ID A0A672GNK2_SALFA Unreviewed; 791 AA.
AC A0A672GNK2;
DT 17-JUN-2020, integrated into UniProtKB/TrEMBL.
DT 17-JUN-2020, sequence version 1.
DT 27-MAR-2024, entry version 17.
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};
OS Salarias fasciatus (Jewelled blenny) (Blennius fasciatus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Blenniimorphae; Blenniiformes; Blennioidei; Blenniidae;
OC Salariinae; Salarias.
OX NCBI_TaxID=181472 {ECO:0000313|Ensembl:ENSSFAP00005018525.1, ECO:0000313|Proteomes:UP000472267};
RN [1] {ECO:0000313|Ensembl:ENSSFAP00005018525.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-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 AlphaFoldDB; A0A672GNK2; -.
DR Ensembl; ENSSFAT00005019256.1; ENSSFAP00005018525.1; ENSSFAG00005009718.1.
DR Proteomes; UP000472267; Unplaced.
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 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: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; 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; 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:UP000472267};
KW Transport {ECO:0000256|ARBA:ARBA00022448}.
FT DOMAIN 174..455
FT /note="FERM"
FT /evidence="ECO:0000259|PROSITE:PS50057"
FT REGION 1..173
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 476..634
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..30
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 31..58
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 64..78
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 87..126
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 135..168
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 476..508
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 546..571
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 587..630
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 791 AA; 88976 MW; 57183FDAF5AF02B4 CRC64;
TVQIQSLNTE TNLSSHVYQH NTGWNEAESQ QKKPRQQEET GQDVRPPSPE DEQLRPRNRN
SAGRGLSRLF SSFLKRRSQC DSDGGGGGGE RAERDEDEAK APIADPEPEL RAEGDQHSVS
SAEVQEEEKE KEEEGGGEDG EKEEKEEKEE KEEKEEKTAE EPRGPRAPRR PKTMQITVTL
LDDTVFECEL DKHAKGQELF MRVCDHLNLL EKDYYGLGIW DTPTRKTWMD LTKEIRRQVQ
GSTYNFTFNV KFYPPDPAQL SEDITRYYLC LQLRKDILQG RLPCSFVTLA LLGSYALQSE
LGEYDPEVHG GDYAKDMKMA QGQTKELEDK MMELHRTYRS MPPAQADLMF LENAKKLSMY
GVDLHQAKDL DGVDIMLGVC SSGLMVYKDK LRINRFPWPK VLKVSYKRSS FFIKIRPSEV
EQYESAIGFK LPNYKAAKKL WKVCVEHHTF FRLTSTEMAT TPRKFLALGS KFRYSGRTQA
QTRQASSLID RPAPLFQRSS SKRNSRSLDG AMALTPDNRS SRPVSAPIMS PVSPGEATPS
PLLAGLHRPD RRDGPAPRGR RPAHRKAEPK AEGQPASPAS RSHGAKAEPS PDLKDLDKTQ
TEIMRHHTSI SELKRSFMES VPEPRPSEWD KRLSTNSPFR TASINGQLQP AVRTISPLLK
TQTITISDVT NSVRGTVSYP DVPLVHTETK TITYESAQPV DNVAERDSGV LLSAQTITSE
TISTTTTTQI TKTVKGGISE TRIEKRIVIT GDTEIDHDKA LAQAIKEAKE QHPDMSVTKV
VVHQETEISP E
//
