ID A0A087XEN5_POEFO Unreviewed; 751 AA.
AC A0A087XEN5;
DT 29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 2.
DT 27-MAR-2024, entry version 44.
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 Poecilia formosa (Amazon molly) (Limia formosa).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Atherinomorphae; Cyprinodontiformes; Poeciliidae; Poeciliinae;
OC Poecilia.
OX NCBI_TaxID=48698 {ECO:0000313|Ensembl:ENSPFOP00000004238.2, ECO:0000313|Proteomes:UP000028760};
RN [1] {ECO:0000313|Proteomes:UP000028760}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=female {ECO:0000313|Proteomes:UP000028760};
RA Schartl M., Warren W.;
RL Submitted (OCT-2013) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSPFOP00000004238.2}
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}.
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; AYCK01007811; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; A0A087XEN5; -.
DR Ensembl; ENSPFOT00000004246.2; ENSPFOP00000004238.2; ENSPFOG00000004131.2.
DR GeneTree; ENSGT00940000157833; -.
DR Proteomes; UP000028760; Unassembled WGS sequence.
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; 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; 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:UP000028760};
KW Transport {ECO:0000256|ARBA:ARBA00022448}.
FT DOMAIN 1..282
FT /note="FERM"
FT /evidence="ECO:0000259|PROSITE:PS50057"
FT REGION 527..549
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 675..751
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 531..546
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 691..720
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 721..751
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 751 AA; 83354 MW; B375A48DDE2F4D9B CRC64;
MQCKVTLLDD TLFECELDKH AKGQELLTKV CDHVNLLEKD YFGLAIWETP TSKTWLEPVK
EIRKQVSGGV YEFTFNVKFY PPDPAQLTED LTRYFLCLQL RKDILQGVLP CSFVTLSLLG
SYTAQSELGE YDPEVHGTDY VKDLNLAPGQ SKELEEKVME LHRTYRSMSP AQADLLFLEN
AKKLAMYGVD LHQAKDLDGV DITLGVCSSG LMVYKDKLRI NRFPWPKVLK ISYKRSSFFI
KIRASEQEQY ESTIGFKLPN YKASKKLWKV CVEHHTFFRV PSVEPPSSRR FLVLGSKFRY
SGRTQAQTRQ ASSMIDRPAP RFTRSASKRL SRNLDGVVST QRGTRPVSAP VFSQAALADA
GIPMAPFDQP QTSTPIKTSR LEERKLEVTV EAAEPSKIEA VSEVKSAVSR EQRDVDSSLI
STINGYIQHE SESERTIEEG VQMRKEFEKP QEDLLRHHAS ISELKRNFME AVPEPRQSEW
DKRLSTHSPF RTVGINGQPL PGADGSVCIS PSCKRSETKT LHEDARSNFG GAEASGSSQS
RQSEPGVVEG LSAPVEESLC DHEEVVLFET LLVPLVEVEM AQLAPPVESD CKALDKIPEE
EGTCLVAPEC SGGIVGLSSP SFFWSDGPKV MRCSQPPLVQ THTVTITAVS NSLPGDISTT
EVPIVPTKTF TYESSKMTDD CTDEDKDSSF STSKTVTSET SSGTTVTTTT THISKVVKSG
SSETRMEKRI VITADSDVDQ EKEKHGGASA L
//
