ID A0A3P8XJ85_ESOLU Unreviewed; 1384 AA.
AC A0A3P8XJ85;
DT 13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT 02-DEC-2020, sequence version 2.
DT 27-MAR-2024, entry version 26.
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 Esox lucius (Northern pike).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Protacanthopterygii; Esociformes;
OC Esocidae; Esox.
OX NCBI_TaxID=8010 {ECO:0000313|Ensembl:ENSELUP00000004632.2, ECO:0000313|Proteomes:UP000265140};
RN [1] {ECO:0000313|Ensembl:ENSELUP00000004632.2, ECO:0000313|Proteomes:UP000265140}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=25069045;
RA Rondeau E.B., Minkley D.R., Leong J.S., Messmer A.M., Jantzen J.R.,
RA von Schalburg K.R., Lemon C., Bird N.H., Koop B.F.;
RT "The genome and linkage map of the northern pike (Esox lucius): conserved
RT synteny revealed between the salmonid sister group and the Neoteleostei.";
RL PLoS ONE 9:e102089-e102089(2014).
RN [2] {ECO:0000313|Ensembl:ENSELUP00000004632.2}
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}.
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DR Ensembl; ENSELUT00000012023.2; ENSELUP00000004632.2; ENSELUG00000005933.2.
DR GeneTree; ENSGT00940000157833; -.
DR Proteomes; UP000265140; LG20.
DR Bgee; ENSELUG00000005933; Expressed in mesonephros and 14 other cell types or tissues.
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 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; 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 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:UP000265140};
KW Transport {ECO:0000256|ARBA:ARBA00022448}.
FT DOMAIN 638..919
FT /note="FERM"
FT /evidence="ECO:0000259|PROSITE:PS50057"
FT REGION 1..632
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1135..1200
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1214..1241
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1312..1362
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 21..69
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 100..114
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 116..498
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 538..594
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 603..631
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1135..1162
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1216..1231
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1321..1351
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1384 AA; 155497 MW; F5630312155029D5 CRC64;
MTTEASALGE AETEGKQTPS GAEPEAEEES KREPCGAEPE TEPENKENPE PEAAEAAVPE
GEKPSEKASE LGPAEASASS AATTDEEQLV KPRQRTSAGR GLSRLFSSFL KRRSQCTDIE
WAEVEKAEKE RKEKTEAGAK EEDLEEEKKE SEAKGEKKVE KVEKNEEKRK DKEGKKKGKE
EKVEEEAVVK KEAEKKKQEE GEAAKKQEKK KKEEEEAAKK QSLKKKKEEE EAGKKAEKKK
KEEEEAVKKE AAKKKKEEEE AAKKAEKKKK EEEEAAKKAE KKKKEEEEAA KKEAVKKKKK
EELEAAKKEA VKKKEEEEKA KKAEKQKKEV EEGVKKEAED KKEEEKKEAE EKKKEEEAAA
KKELEKKKEE EEEVKKELIK KKKEEEVAKK EEEEEVKKEE VKKKKEEEEA AKKEVDKRKE
EEAAAKKELE KKKAEDLTAK KEEEKAVKKS QKGKKKEKEK KEEKEKAEQK EEKKEKEKKE
EKLKAEQKED QREKIEVKKK EGKKKRKGKK KTTESPEGVR SPAEEQVKAP IAAPEPELRT
EPEAEQETQE EVAEVQDHHS VSSADTPEEQ RADAELEMET LAAEEKQQQE TEKPEEEAAE
QEEEKDCNGR GEEEWEKTKA EEKKAADGAK ASRRPRIMQC KVTLLDDTLF ECELDKHAKG
QDLFVKVCDH LNLLERDYYG LAVWETPTSR TWLDASKEIR KQVADYTYEF TFNVKFYPPD
PAQLTEDLTR YYLCLQLRKD ILSGLLPCSF VTLALLGSYT AQSELGEYDP EVHGTDYVKE
LRLAPGQGKE LEEKVMELHR TYRSMSPAQA DMMFLENAKK LSMYGVDLHQ AKDLEGVDIL
LGVCSGGLMV YKDKLRINRF PWPKVLKISY KRSSFFIKIR PSEQEQYEST IGFKLPNYKA
SKKLWKVSVE HHTFFRVSTV EPPSSRSRFL ALGSKFRYSG RTQAQTRQAS SMIDRPAPRF
TRSASKRLSR TIDGVAGTHK AARPVSAPVF SQAALIEAGI PMGPLDLQQP QTSTPIRLPA
HQEDRKLEVT VEAVDEGSAE VKSELMDIEE PVRLRKDFDK PQEDVMKHHA SISELKRNFM
ASVPESRGPS EWEKRLSTHS PFRSLGINGQ PLPGPDGSVF ITPIWEESEP LLLQQEEPGS
TTRPWRGPSP SPSNSAGPGP DSCQNPRSHD APGMVGSCDQ HDEEVDGEEG VGSGITKSQI
PIVEVERAQL PLSLHLHGRE PEEEAKEEPS DTGSGVEQPG GIAGASPAFC FVSGGPHVIR
CFQPPLVRTQ TVTIADVSNS FPTDVTTKHV PIIQTQTKTI TYVAAQVSVD GAEEEKDDSA
LSSMQTTTSE SSSRTSGSAV TTTTTHISKV VKGGMSETRV EKRIVITADS EADIEQGSDG
GAST
//
