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Database: UniProt
Entry: A0A3Q1FTE3_9TELE
LinkDB: A0A3Q1FTE3_9TELE
Original site: A0A3Q1FTE3_9TELE 
ID   A0A3Q1FTE3_9TELE        Unreviewed;      1012 AA.
AC   A0A3Q1FTE3;
DT   10-APR-2019, integrated into UniProtKB/TrEMBL.
DT   10-APR-2019, sequence version 1.
DT   27-MAR-2024, entry version 24.
DE   SubName: Full=FERM domain containing 4A {ECO:0000313|Ensembl:ENSAPOP00000018892.1};
OS   Acanthochromis polyacanthus (spiny chromis).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Ovalentaria; Pomacentridae; Acanthochromis.
OX   NCBI_TaxID=80966 {ECO:0000313|Ensembl:ENSAPOP00000018892.1, ECO:0000313|Proteomes:UP000257200};
RN   [1] {ECO:0000313|Ensembl:ENSAPOP00000018892.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (NOV-2023) to UniProtKB.
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DR   AlphaFoldDB; A0A3Q1FTE3; -.
DR   Ensembl; ENSAPOT00000028617.1; ENSAPOP00000018892.1; ENSAPOG00000022522.1.
DR   GeneTree; ENSGT01020000230354; -.
DR   Proteomes; UP000257200; Unplaced.
DR   GO; GO:0005856; C:cytoskeleton; IEA:InterPro.
DR   GO; GO:0090162; P:establishment of epithelial cell polarity; IEA:InterPro.
DR   CDD; cd14473; FERM_B-lobe; 1.
DR   CDD; cd13191; FERM_C_FRMD4A_FRMD4B; 1.
DR   CDD; cd17199; FERM_F1_FRMD4A; 1.
DR   Gene3D; 1.20.80.10; -; 1.
DR   Gene3D; 2.30.29.30; Pleckstrin-homology domain (PH domain)/Phosphotyrosine-binding domain (PTB); 1.
DR   InterPro; IPR019749; Band_41_domain.
DR   InterPro; IPR021774; CUPID.
DR   InterPro; IPR014352; FERM/acyl-CoA-bd_prot_sf.
DR   InterPro; IPR035963; FERM_2.
DR   InterPro; IPR019748; FERM_central.
DR   InterPro; IPR019747; FERM_CS.
DR   InterPro; IPR000299; FERM_domain.
DR   InterPro; IPR018979; FERM_N.
DR   InterPro; IPR018980; FERM_PH-like_C.
DR   InterPro; IPR047176; FRMD4A/B.
DR   InterPro; IPR041785; FRMD4A/B_FERM_C.
DR   InterPro; IPR011993; PH-like_dom_sf.
DR   InterPro; IPR029071; Ubiquitin-like_domsf.
DR   PANTHER; PTHR46079; FERM DOMAIN-CONTAINING PROTEIN 4; 1.
DR   PANTHER; PTHR46079:SF3; FERM DOMAIN-CONTAINING PROTEIN 4A; 1.
DR   Pfam; PF11819; CUPID; 1.
DR   Pfam; PF09380; FERM_C; 1.
DR   Pfam; PF00373; FERM_M; 1.
DR   Pfam; PF09379; FERM_N; 1.
DR   SMART; SM00295; B41; 1.
DR   SMART; SM01196; FERM_C; 1.
DR   SUPFAM; SSF50729; PH domain-like; 1.
DR   SUPFAM; SSF47031; Second domain of FERM; 1.
DR   SUPFAM; SSF54236; Ubiquitin-like; 1.
DR   PROSITE; PS00660; FERM_1; 1.
DR   PROSITE; PS00661; FERM_2; 1.
DR   PROSITE; PS50057; FERM_3; 1.
PE   4: Predicted;
KW   Reference proteome {ECO:0000313|Proteomes:UP000257200}.
FT   DOMAIN          5..289
FT                   /note="FERM"
FT                   /evidence="ECO:0000259|PROSITE:PS50057"
FT   REGION          332..352
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          511..809
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          863..900
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          913..1012
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        332..351
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        537..554
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        563..577
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        603..682
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        711..750
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        764..784
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        914..942
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        955..1012
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1012 AA;  111999 MW;  CE0C14309F721C4C CRC64;
     MTEGRRCQVH LLDDRKLELL VQPKLMAKDL LDLVASHFNL KEKEYFGIAY TDETGHFSWL
     QLDRRVLEHE FPKKSGPIVL YFCVRFYIES ISYLKDNATI ELFFLNAKSI IYKELIEVDS
     DIVFELASYI LVDQVLWFFF PPKLSTQPAE CYRVIEHYKK LSGQSRGQAI VNYMSIVESL
     PTYGVHYYAV KDKQGIPWWL GLSYKGIFQY DHQDKVKPRK VFQWRQLENL YFREKKFSVE
     VHDPRRASVT RRTFGHSGIA VHTWYACPAL IKSIWAMAIS QHQFYLDRKQ SKSKIHAARS
     LSEIAIDLTE TGTLKTSKLA NMGSKGKIIS GSSGSLLSSG SQESDSSQTA KKDMLAALRA
     RQEALEETLR QRLEELKSIC IREAELTGKL PKEYPLDPGE EPPTVRRKIG TAFKLDEQKI
     LPKGEEEELE RLEREFAIQS QITEAARRLA SDPHVSSKKL KKQRKTSYLN ALKKLQEIEN
     SINEYRVRSG KKPTQRASLI IEEANMCSED SSLSDALVLD DDDPQVTGTP TFSPVASPHK
     GLPPRPPSHS RPPPPQSLDG LRHLHYTRSD YDKSPIKPKM WSESSLDEPY EKVKKRSSHS
     SHRRFPSSGS AEAGGSNSLQ SSPIRSLPHW NSQSSMPSTP DLRTRNPHYI HSTRSVDISP
     TRLHSLSQHF RNRSSSLESQ GKLLVSDPDA HPHTLGSPDF FLGPGRSSNG SDPLDDCSSC
     TSQSSSEHYY PSGGPPGSNP NYSTLGEDSP SKARQRQRQR HRSAGHLGSS NSGSMPNLAA
     KNGSGGGSSG GGMGGGHHGV YLHSQSQPSS QYRIKEYPLY VEGSPNPVVV RSLESDQEGH
     YSVKAQFKTS SSYTAGGLYK EAWGGEEGGE GSGRLTPSRS QIVRTPSLGR EGGGGGGGRA
     AVSEELRCWY QRSSGSLKER SHSHSGSTSS ETGSQQGTLG HGRGSRVGTL VKGSPAASPH
     SQRSMTPSSE HAATPTPPCS PQHILNWQSG GTADSSPTED VCQSPPQPNS DA
//
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