ID K9J7S2_XENTR Unreviewed; 1144 AA.
AC K9J7S2;
DT 06-FEB-2013, integrated into UniProtKB/TrEMBL.
DT 02-JUN-2021, sequence version 4.
DT 27-MAR-2024, entry version 71.
DE SubName: Full=Erythrocyte membrane protein band 4.1-like 3 {ECO:0000313|Ensembl:ENSXETP00000010834};
GN Name=epb41l3 {ECO:0000313|Ensembl:ENSXETP00000010834};
OS Xenopus tropicalis (Western clawed frog) (Silurana tropicalis).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Silurana.
OX NCBI_TaxID=8364 {ECO:0000313|Ensembl:ENSXETP00000010834};
RN [1] {ECO:0000313|Ensembl:ENSXETP00000010834}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Nigerian {ECO:0000313|Ensembl:ENSXETP00000010834};
RX PubMed=20431018; DOI=10.1126/science.1183670;
RA Hellsten U., Harland R.M., Gilchrist M.J., Hendrix D., Jurka J.,
RA Kapitonov V., Ovcharenko I., Putnam N.H., Shu S., Taher L., Blitz I.L.,
RA Blumberg B., Dichmann D.S., Dubchak I., Amaya E., Detter J.C., Fletcher R.,
RA Gerhard D.S., Goodstein D., Graves T., Grigoriev I.V., Grimwood J.,
RA Kawashima T., Lindquist E., Lucas S.M., Mead P.E., Mitros T., Ogino H.,
RA Ohta Y., Poliakov A.V., Pollet N., Robert J., Salamov A., Sater A.K.,
RA Schmutz J., Terry A., Vize P.D., Warren W.C., Wells D., Wills A.,
RA Wilson R.K., Zimmerman L.B., Zorn A.M., Grainger R., Grammer T.,
RA Khokha M.K., Richardson P.M., Rokhsar D.S.;
RT "The genome of the Western clawed frog Xenopus tropicalis.";
RL Science 328:633-636(2010).
RN [2] {ECO:0000313|Ensembl:ENSXETP00000010834}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (DEC-2012) to UniProtKB.
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DR AlphaFoldDB; K9J7S2; -.
DR Ensembl; ENSXETT00000010834; ENSXETP00000010834; ENSXETG00000004959.
DR AGR; Xenbase:XB-GENE-1006073; -.
DR Xenbase; XB-GENE-1006073; epb41l3.
DR HOGENOM; CLU_003623_0_1_1; -.
DR Bgee; ENSXETG00000004959; Expressed in brain and 13 other cell types or tissues.
DR ExpressionAtlas; K9J7S2; baseline.
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; 3.
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 Actin-binding {ECO:0000256|ARBA:ARBA00023203}.
FT DOMAIN 110..391
FT /note="FERM"
FT /evidence="ECO:0000259|PROSITE:PS50057"
FT REGION 1..109
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 924..959
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 7..23
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 24..42
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 59..91
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 924..945
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1144 AA; 128597 MW; EE658AA3DC2A0831 CRC64;
MTSETGSESD SKKDQEKEQQ DPAHQKGISG TQQAQQAGED HQNVGENFPA AAAHSTPLKA
EKNPDKDWDK EAATKPLEYQ QLEDDKVSQK SGSSKLSKSP LKSARRPKNM QAKVMLLDGS
EYSCEVEKRS KGQILFEKVC EHLNLLEKDY FGLVYRDSEN QKNWLDPAKE IKKQTRNGAW
HFSFNVKFYP PDPSQLSEDI TRYYLCLQLR DDIVCGRLPC SFVTLALLGS YSVQSELGDY
DPEEYGSDYV TEFRFAPNQT KELEDKVVEL HKSYRGMTPA EAEMHFLENA KKLSMYGVDL
HHAKDSEGVE IMLGVCASGL LIYRDRLRIN RFAWPKVLKI SYKRNNFYIK IRPGEFEQFE
STIGFKLPNH RAAKRLWKVC VEHHTFFRLL MPEAPPKKFL TLGSKFRYSG RTQAQTRRAS
ALIDRPAPYF ERSSSKRYTM SRSLDGASVN ENHDLYMKDS VSATEVGTGP YITAKGISQT
NLITTVTPEK KAEEERDEEE EKKKKVEIIT TVTTIRHDTK SDQEEDTYAK TQEFDRNQEE
LMKHQTNISE LKRTFLETST DTTTGGEWEK RLSTSPVRLV MRHEEAPMIE PLVPEETKEE
REKREIQMSL ERTSYSMLES QPGDIVKKLR EARATSPVAT SQQIIMQKTI PTSPEGTEDW
VIIDKVPTKV VDGETKTIVT YKVTTVSSDM PAGTFKTSPL GGQSLDALKM ELKSKEEDSK
LKMYTLGRSY DTVSGKVVTM TSKAKEGDKE KTPSSFEIIQ KLEKDIAETI KIAPGTGDYE
ILEPISDDKG RKVPEGPPVK RRMSETLTPI KESDSQLASP VEETLKKVQD KDTEKNLIES
VIFGKAEQFQ DYDVIKADVP SWKDKKLSEW RYTRDQPFTI ATAHYVTESS ASKVVTKQSS
GEKTLEGSDI YSLLESTRKP SEFLGEVTST SQSWAQKTET TTEWDSSSKG QEDAEQKAKE
KVVQGMVSLE ESLVGSVHAS RDAAELAGTV IASSLKGDEG STLKKEPEED LAVDASACYA
QEEQHGSKVH ELLDGKPQVE SPVVKTEIIT FGTIADGEKP DISTKDVPVV HTETKTITYE
SSELGSRTDT DPGMLMSAQT ITSETFGTTT TTHITKTVKG GISETRIEKR IVITGDADID
HDQE
//
