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Database: UniProt
Entry: A0A3Q2V4X4_HAPBU
LinkDB: A0A3Q2V4X4_HAPBU
Original site: A0A3Q2V4X4_HAPBU 
ID   A0A3Q2V4X4_HAPBU        Unreviewed;       842 AA.
AC   A0A3Q2V4X4;
DT   10-APR-2019, integrated into UniProtKB/TrEMBL.
DT   10-APR-2019, sequence version 1.
DT   27-MAR-2024, entry version 19.
DE   SubName: Full=Band 4.1-like protein 1 {ECO:0000313|Ensembl:ENSHBUP00000005540.1};
OS   Haplochromis burtoni (Burton's mouthbrooder) (Chromis burtoni).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Ovalentaria; Cichlomorphae; Cichliformes; Cichlidae; African cichlids;
OC   Pseudocrenilabrinae; Haplochromini; Haplochromis.
OX   NCBI_TaxID=8153 {ECO:0000313|Ensembl:ENSHBUP00000005540.1, ECO:0000313|Proteomes:UP000264840};
RN   [1] {ECO:0000313|Ensembl:ENSHBUP00000005540.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (NOV-2023) to UniProtKB.
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DR   AlphaFoldDB; A0A3Q2V4X4; -.
DR   Ensembl; ENSHBUT00000006825.1; ENSHBUP00000005540.1; ENSHBUG00000006997.1.
DR   GeneTree; ENSGT00940000158442; -.
DR   Proteomes; UP000264840; Unplaced.
DR   GO; GO:0005856; C:cytoskeleton; IEA:InterPro.
DR   GO; GO:0003779; F:actin binding; IEA:InterPro.
DR   GO; GO:0005198; F:structural molecule activity; IEA:InterPro.
DR   GO; GO:0030866; P:cortical actin cytoskeleton organization; IEA:InterPro.
DR   CDD; cd14473; FERM_B-lobe; 1.
DR   CDD; cd13184; FERM_C_4_1_family; 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; IPR008379; Band_4.1_C.
DR   InterPro; IPR019749; Band_41_domain.
DR   InterPro; IPR000798; Ez/rad/moesin-like.
DR   InterPro; IPR014847; FA.
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; IPR011993; PH-like_dom_sf.
DR   InterPro; IPR007477; SAB_dom.
DR   InterPro; IPR029071; Ubiquitin-like_domsf.
DR   PANTHER; PTHR23280; 4.1 G PROTEIN; 1.
DR   PANTHER; PTHR23280:SF24; BAND 4.1-LIKE PROTEIN 1; 1.
DR   Pfam; PF05902; 4_1_CTD; 1.
DR   Pfam; PF08736; FA; 1.
DR   Pfam; PF09380; FERM_C; 1.
DR   Pfam; PF00373; FERM_M; 1.
DR   Pfam; PF09379; FERM_N; 1.
DR   Pfam; PF04382; SAB; 1.
DR   PIRSF; PIRSF002304; Membrane_skeletal_4_1; 1.
DR   PRINTS; PR00935; BAND41.
DR   PRINTS; PR00661; ERMFAMILY.
DR   SMART; SM00295; B41; 1.
DR   SMART; SM01195; FA; 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   Actin-binding {ECO:0000256|ARBA:ARBA00023203};
KW   Reference proteome {ECO:0000313|Proteomes:UP000264840}.
FT   DOMAIN          51..332
FT                   /note="FERM"
FT                   /evidence="ECO:0000259|PROSITE:PS50057"
FT   REGION          1..51
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          403..462
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          484..523
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          625..690
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          735..755
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        10..33
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        403..422
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        435..462
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        497..511
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        630..653
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        663..690
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   842 AA;  95350 MW;  340604E5BEE66179 CRC64;
     MQDSASDSKI AKQDQNKHMD GHRETDDMSE KTSPNKNLKS PQKGSKRLKT APFKVTLLDS
     SEFEGETEKH SKGQTLMDMV CEHLNLLEKD YFGLTFADTD SQKNWLDPSK EIKKQMRNSP
     WHFAFAVKFY PPDPSQLMED ITRYYLCLQL RDDMLSGRLP CSFVTHALLG SYTVQAELGD
     YDQDDHGTDY VSDFRFAPNQ TRELEERVME LHRNYKGMTP AEAEMNFLEN AKKLSMYGVD
     LHHAKDSEGI EIMLGVCANG LLIYRDRLRI NRFAWPKILK ISYKRSNFYI KIRPGEYEQF
     ESTIGFKLPN HRAAKRLWKV CIEHHTFFRL VSPEPPPKGF LVMGSKFRYS GRTQAQTRQA
     SALIDRPAPH FERSTSKRYL LSRSLDGEFS RPVSAMCENH DGLSHRSISE HRRLHSPSGD
     EQETELEPSL EQDEEEKEHE QGREAEQDKD HDGNVTPSRK KEIMFLDKSQ DVLLKHQASI
     NELKRALREP NSKLMNREKR LSATSPTGTP EKKASVGRAM GKEPVNSLSV EGFVQKTLVT
     SPEEPVSTPA IYEEPFADFK KEFGERRPQP SIASEEEQER DTVACMKETH LGIERKCSSM
     TVSSTSSLEA EVDFTVITDL HSGLEDFSKG VPELGERERQ PEVGREDFEE TSRFYSARLM
     GSRDKSPIEE RLPEEGMHHE PPVAKKDPNT VSVAHKLKRA DSKTETHTNG SEAHANVVNV
     SSQNYGVVSP QEAPAAVKEN GSPVKASTQG RESVVSPLTI TAENVTSATT TQVTKTVKGG
     YSETRIEKRI IITGDDDVDQ HQALAMAIQE AKQQHPDMLV TKAVVIRETE SPTEELQQKA
     ES
//
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