ID A0A2K5XLJ5_MANLE Unreviewed; 801 AA.
AC A0A2K5XLJ5;
DT 28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT 28-MAR-2018, sequence version 1.
DT 27-MAR-2024, entry version 28.
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};
GN Name=EPB41 {ECO:0000313|Ensembl:ENSMLEP00000004186.1};
OS Mandrillus leucophaeus (Drill) (Papio leucophaeus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Cercopithecinae; Mandrillus.
OX NCBI_TaxID=9568 {ECO:0000313|Ensembl:ENSMLEP00000004186.1, ECO:0000313|Proteomes:UP000233140};
RN [1] {ECO:0000313|Ensembl:ENSMLEP00000004186.1}
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; A0A2K5XLJ5; -.
DR Ensembl; ENSMLET00000020502.1; ENSMLEP00000004186.1; ENSMLEG00000018623.1.
DR GeneTree; ENSGT00940000157833; -.
DR Proteomes; UP000233140; 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 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; 2.
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:UP000233140};
KW Transport {ECO:0000256|ARBA:ARBA00022448}.
FT DOMAIN 211..492
FT /note="FERM"
FT /evidence="ECO:0000259|PROSITE:PS50057"
FT REGION 1..203
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 519..569
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 582..616
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 20..56
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 57..77
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 91..123
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 159..203
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 587..616
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 801 AA; 89386 MW; 6B379919A8B47CAE CRC64;
MTTEKSLVTE AENSQHQQKE EGEGAINSGQ QEPQQEESCQ TVAEGDNQFE QKLKASNGDT
PTHEDLTKNK ERTSDSRGLS RLFSSFLKRP KSQVSEEEGG KEVESDKEKG EGGQKEIEFG
TSLDEEIILK APIAAPEPEL KTDPSLDLHS LSSAETQPAQ EELREDPDFE TKEGEGLEEC
SKIEVKEESP ESKAEGELKA SQKSIRKHRN MHCKVSLLDD TVYECVVEKH AKGQDLLKRV
CEHLNLLEED YFGLAIWDNA TSKTWLDSAK EIKKQVRGVP WNFTFNVKFY PPDPAQLTED
ITRYYLCLQL RQDIVAGRLP CSFATLALLG SYTIQSELGD YDPELHGVDY VSDFKLAPNQ
TKELEEKVME LHKSYRSMTP AQADLEFLEN AKKLSMYGVD LHKAKDLEGV DIILGVCSSG
LLVYKDKLRI NRFPWPKVLK ISYKRSSFFI KIRPGEQEQY ESTIGFKLPS YRAAKKLWKV
CVEHHTFFRL TSTDTIPKSK FLALGSKFRY SGRTQAQTRQ ASALIDRPAP HFERTASKRA
SRSLDGAAAV DSADRSPRPT SAPAIAQGQV AEGGVLDASA KKTVVPKAQK ETVKAEVKKE
DGPPEQAEPE PTEAWKDLDK SQEEIRKHHA SISELKKNFM ESVPEPRPSE WDKRLSTHSP
FRTLNVNGQI PTGEGPPLVK TQTVTISDNT NAVKSEIPTK DVPIVHTETK TITYEAAQTD
DNSGDLDPGV LLTAQTITSE TTSSTTTTQI TKVTDQLEPP YGTQGQAELV LVQAIKEAKE
QHPDMSVTKV VVHQETEIAD E
//
