ID A0A3P8T250_AMPPE Unreviewed; 1062 AA.
AC A0A3P8T250;
DT 13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT 13-FEB-2019, sequence version 1.
DT 27-MAR-2024, entry version 23.
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 Amphiprion percula (Orange clownfish) (Lutjanus percula).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Pomacentridae; Amphiprion.
OX NCBI_TaxID=161767 {ECO:0000313|Ensembl:ENSAPEP00000019180.1, ECO:0000313|Proteomes:UP000265080};
RN [1] {ECO:0000313|Ensembl:ENSAPEP00000019180.1, ECO:0000313|Proteomes:UP000265080}
RP NUCLEOTIDE SEQUENCE.
RA Lehmann R.;
RT "Finding Nemo's genes: A chromosome-scale reference assembly of the genome
RT of the orange clownfish Amphiprion percula.";
RL Submitted (MAR-2018) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSAPEP00000019180.1}
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; A0A3P8T250; -.
DR STRING; 161767.ENSAPEP00000019180; -.
DR Ensembl; ENSAPET00000019702.1; ENSAPEP00000019180.1; ENSAPEG00000013668.1.
DR GeneTree; ENSGT00940000157833; -.
DR Proteomes; UP000265080; Chromosome 7.
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 CDD; cd17105; FERM_F1_EPB41; 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; IPR021187; EPB4.1_FERM_F1.
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; 5.
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:UP000265080};
KW Transport {ECO:0000256|ARBA:ARBA00022448}.
FT DOMAIN 527..808
FT /note="FERM"
FT /evidence="ECO:0000259|PROSITE:PS50057"
FT REGION 1..524
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 973..1016
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..15
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 16..38
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 81..95
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 97..411
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 448..524
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1062 AA; 120824 MW; CAC8551DB884042B CRC64;
MTTEASAVSE ADTEGKQKTS GAEPEPEPES KQKPEAAVSD PEGEQSSKKA QEQASEPGPA
DVATSPEEEQ LKPRTRTSAG KGLSRLFSNF LKRRSQCSEG EGFEAEKARE EKADKEEKAD
KAEEEKVEEV KSDDKEAKAE EEKTEVTEAK KKEEKVEEKE EKKKVEEKVE KKGSKKKKKE
AKKKAEEKDE EKVTKEETKK KEETLKKKEE AKEEEKPAVE KEEKQETKEE EEKKETAEVK
DKGAEAGKKE EEKADKKVAK KKEKEEKVKK KEEEKAKRKA EEEERIKKRE EEKAKKKEEE
KAREAEKAKK KEEEKVKKKE EEKAKEEKAK KEEEKAKEEE EKIKELKKKE EQKTKEEPKK
KEEEKVKEEV KKKEKEEEKT EEKPKKEEEK GKKKGKNKGK KEEKEVKGSS EEQVKAPIAA
PEPELKTEPE AEQAPDQHSV SSAEIQPAQE EEKGEAVIKK EPEVVEEVKK EDVEEKVEEL
AEQQQEEEAA KGEEKATEQA KKEKPMKEKK TEKKTEEAKG SKRQKTMQCK VTLLDDTQFE
CELDKHAKGQ ELLTKVCDHV NLVEKDYFGL ANWETPTNKT WLEPTKEIRK QVSGAVYEFT
FNVKFYPPDP AQLTEDLTRY FLCLQLRKDI MRGVLPCSFV TLSLLGSYTA QSELGEYDPE
LHGSDYVKDL SLAPGQNKEL EEKVMELHRT YRSMSPAQAD MLFLENAKKL AMYGVDLHQA
KDLDGVDITL GVCSSGLMVY KDKLRINRFP WPKVLKISYK RSSFFIKIRP SEQEQYESTI
GFKLPNYKAS KKLWKVCVEH HTFFRVSTVE PPSSRRFLVL GSKFRYSGRT QAQTRQASSM
IDRPAPRFTR SASKRLSRNL DGVVSTQRGT RPVSAPVFSH AALMEAGIPM ATLDQPQTST
PIKTSMEERK LEVTVEAVEP SKIEAEVKEF DKPQEDLLRH HASISELKRN FMEAVPETRP
SEWDKRLSTH SPFRTLGING QPLPSADGVT VDGTDEDKDG TSESQTITSE TTSGTTVTTT
TTHISKVVKS GSSETRVEKR IVITADSDID QDKGKHGGAS AL
//
