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.
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 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
//