E41L1_RAT
ID E41L1_RAT Reviewed; 879 AA.
AC Q9WTP0; Q9WTP1;
DT 20-MAR-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1999, sequence version 1.
DT 03-AUG-2022, entry version 148.
DE RecName: Full=Band 4.1-like protein 1;
DE AltName: Full=Erythrocyte membrane protein band 4.1-like 1 {ECO:0000312|RGD:71087};
DE AltName: Full=Neuronal protein 4.1;
DE Short=4.1N;
GN Name=Epb41l1 {ECO:0000312|RGD:71087};
GN Synonyms=Epb4.1l1 {ECO:0000312|RGD:71087};
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS S AND L), AND TISSUE SPECIFICITY.
RC STRAIN=Sprague-Dawley; TISSUE=Brain;
RX PubMed=10407168; DOI=10.1016/s0169-328x(99)00139-4;
RA Yamakawa H., Ohara R., Nakajima D., Nakayama M., Ohara O.;
RT "Molecular characterization of a new member of the protein 4.1 family
RT (brain 4.1) in rat brain.";
RL Brain Res. Mol. Brain Res. 70:197-209(1999).
RN [2]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-510, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=16641100; DOI=10.1073/pnas.0600895103;
RA Hoffert J.D., Pisitkun T., Wang G., Shen R.-F., Knepper M.A.;
RT "Quantitative phosphoproteomics of vasopressin-sensitive renal cells:
RT regulation of aquaporin-2 phosphorylation at two sites.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:7159-7164(2006).
RN [3]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-75; SER-378; SER-430;
RP SER-461; SER-466; SER-546; THR-550; SER-564; SER-578; THR-580; SER-648;
RP SER-650; SER-665; SER-666; SER-677; SER-782 AND SER-868, PHOSPHORYLATION
RP [LARGE SCALE ANALYSIS] AT SER-583; SER-587; SER-669; SER-742; SER-766;
RP SER-968; SER-1092 AND SER-1223 (ISOFORM L), AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
CC -!- FUNCTION: May function to confer stability and plasticity to neuronal
CC membrane via multiple interactions, including the spectrin-actin-based
CC cytoskeleton, integral membrane channels and membrane-associated
CC guanylate kinases. {ECO:0000250}.
CC -!- SUBUNIT: Interacts with AGAP2. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Comment=Additional isoforms seem to exist.;
CC Name=S;
CC IsoId=Q9WTP0-1; Sequence=Displayed;
CC Name=L;
CC IsoId=Q9WTP0-2; Sequence=VSP_023981;
CC -!- TISSUE SPECIFICITY: Highest expression in brain, lower in heart and
CC kidney. Within the brain, highest expression in cerebellum.
CC {ECO:0000269|PubMed:10407168}.
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DR EMBL; AB019256; BAA76624.1; -; mRNA.
DR EMBL; AB019257; BAA76625.1; -; mRNA.
DR RefSeq; NP_742087.1; NM_172090.3. [Q9WTP0-1]
DR AlphaFoldDB; Q9WTP0; -.
DR SMR; Q9WTP0; -.
DR BioGRID; 248761; 3.
DR IntAct; Q9WTP0; 2.
DR MINT; Q9WTP0; -.
DR STRING; 10116.ENSRNOP00000052108; -.
DR iPTMnet; Q9WTP0; -.
DR PhosphoSitePlus; Q9WTP0; -.
DR SwissPalm; Q9WTP0; -.
DR jPOST; Q9WTP0; -.
DR PaxDb; Q9WTP0; -.
DR PRIDE; Q9WTP0; -.
DR Ensembl; ENSRNOT00000083476; ENSRNOP00000071547; ENSRNOG00000057817. [Q9WTP0-1]
DR GeneID; 59317; -.
DR KEGG; rno:59317; -.
DR UCSC; RGD:71087; rat. [Q9WTP0-1]
DR CTD; 2036; -.
DR RGD; 71087; Epb41l1.
DR eggNOG; KOG3527; Eukaryota.
DR GeneTree; ENSGT00940000158442; -.
DR InParanoid; Q9WTP0; -.
DR OrthoDB; 193911at2759; -.
DR PhylomeDB; Q9WTP0; -.
DR PRO; PR:Q9WTP0; -.
DR Proteomes; UP000002494; Chromosome 3.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0005856; C:cytoskeleton; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0014069; C:postsynaptic density; ISO:RGD.
DR GO; GO:0032991; C:protein-containing complex; IDA:RGD.
DR GO; GO:0097060; C:synaptic membrane; IDA:RGD.
DR GO; GO:0003779; F:actin binding; IEA:UniProtKB-KW.
DR GO; GO:0005102; F:signaling receptor binding; IPI:RGD.
DR GO; GO:0005198; F:structural molecule activity; IEA:InterPro.
DR GO; GO:0031032; P:actomyosin structure organization; IBA:GO_Central.
DR GO; GO:0030866; P:cortical actin cytoskeleton organization; IEA:InterPro.
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; 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 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 1: Evidence at protein level;
KW Actin-binding; Alternative splicing; Cytoplasm; Cytoskeleton;
KW Phosphoprotein; Reference proteome.
