ID   EPB41_CHICK             Reviewed;          90 AA.
AC   P12264;
DT   01-OCT-1989, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1989, sequence version 1.
DT   03-AUG-2022, entry version 137.
DE   RecName: Full=Protein 4.1;
DE   AltName: Full=Band 4.1;
DE   AltName: Full=Erythrocyte membrane protein band 4.1 {ECO:0000250|UniProtKB:P11171};
DE   Flags: Fragment;
GN   Name=EPB41 {ECO:0000250|UniProtKB:P11171};
OS   Gallus gallus (Chicken).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC   Phasianinae; Gallus.
OX   NCBI_TaxID=9031;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND ALTERNATIVE SPLICING.
RX   PubMed=3474611; DOI=10.1073/pnas.84.13.4432;
RA   Ngai J., Stack J.H., Moon R.T., Lazarides E.;
RT   "Regulated expression of multiple chicken erythroid membrane skeletal
RT   protein 4.1 variants is governed by differential RNA processing and
RT   translational control.";
RL   Proc. Natl. Acad. Sci. U.S.A. 84:4432-4436(1987).
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. May be required
CC       for 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 and DLG1. {ECO:0000250|UniProtKB:P11171}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P11171}.
CC       Cytoplasm, cytoskeleton {ECO:0000250|UniProtKB:P11171}. Cytoplasm, cell
CC       cortex {ECO:0000250|UniProtKB:P11171}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=1;
CC         Comment=A number of isoforms are produced.;
CC       Name=1;
CC         IsoId=P12264-1; Sequence=Displayed;
CC   -!- PTM: Phosphorylated at multiple sites by different protein kinases and
CC       each phosphorylation event selectively modulates the protein's
CC       functions.
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DR   EMBL; M16962; AAA48762.1; -; mRNA.
DR   PIR; A27056; A27056.
DR   AlphaFoldDB; P12264; -.
DR   SMR; P12264; -.
DR   STRING; 9031.ENSGALP00000002021; -.
DR   PaxDb; P12264; -.
DR   VEuPathDB; HostDB:geneid_396493; -.
DR   eggNOG; KOG3527; Eukaryota.
DR   HOGENOM; CLU_003623_0_1_1; -.
DR   InParanoid; P12264; -.
DR   OrthoDB; 262540at2759; -.
DR   PhylomeDB; P12264; -.
DR   Proteomes; UP000000539; Unplaced.
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: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:1904778; P:positive regulation of protein localization to cell cortex; ISS:UniProtKB.
DR   Gene3D; 2.30.29.30; -; 1.
DR   InterPro; IPR021187; Band_41_protein_chordates.
DR   InterPro; IPR000299; FERM_domain.
DR   InterPro; IPR018980; FERM_PH-like_C.
DR   InterPro; IPR011993; PH-like_dom_sf.
DR   PANTHER; PTHR23280:SF12; PTHR23280:SF12; 1.
DR   Pfam; PF09380; FERM_C; 1.
DR   SMART; SM01196; FERM_C; 1.
DR   PROSITE; PS50057; FERM_3; 1.
PE   2: Evidence at transcript level;
KW   Actin-binding; Alternative splicing; Calmodulin-binding; Cell cycle;
KW   Cell division; Cytoplasm; Cytoskeleton; Mitosis; Nucleus; Phosphoprotein;
KW   Reference proteome; Transport.
FT   CHAIN           <1..>90
FT                   /note="Protein 4.1"
FT                   /id="PRO_0000219392"
FT   DOMAIN          <1..>90
FT                   /note="FERM"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00084"
FT   NON_TER         1
FT   NON_TER         90
SQ   SEQUENCE   90 AA;  10395 MW;  8938A0C88816604A CRC64;
     EFLENAKKLS MYGVDLHHAK DLEGVDITLG VCSSGLLVYK DKLRINRFPW PKVLKISYKR
     SSFFIKIRPG EQEQYESTIG FKLPSYRAAK