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Database: UniProt
Entry: A0A3Q1GTY0_9TELE
LinkDB: A0A3Q1GTY0_9TELE
Original site: A0A3Q1GTY0_9TELE 
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.
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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
//
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