ID   EPB41_XENLA             Reviewed;         801 AA.
AC   P11434;
DT   01-OCT-1989, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1989, sequence version 1.
DT   03-AUG-2022, entry version 135.
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};
GN   Name=epb41 {ECO:0000250|UniProtKB:P11171};
OS   Xenopus laevis (African clawed frog).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC   Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX   NCBI_TaxID=8355;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=2186944; DOI=10.1016/0012-1606(90)90297-v;
RA   Spencer M., Giebelhaus D.H., Kelly G.M., Bicknell J., Florio S.K.,
RA   Bunt-Milam A., Moon R.T.;
RT   "Membrane skeleton protein 4.1 in developing Xenopus: expression in
RT   postmitotic cells of the retina.";
RL   Dev. Biol. 139:279-291(1990).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 1-550.
RX   PubMed=2453290; DOI=10.1016/0092-8674(88)90576-4;
RA   Giebelhaus D.H., Eib D.W., Moon R.T.;
RT   "Antisense RNA inhibits expression of membrane skeleton protein 4.1 during
RT   embryonic development of Xenopus.";
RL   Cell 53:601-615(1988).
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. May be required for dynein-dynactin complex
CC       and NUMA1 recruitment at the mitotic cell cortex during anaphase.
CC       {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. {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   -!- TISSUE SPECIFICITY: Found exclusively in photoreceptors following the
CC       terminal mitosis of retinal neurons. When retinal synaptogenesis is
CC       complete, protein 4.1 is also expressed in the inner retina. In adult
CC       amphibian retinas, protein 4.1 is detected in photoreceptors, bipolar
CC       cells, and ganglion cell axons.
CC   -!- PTM: Phosphorylated at multiple sites by different protein kinases and
CC       each phosphorylation event selectively modulates the protein's
CC       functions.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; M20621; AAA49695.1; -; mRNA.
DR   PIR; A37353; A37353.
DR   RefSeq; NP_001081264.1; NM_001087795.1.
DR   AlphaFoldDB; P11434; -.
DR   SMR; P11434; -.
DR   DNASU; 397741; -.
DR   GeneID; 397741; -.
DR   KEGG; xla:397741; -.
DR   CTD; 397741; -.
DR   Xenbase; XB-GENE-865471; epb41.L.
DR   OrthoDB; 262540at2759; -.
DR   Proteomes; UP000186698; Chromosome 2L.
DR   Bgee; 397741; Expressed in lung and 19 other tissues.
DR   GO; GO:0005938; C:cell cortex; ISS:UniProtKB.
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: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: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   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..801
FT                   /note="Protein 4.1"
FT                   /id="PRO_0000219393"
FT   DOMAIN          193..474
FT                   /note="FERM"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00084"
FT   REGION          1..187
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          477..587
FT                   /note="Hydrophilic"
FT   REGION          516..613
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          588..651
FT                   /note="Spectrin--actin-binding"
FT   REGION          653..801
FT                   /note="C-terminal (CTD)"
FT   COMPBIAS        84..108
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        167..186
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        562..590
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   801 AA;  89429 MW;  07FA508552359A0F CRC64;
     MTTEKGLLAE AESPPQDQKQ EGEEEVESCT TQPVVGSGDK DPETEQSQES PSTTSPSTRK
     SKDRHSQGKG LSRLFSSFLK RPKSQVSSDE KEVELLGEKG QDQKDVDEGL GEQLEDDVFL
     KAPIAAPEPE LRTDPSLDLH SLSSAETQPA QEEQKEDQDP EADCEDVEGK EPIKKPEGES
     KASHKVVRRS PNMRCKVTLL DDTVYECDLE KHAKGQDIFK KVCSHLNIVE EDYFGLAIWE
     SPTCKVWLDP LKDIRKQVHG GPCEFTSNVK FYPPDPAQLS EDITRYYLCL QLRKDIFSGR
     LPCSFATLAL LGSYTVQSEV GDYEEDLHGV DYVSEFKLSP NQTKDLEEKV GELHKSYRSM
     TPAQADLEFL ENAKKLTMYG VDIHQAKDLE GVDIKLGVCS GGLMVFKDNL RINRFPWPKV
     LKISYKRSSF FIKIRPGEQE QYESTIGFKL PSYKAAKKLW KVCVEHHTFF RLTSTESIPK
     HRFLSLGSTF RYSGRTQAQT RHASALIDRP APHFVRTGSK RASRSLDGAA VATPEASRTH
     RPVSAPVFPP EFPAVQRKTP GPRVEEMPKK TEEKPKEGMP NQRESPKDVK ATQQDSPSPT
     VNGDKVKDLE KTQDEIIRHH ASIRELKKSF MESVPAPRPS EWDKRLSTHS PFRTLSFNGQ
     VQTGTDGPPL VKTQTVTISN ATNGEKGEIP TKEVPLVHTE TKTITYEAAR SDDVNTDQEP
     GILLTAHTIT SETTSSTTTT QITKTVKGGI SETLIEKRIV ITGDGDLDHD QVLVQAIKEA
     KEQHPDMSVT KGVVHQETEI A