDDTENSRLA AEVYKDMPET SFTRTISNPE VVMKRRRQQK LEKRMQEFRS
     SDGRPDSGGT LRIYADSLKP NIPYKTILLS TTDPADFAVA EALEKYGLER ENPKDYCIAR
     VMLPPGAQHS DEKAAEEIIL DDDECPLQIF REWPNDRGIL VFQLKRRPPD YIPKKSQKHV
     DGKPLHGKER VDGSGYGSAL PPEKLPYLVE LSPDGSDSRD KPKLYRLQLS VTEVGTEKFD
     DGSIQLFGSG IEPHHCDLTN MDGVVTVTPR SMDAETYVDG QRISETTMLH SGMKVQFGAS
     HVFKFVDPSQ DHALPKRSVD GGLMAKGPRQ RPGIVQETTF DLGGDVHSGT ALPASKSSSR
     LDGDRGLSAA STAERGMVKP VVRVEQLPDY RRQESRTQDT PGPDLILPAS IEFRESSEDS
     FLSAIINYTN SSTVHFKLSP TYVLYMACRY VLSSQYRPDV SPAERTHKVI AIVNKMVSMM
     EGVIQKQKNI AGALAFWMAN ASELLNFIKQ DRDLSRITLD AQDVLAHLVQ MAFKYLVHCL
     QSELNNYMPA FLDDPEENSL QRPKIDDVLH TLTGAMSLLR RCRVNAALTI QLFSQLFHFI
     NMWLFNRLVT DPESGLCSHY WGAIIRQQLG HVEAWAEKQG LELAADCHLS RIVQATTLLT
     MDKYAPDDIP NINSTCFKLN SLQLQALLQN YHCAPDEPFV PTDLMEHVVA VAENTADELA
     RSDGREVQLE EDPDLQLPFL LPEDGYSCDV VRNIPNGLQE FLDPLCQRGF CRLIPHPRSP
     GTWTIYFEGA DYESHLMREN TELAQPLRKE PEIITVTLKK QNGMGLSIVA AKGAGQDKLG
     IYVKSVVKGG AADVDGRLAA GDQLLSVDGR SLVGLSQERA AELMTRTSSV VTLEVAKQGA
     IYHGLATLLN QPSPMMQRIS DRRGSGKPRP KSEGFELYNN SAQNGSPESP QMPWAEYSEP
     KKLPGDDRLM KNRADHRSSP NVANEPPSPG GKGAYASGTA AKITSVSTGN LCAEEQTPPP
     RAEAYPIPTQ TYTREYFTFP ASKSQDRTAP PQDQWPRYEE KPHVHTDSSH SSTAVQRVTR
     SQEELREDVG FHLERQRVEA AMERRSDGGD AWLNQGSSLG SSASSQEHLG PPSRAGTPAS
     TLTKSGPGRW KTPAASPPVR TDPPPGHYGA GDGDSVPADS PLPPPPTGAQ VAAERKKREE
     QQRWYEKEKA RLEEERERRR REQERRLGQL RAQAPPPGAP PPGPAAPPPG PAPARAPDTV
     IRELQPQQQP RTIERRDLQY ITVSREELAS GDSLSPDPWK RDAREKLEKQ QQLHIVDLLS
     REIQELQGKA ERSAEESDRL RKLMLEWQFQ KRLQESKQKD EDDEEEEDDD VDTVLLMQRL
     EAERRARQTA MPAISVLDLL QDEERRRQQQ LEEMRTREAE ERARQEEQRA RREAEEKRRQ
     EEGYYSRLEA ERRRQHDEAE RQLLEPEELG LGRPPLPRGY EPPAPGPPPP PQRTASYLQA
     QVLSPDALYS AKLVAYTEEE EEEEEEEDGG PAGPNSYVGS AGTLIGAHDV YRDPREKPSK
     SQDADVPGGP GAPENLTFRE RQRLFSQGHD VSNKVKASRK LTELENELNT K
//
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