(data stored in ACNUC9306 zone)

HOGENOM: PIG9_38_PE2

ID   PIG9_38_PE2                          STANDARD;      PRT;   602 AA.
AC   PIG9_38_PE2; P26044;
DT   00-JAN-0000 (Rel. 1, Created)
DT   00-JAN-0000 (Rel. 2, Last sequence update)
DT   00-JAN-0000 (Rel. 3, Last annotation update)
DE   Flags: Fragments;
DE   RecName: Full=Radixin;AltName: Full=Moesin-B; (PIG9_38.PE2).
GN   Name=RDX;
OS   SUS SCROFA.
OC   Eukaryota; Metazoa; Eumetazoa; Bilateria; Coelomata; Deuterostomia;
OC   Chordata; Craniata; Vertebrata; Gnathostomata; Teleostomi; Euteleostomi;
OC   Sarcopterygii; Tetrapoda; Amniota; Mammalia; Theria; Eutheria;
OC   Laurasiatheria; Cetartiodactyla; Suina; Suidae; Sus.
OX   NCBI_TaxID=9823;
RN   [0]
RP   -.;
RG   -.;
RL   -.;
CC   -!- SEQ. DATA ORIGIN: Translated from the HOGENOM CDS PIG9_38.PE2.
CC       Sus scrofa chromosome 9 Sscrofa9 partial sequence 36574628..37574627
CC       annotated by Ensembl
CC   -!- ANNOTATIONS ORIGIN:RADI_PIG
CC   -!- FUNCTION: Probably plays a crucial role in the binding of the
CC       barbed end of actin filaments to the plasma membrane.
CC   -!- ENZYME REGULATION: A head-to-tail association, of the N-terminal
CC       and C-terminal halves results in a closed conformation (inactive
CC       form) which is incapable of actin or membrane-binding (By
CC       similarity).
CC   -!- SUBUNIT: Binds SLC9A3R1. Interacts with NHERF1, NHERF2, LAYN,
CC       MME/NEP and ICAM2 (By similarity).
CC   -!- SUBCELLULAR LOCATION: Cell membrane; Peripheral membrane protein;
CC       Cytoplasmic side. Cytoplasm, cytoskeleton. Cleavage furrow.
CC       Note=Highly concentrated in the undercoat of the cell-to-cell
CC       adherens junction and the cleavage furrow in the interphase and
CC       mitotic phase, respectively.
CC   -!- DOMAIN: The N-terminal domain interacts with the C-terminal domain
CC       of LAYN. An interdomain interaction between its N-terminal and C-
CC       terminal domains inhibits its ablilty to bind LAYN. In the
CC       presence of acidic phospholipids, the interdomain interaction is
CC       inhibited and this enhances binding to LAYN (By similarity).
CC   -!- PTM: Phosphorylated by tyrosine-protein kinases. Phosphorylation
CC       by ROCK2 suppresses the head-to-tail association of the N-terminal
CC       and C-terminal halves resulting in an opened conformation which is
CC       capable of actin and membrane-binding (By similarity).
CC   -!- SIMILARITY: Contains 1 FERM domain.
CC   -!- GENE_FAMILY: HOG000007113 [ FAMILY / ALN / TREE ]
DR   HOGENOM:Sus_scrofa;ENSSSCG00000015013;ENSSSCT00000016377;ENSSSCP00000015937.
DR   EMBL; M86444; - ;
DR   UniProtKB/Swiss-Prot; P26044; -.
DR   EMBL; M86444; AAB02865.1; -; mRNA.
DR   PIR; S39805; S39805.
DR   RefSeq; NP_001009576.1; NM_001009576.1.
DR   UniGene; Ssc.7954; -.
DR   ProteinModelPortal; P26044; -.
DR   SMR; P26044; 2-374, 494-583.
DR   STRING; P26044; -.
DR   GeneID; 494457; -.
DR   KEGG; ssc:494457; -.
DR   CTD; 5962; -.
DR   GeneTree; ENSGT00600000084066; -.
DR   OrthoDB; EOG4C5CJJ; -.
DR   GO; GO:0032154; C:cleavage furrow; IEA:UniProtKB-SubCell.
DR   GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
DR   GO; GO:0019898; C:extrinsic to membrane; IEA:InterPro.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0003779; F:actin binding; IEA:UniProtKB-KW.
DR   GO; GO:0051693; P:actin filament capping; IEA:UniProtKB-KW.
DR   InterPro; IPR019749; Band_41_domain.
DR   InterPro; IPR019750; Band_41_fam.
DR   InterPro; IPR011174; ERM.
DR   InterPro; IPR011259; ERM_C.
DR   InterPro; IPR000798; Ez/rad/moesin.
DR   InterPro; IPR014352; FERM/acyl-CoA-bd_prot_3-hlx.
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.
DR   InterPro; IPR011993; PH_type.
DR   Gene3D; G3DSA:1.20.80.10; ACBP; 1.
DR   Gene3D; G3DSA:2.30.29.30; PH_type; 1.
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   SUPFAM; SSF47031; FERM_3-hlx; 1.
DR   SUPFAM; SSF48678; Moesin; 1.
DR   PROSITE; PS00660; FERM_1; 1.
DR   PROSITE; PS00661; FERM_2; 1.
DR   PROSITE; PS50057; FERM_3; 1.
DR   HOGENOMDNA; PIG9_38.PE2; -.
KW   ENSSSCG00000015013820036002503210000011;
KW   RADI_PIG; M86444;
KW   Acetylation; Actin capping; Actin-binding; Cell membrane;
KW   Complete proteome; Cytoplasm; Cytoskeleton; Membrane; Phosphoprotein.
SQ   SEQUENCE   602 AA;  UNKNOWN MW;  UNKNOWN CRC64;
     IHKRKEFLKT KIKDKKRRKM PKPINVRVTT MDAELEFAIQ PNTTGKQLFD QVVKTVGLRE
     VWFFGLQYVD SKGYSTWLKL NKKVTQQDVK KENPLQFKFR AKFFPEDVSE ELIQEITQRL
     FFLQVKEAIL NDEIYCPPET AVLLASYAVQ AKYGDYNKEI HKPGYLANDR LLPQRVLEQH
     KLTKEQWEER IQNWHEEHRG MLREDSMMEY LKIAQDLEMY GVNYFEIKNK KGTELWLGVD
     ALGLNIYEHD DKLTPKIGFP WSEIRNISFN DKKFVIKPID KKAPDFVFYA PRLRINKRIL
     ALCMGNHELY MRRRKPDTIE VQQMKAQARE EKHQKQLERA QLENEKKKRE IAEKEKERIE
     REKEELMERL RQIEEQTMKA QKELEEQTRK ALELDQERKR AKEEAERLEK ERRAAEEAKS
     AIAKQAADQM KNQEQLAAEL AEFTAKIALL EEAKKKKEEE ATEWQHKAFA AQEDLEKTKE
     ELKTVMSAPP PPPPPPVVPP TENEHDEHDE NNAEASAELS NDGVMNHRSE EERVTETQKN
     ERVKKQLQAL SSELAQARDE TKKTQNDVLH AENVKAGRDK YKTLRQIRQG NTKQRIDEFE
     AM
//

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