(data stored in ACNUC9306 zone)

HOGENOM: RATX_PE718

ID   RATX_PE718                           STANDARD;      PRT;   576 AA.
AC   RATX_PE718; O35763;
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=Moesin;AltName: Full=Membrane-organizing extension spike
DE   protein; (RATX.PE718).
GN   Name=Msn;
OS   RATTUS NORVEGICUS.
OC   Eukaryota; Metazoa; Eumetazoa; Bilateria; Coelomata; Deuterostomia;
OC   Chordata; Craniata; Vertebrata; Gnathostomata; Teleostomi; Euteleostomi;
OC   Sarcopterygii; Tetrapoda; Amniota; Mammalia; Theria; Eutheria;
OC   Euarchontoglires; Glires; Rodentia; Sciurognathi; Muroidea; Muridae;
OC   Murinae; Rattus.
OX   NCBI_TaxID=10116;
RN   [0]
RP   -.;
RG   -.;
RL   -.;
CC   -!- SEQ. DATA ORIGIN: Translated from the HOGENOM CDS RATX.PE718.
CC       Rattus norvegicus chromosome X RGSC3.4  sequence 1..160699376
CC       annotated by Ensembl
CC   -!- ANNOTATIONS ORIGIN:MOES_RAT
CC   -!- FUNCTION: Probably involved in connections of major cytoskeletal
CC       structures 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. In resting T-cells, part of a PAG1-
CC       SLC9A3R1-MSN complex which is disrupted upon TCR activation.
CC       Interacts with PPP1R16B (By similarity).
CC   -!- SUBCELLULAR LOCATION: Cell membrane; Peripheral membrane protein;
CC       Cytoplasmic side (By similarity). Cytoplasm, cytoskeleton (By
CC       similarity). Apical cell membrane; Peripheral membrane protein;
CC       Cytoplasmic side (By similarity). Cell projection, microvillus
CC       membrane; Peripheral membrane protein; Cytoplasmic side (By
CC       similarity). Note=Phosphorylated form is enriched in microvilli-
CC       like structures at apical membrane. Increased cell membrane
CC       localization of both phosphorylated and non-phosphorylated forms
CC       seen after thrombin treatment (By similarity).
CC   -!- PTM: Phosphorylation on Thr-558 is crucial for the formation of
CC       microvilli-like structures. Phosphorylation by ROCK2 suppresses
CC       the head-to-tail association of the N-terminal and C-terminal
CC       halves resulting in an opened conformation which is capable of
CC       actin and membrane-binding (By similarity).
CC   -!- SIMILARITY: Contains 1 FERM domain.
CC   -!- GENE_FAMILY: HOG000007113 [ FAMILY / ALN / TREE ]
DR   HOGENOM:Rattus_norvegicus;ENSRNOG00000030118;ENSRNOT00000040148;ENSRNOP00000043519.
DR   EMBL; AF004811; - ;
DR   UniProtKB/Swiss-Prot; O35763; -.
DR   EMBL; AF004811; AAB61666.1; -; mRNA.
DR   IPI; IPI00212314; -.
DR   RefSeq; NP_110490.1; NM_030863.1.
DR   UniGene; Rn.2762; -.
DR   ProteinModelPortal; O35763; -.
DR   SMR; O35763; 1-396, 488-577.
DR   IntAct; O35763; 2.
DR   MINT; MINT-4571444; -.
DR   STRING; O35763; -.
DR   PhosphoSite; O35763; -.
DR   World-2DPAGE; 0004:O35763; -.
DR   PRIDE; O35763; -.
DR   GeneID; 81521; -.
DR   KEGG; rno:81521; -.
DR   UCSC; NM_030863; rat.
DR   CTD; 4478; -.
DR   RGD; 621260; Msn.
DR   eggNOG; roNOG13879; -.
DR   GeneTree; ENSGT00600000084066; -.
DR   InParanoid; O35763; -.
DR   OrthoDB; EOG4C5CJJ; -.
DR   NextBio; 615037; -.
DR   ArrayExpress; O35763; -.
DR   Genevestigator; O35763; -.
DR   GermOnline; ENSRNOG00000030118; Rattus norvegicus.
DR   GO; GO:0016324; C:apical plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0009986; C:cell surface; IDA:RGD.
DR   GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
DR   GO; GO:0019898; C:extrinsic to membrane; IEA:InterPro.
DR   GO; GO:0031527; C:filopodium membrane; IDA:RGD.
DR   GO; GO:0009898; C:internal side of plasma membrane; IDA:RGD.
DR   GO; GO:0031528; C:microvillus membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0030667; C:secretory granule membrane; IDA:RGD.
DR   GO; GO:0005625; C:soluble fraction; IDA:RGD.
DR   GO; GO:0003779; F:actin binding; IDA:RGD.
DR   GO; GO:0030674; F:protein binding, bridging; TAS:RGD.
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; RATX.PE718; -.
KW   ENSRNOG00000030118820036002503210000011;
KW   Msn; MOES_RAT; AF004811;
KW   Acetylation; Cell membrane; Cell projection; Complete proteome;
KW   Cytoplasm; Cytoskeleton; Direct protein sequencing; Membrane;
KW   Phosphoprotein; Reference proteome.
SQ   SEQUENCE   576 AA;  UNKNOWN MW;  UNKNOWN CRC64;
     PKGISVRVTT MDAELEFAIQ PNTTGKQLFD QVVKTIGLRE VWFFGLQYQD TKAFSTWLKL
     NKKVTAQDVR KESPLLFKFR AKFYPEDVSE ELIQDITQRL FFLQVKEGIL NDDIYCPPET
     AVLLASYAVQ SKYGDFNKEV HKSGYLAGDK LLPQRVLEQH KLNKDQWEER IQVWHEEHRG
     MLREDAVLEY LKIAQDLEMY GVNYFSIKNK KGSELWLGVD ALGLNIYEQN DRLTPKIGFP
     WSEIRNISFN DKKFVIKPID KKAPDFVFYA PRLRINKRIL ALCMGNHELY MRRRKPDTIE
     VQQMKAQARE EKHQKQMERA LLENEKKKRE LAEKEKEKIE REKEELMEKL KQIEEQTKKA
     QQELEEQTRR ALELEQERKR AQSEAEKLAK ERQEAEEAKE ALLQASRDQK KTQEQLASEM
     AELTARISQL EMARKKKESE AEEWQQKAQM VQEDLEKTRA ELKTAMSTPH VAEPAENEHD
     EQDENGAEAS AELRADAMAK DRSEEERTTE AEKNERVQKH LKALTSELAN ARDESKKTTN
     DMIHAENMRL GRDKYKTLRQ IRQGNTKQRI DEFESM
//

If you have problems or comments...

PBIL Back to PBIL home page