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Database: UniProt
Entry: A0A3B4G660_9CICH
LinkDB: A0A3B4G660_9CICH
Original site: A0A3B4G660_9CICH 
ID   A0A3B4G660_9CICH        Unreviewed;      1021 AA.
AC   A0A3B4G660;
DT   05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT   05-DEC-2018, sequence version 1.
DT   27-MAR-2024, entry version 26.
DE   SubName: Full=FERM domain containing 4A {ECO:0000313|Ensembl:ENSPNYP00000018360.1};
OS   Pundamilia nyererei.
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Ovalentaria; Cichlomorphae; Cichliformes; Cichlidae; African cichlids;
OC   Pseudocrenilabrinae; Haplochromini; Pundamilia.
OX   NCBI_TaxID=303518 {ECO:0000313|Ensembl:ENSPNYP00000018360.1, ECO:0000313|Proteomes:UP000261460};
RN   [1] {ECO:0000313|Ensembl:ENSPNYP00000018360.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (SEP-2023) to UniProtKB.
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DR   AlphaFoldDB; A0A3B4G660; -.
DR   STRING; 303518.ENSPNYP00000018360; -.
DR   Ensembl; ENSPNYT00000018820.1; ENSPNYP00000018360.1; ENSPNYG00000013853.1.
DR   GeneTree; ENSGT01020000230354; -.
DR   Proteomes; UP000261460; Unplaced.
DR   GO; GO:0005856; C:cytoskeleton; IEA:InterPro.
DR   GO; GO:0008092; F:cytoskeletal protein binding; 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; IPR000798; Ez/rad/moesin-like.
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   PRINTS; PR00935; BAND41.
DR   PRINTS; PR00661; ERMFAMILY.
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;
FT   DOMAIN          5..302
FT                   /note="FERM"
FT                   /evidence="ECO:0000259|PROSITE:PS50057"
FT   REGION          345..365
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          515..805
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          875..914
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          927..1021
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        345..364
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        550..567
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        576..590
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        616..696
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        724..763
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        777..792
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        928..955
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        963..1021
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1021 AA;  112729 MW;  D2E0E38F55B33002 CRC64;
     MTEGRRCQVH LLDDRKLELL VQPKLMAKDL LDLVASHFNL KEKEYFGIAY TDETGHFSWL
     QLDRRVLEHE FPKKSGPIVL YFCVRFYIES ISYLKDNATI ELFFLNAKSI IYKELIEVDS
     EVVFELASYI LQVSFNDATR SDLKKLPALP TQALKEHPSL AYCEDRVIEH YKKLSGQSRG
     QAIVNYMSIV ESLPTYGVHY YSVKDKQGIP WWLGLSYKGI FQYDYQDKVK PRKVFQWRQL
     ENLYFREKKF SVEVHDPRRA SVTRRTFGHS GIAVHTWYAC PALIKSIWAM AISQHQFYLD
     RKQSKSKIHA ARSLSEIAID LTETGTLKTS KLANMGSKGK IISGSSGSLL SSGSQESDSS
     QTAKKDMLAA LRARQEALEE TLKQRLEELK SICIREAELT GKLPKEYPLD PGEEPPTVRR
     KIGTAFKLDE QKILPKGEEE ELERLEREFA IQSQITEAAR RLASDPHVSS KKLKKQRKTS
     YLNALKKLQE IENSINEYRV RSGKKPTQRA SLIIEEANIG SEDSSLSDAL VLDDDDPQVT
     GTPTFSPVAS PHKGLPPRPP SHSRPPPPQS LDGLRHLHYT RSDYDKSPIK PKMWSESSLD
     EPYEKVKKRS SHSSHRRFPS SGSAEAGGSN SLQSSPIRSL PHWNSQSSMP STPDLRTRTP
     HYVHSTRSVD ISPTRLHSLS QHFRNRSSSL ESQGKLLASD SDAHPHTLGS PDFFLGPGRS
     SNGSDPLDDC SSCTSQSSSE HYYPSGGPPG SNPNYSTLGE DSPSKARQRQ RQRHRSAGHL
     GSSNSGSMPN LAAKNGSGGG LGGSGVGGGH HGVYLHSQSQ PSSQYRIKEY PLYVEGSPNP
     VVVRSLESDQ EGHYSVKAQF KTSSSYTAGG LYKEAWGGEE GGEGSGRLTP SRSQIVRTPS
     LGREGGGGGG GGRAAVSEEL RCWYQRSSGS LKERSHSHSG STSSETGSQQ GTLGHGRGSR
     AIATSASPHS QRSMTPSSEH AATPTPPCSP QHILNWQSGG TADCSPTEDV CQSPPQPSSD
     A
//
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