ID A0A6J3PZ25_TURTR Unreviewed; 886 AA.
AC A0A6J3PZ25;
DT 07-OCT-2020, integrated into UniProtKB/TrEMBL.
DT 07-OCT-2020, sequence version 1.
DT 27-MAR-2024, entry version 13.
DE RecName: Full=Protein 4.1 {ECO:0000256|ARBA:ARBA00023658};
DE AltName: Full=Band 4.1 {ECO:0000256|ARBA:ARBA00030419};
DE AltName: Full=Erythrocyte membrane protein band 4.1 {ECO:0000256|ARBA:ARBA00032586};
GN Name=EPB41 {ECO:0000313|RefSeq:XP_033695254.1};
OS Tursiops truncatus (Atlantic bottle-nosed dolphin) (Delphinus truncatus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Whippomorpha; Cetacea; Odontoceti;
OC Delphinidae; Tursiops.
OX NCBI_TaxID=9739 {ECO:0000313|Proteomes:UP000245320, ECO:0000313|RefSeq:XP_033695254.1};
RN [1] {ECO:0000313|RefSeq:XP_033695254.1}
RP IDENTIFICATION.
RC TISSUE=Spleen {ECO:0000313|RefSeq:XP_033695254.1};
RG RefSeq;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cell cortex
CC {ECO:0000256|ARBA:ARBA00004544}. Cytoplasm, cytoskeleton
CC {ECO:0000256|ARBA:ARBA00004245}. Nucleus
CC {ECO:0000256|ARBA:ARBA00004123}.
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DR RefSeq; XP_033695254.1; XM_033839363.1.
DR AlphaFoldDB; A0A6J3PZ25; -.
DR Proteomes; UP000245320; Chromosome 1.
DR GO; GO:0005938; C:cell cortex; IEA:UniProtKB-SubCell.
DR GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0003779; F:actin binding; IEA:InterPro.
DR GO; GO:0005516; F:calmodulin binding; IEA:UniProtKB-KW.
DR GO; GO:0005198; F:structural molecule activity; IEA:InterPro.
DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
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; cd17105; FERM_F1_EPB41; 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; IPR021187; EPB4.1_FERM_F1.
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:SF12; PROTEIN 4.1; 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; 1.
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 Calmodulin-binding {ECO:0000256|ARBA:ARBA00022860};
KW Cell cycle {ECO:0000256|ARBA:ARBA00023306};
KW Cell division {ECO:0000256|ARBA:ARBA00022618};
KW Mitosis {ECO:0000256|ARBA:ARBA00022776};
KW Reference proteome {ECO:0000313|Proteomes:UP000245320};
KW Transport {ECO:0000256|ARBA:ARBA00022448}.
FT DOMAIN 234..515
FT /note="FERM"
FT /evidence="ECO:0000259|PROSITE:PS50057"
FT REGION 29..147
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 175..226
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 542..609
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 685..755
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 33..62
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 82..102
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 116..146
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 181..226
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 711..736
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 886 AA; 98793 MW; 06C280DECF616E44 CRC64;
MGIVIILPLS TSGVIVKVKG DAAFVESEKS LVAEAENPQQ QQQKEEGEGA TNSGQQETQL
EEAPQAAAEG DNQCEQKLKT SNGDTPTHED LTKNKERTSE NRGLSRLFSS FLKRPKSQVS
EEEGKEVESA KEKGEGHKEI EFGASLDEEI ILKAPIAAPE PELKTDPSLD LHSLSSAETQ
PAQEEHREDP DFQTEEGGGL EDCSKTEVKE ESPESVAERE LKASQKSIRR HRNMHCKVSL
LDDTVYECVV EKHAKGQDLL KRVCEHLNLL EEDYFSLAIW DNATSKTWLD SAKEIKKQVR
GVPWNFTFNV KFYPPDPAQL TEDITRYYLC LQLRQDIVAG RLPCSFATLA LLGSYTIQSE
LGDYDPELHG ADYVSDFKLA PNQTKELEEK VMELHKSYRS MTPAQADLEF LENAKKLSMY
GVDLHKAKDL EGVDIILGVC SSGLLVYKDK LRINRFPWPK VLKISYKRSS FFIKIRPGEQ
EQYESTIGFK LPSYRAAKKL WKVCVEHHTF FRLTSTDTIP KSKFLALGSK FRYSGRTQAQ
TRQASALIDR PAPHFERTAS KRASRSLDGA AIDSADRSPR PTSAPAIAQS QAAEGSVPGA
PVKKGVVSKT PKETVQVEVK KEEVPPEQPE PELTEVWKDL DKSQEEIKKH HASISELKKN
FMESVPEPQP SEWDKRLSTH SPFRTLNING QIPTGEGVKK TSVLPSERKV GGPETQERAL
LVQDEEKIKR QERSTESALP QQENEEILPK PPLVKTQTVT ISDTANAVKS EIPTKDVPIV
HTETKTITYE AAQTDDSNGD LDPGVLLTAQ TITSETTSST TTTQITKTVK GGISETRIEK
RIVITGDADI DHDQVLVQAI KEAKEQHPDM SVTKVVVHQE TEISEE
//
