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Database: UniProt
Entry: A0A3Q3GPG7_KRYMA
LinkDB: A0A3Q3GPG7_KRYMA
Original site: A0A3Q3GPG7_KRYMA 
ID   A0A3Q3GPG7_KRYMA        Unreviewed;      1041 AA.
AC   A0A3Q3GPG7;
DT   10-APR-2019, integrated into UniProtKB/TrEMBL.
DT   10-APR-2019, sequence version 1.
DT   27-MAR-2024, entry version 22.
DE   SubName: Full=Erythrocyte membrane protein band 4.1 like 2 {ECO:0000313|Ensembl:ENSKMAP00000025297.1};
GN   Name=EPB41L2 {ECO:0000313|Ensembl:ENSKMAP00000025297.1};
OS   Kryptolebias marmoratus (Mangrove killifish) (Rivulus marmoratus).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Ovalentaria; Atherinomorphae; Cyprinodontiformes; Rivulidae; Kryptolebias.
OX   NCBI_TaxID=37003 {ECO:0000313|Ensembl:ENSKMAP00000025297.1, ECO:0000313|Proteomes:UP000264800};
RN   [1] {ECO:0000313|Ensembl:ENSKMAP00000025297.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (NOV-2023) to UniProtKB.
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DR   AlphaFoldDB; A0A3Q3GPG7; -.
DR   Ensembl; ENSKMAT00000025617.1; ENSKMAP00000025297.1; ENSKMAG00000018675.1.
DR   GeneTree; ENSGT00940000155617; -.
DR   Proteomes; UP000264800; 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; cd17106; FERM_F1_EPB41L; 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; 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; 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:UP000264800}.
FT   DOMAIN          198..480
FT                   /note="FERM"
FT                   /evidence="ECO:0000259|PROSITE:PS50057"
FT   REGION          1..180
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          682..715
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          739..917
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        20..34
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        35..57
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        61..81
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        82..173
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        690..705
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        746..764
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        857..880
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1041 AA;  115543 MW;  23258CEA7CFB8FF7 CRC64;
     MTTEAGSETE VKENAEESAA PPDQSEQAKQ ESQEVANAEG EEKGKEKEKD GKKITRYLPT
     WFKKQKSQSQ TSPTKDVQPT EEPASKATEE EEGPVPEVNG HAEDVEEKEE VKLEQVKEAE
     AESHSNASTD TEPAKEEKVE EGAERSSDET KKTKEAEGGE EEKKEKEQVE AEGEGGDSQT
     SIFQSPLRLV RKTKMKVVVC HVALLDGTDF TCEVEKRAKG QYLFFKVCEH LNLLEKDYFG
     LTYKDNHEEK CWLDPTKEIK RQIRSNNWQF AFSVKFYPPD PSLLTEDITR YLLCLQLRED
     VASGRLPCSF VTHALLGSYT LQAEFGDYEP EQPRPLDFIS QLTLASNQNK EMEEKILELH
     KSHRGMTPAQ ADLQFLENAK KLSMYGVDLH HAKDSEAVDI MLGVCANGLL VYKDRLRINR
     FAWPKILKIS YKRNNFYIKI RPGETEQFES TVGFKLQNHR SAKRLWKVCV ENHSFFRLNA
     PEPPTKAHFL TLGSKFRYSG RTQAQTRLAS SLIDRPAPSF ERTSSKRISR SLDGAPVISI
     TEAGRDMAEN GREPHLELHS DSKDHDKTQD EVLKHQASIS QLKRSFMEAP PPSPPQPNQW
     EKRLTSSPAS IRVQQQQVSL EEEMASVLFS SRHAGAGFYS AACGFREATL DGVRTTRSPA
     AITAAACSSS EPQRLLISPP AALSASEVGA PQTEAASPDN TISKPKEPAK TTEVEIEETV
     VIQEVSKAAK PGLVTVTIAS DAEVDAPPAE EQETQQDSAQ VEEEVAAEEV QQGKPESVSS
     ESESEDEAEY QPEVSVSISQ TQIPEEKEEE EEPEKDDRDK GAEEQVSALE VPSLPAELSH
     PAEETIQEEE EEFRKEETDA EEKTAEKEKE SERETEESTE DPMVTPDEAP DSPTPPVETV
     AAAASPAPAE EEEEPKVNGE ASLVEVEPRP QVICCSEPPV VKTEMVTISD TFAAQKTEIA
     TKEVPIVHTE TKTITYEAAQ LDGNGDGEPG VLMTAQTITS ESLCTTTTTH ITKTLKGGLS
     ETRIEKRIVI TGDCDIDHDQ N
//
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