GenomeNet

Database: UniProt
Entry: A0A5F9DWC7_RABIT
LinkDB: A0A5F9DWC7_RABIT
Original site: A0A5F9DWC7_RABIT 
ID   A0A5F9DWC7_RABIT        Unreviewed;      1070 AA.
AC   A0A5F9DWC7;
DT   11-DEC-2019, integrated into UniProtKB/TrEMBL.
DT   11-DEC-2019, sequence version 1.
DT   24-JAN-2024, entry version 14.
DE   SubName: Full=Erythrocyte membrane protein band 4.1 like 3 {ECO:0000313|Ensembl:ENSOCUP00000049980.1};
GN   Name=EPB41L3 {ECO:0000313|Ensembl:ENSOCUP00000049980.1};
OS   Oryctolagus cuniculus (Rabbit).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Lagomorpha; Leporidae; Oryctolagus.
OX   NCBI_TaxID=9986 {ECO:0000313|Ensembl:ENSOCUP00000049980.1, ECO:0000313|Proteomes:UP000001811};
RN   [1] {ECO:0000313|Ensembl:ENSOCUP00000049980.1, ECO:0000313|Proteomes:UP000001811}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Thorbecke inbred {ECO:0000313|Ensembl:ENSOCUP00000049980.1,
RC   ECO:0000313|Proteomes:UP000001811};
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:ENSOCUP00000049980.1}
RP   IDENTIFICATION.
RC   STRAIN=Thorbecke {ECO:0000313|Ensembl:ENSOCUP00000049980.1};
RG   Ensembl;
RL   Submitted (JUL-2023) to UniProtKB.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AAGW02031560; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AAGW02031561; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AAGW02031562; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AAGW02031563; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AAGW02031564; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   AlphaFoldDB; A0A5F9DWC7; -.
DR   Ensembl; ENSOCUT00000064382.1; ENSOCUP00000049980.1; ENSOCUG00000021196.3.
DR   GeneTree; ENSGT00940000157047; -.
DR   Proteomes; UP000001811; Chromosome 9.
DR   Bgee; ENSOCUG00000021196; Expressed in testis and 16 other cell types or tissues.
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; 2.
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   Reference proteome {ECO:0000313|Proteomes:UP000001811}.
FT   DOMAIN          110..391
FT                   /note="FERM"
FT                   /evidence="ECO:0000259|PROSITE:PS50057"
FT   REGION          1..66
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          479..570
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          693..733
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          794..827
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          846..939
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        488..511
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        542..560
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        794..811
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        879..897
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        904..931
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1070 AA;  118364 MW;  F849376656852AA5 CRC64;
     MTTESGSDSE SKPDQEAEPQ EAAGPQGRPG PQPGPEPPSE EQQALEQFEE AAAHSTPVRK
     EVTDKEQEFA AAAAKQLEYQ QLEDDKLSQK SSSSKLSRSP LKIVKKPKSM QCKVILLDGS
     EYTCDVEKRS RGQVLFDKVC EHLNLLEKDY FGLTYRDAEN QKNWLDPAKE IKKQIRSGAW
     HFSFNVKFYP PDPAQLSEDI TRYYLCLQLR DDVVSGRLPC SFVTLALLGS YTVQSELGDY
     DPDECGNDYI SEFRFAPNHT KELEDKVIEL HKSHRGMTPA EAEMHFLENA KKLSMYGVDL
     HHAKDSEGVE IMLGVCASGL LIYRDRLRIN RFAWPKVLKI SYKRNNFYIK IRPGEFEQFE
     STIGFKLPNH RAAKRLWKVC VEHHTFFRLL LPEAPPKKFL TLGSKFRYSG RTQAQTRRAS
     ALIDRPAPYF ERSSSKRYTM SRSLDGASVN ENHEIYMKDS MSAAEVGTGQ YATTKGISQT
     NLITTVTPEK KAEEERDEED NRRKKAEEAT PVAAVRPEGK SPGLGTDSCP LSPPSAHHTP
     ASSTELRRRC KEKEHALPGC EAPKAQHMRG EPTLDPDGQG KAYVGDQDVA FSCRQQTGKG
     TTLFSFSLQL PESFPSLLDD DGYLSFPNLS ETNLLPQSLQ HYLPIRSPSL VPCFLFIFFF
     LVSASFSVPY ALTLSFPLAL CLCYLEPKAA SLSASLDNDP SDSSEEETDS ERTDTAADGE
     TTATESDQEE DAELKAQELD KTQDELMKHQ TNISELKRTF LETSTDTAVT NEWEKRLSTS
     PVRLAARQED APMIEPLVPE EKMDAKPEPS EAEAESTPLQ QPLGAEKVAQ ETVLVEERRV
     MIVHASGDAS SAAGDEVEAA APPAPTADAP GTKAKEGSGV SEGAKEESRE DAEKAAPQQE
     EAAAAPLERE EEQSAAIHVS ETLEQKPHFE SSTVKTETVS FGSISPGGVK LDMSTKEVPV
     VHTETKTITY ESSQVDPGAD LEPGVLMSAQ TITSETTSTT TTTHITKTVK GGISETRIEK
     RIVITGDADI DHDQALAQAI KEAKEQHPDM SVTKVVVHKE TEITPEDGED
//
DBGET integrated database retrieval system