ID A0A4W3J8F9_CALMI Unreviewed; 606 AA. AC A0A4W3J8F9; DT 18-SEP-2019, integrated into UniProtKB/TrEMBL. DT 18-SEP-2019, sequence version 1. DT 18-JUN-2025, entry version 28. DE SubName: Full=Moesin b {ECO:0000313|Ensembl:ENSCMIP00000035851.1}; OS Callorhinchus milii (Ghost shark). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Chondrichthyes; OC Holocephali; Chimaeriformes; Callorhinchidae; Callorhinchus. OX NCBI_TaxID=7868 {ECO:0000313|Ensembl:ENSCMIP00000035851.1, 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:ENSCMIP00000035851.1} RP IDENTIFICATION. RG Ensembl; RL Submitted (MAR-2025) to UniProtKB. CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|ARBA:ARBA00004202}; CC Peripheral membrane protein {ECO:0000256|ARBA:ARBA00004202}. 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; A0A4W3J8F9; -. DR FunCoup; A0A4W3J8F9; 648. DR STRING; 7868.ENSCMIP00000035851; -. DR Ensembl; ENSCMIT00000036380.1; ENSCMIP00000035851.1; ENSCMIG00000014840.1. DR GeneTree; ENSGT01090000260082; -. DR InParanoid; A0A4W3J8F9; -. DR OMA; WEERIMS; -. DR Proteomes; UP000314986; Unassembled WGS sequence. DR GO; GO:0005856; C:cytoskeleton; IEA:InterPro. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell. DR GO; GO:0003779; F:actin binding; IEA:InterPro. DR CDD; cd14473; FERM_B-lobe; 1. DR CDD; cd13194; FERM_C_ERM; 1. DR CDD; cd17187; FERM_F1_ERM; 1. DR FunFam; 2.30.29.30:FF:000003; Radixin isoform 1; 1. DR FunFam; 1.20.80.10:FF:000002; radixin isoform X1; 1. DR FunFam; 3.10.20.90:FF:000013; radixin isoform X1; 1. DR FunFam; 1.20.5.450:FF:000001; radixin isoform X2; 1. DR Gene3D; 1.20.5.450; -; 1. DR Gene3D; 1.20.80.10; -; 1. DR Gene3D; 6.10.360.10; -; 1. DR Gene3D; 3.10.20.90; Phosphatidylinositol 3-kinase Catalytic Subunit, Chain A, domain 1; 1. DR Gene3D; 2.30.29.30; Pleckstrin-homology domain (PH domain)/Phosphotyrosine-binding domain (PTB); 1. DR InterPro; IPR019749; Band_41_domain. DR InterPro; IPR011174; ERM. DR InterPro; IPR011259; ERM_C_dom. DR InterPro; IPR041789; ERM_FERM_C. DR InterPro; IPR046810; ERM_helical. DR InterPro; IPR000798; Ez/rad/moesin-like. 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; IPR008954; Moesin_tail_sf. DR InterPro; IPR011993; PH-like_dom_sf. DR InterPro; IPR029071; Ubiquitin-like_domsf. DR PANTHER; PTHR23281; MERLIN/MOESIN/EZRIN/RADIXIN; 1. DR Pfam; PF00769; ERM_C; 1. DR Pfam; PF20492; ERM_helical; 1. DR Pfam; PF09380; FERM_C; 1. DR Pfam; PF00373; FERM_M; 1. DR Pfam; PF09379; FERM_N; 1. DR PIRSF; PIRSF002305; ERM; 1. DR PRINTS; PR00935; BAND41. DR PRINTS; PR00661; ERMFAMILY. DR SMART; SM00295; B41; 1. DR SMART; SM01196; FERM_C; 1. DR SUPFAM; SSF48678; Moesin tail domain; 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 Cell membrane {ECO:0000256|ARBA:ARBA00022475}; KW Membrane {ECO:0000256|ARBA:ARBA00023136}; KW Reference proteome {ECO:0000313|Proteomes:UP000314986}. FT DOMAIN 30..320 FT /note="FERM" FT /evidence="ECO:0000259|PROSITE:PS50057" FT REGION 328..369 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 399..442 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 485..545 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 333..369 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 399..428 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 505..515 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 517..526 FT /note="Low complexity" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 528..545 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT BINDING 85..88 FT /ligand="a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo- FT inositol)" FT /ligand_id="ChEBI:CHEBI:57880" FT /evidence="ECO:0000256|PIRSR:PIRSR002305-1" FT BINDING 303 FT /ligand="a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo- FT inositol)" FT /ligand_id="ChEBI:CHEBI:57880" FT /evidence="ECO:0000256|PIRSR:PIRSR002305-1" SQ SEQUENCE 606 AA; 71351 MW; 7E673FC07BC19DAB CRC64; VCSECGYNRI YTDALKKCNM LMDKLLWVYI NVRVTTMDAE LEFAIQPNTT GKQLFDQVVK TVGLREVWFF GLQYQDTKGF STWLKLNKKV TQQDVRKESP LLFKFRAKFF PEDVSEELIQ EITQRLFFLQ VKEGILNDDI YCPPETAVLL ASYAVQVKHG DFSKDAHKAG YLTNDRLLPQ RVLEQHKLNK EQWEDRIQIW HEEHRGMLRE DAMMEYLKIA QDLEMYGVNY FDIKNKKGSE LWLGVDALGL NIYEHDDRLT PKIGFPWSEI RNISFNDKKF VIKPIDKKAP DFVFLAPRLR INKRILALCM GNHELYMRRR KPDTIEVQQM KAQAREEKHQ KQLDRAQLEN EKKKREQAEK DREKIEREKD ELMEKLKQIE EQTLKAQKEL EEQTRRALEL EQERKRSQEE AERIEQDRKA AEEEKDALIK QSENQQKNQE ELALELSALS SKIAQLEMTK QKKEDEAIEW QKKAEVVQQD LEKTKEELKS ATCPPPTQVI ILQAENDHGD EHDENSAEAS AELSSEGTTK DRSEEERMTE AEKNVRVQRQ LLTLTSELAQ ARDETKKTQN DILHAENVKA GRDKYKTLRQ IRQGNTKQRI DEFESM //