ID   A0A4W3J8F9_CALMI        Unreviewed;       606 AA.
AC   A0A4W3J8F9;
DT   18-SEP-2019, integrated into UniProtKB/TrEMBL.
DT   18-SEP-2019, sequence version 1.
DT   11-DEC-2019, entry version 4.
DE   RecName: Full=FERM domain-containing protein {ECO:0000259|PROSITE:PS50057};
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, 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}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (JUL-2019) to UniProtKB.
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DR   Ensembl; ENSCMIT00000036380; ENSCMIP00000035851; ENSCMIG00000014840.
DR   Proteomes; UP000314986; Unassembled WGS sequence.
DR   GO; GO:0005856; C:cytoskeleton; IEA:InterPro.
DR   GO; GO:0003779; F:actin binding; IEA:InterPro.
DR   CDD; cd14473; FERM_B-lobe; 1.
DR   CDD; cd13194; FERM_C_ERM; 1.
DR   Gene3D; 1.20.80.10; -; 1.
DR   Gene3D; 1.25.40.1020; -; 1.
DR   Gene3D; 2.30.29.30; -; 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; 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   Pfam; PF00769; ERM; 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; SSF47031; SSF47031; 1.
DR   SUPFAM; SSF48678; SSF48678; 1.
DR   SUPFAM; SSF54236; SSF54236; 1.
DR   PROSITE; PS00660; FERM_1; 1.
DR   PROSITE; PS00661; FERM_2; 1.
DR   PROSITE; PS50057; FERM_3; 1.
PE   4: Predicted;
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Reference proteome {ECO:0000313|Proteomes:UP000314986}.
FT   DOMAIN          30..320
FT                   /note="FERM"
FT                   /evidence="ECO:0000259|PROSITE:PS50057"
FT   REGION          85..88
FT                   /note="Phosphatidylinositol binding"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR002305-1"
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   COILED          183..203
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        399..431
FT                   /note="Polyampholyte"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        505..544
FT                   /note="Polyampholyte"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         303
FT                   /note="Phosphatidylinositol"
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
//