ID A0A3Q1GTY0_9TELE Unreviewed; 1061 AA.
AC A0A3Q1GTY0;
DT 10-APR-2019, integrated into UniProtKB/TrEMBL.
DT 10-APR-2019, sequence version 1.
DT 27-MAR-2024, entry version 20.
DE SubName: Full=Band 4.1-like protein 2 {ECO:0000313|Ensembl:ENSAPOP00000033149.1};
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:ENSAPOP00000033149.1, ECO:0000313|Proteomes:UP000257200};
RN [1] {ECO:0000313|Ensembl:ENSAPOP00000033149.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR STRING; 80966.ENSAPOP00000033149; -.
DR Ensembl; ENSAPOT00000027738.1; ENSAPOP00000033149.1; ENSAPOG00000021574.1.
DR Ensembl; ENSAPOT00000027797.1; ENSAPOP00000018250.1; ENSAPOG00000021574.1.
DR GeneTree; ENSGT00940000155617; -.
DR OrthoDB; 5391231at2759; -.
DR Proteomes; UP000257200; 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 CDD; cd17106; FERM_F1_EPB41L; 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:SF20; BAND 4.1-LIKE PROTEIN 3; 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; 4.
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:UP000257200}.
FT DOMAIN 205..487
FT /note="FERM"
FT /evidence="ECO:0000259|PROSITE:PS50057"
FT REGION 1..189
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 712..731
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 779..837
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 867..887
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 7..56
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 64..80
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 99..162
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 779..808
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1061 AA; 118302 MW; CFE1558E961528D1 CRC64;
MTTEAGSETE VKEKAEESAA QPDQSEKAAE ETKEVANAEG EEKEKEKEKE GKEGKGISRY
LPTWLKKQKS QSQTSPTKEA PPTEEPVAKV TQEEEGPAPE VNGHAEEVEE KEEVKSEQVK
EKEAESHSNA SADTEPAKEE KVDESTEKSP EETEKEATEG EGAEEEKTEE QEGEKEAKGG
GGEEGQTSIF QSPLRLVRKN KMKLVVCHVT LLDGTDFSCE VEKRAKGQFL FFKVCEHLNL
LEKDYFGLTY MDSHEEKCWL DPTKEIKRQI RSNNWQFAFN VKFYPPDPSL LTEDITRYLL
CLQLREDVSS GRLPCSFVTH ALLGSYTLQA EFGDHEPDQP RPLDYISQAT FAPNQNKEME
EKILELHKSH RGMTPAQADA QFLENAKKLS MYGVDLHHAK DSEGVDIMLG VCANGLLVYK
DRLRINRFAW PKILKISYKR NNFYIKIRPG ETEQFESTVG FKLQNHRSAK RLWKVCVENH
SFFRLNAPEP PTKARFLTLG SKFRYSGRTQ AQTRLASSLI DRPAPNFERT SSKRISRSLD
GAPVISITEA TAENGREPHL ELQSDSKSPL RVHGDNIYVR HSNLMLEDHD KTQEEVLKHQ
ASISQLKRSF MEAPPPSPPQ PNQWEKRLTS SPATSIRIQQ QQVSLEEEIA SVLFSRHSAA
GFHSVDETDC SVPEATLDAV ICSASAAVCS SSSPQKLLIS STMSAAEVVE PQTEAAPADN
TISDTKEPAK TTEVEIEETV VVQEVSRVAK PGVVTVTAGL PAAEQETRKQ EVRVVEEEVM
LKEEEEEVKP TKQESVSSES ESEEEAEYHP NMPIAQIPEE KEDEEEQEET TKKKEEVEED
VLVLDAPSIP AEEETNRAED DMKKIETEES TDDPMVTPDE APNGILLPEE GVTAPALEKE
EPKVNGEASL VEAEPRPQVI CCSEPPVVKT EMVTISDTFA AQKTEIATKE VPIVHTETKT
ITYEAAQLDG NGDGEPGVLM TAQTITSESL CTTTTTHITK TLKGGLSETR IEKRIVITGD
CDIDHDQALA QAIKEAKEQH PDMSVTRVVV HKETELAEEE D
//