ID G1NXA7_MYOLU Unreviewed; 805 AA.
AC G1NXA7;
DT 19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT 19-OCT-2011, sequence version 1.
DT 27-MAR-2024, entry version 69.
DE SubName: Full=Erythrocyte membrane protein band 4.1 like 4B {ECO:0000313|Ensembl:ENSMLUP00000001998.2};
GN Name=EPB41L4B {ECO:0000313|Ensembl:ENSMLUP00000001998.2};
OS Myotis lucifugus (Little brown bat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Chiroptera; Microchiroptera; Vespertilionidae;
OC Myotis.
OX NCBI_TaxID=59463 {ECO:0000313|Ensembl:ENSMLUP00000001998.2, ECO:0000313|Proteomes:UP000001074};
RN [1] {ECO:0000313|Ensembl:ENSMLUP00000001998.2, ECO:0000313|Proteomes:UP000001074}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=21993624; DOI=10.1038/nature10530;
RA Lindblad-Toh K., Garber M., Zuk O., Lin M.F., Parker B.J., Washietl S.,
RA Kheradpour P., Ernst J., Jordan G., Mauceli E., Ward L.D., Lowe C.B.,
RA Holloway A.K., Clamp M., Gnerre S., Alfoldi J., Beal K., Chang J.,
RA Clawson H., Cuff J., Di Palma F., Fitzgerald S., Flicek P., Guttman M.,
RA Hubisz M.J., Jaffe D.B., Jungreis I., Kent W.J., Kostka D., Lara M.,
RA Martins A.L., Massingham T., Moltke I., Raney B.J., Rasmussen M.D.,
RA Robinson J., Stark A., Vilella A.J., Wen J., Xie X., Zody M.C., Baldwin J.,
RA Bloom T., Chin C.W., Heiman D., Nicol R., Nusbaum C., Young S.,
RA Wilkinson J., Worley K.C., Kovar C.L., Muzny D.M., Gibbs R.A., Cree A.,
RA Dihn H.H., Fowler G., Jhangiani S., Joshi V., Lee S., Lewis L.R.,
RA Nazareth L.V., Okwuonu G., Santibanez J., Warren W.C., Mardis E.R.,
RA Weinstock G.M., Wilson R.K., Delehaunty K., Dooling D., Fronik C.,
RA Fulton L., Fulton B., Graves T., Minx P., Sodergren E., Birney E.,
RA Margulies E.H., Herrero J., Green E.D., Haussler D., Siepel A., Goldman N.,
RA Pollard K.S., Pedersen J.S., Lander E.S., Kellis M.;
RT "A high-resolution map of human evolutionary constraint using 29 mammals.";
RL Nature 478:476-482(2011).
RN [2] {ECO:0000313|Ensembl:ENSMLUP00000001998.2}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
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DR EMBL; AAPE02016274; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AAPE02016275; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; G1NXA7; -.
DR STRING; 59463.ENSMLUP00000001998; -.
DR Ensembl; ENSMLUT00000002191.2; ENSMLUP00000001998.2; ENSMLUG00000002183.2.
DR eggNOG; KOG3530; Eukaryota.
DR GeneTree; ENSGT00940000158331; -.
DR HOGENOM; CLU_003623_5_0_1; -.
DR InParanoid; G1NXA7; -.
DR OMA; EKNEACM; -.
DR TreeFam; TF319780; -.
DR Proteomes; UP000001074; Unassembled WGS sequence.
DR GO; GO:0045177; C:apical part of cell; IEA:Ensembl.
DR GO; GO:0005856; C:cytoskeleton; IEA:InterPro.
DR GO; GO:0005829; C:cytosol; IEA:Ensembl.
DR GO; GO:0005886; C:plasma membrane; IEA:Ensembl.
DR GO; GO:0008092; F:cytoskeletal protein binding; IEA:InterPro.
DR GO; GO:0031032; P:actomyosin structure organization; IEA:Ensembl.
DR GO; GO:0045785; P:positive regulation of cell adhesion; IEA:Ensembl.
DR GO; GO:0010628; P:positive regulation of gene expression; IEA:Ensembl.
DR GO; GO:0051549; P:positive regulation of keratinocyte migration; IEA:Ensembl.
DR GO; GO:0042060; P:wound healing; IEA:Ensembl.
DR CDD; cd14473; FERM_B-lobe; 1.
DR CDD; cd13186; FERM_C_NBL4_NBL5; 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; IPR019749; Band_41_domain.
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:SF18; BAND 4.1-LIKE PROTEIN 4B; 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; PS00661; FERM_2; 1.
DR PROSITE; PS50057; FERM_3; 1.
PE 4: Predicted;
KW Reference proteome {ECO:0000313|Proteomes:UP000001074}.
FT DOMAIN 1..267
FT /note="FERM"
FT /evidence="ECO:0000259|PROSITE:PS50057"
FT REGION 353..447
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 557..592
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 609..658
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 398..415
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 430..446
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 567..591
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 627..642
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 805 AA; 90379 MW; D1D0058F6FC121F5 CRC64;
KHAKGQDLFD QIVYHLDLVE TDYFGLQFLD SAQVAHWLDH SKPIKKQMKT GPAYALHFRV
KYYSSEPNNL REEFTRYLFV LQLRHDILSG KLKCPYETAV ELAALCLQAE LGECELPEHT
PELVSEFRFI PNQTEAMEFD IFQRWKECRG KSPAQAELSY LNKAKWLEMY GVDMHVVRGR
DGCEYSLGLT PTGILIFEGA NKIGLFFWPK ITKMDFKKSK LTLVVVEDDD QGREQEHTFV
FRLDSAKTCK HLWKCAVEHH AFFRLRTPGN SKSNRSDFIR LGSRFRFSGR TEYQATHGAR
LRRTSTFERK PSKRYPSRRH STFKASNPVI AAQLCSKTNP EVHNYQPQYH PNIHPSQPRW
HPHSPNVSYP LPSPGLSSSD RLPFGIEENG GTPFTTKASG RHHHHHHHQH QHQHQHHPNY
GLSLTLENKE GPLRSPNSSS KSLTKLTPGA PALFNEAATH LKKLELDTVK APGPWPTLHI
NINKVEEKKV SEKTLQTPLL PSPVADHVKC NILKAQLENA SRVSAQAGKE ESTFVNINKK
SSLQDANVRS PIPIRVETGQ PAVEKPEIKP PRVRKLTRQY SFNRSDEDDL PPELAEAVGM
TTTATTSTTT AAAATQVSAP LASPKVHKVT SPQNSEAKSP LSPGAKSPSD RGGAFTLEPG
DLLMDFTEAT PLAEPTSAPH CAHSRCSPPL SLPMKEETTG VCMHPPIKTR LIKTFPVDPV
TSFPEPFIAG PQFTADFRDS KLQCCPGQSS PLIPAVTLRP LTETISTVQT IYTTRKPVSL
AASAETLRQE LEREKMMKRL LMTEL
//