ID A0A3B1IQ34_ASTMX Unreviewed; 1147 AA.
AC A0A3B1IQ34;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE SubName: Full=Band 4.1-like protein 1 {ECO:0000313|Ensembl:ENSAMXP00000031836.1};
OS Astyanax mexicanus (Blind cave fish) (Astyanax fasciatus mexicanus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Characiformes;
OC Characoidei; Characidae; Astyanax.
OX NCBI_TaxID=7994 {ECO:0000313|Ensembl:ENSAMXP00000031836.1, ECO:0000313|Proteomes:UP000018467};
RN [1] {ECO:0000313|Proteomes:UP000018467}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=female {ECO:0000313|Proteomes:UP000018467};
RA Jeffery W., Warren W., Wilson R.K.;
RL Submitted (MAR-2013) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Proteomes:UP000018467}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=female {ECO:0000313|Proteomes:UP000018467};
RX PubMed=25329095; DOI=10.1038/ncomms6307;
RA McGaugh S.E., Gross J.B., Aken B., Blin M., Borowsky R., Chalopin D.,
RA Hinaux H., Jeffery W.R., Keene A., Ma L., Minx P., Murphy D., O'Quin K.E.,
RA Retaux S., Rohner N., Searle S.M., Stahl B.A., Tabin C., Volff J.N.,
RA Yoshizawa M., Warren W.C.;
RT "The cavefish genome reveals candidate genes for eye loss.";
RL Nat. Commun. 5:5307-5307(2014).
RN [3] {ECO:0000313|Ensembl:ENSAMXP00000031836.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
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DR AlphaFoldDB; A0A3B1IQ34; -.
DR Ensembl; ENSAMXT00000052497.1; ENSAMXP00000031836.1; ENSAMXG00000002656.2.
DR GeneTree; ENSGT00940000155617; -.
DR Proteomes; UP000018467; Unassembled WGS sequence.
DR Bgee; ENSAMXG00000002656; Expressed in brain and 10 other cell types or tissues.
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:SF24; BAND 4.1-LIKE PROTEIN 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 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:UP000018467}.
FT DOMAIN 61..346
FT /note="FERM"
FT /evidence="ECO:0000259|PROSITE:PS50057"
FT REGION 1..62
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 433..659
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 689..836
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 13..44
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 45..59
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 433..509
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 525..554
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 609..626
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 716..735
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 750..769
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 775..795
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 810..836
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1147 AA; 129557 MW; DC1ED51A3B0C62BF CRC64;
MSEKGSASDM KNAMEGDSRR VNQDHDSKMS DEHRDTDDSS EKTPSRVSRS PQKSSKRPKT
VPVKVSLLDG SDYEVGVEKA CKGQTLLDMV CEHLNLLEKD YFGLLFYDTD SQKNWLDPSK
EIKKQIRVGS WQFSFSVKFY PPDPSQLIED ITRYYLCLQL REDMLSGRLP CSFVTHALLG
SYAVQAELGD YDPEEHGPDY VSEFRFAPSQ TRELEERVME LHRTYRGMSP AEAEVNFLEN
AKKLSMYGVD LHHAKDSEGI DIMLGVCASG LLIYRDRLRI NRFAWPKILK ISYKRSNFYI
KIRPGEVEKK YEQFESTIGF KLPNHRASKR LWKVCIEHHT FFRLVSPEPP PKGFLVIGSK
FRYSGRTQAQ TRQASALIDR PAPQFERSIS RRYMLSRSLD GASALGDTMD RLSQHTPSEP
TPSMEYMEAS HEQYFDQEQD QPEDRDSESE ATPSKTMELK SDQDLAPRPK QEQFLDKPED
VLQKHQASIN ELKRALREPN SKLVHREKRL SAASSGSTPE KKAASEEPLL IEKPDGCQRE
LTLSSKEEKN KSPARIDPSL TASQREGEEV MRGKIHTPHG GVVGSYAVTR KAKKNSIPSP
EKPQRSMAKG SVLRNQHSQD SYSFGDDENG NGLPYERHVE NRVENSIHTN GYDEYPAERH
WTDRRYMRTG REEDAVNSTV DFWNYEEKSW GEASPNAAVD KHMRDQYNGS RWQKHANAEG
GKDKTHRRQE SEDSTDSVRS ITPQSEGKRA VPLKPERSKK LKGNKGVKPN EDQPESLSRS
VDETEATKSN EESSGSEKEP LPTPAIHAEP QEDAQREPWE RRLGSVSEDD PDPETLYLKE
THLGIERKCS SITVSSTSSL EAEVDFTVLM DLQTGMEEFS RGMSELGEKD FSSELGLSDR
DRPTHPAFIL GADPIILPEE KHADIWRTVE ESKPVAHVVE QKPVEERKPE PFVPKKAPRS
VKAAQALKKE SAELASMQAV RREGSEIASF QPHSSDIIAS QALRKTEVKI ETQPNGSEVT
TTIMEITDQD HGMHGLREGS FTMTERISPV SFGSLARDGS GSPLMVTESV TSTTTTHVTK
TVKGGYSETR IEKRIIITGD DDVDQDQALA MAIKEAKQQH PDMLVTKAVV VRETESSTHD
PHEESKS
//