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Database: UniProt
Entry: H2SUX6_TAKRU
LinkDB: H2SUX6_TAKRU
Original site: H2SUX6_TAKRU 
ID   H2SUX6_TAKRU            Unreviewed;       763 AA.
AC   H2SUX6;
DT   21-MAR-2012, integrated into UniProtKB/TrEMBL.
DT   17-JUN-2020, sequence version 3.
DT   27-MAR-2024, entry version 66.
DE   SubName: Full=Erythrocyte membrane protein band 4.1 like 3 {ECO:0000313|Ensembl:ENSTRUP00000016214.3};
GN   Name=EPB41L3 {ECO:0000313|Ensembl:ENSTRUP00000016214.3};
OS   Takifugu rubripes (Japanese pufferfish) (Fugu rubripes).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Eupercaria; Tetraodontiformes; Tetradontoidea; Tetraodontidae; Takifugu.
OX   NCBI_TaxID=31033 {ECO:0000313|Ensembl:ENSTRUP00000016214.3, ECO:0000313|Proteomes:UP000005226};
RN   [1] {ECO:0000313|Ensembl:ENSTRUP00000016214.3, ECO:0000313|Proteomes:UP000005226}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=21551351;
RA   Kai W., Kikuchi K., Tohari S., Chew A.K., Tay A., Fujiwara A., Hosoya S.,
RA   Suetake H., Naruse K., Brenner S., Suzuki Y., Venkatesh B.;
RT   "Integration of the genetic map and genome assembly of fugu facilitates
RT   insights into distinct features of genome evolution in teleosts and
RT   mammals.";
RL   Genome Biol. Evol. 3:424-442(2011).
RN   [2] {ECO:0000313|Ensembl:ENSTRUP00000016214.3}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (NOV-2023) to UniProtKB.
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DR   AlphaFoldDB; H2SUX6; -.
DR   Ensembl; ENSTRUT00000016286.3; ENSTRUP00000016214.3; ENSTRUG00000006598.3.
DR   GeneTree; ENSGT00940000157047; -.
DR   Proteomes; UP000005226; Chromosome 22.
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   Gene3D; 1.20.80.10; -; 1.
DR   Gene3D; 2.30.29.30; Pleckstrin-homology domain (PH domain)/Phosphotyrosine-binding domain (PTB); 1.
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   Actin-binding {ECO:0000256|ARBA:ARBA00023203};
KW   Reference proteome {ECO:0000313|Proteomes:UP000005226}.
FT   DOMAIN          79..360
FT                   /note="FERM"
FT                   /evidence="ECO:0000259|PROSITE:PS50057"
FT   REGION          1..71
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          440..489
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          557..580
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          593..624
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        11..25
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        447..467
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        593..622
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   763 AA;  85540 MW;  F7672A173A664EF4 CRC64;
     MTTESGADSE AKQPQENKET EKGISKAAEP ASPVQLPAAA GHSTPARKQQ DSLDEDQLSH
     SSSRLSRSPL KGVKKAKIMQ CKVTLLDNSD YTIDVEKGAR GQMLFDKVCE HLNLLERDYF
     GITYRDVENQ KNWLDPSKEL KKQIRTGPWN FAFNVKFYPP DPVQLAEDIT RYYLCLQLRD
     DVVSGRLPCS FATHTVLGSY TVQSELGDYD HEELGSDYLS ELRLAPNQTK ELEEKVMELH
     KSYKGMTPGE AEMHFLENAK KLSMYGVDLH HAKDSEGVEI MLGVCSSGLL IYRDRLRINR
     FAWPKILKIS YKRNNFYIKI RPGEFEQFES TIGFKLPNHR AAKRLWKVCV EHHTFFRLVS
     PEAPPKKFLS LGSKFRYSGR TQAQTRRASS QIIRPAPFFE RSSSKRYNMS RSLDGAPIME
     NHETLMKDSS ADGVARVKGN IITTVTPERK AEEENGEQED AKNDAADKPD PAASSPLHQE
     TKTDSEQTDF AIDGEMTATE SEADEESEIQ TQFSCIRRVK GENIFIRHIN LMLEDTSSPA
     EVVKHQTNIS ELKRSFLETG DGTQGPTEWE KRLSSSPMCS PRFDEAPMIE PLDTEEKQFD
     GEETKELESK ATETHSEPKE NPVVATETEA AGAKSTVPVS LDTTDAGTKE MPVIHTETKT
     ITYESAEVDT NGDFDPGVLL SAQTITSETT STTTTTHITK MVKGGISETR IEKRIVISGD
     ADIDHDQALA QAIKEAKEQH PDMSVTKVVV HKETEITPEE GED
//
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