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Database: UniProt
Entry: A0A2K6JRC6_RHIBE
LinkDB: A0A2K6JRC6_RHIBE
Original site: A0A2K6JRC6_RHIBE 
ID   A0A2K6JRC6_RHIBE        Unreviewed;       906 AA.
AC   A0A2K6JRC6;
DT   28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT   28-MAR-2018, sequence version 1.
DT   27-MAR-2024, entry version 24.
DE   SubName: Full=Erythrocyte membrane protein band 4.1 like 3 {ECO:0000313|Ensembl:ENSRBIP00000001575.1};
GN   Name=EPB41L3 {ECO:0000313|Ensembl:ENSRBIP00000001575.1};
OS   Rhinopithecus bieti (Black snub-nosed monkey) (Pygathrix bieti).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC   Cercopithecidae; Colobinae; Rhinopithecus.
OX   NCBI_TaxID=61621 {ECO:0000313|Ensembl:ENSRBIP00000001575.1, ECO:0000313|Proteomes:UP000233180};
RN   [1] {ECO:0000313|Ensembl:ENSRBIP00000001575.1, ECO:0000313|Proteomes:UP000233180}
RP   NUCLEOTIDE SEQUENCE.
RA   Wu, C.-I. and Zhang, Y.;
RT   "Genome of Rhinopithecus bieti.";
RL   Submitted (JUN-2016) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Ensembl:ENSRBIP00000001575.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (SEP-2023) to UniProtKB.
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DR   RefSeq; XP_017723406.1; XM_017867917.1.
DR   Ensembl; ENSRBIT00000008738.1; ENSRBIP00000001575.1; ENSRBIG00000008131.1.
DR   Ensembl; ENSRBIT00000008957.1; ENSRBIP00000001616.1; ENSRBIG00000008131.1.
DR   GeneID; 108526911; -.
DR   CTD; 23136; -.
DR   GeneTree; ENSGT00940000157047; -.
DR   OrthoDB; 5319111at2759; -.
DR   Proteomes; UP000233180; Unplaced.
DR   GO; GO:0005856; C:cytoskeleton; IEA:InterPro.
DR   GO; GO:0003779; F:actin binding; IEA:InterPro.
DR   GO; GO:0005198; F:structural molecule activity; IEA:InterPro.
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; cd17203; FERM_F1_EPB41L3; 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; IPR030691; Band4.1-L3_FERM_F1.
DR   InterPro; IPR008379; Band_4.1_C.
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; IPR007477; SAB_dom.
DR   InterPro; IPR029071; Ubiquitin-like_domsf.
DR   PANTHER; PTHR23280; 4.1 G PROTEIN; 1.
DR   PANTHER; PTHR23280:SF20; BAND 4.1-LIKE PROTEIN 3; 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   Reference proteome {ECO:0000313|Proteomes:UP000233180}.
FT   DOMAIN          110..391
FT                   /note="FERM"
FT                   /evidence="ECO:0000259|PROSITE:PS50057"
FT   REGION          1..43
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          483..543
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          736..782
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        488..543
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        736..751
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   906 AA;  101069 MW;  BB108AB7B225248B CRC64;
     MTTESGSDSE SKPDQEAEPQ EAEGAQGRAG APVPEPPSEE QQQVLEQFAS AAAHSTPVRR
     EVTDKEQEFA ARAAKQLEYQ QLEDDKLSQK SYSSKLSRSP LKIAKKPKSM QCKVILLDGS
     EYTCDVEKRS RGQVLFDKVC EHLNLLEKDY FGLTYRDAEN QKNWLDPAKE IKKQVRSGAW
     HFSFNVKFYP PDPAQLSEDI TRYYLCLQLR DDIVSGRLPC SFVTLALLGS YTVQSELGDY
     DPDECGSDYI SEFRFAPNHT KELEDKVIEL HKSHRGMTPA EAEMHFLENA KKLSMYGVDL
     HHAKDSEGVE IMLGVCASGL LIYRDRLRIN RFAWPKVLKI SYKRNNFYIK IRPGEFEQFE
     STIGFKLPNH RAAKRLWKVC VEHHTFFRLL LPEAPPKKFL TLGSKFRYSG RTQAQTRRAS
     ALIDRPAPYF ERSSSKRYTM SRSLDGASVN ENHEIYMKDS VSAAEVGTGQ YATTKGISQT
     NLITTVTPEK KAEEERDEEE DKRRKGEEVT PVSAIRHEGK TDSERTDTAA DGETTATEEL
     EKTQDDLMKH QTNISELKRT FLETSTDTAV TNEWEKRLST SPVRLAARQE DAPMIEPLVP
     EETKQSSGEK LMDGSEIFSL LESARKPTEF IGGVTSTSQS WVQKMETKTE SSGIETEPTV
     HRLPLSTEKV VQETVLVEER HVVHASGDAS YSVGDSGDTA AQPAFTGIKG KEGSALMEGS
     KEEGGEEVAK AVLEQEETAA ASRERQEEQS AAIHVSETLE QKPHFESSTV KTETISFGSA
     SPGGVKLEIS TKEVPVVHTE TKTITYESSQ VDPGTDLEPG VLMSAQTITS ETTSTTTTTH
     ITKTVKGGIS ETRIEKRIVI TGDADIDHDQ ALAQAIKEAK EQHPDMSVTK VVVHKETEIT
     PEDGED
//
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