EPB41_BOVIN
ID EPB41_BOVIN Reviewed; 617 AA.
AC Q9N179;
DT 05-DEC-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 129.
DE RecName: Full=Protein 4.1;
DE Short=P4.1;
DE AltName: Full=4.1R;
DE AltName: Full=Band 4.1;
DE AltName: Full=Erythrocyte membrane protein band 4.1 {ECO:0000250|UniProtKB:P11171};
GN Name=EPB41 {ECO:0000250|UniProtKB:P11171}; Synonyms=E41P;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=Japanese black; TISSUE=Bone marrow;
RA Saito D., Inaba M., Koshino I., Matsumoto M., Ono K.;
RT "The interaction of bovine red blood cell protein 4.1 with red blood cell
RT membranes.";
RL Submitted (JAN-2000) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Protein 4.1 is a major structural element of the erythrocyte
CC membrane skeleton. It plays a key role in regulating membrane physical
CC properties of mechanical stability and deformability by stabilizing
CC spectrin-actin interaction. Recruits DLG1 to membranes. Required for
CC dynein-dynactin complex and NUMA1 recruitment at the mitotic cell
CC cortex during anaphase. {ECO:0000250|UniProtKB:P11171}.
CC -!- SUBUNIT: Binds with a high affinity to glycophorin and with lower
CC affinity to band III protein. Associates with the nuclear mitotic
CC apparatus. Binds calmodulin, CENPJ and DLG1. Also found to associate
CC with contractile apparatus and tight junctions. Interacts with NUMA1;
CC this interaction is negatively regulated by CDK1 during metaphase and
CC promotes anaphase-specific localization of NUMA1 in symmetrically
CC dividing cells. Interacts with ATP2B1; regulates small intestinal
CC calcium absorption through regulation of membrane expression of ATP2B1
CC (By similarity). {ECO:0000250|UniProtKB:P11171,
CC ECO:0000250|UniProtKB:P48193}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P11171}.
CC Cytoplasm, cytoskeleton {ECO:0000250|UniProtKB:P11171}. Cytoplasm, cell
CC cortex {ECO:0000250|UniProtKB:P11171}.
CC -!- PTM: Phosphorylated at multiple sites by different protein kinases and
CC each phosphorylation event selectively modulates the protein's
CC functions. {ECO:0000250}.
CC -!- PTM: Phosphorylation on Tyr-413 reduces the ability of 4.1 to promote
CC the assembly of the spectrin/actin/4.1 ternary complex. {ECO:0000250}.
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DR EMBL; AF222767; AAF61703.1; -; mRNA.
DR RefSeq; NP_776736.1; NM_174311.1.
DR AlphaFoldDB; Q9N179; -.
DR BMRB; Q9N179; -.
DR SMR; Q9N179; -.
DR STRING; 9913.ENSBTAP00000008765; -.
DR PRIDE; Q9N179; -.
DR Ensembl; ENSBTAT00000008760; ENSBTAP00000008760; ENSBTAG00000006667.
DR GeneID; 281753; -.
DR KEGG; bta:281753; -.
DR CTD; 2035; -.
DR VEuPathDB; HostDB:ENSBTAG00000006667; -.
DR VGNC; VGNC:28519; EPB41.
DR eggNOG; KOG3527; Eukaryota.
DR GeneTree; ENSGT00940000157833; -.
DR InParanoid; Q9N179; -.
DR OrthoDB; 262540at2759; -.
DR Proteomes; UP000009136; Chromosome 2.
DR Bgee; ENSBTAG00000006667; Expressed in thymus and 108 other tissues.
DR ExpressionAtlas; Q9N179; baseline.
DR GO; GO:0016323; C:basolateral plasma membrane; ISS:UniProtKB.
DR GO; GO:0005938; C:cell cortex; ISS:UniProtKB.
DR GO; GO:0005856; C:cytoskeleton; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0003779; F:actin binding; IEA:UniProtKB-KW.
DR GO; GO:0005516; F:calmodulin binding; IEA:UniProtKB-KW.
DR GO; GO:0005198; F:structural molecule activity; IEA:InterPro.
