MOES_RAT
ID MOES_RAT Reviewed; 577 AA.
AC O35763;
DT 27-JUN-2003, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 164.
DE RecName: Full=Moesin {ECO:0000250|UniProtKB:P26038};
DE AltName: Full=Membrane-organizing extension spike protein;
GN Name=Msn {ECO:0000312|RGD:621260};
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND PHOSPHORYLATION.
RX PubMed=10945828;
RA Theoharides T.C., Wang L., Pang X., Letourneau R., Culm K.E., Basu S.,
RA Wang Y., Correia I.;
RT "Cloning and cellular localization of the rat mast cell 78-kDa protein
RT phosphorylated in response to the mast cell 'stabilizer' cromolyn.";
RL J. Pharmacol. Exp. Ther. 294:810-821(2000).
RN [2]
RP PROTEIN SEQUENCE OF 262-272, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC STRAIN=Sprague-Dawley; TISSUE=Spinal cord;
RA Lubec G., Afjehi-Sadat L.;
RL Submitted (DEC-2006) to UniProtKB.
RN [3]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-407, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
CC -!- FUNCTION: Ezrin-radixin-moesin (ERM) family protein that connects the
CC actin cytoskeleton to the plasma membrane and thereby regulates the
CC structure and function of specific domains of the cell cortex. Tethers
CC actin filaments by oscillating between a resting and an activated state
CC providing transient interactions between moesin and the actin
CC cytoskeleton. Once phosphorylated on its C-terminal threonine, moesin
CC is activated leading to interaction with F-actin and cytoskeletal
CC rearrangement. These rearrangements regulate many cellular processes,
CC including cell shape determination, membrane transport, and signal
CC transduction. The role of moesin is particularly important in immunity
CC acting on both T and B-cells homeostasis and self-tolerance, regulating
CC lymphocyte egress from lymphoid organs (By similarity). Modulates
CC phagolysosomal biogenesis in macrophages (By similarity). Participates
CC also in immunologic synapse formation (By similarity).
CC {ECO:0000250|UniProtKB:P26038, ECO:0000250|UniProtKB:P26041}.
CC -!- ACTIVITY REGULATION: A head-to-tail association, of the N-terminal and
CC C-terminal halves results in a closed conformation (inactive form)
CC which is incapable of actin or membrane-binding.
CC {ECO:0000250|UniProtKB:P26038}.
CC -!- SUBUNIT: In resting T-cells, part of a PAG1-SLC9A3R1-MSN complex which
CC is disrupted upon TCR activation. Interacts with SLC9A3R1. Interacts
CC with PPP1R16B. Interacts with PDZD8. Interacts with SELPLG and SYK;
CC these interaction mediate the activation of SYK by SELPLG. Interacts
CC with PDPN (via cytoplasmic domain); this interaction activates RHOA and
CC promotes epithelial-mesenchymal transition. Interacts with SPN/CD43
CC cytoplasmic tail (By similarity). Interacts with CD44 (By similarity).
CC Interacts with ICAM2 (By similarity). Interacts with ICAM3 (via C-
CC terminus). Interacts with PDZD8. Interacts with F-actin. Interacts with
CC CD46 (By similarity). Interacts with PTPN6 (By similarity).
CC {ECO:0000250|UniProtKB:P26038, ECO:0000250|UniProtKB:P26041}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:P26038};
CC Peripheral membrane protein {ECO:0000250|UniProtKB:P26041}; Cytoplasmic
CC side {ECO:0000250|UniProtKB:P26041}. Cytoplasm, cytoskeleton
CC {ECO:0000250|UniProtKB:P26041}. Apical cell membrane
CC {ECO:0000250|UniProtKB:P26041}; Peripheral membrane protein
CC {ECO:0000250|UniProtKB:P26041}; Cytoplasmic side
CC {ECO:0000250|UniProtKB:P26041}. Cell projection, microvillus membrane
CC {ECO:0000250|UniProtKB:P26041}; Peripheral membrane protein
CC {ECO:0000250|UniProtKB:P26041}; Cytoplasmic side
CC {ECO:0000250|UniProtKB:P26041}. Cell projection, microvillus
CC {ECO:0000250|UniProtKB:P26041}. Note=Phosphorylated form is enriched in
CC microvilli-like structures at apical membrane. Increased cell membrane
CC localization of both phosphorylated and non-phosphorylated forms seen
CC after thrombin treatment (By similarity). Localizes at the uropods of T
CC lymphoblasts (By similarity). {ECO:0000250|UniProtKB:P26038,
CC ECO:0000250|UniProtKB:P26041}.
