(data stored in ACNUC9306 zone)

HOGENOM: BOVIN15_20_PE3

ID   BOVIN15_20_PE3                       STANDARD;      PRT;   583 AA.
AC   BOVIN15_20_PE3; Q32LP2;
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   RecName: Full=Radixin; (BOVIN15_20.PE3).
GN   Name=RDX;
OS   BOS TAURUS.
OC   Eukaryota; Metazoa; Eumetazoa; Bilateria; Coelomata; Deuterostomia;
OC   Chordata; Craniata; Vertebrata; Gnathostomata; Teleostomi; Euteleostomi;
OC   Sarcopterygii; Tetrapoda; Amniota; Mammalia; Theria; Eutheria;
OC   Laurasiatheria; Cetartiodactyla; Ruminantia; Pecora; Bovidae; Bovinae; Bos.
OX   NCBI_TaxID=9913;
RN   [0]
RP   -.;
RG   -.;
RL   -.;
CC   -!- SEQ. DATA ORIGIN: Translated from the HOGENOM CDS BOVIN15_20.PE3.
CC       Bos taurus chromosome 15 Btau_4.0 partial sequence 18519180..19519179
CC       annotated by Ensembl
CC   -!- ANNOTATIONS ORIGIN:RADI_BOVIN
CC   -!- FUNCTION: Probably plays a crucial role in the binding of the
CC       barbed end of actin filaments to the plasma membrane (By
CC       similarity).
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 (By similarity). Cytoplasm, cytoskeleton (By
CC       similarity). Cleavage furrow. Note=Highly concentrated in the
CC       undercoat of the cell-to-cell adherens junction and the cleavage
CC       furrow in the interphase and mitotic phase, respectively (By
CC       similarity).
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:Bos_taurus;ENSBTAG00000004672;ENSBTAT00000033851;ENSBTAP00000033759.
DR   EMBL; BC109485; - ;
DR   EMBL; BC149864; - ;
DR   UniProtKB/Swiss-Prot; Q32LP2; -.
DR   EMBL; BC109485; AAI09486.1; -; mRNA.
DR   IPI; IPI00711368; -.
DR   RefSeq; NP_001069217.1; NM_001075749.1.
DR   UniGene; Bt.35977; -.
DR   HSSP; P26043; 2D2Q.
DR   ProteinModelPortal; Q32LP2; -.
DR   SMR; Q32LP2; 1-374, 494-583.
DR   STRING; Q32LP2; -.
DR   PRIDE; Q32LP2; -.
DR   Ensembl; ENSBTAT00000033851; ENSBTAP00000033759; ENSBTAG00000004672.
DR   GeneID; 517111; -.
DR   KEGG; bta:517111; -.
DR   CTD; 5962; -.
DR   eggNOG; maNOG15414; -.
DR   GeneTree; ENSGT00600000084066; -.
DR   InParanoid; Q32LP2; -.
DR   OMA; DGVMNHR; -.
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; BOVIN15_20.PE3; -.
KW   ENSBTAG00000004672fold_1320000031; ENSBTAP00000033759fold_1320000031;
KW   A6QQJ5_BOVIN; BC109485; BC149864;
KW   Acetylation; Actin capping; Actin-binding; Cell membrane;
KW   Complete proteome; Cytoplasm; Cytoskeleton; Membrane; Phosphoprotein;
KW   Reference proteome.
SQ   SEQUENCE   583 AA;  UNKNOWN MW;  UNKNOWN CRC64;
     MPKPINVRVT TMDAELEFAI QPNTTGKQLF DQVVKTVGLR EVWFFGLQYV DSKGYSTWLK
     LNKKVTQQDV KKENPLQFKF RAKFFPEDVS EELIQEITQR LFFLQVKEAI LNDEIYCPPE
     TAVLLASYAV QAKYGDYNKE IHKPGYLAND RLLPQRVLEQ HKLTKEQWEE RIQNWHEEHR
     GMLREDSMME YLKIAQDLEM YGVNYFEIKN KKGTELWLGV DALGLNIYEH DDKLTPKIGF
     PWSEIRNISF NDKKFVIKPI DKKAPDFVFY APRLRINKRI LALCMGNHEL YMRRRKPDTI
     EVQQMKAQAR EEKHQKQLER AQLENEKKKR EIAEKEKERI EREKEELMER LRQIEEQTMK
     AQKELEEQTR KALELDQERK RAKEEAERLE KERQAAEEAK SALAKQAADQ MKNQEQLAAE
     LAEFTAKIAL LEEAKKKKEE EATEWQHKAF AAQEDLEKTK EELKTVMSAP PPPPPPPVIP
     PTENEHDEHD ENNAEASAEL SNDGVMNHRS EEERVTETQK NERVKKQLQA LSSELAQARD
     ETKKTQNDVL HAENVKAGRD KYKTLRQIRQ GNTKQRIDEF EAM
//

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