DR GO; GO:0031032; P:actomyosin structure organization; IBA:GO_Central.
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 GO; GO:1904778; P:positive regulation of protein localization to cell cortex; ISS:UniProtKB.
DR GO; GO:0051924; P:regulation of calcium ion transport; ISS:UniProtKB.
DR GO; GO:1904478; P:regulation of intestinal absorption; ISS:UniProtKB.
DR CDD; cd14473; FERM_B-lobe; 1.
DR Gene3D; 1.20.80.10; -; 1.
DR Gene3D; 2.30.29.30; -; 1.
DR InterPro; IPR008379; Band_4.1_C.
DR InterPro; IPR019749; Band_41_domain.
DR InterPro; IPR021187; Band_41_protein_chordates.
DR InterPro; IPR000798; Ez/rad/moesin-like.
DR InterPro; IPR014847; FERM-adjacent.
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:SF12; PTHR23280:SF12; 2.
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 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; SSF47031; SSF47031; 1.
DR SUPFAM; SSF54236; SSF54236; 1.
DR PROSITE; PS00660; FERM_1; 1.
DR PROSITE; PS00661; FERM_2; 1.
DR PROSITE; PS50057; FERM_3; 1.
PE 2: Evidence at transcript level;
KW Actin-binding; Calmodulin-binding; Cell cycle; Cell division; Cytoplasm;
KW Cytoskeleton; Mitosis; Nucleus; Phosphoprotein; Reference proteome;
KW Transport.
FT CHAIN 1..617
FT /note="Protein 4.1"
FT /id="PRO_0000219388"
FT DOMAIN 1..282
FT /note="FERM"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00084"
FT REGION 308..401
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 401..466
FT /note="Spectrin--actin-binding"
FT REGION 467..617
FT /note="C-terminal (CTD)"
FT COMPBIAS 376..401
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 13
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:P48193"
FT MOD_RES 169
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P11171"
FT MOD_RES 312
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P11171"
FT MOD_RES 331
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P11171"
FT MOD_RES 333
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P11171"
FT MOD_RES 413
FT /note="Phosphotyrosine; by EGFR"
FT /evidence="ECO:0000250|UniProtKB:P11171"
FT MOD_RES 417
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P48193"
FT MOD_RES 427
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P11171"
FT MOD_RES 437
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P11171"
FT MOD_RES 462
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P11171"
FT MOD_RES 465
FT /note="Phosphoserine; by CDK1"
FT /evidence="ECO:0000250|UniProtKB:P11171"
FT MOD_RES 489
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P11171"
FT MOD_RES 612
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P11171"
SQ SEQUENCE 617 AA; 69258 MW; 5B49D5008AD900FB CRC64;
MHCKVSLLDD TVYECVVEKH AKGQDLLKRV CEHLNLLEED YFGLAIWDNA TSKTWLDSAK
EIKKQVRGVP WNFTFNVKFY PPDPAQLTED ITRYYLCLQL RQDIVSGRLP CSFATLALLG
SYTIQSELGD YDPELHGADY VSDFKLAPNQ TKELEEKVME LHKSYRSMTP AQADLEFLEN
AKKLSMYGVD LHKAKDLEGV DIILGVCSSG LLVYKEKLRI NRFPWPKVLK ISYKRSSFFI
KIRPGEQEQY ESTIGFKLPS YRAAKKLWKV CVEHHTFFRL TSTDTIPKSK FLALGSKFRY
SGRTQAQTRQ ASALIDRPAP HFERTASKRA SRSLDGAAAV EPADRTPRPT SAPAIAPSPA
AEGGVPGAPV KKAQKETVQV EVKQEEAPPE DAEPEPSEAW KKKRERLDGE NIYIRHSNLM
LEDLDKSQEE IKKHHASISE LKKNFMESVP EPRPSEWDKR LSTHSPFRTL NINGQIPTGE
GPPLVKTQTV TISDTANAVK SEIPTKDVPI VHTETKTITY EAAQTDDSNG DLDPGVLLTA
QTITSETTSS TTTTQITKTV KGGISETRIE KRIVITGDAD IDHDQVLVQA IKEAKEQHPD
MSVTKVVVHQ ETEISEE