CC -!- DOMAIN: The [IL]-x-C-x-x-[DE] motif is a proposed target motif for
CC cysteine S-nitrosylation mediated by the iNOS-S100A8/A9
CC transnitrosylase complex. {ECO:0000250|UniProtKB:P26038}.
CC -!- PTM: Phosphorylation on Thr-558 is crucial for the formation of
CC microvilli-like structures. Phosphorylation by ROCK2 suppresses the
CC head-to-tail association of the N-terminal and C-terminal halves
CC resulting in an opened conformation which is capable of actin and
CC membrane-binding. Phosphorylation on Thr-558 by STK10 negatively
CC regulates lymphocyte migration and polarization (By similarity).
CC {ECO:0000250}.
CC -!- PTM: S-nitrosylation of Cys-117 is induced by interferon-gamma and
CC oxidatively-modified low-densitity lipoprotein (LDL(ox)) implicating
CC the iNOS-S100A8/9 transnitrosylase complex.
CC {ECO:0000250|UniProtKB:P26038}.
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DR EMBL; AF004811; AAB61666.1; -; mRNA.
DR RefSeq; NP_110490.1; NM_030863.1.
DR AlphaFoldDB; O35763; -.
DR SMR; O35763; -.
DR BioGRID; 249518; 3.
DR CORUM; O35763; -.
DR IntAct; O35763; 5.
DR MINT; O35763; -.
DR STRING; 10116.ENSRNOP00000068359; -.
DR iPTMnet; O35763; -.
DR PhosphoSitePlus; O35763; -.
DR World-2DPAGE; 0004:O35763; -.
DR jPOST; O35763; -.
DR PaxDb; O35763; -.
DR PRIDE; O35763; -.
DR GeneID; 81521; -.
DR KEGG; rno:81521; -.
DR CTD; 4478; -.
DR RGD; 621260; Msn.
DR eggNOG; KOG3529; Eukaryota.
DR InParanoid; O35763; -.
DR OrthoDB; 627741at2759; -.
DR PhylomeDB; O35763; -.
DR Reactome; R-RNO-437239; Recycling pathway of L1.
DR PRO; PR:O35763; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0005912; C:adherens junction; IBA:GO_Central.
DR GO; GO:0045177; C:apical part of cell; ISO:RGD.
DR GO; GO:0016324; C:apical plasma membrane; ISO:RGD.
DR GO; GO:0016323; C:basolateral plasma membrane; ISO:RGD.
DR GO; GO:0071944; C:cell periphery; ISO:RGD.
DR GO; GO:0009986; C:cell surface; IDA:RGD.
DR GO; GO:0051286; C:cell tip; IDA:RGD.
DR GO; GO:0009898; C:cytoplasmic side of plasma membrane; IDA:RGD.
DR GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
DR GO; GO:0030175; C:filopodium; ISO:RGD.
DR GO; GO:0031527; C:filopodium membrane; IDA:RGD.
DR GO; GO:0005902; C:microvillus; ISS:UniProtKB.
DR GO; GO:0031528; C:microvillus membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; ISO:RGD.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0031143; C:pseudopodium; ISO:RGD.
DR GO; GO:0030667; C:secretory granule membrane; IDA:RGD.
DR GO; GO:0030315; C:T-tubule; IDA:RGD.
DR GO; GO:0001931; C:uropod; ISO:RGD.
DR GO; GO:0003779; F:actin binding; IDA:RGD.
DR GO; GO:0050839; F:cell adhesion molecule binding; ISO:RGD.
DR GO; GO:0003725; F:double-stranded RNA binding; ISO:RGD.
DR GO; GO:0019899; F:enzyme binding; ISO:RGD.
DR GO; GO:0019901; F:protein kinase binding; ISO:RGD.
DR GO; GO:0030674; F:protein-macromolecule adaptor activity; TAS:RGD.
DR GO; GO:0005102; F:signaling receptor binding; ISO:RGD.
DR GO; GO:0071394; P:cellular response to testosterone stimulus; ISO:RGD.
DR GO; GO:0061028; P:establishment of endothelial barrier; ISO:RGD.
DR GO; GO:0045198; P:establishment of epithelial cell apical/basal polarity; ISO:RGD.
DR GO; GO:0022612; P:gland morphogenesis; ISO:RGD.
DR GO; GO:0001771; P:immunological synapse formation; ISS:UniProtKB.
