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Database: UniProt
Entry: A0A667XY20_9TELE
LinkDB: A0A667XY20_9TELE
Original site: A0A667XY20_9TELE 
ID   A0A667XY20_9TELE        Unreviewed;       628 AA.
AC   A0A667XY20;
DT   17-JUN-2020, integrated into UniProtKB/TrEMBL.
DT   17-JUN-2020, sequence version 1.
DT   27-MAR-2024, entry version 16.
DE   RecName: Full=Protein 4.1 {ECO:0000256|ARBA:ARBA00023658};
DE   AltName: Full=Band 4.1 {ECO:0000256|ARBA:ARBA00030419};
DE   AltName: Full=Erythrocyte membrane protein band 4.1 {ECO:0000256|ARBA:ARBA00032586};
OS   Myripristis murdjan (pinecone soldierfish).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Holocentriformes; Holocentridae; Myripristis.
OX   NCBI_TaxID=586833 {ECO:0000313|Ensembl:ENSMMDP00005020162.1, ECO:0000313|Proteomes:UP000472263};
RN   [1] {ECO:0000313|Ensembl:ENSMMDP00005020162.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (SEP-2023) to UniProtKB.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cell cortex
CC       {ECO:0000256|ARBA:ARBA00004544}. Cytoplasm, cytoskeleton
CC       {ECO:0000256|ARBA:ARBA00004245}. Nucleus
CC       {ECO:0000256|ARBA:ARBA00004123}.
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DR   AlphaFoldDB; A0A667XY20; -.
DR   Ensembl; ENSMMDT00005020638.1; ENSMMDP00005020162.1; ENSMMDG00005009494.1.
DR   GeneTree; ENSGT00940000157833; -.
DR   Proteomes; UP000472263; Unplaced.
DR   GO; GO:0005938; C:cell cortex; IEA:UniProtKB-SubCell.
DR   GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0003779; F:actin binding; IEA:InterPro.
DR   GO; GO:0005516; F:calmodulin binding; IEA:UniProtKB-KW.
DR   GO; GO:0005198; F:structural molecule activity; IEA:InterPro.
DR   GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR   GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
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:SF12; PROTEIN 4.1; 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; 2.
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   Calmodulin-binding {ECO:0000256|ARBA:ARBA00022860};
KW   Cell cycle {ECO:0000256|ARBA:ARBA00023306};
KW   Cell division {ECO:0000256|ARBA:ARBA00022618};
KW   Mitosis {ECO:0000256|ARBA:ARBA00022776};
KW   Reference proteome {ECO:0000313|Proteomes:UP000472263};
KW   Transport {ECO:0000256|ARBA:ARBA00022448}.
FT   DOMAIN          1..282
FT                   /note="FERM"
FT                   /evidence="ECO:0000259|PROSITE:PS50057"
FT   REGION          540..570
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        548..570
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   628 AA;  70702 MW;  D4D0C3A0CBF9C4C9 CRC64;
     MQCTVTLLDD AQFECELDKH AKGQELFMQV CDHLNLLEKD YFGLANWETP TSKTWLDPSK
     EIRKQVPGAV YEFTFNVKFY PPDPAQLTED LTRYYLCLQL RKDIIRGTLP CSFVTLSLLG
     SYTAQSELGE YDPEIHGTDY VKELNLATGQ TQELEEKVME LHRTYRSMSP AQADMLFLEN
     AKKLAMYGVD LHQAKDLEGV DIMLGVCSSG LMVYKDKLRI NRFPWPKVLK ISYKRSSFFI
     KIRPSEQEQY ESTIGFKLPN YKASKKLWKV CVEHHTFFRV STVEPPSSRR FLALGSKFRY
     SGRTQAQTRQ ASAEIVRPAP RFTRSASKRL SRNLDGVVGM QKGTRPVSAP VFSQAALAEA
     GIPVALDQPQ TSTPIKTSRK EERKLEVTVE TVEPPKTETA AEVKVFEFSN HYPLTRSFCN
     TIPMKEFDKP QEDLLRHHAS ISELKRNFME SVPEARPSEW DKRLSTHSPF RTLGINGQCN
     TRVWSLPLMG LCSHPQPPLV QTQTVTITAI SNSLSSDIST TEVPIVPTKT ITYESSKATV
     DEADGTKDGA TLSSTRTSTS ESTSGTTVTT TTTHISKVVK GGSSETRVEK RIVITADSEA
     DQDQLYLPRT HTHKIFHQST SAPKMVLV
//
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