FT CHAIN 1..879
FT /note="Band 4.1-like protein 1"
FT /id="PRO_0000281128"
FT DOMAIN 97..378
FT /note="FERM"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00084"
FT REGION 1..64
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 428..501
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 483..541
FT /note="Spectrin--actin-binding"
FT /evidence="ECO:0000250"
FT REGION 514..596
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 633..687
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 718..742
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 744..879
FT /note="C-terminal (CTD)"
FT COMPBIAS 41..64
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 447..501
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 514..538
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 554..580
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 638..656
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 30
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9Z2H5"
FT MOD_RES 75
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 79
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9H4G0"
FT MOD_RES 343
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:Q9Z2H5"
FT MOD_RES 378
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 430
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 437
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9H4G0"
FT MOD_RES 461
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 466
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 475
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9H4G0"
FT MOD_RES 510
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:16641100"
FT MOD_RES 540
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9H4G0"
FT MOD_RES 541
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9H4G0"
FT MOD_RES 544
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9H4G0"
FT MOD_RES 546
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 550
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 564
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 578
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 580
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 639
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9Z2H5"
FT MOD_RES 648
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 650
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 665
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 666
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 671
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9Z2H5"
FT MOD_RES 677
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 684
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9Z2H5"
FT MOD_RES 685
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9Z2H5"
FT MOD_RES 721
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9Z2H5"
FT MOD_RES 782
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 868
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT VAR_SEQ 556
FT /note="E -> EAQRIQDTSRQDLVPGTATGLEMFTQKSLAASPEGSEHWVFIERVYT
FT RPEDLGLLTVAATQRKESGSSLSGILADGRLSKVDILVDKFKVEVATEETVRTRRTSTQ
FT QQGKMLASPEDFETVREEDRGGPGEATSTDKLPEGSRLKLRNHGVSNGQLESQVEWGLE
FT RPQTWGRPTAAGLGPVQGEVLSPTSDKGGLQSFLLDPAQAEARADSSDETDTSFAERSF
FT CLHYGEKDSEDQLLAPPSEHREEHPDALPGDGTWLELAGVHTENWELKSSDPRASAPGS
FT SQHKDQAHKAPSAEEAWTPRDHGRPDDPQGAAVGQTFEEVWENTQQRLEGELVQPLASV
FT AEDEVPTNMDWMGKTEKSPPARRKKSPPGRGGGVHLDAQACALLRTIPPCVRKPARPDQ
FT GSFLPKEKGTVSPPAVEPETEDRETVSPLPVSSGHTEVLAAMEGTSLSPLPPGSRGPSE
FT SREFFRDQFPVVLKYIHLPEESPVPKDPHGDRKAPPVASKKPRFVPEGSEEPVLLGELM
FT FPSGKQETSLQDWDQGGSQEDISKTSVANKIRIFETHGAEACRASQGEMRSLPHELPSG
FT ASPGQVEQQDNLLDLGFVQLQPPGDLATPTTYHQERCTDPELVSPDSGCETTLEEATGS
FT KSGDAGREDKSSFRRLAPNTPGKGGRLRFASPPGPQ (in isoform L)"
FT /evidence="ECO:0000303|PubMed:10407168"
FT /id="VSP_023981"
FT MOD_RES Q9WTP0-2:583
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES Q9WTP0-2:587
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES Q9WTP0-2:669
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES Q9WTP0-2:742
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES Q9WTP0-2:766
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES Q9WTP0-2:968
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES Q9WTP0-2:1092
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES Q9WTP0-2:1223
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
SQ SEQUENCE 879 AA; 98243 MW; 3B987785C6D93910 CRC64;
MTTETGPDSE VKKAQEETPQ QPEAAAAVTT PVTPAGHSHP ETNSNEKHLT QQDTRPAEQS
LDMEEKDYCE ADGLSERTTP SKAQKSPQKI AKKFKSATCR VTLLDASEYE CEVEKHGRGQ
VLFDLVCEHL NLLEKDYFGL TFCDADSQKN WLDPSKEIKK QIRSSPWNFA FTVKFYPPDP
AQLTEDITRY YLCLQLRADI ITGRLPCSFV THALLGSYAV QAELGDHDTE EHVGNYVSEL
RFAPNQTREL EERIMELHKT YRGMTPGEAE IHFLENAKKL SMYGVDLHHA KDSEGIDIML
GVCANGLLIY RDRLRINRFA WPKILKISYK RSNFYIKIRP GEYEQFESTI GFKLPNHRSA
KRLWKVCIEH HTFFRLVSPE PPPKGFLVMG SKFRYSGRTQ AQTRQASALI DRPAPFFERS
SSKRYTMSRS LDGAEFSRPA SVSENHDAGP DGDKREDDAE SGGRRSEAEE GEVRTPTKIK
ELKPEQETTP RHKQEFLDKP EDVLLKHQAS INELKRTLKE PNSKLIHRDR DWERERRLPS
SPASPSPKGT PEKASERAGL REGSEEKVKP PRPRAPESDT GDEDQDQERD AVFLKDNHLA
IERKCSSITV SSTSSLEAEV DFTVIGDYHG GAFEDFSRSL PELDRDKSDS ETEGLVFARD
LKGPSSQEDE SGGIEDSPDR GACSTPELPQ FESVKAETMT VSSLAIRKKI EPEAMLQSRV
STADSTQVDG GAPAAKDFMT TPPCITTETI STTMENSLKS GKGAAAMIPG PQTVATEIRS
LSPIIGKDVL TSTYGATAET LSTSTTTHVT KTVKGGFSET RIEKRIIITG DEDVDQDQAL
ALAIKEAKLQ HPDMLVTKAV VYRETDPSPE ERDKKPQES