DR GO; GO:0007159; P:leukocyte cell-cell adhesion; ISO:RGD.
DR GO; GO:0050900; P:leukocyte migration; ISO:RGD.
DR GO; GO:0022614; P:membrane to membrane docking; ISO:RGD.
DR GO; GO:2000643; P:positive regulation of early endosome to late endosome transport; ISO:RGD.
DR GO; GO:0010628; P:positive regulation of gene expression; ISO:RGD.
DR GO; GO:0071803; P:positive regulation of podosome assembly; ISO:RGD.
DR GO; GO:1902966; P:positive regulation of protein localization to early endosome; ISO:RGD.
DR GO; GO:0008360; P:regulation of cell shape; ISO:RGD.
DR GO; GO:0008361; P:regulation of cell size; ISO:RGD.
DR GO; GO:2000401; P:regulation of lymphocyte migration; ISO:RGD.
DR GO; GO:1902115; P:regulation of organelle assembly; ISO:RGD.
DR GO; GO:0070489; P:T cell aggregation; ISS:UniProtKB.
DR GO; GO:0072678; P:T cell migration; ISS:UniProtKB.
DR GO; GO:0042098; P:T cell proliferation; ISS:UniProtKB.
DR CDD; cd14473; FERM_B-lobe; 1.
DR CDD; cd13194; FERM_C_ERM; 1.
DR Gene3D; 1.20.80.10; -; 1.
DR Gene3D; 2.30.29.30; -; 1.
DR Gene3D; 6.10.360.10; -; 1.
DR InterPro; IPR019749; Band_41_domain.
DR InterPro; IPR011174; ERM.
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 PANTHER; PTHR23281; PTHR23281; 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 1: Evidence at protein level;
KW Acetylation; Cell membrane; Cell projection; Cytoplasm; Cytoskeleton;
KW Direct protein sequencing; Membrane; Phosphoprotein; Reference proteome;
KW S-nitrosylation.
FT CHAIN 1..577
FT /note="Moesin"
FT /id="PRO_0000219419"
FT DOMAIN 2..295
FT /note="FERM"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00084"
FT REGION 322..342
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 358..453
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 468..549
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 115..120
FT /note="[IL]-x-C-x-x-[DE] motif"
FT /evidence="ECO:0000250|UniProtKB:P26038"
FT COMPBIAS 358..416
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 430..453
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 485..549
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 74
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P26038"
FT MOD_RES 79
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P26038"
FT MOD_RES 83
FT /note="N6-succinyllysine"
FT /evidence="ECO:0000250|UniProtKB:P26043"
FT MOD_RES 116
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:P26038"
FT MOD_RES 117
FT /note="S-nitrosocysteine"
FT /evidence="ECO:0000250|UniProtKB:P26038"
FT MOD_RES 139
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P26038"
FT MOD_RES 165
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P26041"
FT MOD_RES 407
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 527
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P26038"
FT MOD_RES 558
FT /note="Phosphothreonine; by ROCK2 and STK10"
FT /evidence="ECO:0000250|UniProtKB:P26038"
SQ SEQUENCE 577 AA; 67739 MW; 49F47973D6C8FDC8 CRC64;
MPKTISVRVT TMDAELEFAI QPNTTGKQLF DQVVKTIGLR EVWFFGLQYQ DTKAFSTWLK
LNKKVTAQDV RKESPLLFKF RAKFYPEDVS EELIQDITQR LFFLQVKEGI LNDDIYCPPE
TAVLLASYAV QSKYGDFNKE VHKSGYLAGD KLLPQRVLEQ HKLNKDQWEE RIQVWHEEHR
GMLREDAVLE YLKIAQDLEM YGVNYFSIKN KKGSELWLGV DALGLNIYEQ NDRLTPKIGF
PWSEIRNISF NDKKFVIKPI DKKAPDFVFY APRLRINKRI LALCMGNHEL YMRRRKPDTI
EVQQMKAQAR EEKHQKQMER ALLENEKKKR ELAEKEKEKI EREKEELMEK LKQIEEQTKK
AQQELEEQTR RALELEQERK RAQSEAEKLA KERQEAEEAK EALLQASRDQ KKTQEQLASE
MAELTARVSQ LEMARKKKES EAEECHQKAQ MVQEDLEKTR AELKTAMSTP HVAEPAENEH
DEQDENGAEA SAELRADAMA KDRSEEERTT EAEKNERVQK HLKALTSELA NARDESKKTT
NDMIHAENMR LGRDKYKTLR QIRQGNTKQR IDEFESM
