ID A0A4W3I4N8_CALMI Unreviewed; 973 AA.
AC A0A4W3I4N8;
DT 18-SEP-2019, integrated into UniProtKB/TrEMBL.
DT 18-SEP-2019, sequence version 1.
DT 27-MAR-2024, entry version 19.
DE SubName: Full=Erythrocyte membrane protein band 4.1 like 2 {ECO:0000313|Ensembl:ENSCMIP00000024904.1};
GN Name=EPB41L2 {ECO:0000313|Ensembl:ENSCMIP00000024904.1};
OS Callorhinchus milii (Ghost shark).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Chondrichthyes;
OC Holocephali; Chimaeriformes; Callorhinchidae; Callorhinchus.
OX NCBI_TaxID=7868 {ECO:0000313|Ensembl:ENSCMIP00000024904.1, ECO:0000313|Proteomes:UP000314986};
RN [1] {ECO:0000313|Proteomes:UP000314986}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=17185593; DOI=10.1126/science.1130708;
RA Venkatesh B., Kirkness E.F., Loh Y.H., Halpern A.L., Lee A.P., Johnson J.,
RA Dandona N., Viswanathan L.D., Tay A., Venter J.C., Strausberg R.L.,
RA Brenner S.;
RT "Ancient noncoding elements conserved in the human genome.";
RL Science 314:1892-1892(2006).
RN [2] {ECO:0000313|Proteomes:UP000314986}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=17407382;
RA Venkatesh B., Kirkness E.F., Loh Y.H., Halpern A.L., Lee A.P., Johnson J.,
RA Dandona N., Viswanathan L.D., Tay A., Venter J.C., Strausberg R.L.,
RA Brenner S.;
RT "Survey sequencing and comparative analysis of the elephant shark
RT (Callorhinchus milii) genome.";
RL PLoS Biol. 5:E101-E101(2007).
RN [3] {ECO:0000313|Proteomes:UP000314986}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=24402279; DOI=10.1038/nature12826;
RG International Elephant Shark Genome Sequencing Consortium;
RA Venkatesh B., Lee A.P., Ravi V., Maurya A.K., Lian M.M., Swann J.B.,
RA Ohta Y., Flajnik M.F., Sutoh Y., Kasahara M., Hoon S., Gangu V., Roy S.W.,
RA Irimia M., Korzh V., Kondrychyn I., Lim Z.W., Tay B.H., Tohari S.,
RA Kong K.W., Ho S., Lorente-Galdos B., Quilez J., Marques-Bonet T.,
RA Raney B.J., Ingham P.W., Tay A., Hillier L.W., Minx P., Boehm T.,
RA Wilson R.K., Brenner S., Warren W.C.;
RT "Elephant shark genome provides unique insights into gnathostome
RT evolution.";
RL Nature 505:174-179(2014).
RN [4] {ECO:0000313|Ensembl:ENSCMIP00000024904.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-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; A0A4W3I4N8; -.
DR Ensembl; ENSCMIT00000025316.1; ENSCMIP00000024904.1; ENSCMIG00000010897.1.
DR GeneTree; ENSGT00940000155617; -.
DR Proteomes; UP000314986; Unassembled WGS sequence.
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:SF17; BAND 4.1-LIKE PROTEIN 2; 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; 4.
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:UP000314986}.
FT DOMAIN 240..521
FT /note="FERM"
FT /evidence="ECO:0000259|PROSITE:PS50057"
FT REGION 1..148
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 173..232
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 543..609
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 727..793
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 808..849
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 8..23
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 44..76
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 117..138
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 193..231
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 563..605
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 740..765
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 772..791
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 973 AA; 109868 MW; 5B1B3E46C6842CC0 CRC64;
MATDVGSKPE IKEFKETEQD QPQDSNLKDS VNAKQEQNDT KEDQQSVSTE QLVSEHEPSS
PSTSTASPSS SERKEQSGGK GLSRFLPGWL KKQKSLTLVQ PIEDKVAENT NDTPPEESET
PPEECEPLPE ESEPLPEESE PVEKEQLELV KIPCESEMVK EAVPTAEVIK VDDREEECPL
SSAEIQPAKE EKNAAGTLEK DTDLKSEEIT IEEKGSGEPK KDDDSNKKSP LKIPKMMKAV
QCKVLMLDGS EYTFEIEKRS KGQLLMDKVC EQINLLERDY FGLTFRDAAD QKNWLDPAKE
IKKQIRSWPW QFAFNVKFYP PDPIQLTEDI TRYYLCLQLR QDIISGRLPC SFVTHALLGS
FTLQAELGDY DEDEHRADYV SEFQFAPNHT KELEEKVVEL HKTHRGLTPA QADTQFLENA
KKLSMYGVDL HHAKDSEGVD IMLGVCANGL LIYKDRLRIN RFAWPKILKI SYKRSNFYIK
IRPGEMEQFE STIGFKLPNH RAAKKLWKVC VEHHTFFRLV SPEQPPKTKF LTLGSKFRYS
GRTQAQTRQA SNLIDRPAPY FERTSSKRTS RSLDGAPVDT MNDVQDSSTP AVSQSSTAEV
TVTTTDEKTA AKDKTTPFKT AQLDMPVEKN KSLGIDGGNI YIRHSNLMLE DLDKTQEDVL
KHQASISELK RSFMESTPEP RPNEWEKRFN SPLLLQTEGS SDEKQKPEMK EQAEVVVEET
IVIEERKRTS NRSKVKKETT VESNTVMPPS KVTAKEGSVS SSDSNSESED EAEYNPQTKE
GENENQEEQN KFEMLNRVAV EFKMVMKATK EPRVDEISDQ LENVQEEMQK GEIQEEIQTE
EQEDTKPKIN GDVSHVDSDS DPQVVCYSEP PVVKTEMVTI SDTVSSDKME IATKEVPIVQ
TETKTITYEA AQGDGSGDND PGVLMSAQTI TSESVCTTMT THITKTVKGG VSETRIEKRI
VITGDTDIDH DQK
//
